{"search_session":{},"preferences":{"l":"en","queryLanguage":"en"},"patentId":"US_2008_0207497_A1","frontPageModel":{"patentViewModel":{"ref":{"entityRefType":"PATENT","entityRefId":"125-560-489-712-087"},"entityMetadata":{"linkedIds":{"empty":true},"tags":[],"collections":[{"id":191230,"type":"PATENT","title":"CellAdhesionANDSubtrateANDCancerCell","description":"","access":"OPEN_ACCESS","displayAvatar":false,"attested":false,"itemCount":50000,"tags":[],"user":{"id":404574126,"username":"JaimeGarcia","firstName":"","lastName":"","created":"2021-05-17T13:10:07.000Z","displayName":"JaimeGarcia","accountType":"PERSONAL","isOauthOnly":false},"notes":[],"sharedType":"PUBLISHED","hasLinkedSavedQueries":false,"savedQueries":[],"created":"2021-05-17T14:10:45Z","updated":"2021-05-17T14:10:50Z","lastEventDate":"2021-05-17T14:10:50Z"},{"id":191231,"type":"PATENT","title":"CellAdhesionANDsubstrateANDLeukemia","description":"","access":"OPEN_ACCESS","displayAvatar":false,"attested":false,"itemCount":50000,"tags":[],"user":{"id":404574126,"username":"JaimeGarcia","firstName":"","lastName":"","created":"2021-05-17T13:10:07.000Z","displayName":"JaimeGarcia","accountType":"PERSONAL","isOauthOnly":false},"notes":[],"sharedType":"PUBLISHED","hasLinkedSavedQueries":false,"savedQueries":[],"created":"2021-05-17T14:13:25Z","updated":"2021-05-17T14:13:28Z","lastEventDate":"2021-05-17T14:13:28Z"},{"id":199891,"type":"PATENT","title":"2010","description":"","access":"OPEN_ACCESS","displayAvatar":true,"attested":false,"itemCount":40220,"tags":[],"user":{"id":357745025,"username":"ZhangShuang","firstName":"Shuang","lastName":"Zhang","created":"2020-06-19T02:36:06.000Z","displayName":"Shuang Zhang","preferences":"{\"usage\":\"public\"}","accountType":"PERSONAL","isOauthOnly":false},"notes":[],"sharedType":"PUBLISHED","hasLinkedSavedQueries":false,"savedQueries":[],"created":"2022-03-23T10:14:55Z","updated":"2022-03-23T10:14:58Z","lastEventDate":"2022-03-23T10:14:58Z"},{"id":204920,"type":"PATENT","title":"CAR","description":"","access":"OPEN_ACCESS","displayAvatar":true,"attested":false,"itemCount":50000,"tags":[],"user":{"id":476754895,"username":"Theresa01","firstName":"","lastName":"","created":"2022-10-30T09:22:28.000Z","displayName":"Theresa01","accountType":"PERSONAL","isOauthOnly":false},"notes":[],"sharedType":"PUBLISHED","hasLinkedSavedQueries":false,"savedQueries":[],"created":"2022-10-30T09:29:58Z","updated":"2022-10-30T09:30:07Z","lastEventDate":"2022-10-30T09:30:07Z"},{"id":217860,"type":"PATENT","title":"Fermentation Yeast","description":"","access":"OPEN_ACCESS","displayAvatar":true,"avatar":{"id":4945,"key":"lens/avatar/268e0596-43ad-4136-8380-90b558256426"},"attested":false,"itemCount":2205,"tags":[],"user":{"id":150912620,"username":"Aaron","firstName":"Aaron","lastName":"Ballagh","created":"2016-04-19T11:31:15.000Z","displayName":"Aaron Ballagh","profilePictureKey":"lens/avatar/4c7ebafd-a645-4928-80f0-86226d3aba10","avatar":{"id":1420,"key":"lens/avatar/4c7ebafd-a645-4928-80f0-86226d3aba10"},"preferences":"{\"fontSize\":100,\"beta\":true,\"usage\":\"professional\"}","accountType":"PERSONAL","isOauthOnly":false},"notes":[],"sharedType":"PUBLISHED","hasLinkedSavedQueries":true,"savedQueries":[],"created":"2024-02-20T22:32:57Z","updated":"2024-02-20T22:45:24Z","lastEventDate":"2024-02-20T22:45:24Z"}],"notes":[],"inventorships":[],"privateCollections":[],"publicCollections":[{"id":191230,"type":"PATENT","title":"CellAdhesionANDSubtrateANDCancerCell","description":"","access":"OPEN_ACCESS","displayAvatar":false,"attested":false,"itemCount":50000,"tags":[],"user":{"id":404574126,"username":"JaimeGarcia","firstName":"","lastName":"","created":"2021-05-17T13:10:07.000Z","displayName":"JaimeGarcia","accountType":"PERSONAL","isOauthOnly":false},"notes":[],"sharedType":"PUBLISHED","hasLinkedSavedQueries":false,"savedQueries":[],"created":"2021-05-17T14:10:45Z","updated":"2021-05-17T14:10:50Z","lastEventDate":"2021-05-17T14:10:50Z"},{"id":191231,"type":"PATENT","title":"CellAdhesionANDsubstrateANDLeukemia","description":"","access":"OPEN_ACCESS","displayAvatar":false,"attested":false,"itemCount":50000,"tags":[],"user":{"id":404574126,"username":"JaimeGarcia","firstName":"","lastName":"","created":"2021-05-17T13:10:07.000Z","displayName":"JaimeGarcia","accountType":"PERSONAL","isOauthOnly":false},"notes":[],"sharedType":"PUBLISHED","hasLinkedSavedQueries":false,"savedQueries":[],"created":"2021-05-17T14:13:25Z","updated":"2021-05-17T14:13:28Z","lastEventDate":"2021-05-17T14:13:28Z"},{"id":199891,"type":"PATENT","title":"2010","description":"","access":"OPEN_ACCESS","displayAvatar":true,"attested":false,"itemCount":40220,"tags":[],"user":{"id":357745025,"username":"ZhangShuang","firstName":"Shuang","lastName":"Zhang","created":"2020-06-19T02:36:06.000Z","displayName":"Shuang Zhang","preferences":"{\"usage\":\"public\"}","accountType":"PERSONAL","isOauthOnly":false},"notes":[],"sharedType":"PUBLISHED","hasLinkedSavedQueries":false,"savedQueries":[],"created":"2022-03-23T10:14:55Z","updated":"2022-03-23T10:14:58Z","lastEventDate":"2022-03-23T10:14:58Z"},{"id":204920,"type":"PATENT","title":"CAR","description":"","access":"OPEN_ACCESS","displayAvatar":true,"attested":false,"itemCount":50000,"tags":[],"user":{"id":476754895,"username":"Theresa01","firstName":"","lastName":"","created":"2022-10-30T09:22:28.000Z","displayName":"Theresa01","accountType":"PERSONAL","isOauthOnly":false},"notes":[],"sharedType":"PUBLISHED","hasLinkedSavedQueries":false,"savedQueries":[],"created":"2022-10-30T09:29:58Z","updated":"2022-10-30T09:30:07Z","lastEventDate":"2022-10-30T09:30:07Z"},{"id":217860,"type":"PATENT","title":"Fermentation Yeast","description":"","access":"OPEN_ACCESS","displayAvatar":true,"avatar":{"id":4945,"key":"lens/avatar/268e0596-43ad-4136-8380-90b558256426"},"attested":false,"itemCount":2205,"tags":[],"user":{"id":150912620,"username":"Aaron","firstName":"Aaron","lastName":"Ballagh","created":"2016-04-19T11:31:15.000Z","displayName":"Aaron Ballagh","profilePictureKey":"lens/avatar/4c7ebafd-a645-4928-80f0-86226d3aba10","avatar":{"id":1420,"key":"lens/avatar/4c7ebafd-a645-4928-80f0-86226d3aba10"},"preferences":"{\"fontSize\":100,\"beta\":true,\"usage\":\"professional\"}","accountType":"PERSONAL","isOauthOnly":false},"notes":[],"sharedType":"PUBLISHED","hasLinkedSavedQueries":true,"savedQueries":[],"created":"2024-02-20T22:32:57Z","updated":"2024-02-20T22:45:24Z","lastEventDate":"2024-02-20T22:45:24Z"}],"privateNotes":[],"landscapeCollections":[],"landscapeNotes":[]},"document":{"record_lens_id":"125-560-489-712-087","lens_id":["125-560-489-712-087","137-813-441-514-522"],"doc_key":"US_20080207497_A1_20080828","created":"2016-01-15T10:36:20.487","docdb_id":288965933,"lens_internal":{"earliest_lens_id_created_time":"2016-01-15T10:36:20.487","last_modified":"2024-03-25T17:12:53.959","legacy_pub_key":"US_2008_0207497_A1","has_doc_lang":true,"has_biblio_lang":true,"has_all_title_lang":true,"has_all_abstract_lang":true,"has_all_claims_lang":true,"has_description_lang":true},"jurisdiction":"US","doc_number":"20080207497","kind":"A1","date_published":"2008-08-28","year_published":2008,"ids":["US_2008_0207497_A1","125-560-489-712-087","137-813-441-514-522","US_20080207497_A1_20080828","US","20080207497","A1","US20080207497A1","US20080207497","20080207497A1"],"lang":"en","publication_type":"PATENT_APPLICATION","application_reference":{"jurisdiction":"US","doc_number":"42616106","kind":"A","date":"2006-06-23"},"priority_claim":[{"jurisdiction":"US","doc_number":"42616106","kind":"A","date":"2006-06-23"},{"jurisdiction":"US","doc_number":"617701","kind":"A","date":"2001-12-04"},{"jurisdiction":"US","doc_number":"25102200","kind":"P","date":"2000-12-04"},{"jurisdiction":"US","doc_number":"25682400","kind":"P","date":"2000-12-20"}],"priority_claim.source":"DOCDB","earliest_priority_claim_date":"2000-12-04","title":{"en":[{"text":"CYTOTOXIC T-LYMPHOCYTE-INDUCING IMMUNOGENS FOR PREVENTION, TREATMENT, AND DIAGNOSIS OF CANCER","lang":"en","source":"DOCDB","data_format":"DOCDBA"}]},"title_lang":["en"],"has_title":true,"applicant":[{"name":"IMMUNOTOPE INC","residence":"US","sequence":1,"app_type":"applicant"}],"applicant_count":1,"has_applicant":true,"inventor":[{"name":"RAMAKRISHNA VENKY","residence":"US","sequence":1},{"name":"ROSS MARK M","residence":"US","sequence":2},{"name":"PHILIP RAMILA","residence":"US","sequence":3},{"name":"KELLER LORRAINE H","residence":"US","sequence":4}],"inventor_count":4,"has_inventor":true,"agent":[],"agent_count":0,"has_agent":false,"owner":[{"name":"IMMUNOTOPE INC","address":"THE PENNSYLVANIA BIOTECHNOLOGY CENTER, 3805 OLD EASTON ROAD, DOYLESTOWN, PENNSYLVANIA, 18902","sequence":2,"recorded_date":"2008-02-05","execution_date":"2008-01-23","is_current_owner":true}],"owner_count":1,"owner_all":[{"name":"IMMUNOTOPE INC","address":"THE PENNSYLVANIA BIOTECHNOLOGY CENTER, 3805 OLD EASTON ROAD, DOYLESTOWN, PENNSYLVANIA, 18902","sequence":2,"recorded_date":"2008-02-05","execution_date":"2008-01-23","is_current_owner":true}],"owner_all_count":1,"has_owner":true,"has_examiner":false,"class_ipcr":[{"symbol":"A61K38/16","version_indicator":"2006-01-01","class_symbol_position":"F","class_value":"I","action_date":"2008-08-28","class_status":"B","class_data_source":"H","generating_office":"US","sequence":1},{"symbol":"A61K39/00","version_indicator":"2006-01-01","class_value":"I","action_date":"2018-06-29","class_status":"R","class_data_source":"M","generating_office":"EP","sequence":2},{"symbol":"A61P35/00","version_indicator":"2006-01-01","class_symbol_position":"L","class_value":"I","action_date":"2008-08-28","class_status":"B","class_data_source":"H","generating_office":"US","sequence":3}],"class_ipcr.first_symbol":"A61K38/16","class_ipcr.later_symbol":["A61K39/00","A61P35/00"],"class_ipcr.inv_symbol":["A61K38/16","A61K39/00","A61P35/00"],"class_ipcr.add_symbol":[],"class_ipcr.source":"DOCDB","class_cpc":[{"symbol":"A61K38/19","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"I","action_date":"2013-01-01","class_status":"B","class_data_source":"H","generating_office":"EP","sequence":1},{"symbol":"A61K39/00","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"A","action_date":"2024-01-29","class_status":"R","class_data_source":"H","generating_office":"EP","sequence":2},{"symbol":"A61K39/0011","version_indicator":"2013-01-01","class_symbol_position":"F","class_value":"I","action_date":"2024-02-09","class_status":"R","class_data_source":"H","generating_office":"EP","sequence":3},{"symbol":"A61K2039/522","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"A","action_date":"2013-01-01","class_status":"B","class_data_source":"H","generating_office":"EP","sequence":4},{"symbol":"A61K2039/53","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"A","action_date":"2013-01-01","class_status":"B","class_data_source":"H","generating_office":"EP","sequence":5},{"symbol":"C07K14/47","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"I","action_date":"2013-01-01","class_status":"B","class_data_source":"H","generating_office":"EP","sequence":6},{"symbol":"C07K14/4738","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"I","action_date":"2013-01-01","class_status":"B","class_data_source":"H","generating_office":"EP","sequence":7},{"symbol":"C07K14/4748","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"I","action_date":"2013-01-01","class_status":"B","class_data_source":"H","generating_office":"EP","sequence":8},{"symbol":"C07K14/485","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"I","action_date":"2013-01-01","class_status":"B","class_data_source":"H","generating_office":"EP","sequence":9},{"symbol":"C07K14/705","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"I","action_date":"2013-01-01","class_status":"B","class_data_source":"H","generating_office":"EP","sequence":10},{"symbol":"C07K14/70546","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"I","action_date":"2013-01-01","class_status":"B","class_data_source":"H","generating_office":"EP","sequence":11},{"symbol":"C07K14/71","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"I","action_date":"2013-01-01","class_status":"B","class_data_source":"H","generating_office":"EP","sequence":12},{"symbol":"C12N5/0636","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"I","action_date":"2024-01-29","class_status":"R","class_data_source":"H","generating_office":"EP","sequence":13},{"symbol":"G01N33/57484","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"I","action_date":"2013-01-01","class_status":"B","class_data_source":"H","generating_office":"EP","sequence":14},{"symbol":"A61K38/18","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"I","action_date":"2013-04-04","class_status":"B","class_data_source":"H","generating_office":"EP","sequence":15},{"symbol":"A61K9/127","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"I","action_date":"2013-02-28","class_status":"B","class_data_source":"H","generating_office":"EP","sequence":16},{"symbol":"A61P35/00","version_indicator":"2018-01-01","class_symbol_position":"L","class_value":"I","action_date":"2020-03-27","class_status":"B","class_data_source":"H","generating_office":"EP","sequence":17},{"symbol":"A61P37/04","version_indicator":"2018-01-01","class_symbol_position":"L","class_value":"I","action_date":"2020-03-31","class_status":"B","class_data_source":"H","generating_office":"EP","sequence":18},{"symbol":"A61K2039/812","version_indicator":"2018-08-01","class_symbol_position":"L","class_value":"A","action_date":"2020-12-18","class_status":"R","class_data_source":"H","generating_office":"EP","sequence":19},{"symbol":"A61K39/4611","version_indicator":"2023-05-01","class_symbol_position":"L","class_value":"I","action_date":"2024-01-29","class_status":"R","class_data_source":"H","generating_office":"EP","sequence":20},{"symbol":"A61K39/4644","version_indicator":"2023-05-01","class_symbol_position":"L","class_value":"I","action_date":"2024-01-29","class_status":"R","class_data_source":"H","generating_office":"EP","sequence":21},{"symbol":"A61K39/0011","version_indicator":"2013-01-01","class_symbol_position":"F","class_value":"I","action_date":"2020-05-28","class_status":"B","class_data_source":"H","generating_office":"US","sequence":24},{"symbol":"C07K14/47","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"I","action_date":"2019-10-11","class_status":"B","class_data_source":"H","generating_office":"US","sequence":25},{"symbol":"C07K14/705","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"I","action_date":"2019-10-11","class_status":"B","class_data_source":"H","generating_office":"US","sequence":26},{"symbol":"A61K39/00","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"A","action_date":"2019-10-11","class_status":"B","class_data_source":"H","generating_office":"US","sequence":27},{"symbol":"A61K2039/522","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"A","action_date":"2019-10-11","class_status":"B","class_data_source":"H","generating_office":"US","sequence":28},{"symbol":"A61K2039/53","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"A","action_date":"2019-10-11","class_status":"B","class_data_source":"H","generating_office":"US","sequence":29},{"symbol":"C07K14/4748","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"I","action_date":"2019-10-11","class_status":"B","class_data_source":"H","generating_office":"US","sequence":30},{"symbol":"G01N33/57484","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"I","action_date":"2019-10-11","class_status":"B","class_data_source":"H","generating_office":"US","sequence":31},{"symbol":"A61K2039/5158","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"A","action_date":"2019-10-11","class_status":"B","class_data_source":"H","generating_office":"US","sequence":32},{"symbol":"C07K14/485","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"I","action_date":"2019-10-11","class_status":"B","class_data_source":"H","generating_office":"US","sequence":33},{"symbol":"A61K38/19","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"I","action_date":"2019-10-11","class_status":"B","class_data_source":"H","generating_office":"US","sequence":34},{"symbol":"C07K14/70546","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"I","action_date":"2019-10-11","class_status":"B","class_data_source":"H","generating_office":"US","sequence":35},{"symbol":"C12N5/0636","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"I","action_date":"2019-10-11","class_status":"B","class_data_source":"H","generating_office":"US","sequence":36},{"symbol":"C07K14/4738","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"I","action_date":"2019-10-11","class_status":"B","class_data_source":"H","generating_office":"US","sequence":37},{"symbol":"A61K2039/5154","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"A","action_date":"2019-10-11","class_status":"B","class_data_source":"H","generating_office":"US","sequence":38},{"symbol":"C07K14/71","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"I","action_date":"2019-10-11","class_status":"B","class_data_source":"H","generating_office":"US","sequence":39},{"symbol":"A61K9/127","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"I","action_date":"2019-10-11","class_status":"B","class_data_source":"H","generating_office":"US","sequence":40},{"symbol":"A61K38/18","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"I","action_date":"2019-10-11","class_status":"B","class_data_source":"H","generating_office":"US","sequence":41},{"symbol":"A61K2039/812","version_indicator":"2018-08-01","class_symbol_position":"L","class_value":"A","action_date":"2020-05-28","class_status":"B","class_data_source":"C","generating_office":"US","sequence":42}],"class_cpc_cset":[{"class":[{"symbol":"A61K38/19","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"I","action_date":"2013-01-01","class_status":"B","class_data_source":"H","generating_office":"EP"},{"symbol":"A61K2300/00","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"I","action_date":"2013-01-01","class_status":"B","class_data_source":"H","generating_office":"EP"}],"sequence":22},{"class":[{"symbol":"A61K38/18","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"I","action_date":"2013-04-04","class_status":"B","class_data_source":"H","generating_office":"EP"},{"symbol":"A61K2300/00","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"I","action_date":"2013-04-04","class_status":"B","class_data_source":"H","generating_office":"EP"}],"sequence":23},{"class":[{"symbol":"A61K38/19","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"I","action_date":"2019-10-11","class_status":"B","class_data_source":"H","generating_office":"US"},{"symbol":"A61K2300/00","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"I","action_date":"2019-10-11","class_status":"B","class_data_source":"H","generating_office":"US"}],"sequence":43},{"class":[{"symbol":"A61K38/18","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"I","action_date":"2019-10-11","class_status":"B","class_data_source":"H","generating_office":"US"},{"symbol":"A61K2300/00","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"I","action_date":"2019-10-11","class_status":"B","class_data_source":"H","generating_office":"US"}],"sequence":44}],"class_cpc.first_symbol":"A61K39/0011","class_cpc.later_symbol":["A61K38/19","A61K39/00","A61K2039/522","A61K2039/53","C07K14/47","C07K14/4738","C07K14/4748","C07K14/485","C07K14/705","C07K14/70546","C07K14/71","C12N5/0636","G01N33/57484","A61K38/18","A61K9/127","A61P35/00","A61P37/04","A61K2039/812","A61K39/4611","A61K39/4644","C07K14/47","C07K14/705","A61K39/00","A61K2039/522","A61K2039/53","C07K14/4748","G01N33/57484","A61K2039/5158","C07K14/485","A61K38/19","C07K14/70546","C12N5/0636","C07K14/4738","A61K2039/5154","C07K14/71","A61K9/127","A61K38/18","A61K2039/812"],"class_cpc.inv_symbol":["A61K38/19","A61K39/0011","C07K14/47","C07K14/4738","C07K14/4748","C07K14/485","C07K14/705","C07K14/70546","C07K14/71","C12N5/0636","G01N33/57484","A61K38/18","A61K9/127","A61P35/00","A61P37/04","A61K39/4611","A61K39/4644","A61K39/0011","C07K14/47","C07K14/705","C07K14/4748","G01N33/57484","C07K14/485","A61K38/19","C07K14/70546","C12N5/0636","C07K14/4738","C07K14/71","A61K9/127","A61K38/18"],"class_cpc.add_symbol":["A61K39/00","A61K2039/522","A61K2039/53","A61K2039/812","A61K39/00","A61K2039/522","A61K2039/53","A61K2039/5158","A61K2039/5154","A61K2039/812"],"class_cpc.source":"DOCDB","class_national":[{"symbol":"514/12","symbol_position":"F"}],"class_national.first_symbol":"514/12","class_national.later_symbol":[],"class_national.source":"DOCDB","reference_cited":[{"patent":{"num":1,"document_id":{"jurisdiction":"US","doc_number":"6168804","kind":"B1","date":"2001-01-02","name":"SAMUEL JOHN [CA], et al"},"lens_id":"161-938-295-910-728","category":[],"us_category":[],"cited_phase":"PRS","rel_claims":[],"sequence":1}},{"patent":{"num":2,"document_id":{"jurisdiction":"US","doc_number":"4501728","kind":"A","date":"1985-02-26","name":"GEHO W BLAIR [US], et al"},"lens_id":"067-717-278-391-368","category":[],"us_category":[],"cited_phase":"PRS","rel_claims":[],"sequence":2}},{"patent":{"num":3,"document_id":{"jurisdiction":"US","doc_number":"4722848","kind":"A","date":"1988-02-02","name":"PAOLETTI ENZO [US], et al"},"lens_id":"175-160-135-728-656","category":[],"us_category":[],"cited_phase":"PRS","rel_claims":[],"sequence":3}},{"patent":{"num":4,"document_id":{"jurisdiction":"US","doc_number":"6867283","kind":"B2","date":"2005-03-15","name":"BARNEA EILON [IL], et al"},"lens_id":"108-804-886-819-568","category":[],"us_category":[],"cited_phase":"PRS","rel_claims":[],"sequence":4}},{"patent":{"num":5,"document_id":{"jurisdiction":"US","doc_number":"6548064","kind":"B1","date":"2003-04-15","name":"TURECI OZLEM [DE], et al"},"lens_id":"150-029-335-247-426","category":[],"us_category":[],"cited_phase":"PRS","rel_claims":[],"sequence":5}},{"patent":{"num":6,"document_id":{"jurisdiction":"US","doc_number":"5019369","kind":"A","date":"1991-05-28","name":"PRESANT CARY A [US], et al"},"lens_id":"131-596-750-988-194","category":[],"us_category":[],"cited_phase":"PRS","rel_claims":[],"sequence":6}},{"patent":{"num":7,"document_id":{"jurisdiction":"US","doc_number":"5747269","kind":"A","date":"1998-05-05","name":"RAMMENSEE HANS-GEORG [DE], et al"},"lens_id":"135-414-193-969-286","category":[],"us_category":[],"cited_phase":"PRS","rel_claims":[],"sequence":7}},{"patent":{"num":8,"document_id":{"jurisdiction":"US","doc_number":"4837028","kind":"A","date":"1989-06-06","name":"ALLEN THERESA M [CA]"},"lens_id":"159-393-429-720-083","category":[],"us_category":[],"cited_phase":"PRS","rel_claims":[],"sequence":8}},{"patent":{"num":9,"document_id":{"jurisdiction":"US","doc_number":"5635363","kind":"A","date":"1997-06-03","name":"ALTMAN JOHN D [US], et al"},"lens_id":"096-891-224-777-877","category":[],"us_category":[],"cited_phase":"PRS","rel_claims":[],"sequence":9}},{"patent":{"num":10,"document_id":{"jurisdiction":"US","doc_number":"5763219","kind":"A","date":"1998-06-09","name":"KEYOMARSI KHANDAN [US]"},"lens_id":"026-857-801-805-551","category":[],"us_category":[],"cited_phase":"PRS","rel_claims":[],"sequence":10}},{"patent":{"num":11,"document_id":{"jurisdiction":"US","doc_number":"4844893","kind":"A","date":"1989-07-04","name":"HONSIK CYRIL J [US], et al"},"lens_id":"110-336-075-626-567","category":[],"us_category":[],"cited_phase":"PRS","rel_claims":[],"sequence":11}},{"patent":{"num":12,"document_id":{"jurisdiction":"US","doc_number":"5645994","kind":"A","date":"1997-07-08","name":"HUANG WAI MUN [US]"},"lens_id":"125-782-833-511-975","category":[],"us_category":[],"cited_phase":"PRS","rel_claims":[],"sequence":12}},{"patent":{"num":13,"document_id":{"jurisdiction":"US","doc_number":"7083789","kind":"B2","date":"2006-08-01","name":"RAMAKRISHNA VENKY [US], et al"},"lens_id":"096-832-464-507-462","category":[],"us_category":[],"cited_phase":"PRS","rel_claims":[],"sequence":13}},{"patent":{"num":14,"document_id":{"jurisdiction":"US","doc_number":"7087712","kind":"B1","date":"2006-08-08","name":"BROSSART PETER [DE], et al"},"lens_id":"054-222-551-792-802","category":[],"us_category":[],"cited_phase":"PRS","rel_claims":[],"sequence":14}},{"patent":{"num":15,"document_id":{"jurisdiction":"US","doc_number":"4690915","kind":"A","date":"1987-09-01","name":"ROSENBERG STEVEN A [US]"},"lens_id":"066-958-731-500-413","category":[],"us_category":[],"cited_phase":"PRS","rel_claims":[],"sequence":15}},{"patent":{"num":16,"document_id":{"jurisdiction":"US","doc_number":"7270819","kind":"B2","date":"2007-09-18","name":"TURECI OZLEM [DE], et al"},"lens_id":"074-318-404-138-757","category":[],"us_category":[],"cited_phase":"PRS","rel_claims":[],"sequence":16}},{"patent":{"num":17,"document_id":{"jurisdiction":"US","doc_number":"5972643","kind":"A","date":"1999-10-26","name":"LOBANENKOV VICTOR L [US], et al"},"lens_id":"165-403-263-796-080","category":[],"us_category":[],"cited_phase":"PRS","rel_claims":[],"sequence":17}},{"patent":{"num":18,"document_id":{"jurisdiction":"US","doc_number":"6140464","kind":"A","date":"2000-10-31","name":"PFREUNDSCHUH MICHAEL [DE], et al"},"lens_id":"037-190-947-361-072","category":[],"us_category":[],"cited_phase":"PRS","rel_claims":[],"sequence":18}},{"patent":{"num":19,"document_id":{"jurisdiction":"US","doc_number":"4235871","kind":"A","date":"1980-11-25","name":"PAPAHADJOPOULOS DEMETRIOS P [US], et al"},"lens_id":"060-160-799-009-187","category":[],"us_category":[],"cited_phase":"PRS","rel_claims":[],"sequence":19}},{"patent":{"num":20,"document_id":{"jurisdiction":"US","doc_number":"2004236091","kind":"A1","date":"2004-11-25","name":"CHICZ ROMAN M [US], et al"},"lens_id":"016-313-558-174-332","category":[],"us_category":[],"cited_phase":"PRS","rel_claims":[],"sequence":20}}],"reference_cited.source":"DOCDB","reference_cited.patent_count":20,"cites_patent":true,"reference_cited.npl_count":0,"reference_cited.npl_resolved_count":0,"cites_npl":false,"cites_resolved_npl":false,"cited_by":{"patent_count":69,"patent":[{"lens_id":"102-158-852-675-875","document_id":{"jurisdiction":"US","doc_number":"9545437","kind":"B2"}},{"lens_id":"186-132-942-321-140","document_id":{"jurisdiction":"JP","doc_number":"2016047825","kind":"A"}},{"lens_id":"142-153-340-111-978","document_id":{"jurisdiction":"US","doc_number":"9289478","kind":"B2"}},{"lens_id":"147-689-927-157-85X","document_id":{"jurisdiction":"WO","doc_number":"2016127249","kind":"A1"}},{"lens_id":"188-562-950-788-325","document_id":{"jurisdiction":"US","doc_number":"11136352","kind":"B2"}},{"lens_id":"112-575-167-063-643","document_id":{"jurisdiction":"KR","doc_number":"20160103558","kind":"A"}},{"lens_id":"061-096-481-500-93X","document_id":{"jurisdiction":"JP","doc_number":"2012522488","kind":"A"}},{"lens_id":"142-063-948-759-386","document_id":{"jurisdiction":"US","doc_number":"20170298109","kind":"A1"}},{"lens_id":"184-467-883-869-449","document_id":{"jurisdiction":"US","doc_number":"10487126","kind":"B2"}},{"lens_id":"135-265-373-803-826","document_id":{"jurisdiction":"US","doc_number":"10788494","kind":"B2"}},{"lens_id":"136-282-900-017-167","document_id":{"jurisdiction":"US","doc_number":"20080038285","kind":"A1"}},{"lens_id":"093-468-964-607-964","document_id":{"jurisdiction":"US","doc_number":"9017688","kind":"B2"}},{"lens_id":"002-025-848-701-458","document_id":{"jurisdiction":"US","doc_number":"9945858","kind":"B2"}},{"lens_id":"133-713-952-165-957","document_id":{"jurisdiction":"US","doc_number":"11667706","kind":"B2"}},{"lens_id":"121-367-117-872-59X","document_id":{"jurisdiction":"KR","doc_number":"20200123696","kind":"A"}},{"lens_id":"128-658-254-691-829","document_id":{"jurisdiction":"US","doc_number":"9458447","kind":"B2"}},{"lens_id":"151-635-763-659-570","document_id":{"jurisdiction":"US","doc_number":"20110288270","kind":"A1"}},{"lens_id":"177-365-891-769-746","document_id":{"jurisdiction":"EP","doc_number":"3256488","kind":"A4"}},{"lens_id":"087-387-927-145-869","document_id":{"jurisdiction":"US","doc_number":"10494429","kind":"B2"}},{"lens_id":"183-157-206-054-138","document_id":{"jurisdiction":"US","doc_number":"10597446","kind":"B2"}},{"lens_id":"198-723-553-589-119","document_id":{"jurisdiction":"CN","doc_number":"104774260","kind":"A"}},{"lens_id":"054-979-432-342-811","document_id":{"jurisdiction":"WO","doc_number":"2021034179","kind":"A1"}},{"lens_id":"143-464-526-148-319","document_id":{"jurisdiction":"US","doc_number":"7811828","kind":"B2"}},{"lens_id":"199-424-550-822-145","document_id":{"jurisdiction":"JP","doc_number":"2018505682","kind":"A"}},{"lens_id":"187-289-149-797-057","document_id":{"jurisdiction":"CN","doc_number":"102170901","kind":"A"}},{"lens_id":"069-865-927-990-457","document_id":{"jurisdiction":"US","doc_number":"10654904","kind":"B2"}},{"lens_id":"164-254-481-674-249","document_id":{"jurisdiction":"US","doc_number":"9296823","kind":"B2"}},{"lens_id":"092-623-607-616-644","document_id":{"jurisdiction":"US","doc_number":"20120128705","kind":"A1"}},{"lens_id":"144-901-927-159-94X","document_id":{"jurisdiction":"WO","doc_number":"2017053735","kind":"A1"}},{"lens_id":"084-020-334-156-837","document_id":{"jurisdiction":"KR","doc_number":"20180088494","kind":"A"}},{"lens_id":"053-140-697-102-848","document_id":{"jurisdiction":"US","doc_number":"20150125478","kind":"A1"}},{"lens_id":"086-691-202-203-742","document_id":{"jurisdiction":"US","doc_number":"10793599","kind":"B2"}},{"lens_id":"021-097-364-745-413","document_id":{"jurisdiction":"US","doc_number":"10227381","kind":"B2"}},{"lens_id":"188-282-760-552-235","document_id":{"jurisdiction":"US","doc_number":"10597447","kind":"B2"}},{"lens_id":"171-103-344-264-601","document_id":{"jurisdiction":"US","doc_number":"8653234","kind":"B2"}},{"lens_id":"072-072-058-787-534","document_id":{"jurisdiction":"KR","doc_number":"20210020826","kind":"A"}},{"lens_id":"129-348-302-736-714","document_id":{"jurisdiction":"US","doc_number":"9993540","kind":"B2"}},{"lens_id":"096-418-680-154-071","document_id":{"jurisdiction":"CN","doc_number":"102448980","kind":"A"}},{"lens_id":"060-271-587-169-623","document_id":{"jurisdiction":"US","doc_number":"11519912","kind":"B2"}},{"lens_id":"047-283-135-301-686","document_id":{"jurisdiction":"US","doc_number":"8552146","kind":"B2"}},{"lens_id":"155-717-115-036-206","document_id":{"jurisdiction":"CN","doc_number":"107337733","kind":"A"}},{"lens_id":"151-543-547-796-652","document_id":{"jurisdiction":"US","doc_number":"10857219","kind":"B2"}},{"lens_id":"127-412-877-806-585","document_id":{"jurisdiction":"WO","doc_number":"2012135332","kind":"A1"}},{"lens_id":"199-811-506-800-723","document_id":{"jurisdiction":"US","doc_number":"11905319","kind":"B2"}},{"lens_id":"138-085-139-318-815","document_id":{"jurisdiction":"US","doc_number":"11208434","kind":"B2"}},{"lens_id":"023-359-962-161-418","document_id":{"jurisdiction":"US","doc_number":"10265389","kind":"B2"}},{"lens_id":"198-598-521-435-035","document_id":{"jurisdiction":"JP","doc_number":"6053255","kind":"B2"}},{"lens_id":"080-943-020-681-970","document_id":{"jurisdiction":"US","doc_number":"8557955","kind":"B2"}},{"lens_id":"003-951-442-788-089","document_id":{"jurisdiction":"US","doc_number":"20190119342","kind":"A1"}},{"lens_id":"172-253-185-530-553","document_id":{"jurisdiction":"US","doc_number":"20100158929","kind":"A1"}},{"lens_id":"085-443-837-839-77X","document_id":{"jurisdiction":"JP","doc_number":"2016145210","kind":"A"}},{"lens_id":"054-665-128-323-761","document_id":{"jurisdiction":"US","doc_number":"20120288514","kind":"A1"}},{"lens_id":"149-761-208-789-080","document_id":{"jurisdiction":"CN","doc_number":"103429254","kind":"A"}},{"lens_id":"193-515-588-610-581","document_id":{"jurisdiction":"US","doc_number":"9283267","kind":"B2"}},{"lens_id":"049-126-615-818-792","document_id":{"jurisdiction":"US","doc_number":"20190010190","kind":"A1"}},{"lens_id":"046-619-677-376-818","document_id":{"jurisdiction":"US","doc_number":"10414813","kind":"B2"}},{"lens_id":"150-300-765-217-45X","document_id":{"jurisdiction":"CN","doc_number":"106913863","kind":"A"}},{"lens_id":"085-201-589-902-044","document_id":{"jurisdiction":"KR","doc_number":"20200085381","kind":"A"}},{"lens_id":"155-076-583-769-809","document_id":{"jurisdiction":"US","doc_number":"10822404","kind":"B2"}},{"lens_id":"010-975-348-810-235","document_id":{"jurisdiction":"CN","doc_number":"113447656","kind":"A"}},{"lens_id":"035-351-441-328-816","document_id":{"jurisdiction":"EP","doc_number":"2414383","kind":"A4"}},{"lens_id":"009-121-197-073-084","document_id":{"jurisdiction":"US","doc_number":"20220054613","kind":"A1"}},{"lens_id":"108-363-205-828-725","document_id":{"jurisdiction":"WO","doc_number":"2015038884","kind":"A3"}},{"lens_id":"152-518-432-109-471","document_id":{"jurisdiction":"WO","doc_number":"2012051207","kind":"A3"}},{"lens_id":"184-511-813-255-092","document_id":{"jurisdiction":"CN","doc_number":"103748113","kind":"A"}},{"lens_id":"138-806-474-708-498","document_id":{"jurisdiction":"US","doc_number":"9920120","kind":"B2"}},{"lens_id":"068-642-724-901-130","document_id":{"jurisdiction":"US","doc_number":"9353188","kind":"B2"}},{"lens_id":"018-299-797-524-71X","document_id":{"jurisdiction":"JP","doc_number":"2013505296","kind":"A"}},{"lens_id":"132-736-172-801-444","document_id":{"jurisdiction":"US","doc_number":"10383925","kind":"B2"}}]},"cited_by_patent":true,"family":{"simple":{"size":9,"id":192478061,"member":[{"lens_id":"151-396-920-560-721","document_id":{"jurisdiction":"CA","doc_number":"2659124","kind":"A1","date":"2007-12-27"}},{"lens_id":"115-271-724-136-152","document_id":{"jurisdiction":"US","doc_number":"7919467","kind":"B2","date":"2011-04-05"}},{"lens_id":"088-621-029-791-980","document_id":{"jurisdiction":"AU","doc_number":"2007260824","kind":"A1","date":"2007-12-27"}},{"lens_id":"026-581-389-439-910","document_id":{"jurisdiction":"EP","doc_number":"2043679","kind":"A2","date":"2009-04-08"}},{"lens_id":"125-560-489-712-087","document_id":{"jurisdiction":"US","doc_number":"20080207497","kind":"A1","date":"2008-08-28"}},{"lens_id":"050-734-965-130-159","document_id":{"jurisdiction":"WO","doc_number":"2007150077","kind":"A2","date":"2007-12-27"}},{"lens_id":"076-781-313-696-064","document_id":{"jurisdiction":"US","doc_number":"20110142919","kind":"A1","date":"2011-06-16"}},{"lens_id":"115-885-524-731-965","document_id":{"jurisdiction":"EP","doc_number":"2043679","kind":"A4","date":"2010-04-14"}},{"lens_id":"092-784-427-134-418","document_id":{"jurisdiction":"WO","doc_number":"2007150077","kind":"A8","date":"2008-08-28"}}]},"extended":{"size":9,"id":192324939,"member":[{"lens_id":"151-396-920-560-721","document_id":{"jurisdiction":"CA","doc_number":"2659124","kind":"A1","date":"2007-12-27"}},{"lens_id":"092-784-427-134-418","document_id":{"jurisdiction":"WO","doc_number":"2007150077","kind":"A8","date":"2008-08-28"}},{"lens_id":"088-621-029-791-980","document_id":{"jurisdiction":"AU","doc_number":"2007260824","kind":"A1","date":"2007-12-27"}},{"lens_id":"026-581-389-439-910","document_id":{"jurisdiction":"EP","doc_number":"2043679","kind":"A2","date":"2009-04-08"}},{"lens_id":"125-560-489-712-087","document_id":{"jurisdiction":"US","doc_number":"20080207497","kind":"A1","date":"2008-08-28"}},{"lens_id":"076-781-313-696-064","document_id":{"jurisdiction":"US","doc_number":"20110142919","kind":"A1","date":"2011-06-16"}},{"lens_id":"050-734-965-130-159","document_id":{"jurisdiction":"WO","doc_number":"2007150077","kind":"A2","date":"2007-12-27"}},{"lens_id":"115-885-524-731-965","document_id":{"jurisdiction":"EP","doc_number":"2043679","kind":"A4","date":"2010-04-14"}},{"lens_id":"115-271-724-136-152","document_id":{"jurisdiction":"US","doc_number":"7919467","kind":"B2","date":"2011-04-05"}}]}},"sequence":{"seq_list_key":"US_20080207497_A1","type":["P"],"length_bucket":["AA_301","AA_1_50","AA_51_300"],"length":[1024,1025,2054,8,3080,1032,9,10,11,12,1038,1040,1041,1042,20,1047,1052,2077,35,1066,2090,3117,1070,1071,1073,2099,1077,1080,57,5179,1083,1085,1087,5183,1090,68,72,74,75,78,2135,2136,88,2137,1117,1118,95,3169,1123,101,3174,1127,1132,108,2157,1133,110,111,1137,114,1139,1140,1141,117,122,123,124,1150,1153,1157,137,3210,139,1164,140,1165,143,145,148,1172,1173,149,150,151,152,2202,1181,158,162,163,164,1191,169,1193,172,1198,174,176,2225,1202,181,1205,1210,3259,2235,190,191,193,194,195,196,197,1221,198,202,1227,204,205,206,207,1232,1233,211,213,1237,214,215,216,1243,219,220,221,222,223,226,228,1253,229,233,1257,1258,236,3312,242,243,1268,244,1269,245,1272,248,249,252,4349,253,1278,254,256,259,262,263,266,267,4363,271,2321,276,281,284,288,1312,1313,291,292,4388,293,2341,294,295,1320,297,299,300,301,2349,2351,1328,304,305,2353,306,307,1332,308,309,310,311,313,314,1338,315,2363,316,317,319,323,324,330,333,336,338,342,1368,344,1369,3418,346,348,350,1374,351,353,354,355,357,358,1382,359,360,361,362,1386,366,1390,367,368,369,370,371,372,373,375,1400,376,1401,377,379,380,381,383,1408,386,387,2436,388,390,391,393,4490,2442,394,1419,398,400,403,404,405,407,411,412,415,1440,418,2467,420,1445,2471,1447,2472,1451,428,429,430,1454,435,1462,438,1463,439,440,1464,441,443,444,446,4544,450,453,454,456,458,461,462,465,466,468,1493,1494,471,475,1499,476,478,480,1504,481,482,483,485,488,490,2540,493,2541,1521,499,500,503,504,505,1529,2555,507,1531,2556,508,509,510,513,514,515,516,1543,522,523,525,526,527,529,531,532,534,535,2584,536,1560,539,1563,540,1564,541,543,548,4646,550,1574,551,554,556,557,558,1583,559,561,562,572,575,2623,1600,579,1607,5703,585,1609,3657,4684,1615,593,594,595,597,1621,3670,598,2646,599,600,2649,601,3674,1626,604,605,606,607,612,614,615,616,619,620,621,622,623,625,627,628,629,633,638,639,640,642,643,644,22152,649,652,2701,654,655,661,662,663,664,2715,671,1695,672,1696,1698,677,1704,681,684,686,691,1717,1722,702,703,704,1729,706,707,709,711,712,713,715,1739,716,723,1749,729,1755,731,732,733,734,735,736,1761,4834,739,6885,743,745,746,747,749,750,756,761,766,767,769,770,771,772,1798,777,1801,778,1805,782,783,784,787,793,794,795,2843,1820,796,1822,800,802,810,1838,814,2863,816,819,821,822,824,829,2880,834,1863,839,1864,1865,1872,851,3924,857,1885,865,867,871,4967,1896,872,874,875,879,881,882,883,889,891,892,1918,896,901,904,906,907,910,1935,913,1938,916,919,925,927,928,929,931,932,936,943,944,2992,946,948,949,1976,953,955,957,960,963,966,970,973,977,2003,979,981,984,2010,2012,994,2024,4074,1003,1006,1011,3060,1013,2042,1023],"organism":[{"name":"Homo sapiens","tax_id":9606}],"document_location":["DDESC","BSUMM","CLAIM"],"count":1533,"data_source":["USPTO_PSIPS"]},"has_sequence":true,"legal_status":{"ipr_type":"patent for invention","granted":true,"earliest_filing_date":"2001-12-04","grant_date":"2011-04-05","anticipated_term_date":"2021-12-04","discontinuation_date":"2019-05-13","has_disclaimer":false,"patent_status":"EXPIRED","publication_count":2,"has_spc":false,"has_grant_event":true,"has_entry_into_national_phase":false},"abstract":{"en":[{"text":"The present invention relates to compositions and methods for the prevention, treatment, and diagnosis of cancer, especially carcinomas, such as ovarian carcinoma. The invention discloses peptides, polypeptides, and polynucleotides that can be used to stimulate a CTL response against cancer.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"}]},"abstract_lang":["en"],"has_abstract":true,"claim":{"en":[{"text":"1 . A method for treating a subject with cancer, said cancer characterized by tumor cells expressing any class I MHC molecule, comprising administering to said subject a composition comprising at least one polypeptide comprising an epitopic peptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 1 to 791 and 1514 to 1533 in an amount sufficient to induce a CTL response to said tumor cells; or at least one polypeptide comprising an epitopic peptide having at least one amino acid difference from an amino acid sequence selected from the group consisting of SEQ ID NO: 1 to 791 and 1514 to 1533 in an amount sufficient to induce a CTL response to said tumor cells.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"2 . The method of claim 1 , wherein said amino acid difference from an amino acid sequence selected from the group consisting of SEQ ID NO: 1 to 791 and 1514 to 1533 is the result of a conservative amino acid substitution.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"3 . The method of claim 1 , wherein said amino acid difference from an amino acid sequence selected from the group consisting of SEQ ID NO: 1 to 791 and 1514 to 1533 is the result of a substitution of one hydrophobic amino acid with another hydrophobic amino acid.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"4 . The method of claim 1 , wherein said amino acid difference from an amino acid sequence selected from the group consisting of SEQ ID NO: 1 to 791 and 1514 to 1533 is the result of an addition or deletion of one amino acid to or from said epitopic peptide.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"5 . The method of claim 1 , wherein said composition further comprises an adjuvant.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"6 . The method of claim 5 , wherein said adjuvant is selected from the group consisting of complete Freund's adjuvant, incomplete Freund's adjuvant, Montanide ISA-51, LAG-3, aluminum phosphate, aluminum hydroxide, alum, and saponin.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"7 . The method of claim 1 , wherein said composition further comprises a cytokine.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"8 . The method of claim 5 , wherein said cytokine is selected from the group consisting of IL-1, IL-2, IL-7, IL-12, IL-15, TNF, SCF and GM-CSF.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"9 . The method of claim 1 , where in said composition further comprises a vehicle.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"10 . The method of claim 9 , where said vehicle is selected from the group consisting of a liposome, an immunostimulating complex (ISCOM), and slow-releasing particles.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"11 . The method of claim 10 , where in said liposome comprises an emulsion, a foam, a micel, an insoluble monolayer, a liquid crystal, a phospholipid dispersion, or a lamellar layer.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"12 . The method of claim 1 , wherein said polypeptide consists of an amino acid sequence selected from the group consisting of SEQ ID NO: 1 to 791 and 1514 to 1533; or an amino acid sequence having at least one amino acid difference from an amino acid sequence selected from the group consisting of SEQ ID NO: 1 to 791 and 1514 to 1533.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"13 . A method for treating a subject with cancer, said cancer characterized by tumor cells expressing any class I MHC molecule, said method comprising administering to said subject a composition comprising a polynucleotide comprising a nucleic acid sequence encoding at least one polypeptide comprising an epitopic peptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 1 to 791 and 1514 to 1533 in an amount sufficient to induce a CTL response to said tumor cells; or at least one polypeptide comprising an epitopic peptide comprising one amino acid difference from an amino acid sequence selected from the group consisting of SEQ ID NO: 1 to 791 and 1514 to 1533 in an amount sufficient to induce a CTL response to said tumor cells.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"14 . The method of claim 13 , wherein said polynucleotide further comprises an expression vector.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"15 - 23 . (canceled)","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"24 . A method for treating a subject with cancer, said cancer characterized by tumor cells expressing any class I MHC molecule and a gene coding for an epitopic sequence of at least one of SEQ ID NO: 792 to 1513, whereby the CTLs of claim 20 are administered in an amount sufficient to destroy the tumor cells through direct lysis or to effect the destruction of the tumor cells indirectly through the elaboration of cytokines.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"25 . The method of claim 1 wherein said cancer is carcinoma.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"26 . The method of claim 1 wherein said cancer is ovarian carcinoma.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"27 - 30 . (canceled)","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"31 . The method of claim 1 wherein said polypeptide comprises at least two epitopic peptides.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"32 . The method of claim 31 wherein said polypeptide comprises at least three epitopic peptides.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"33 . The method of claim 31 , said polypeptide comprising a first epitopic peptide and a second epitopic peptide, wherein said first epitopic peptide comprises the amino acid sequence of SEQ ID NO: 1 to 791 and 1514 to 1533 and said second epitopic peptide comprises an amino acid sequence selected from the group consisting of SEQ ID NOS: 1 to 791 and 1514 to 1533.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"}]},"claim_lang":["en"],"has_claim":true,"description":{"en":{"text":"CROSS-REFERENCE TO RELATED APPLICATIONS This application is a continuation-in-part of U.S. application Ser. No. 10/006,177, filed Dec. 4, 2001, which claims priority from U.S. provisional application No. 60/251,022, filed Dec. 4, 2000, and U.S. provisional application No. 60/256,824, filed Dec. 20, 2000, the disclosures of which are all herein incorporated by reference in their entireties. FIELD OF THE INVENTION The present invention relates generally to the field of immunogens whose structures incorporate polypeptides comprising epitopic peptides derived from proteins expressed by cancer cells and to uses of said immunogens in eliciting cytotoxic T lymphocyte (CTL) responses for the diagnosis, prevention and treatment of cancer, preferably carcinoma, most preferably ovarian carcinoma. BACKGROUND OF THE INVENTION The mammalian immune system has evolved a variety of mechanisms to protect the host from cancerous cells, an important component of this response being mediated by cells referred to as T cells. Cytotoxic T lymphocytes (CTLs) are specialized T cells that function primarily by recognizing and killing cancerous cells or infected cells, but also by secreting soluble molecules referred to as cytokines that can mediate a variety of effects on the immune system. Evidence suggests that immunotherapy designed to stimulate a tumor-specific CTL response would be effective in controlling cancer. For example, it has been shown that human CTLs recognize sarcomas (Slovin, S. F. et al., J. Immunol., 137:3042-3048, (1987)), renal cell carcinomas (Schendel, D. J. et al., J. Immunol., 151:4209-4220, (1993)), colorectal carcinomas (Jacob, L. et al., Int. J. Cancer, 71:325-332, (1997)), ovarian carcinomas (Loannides, C. G. et al., J. Immunol., 146:1700-1707, (1991)) (Peoples, G. E. et al., Surgery, 114:227-234, (1993)), pancreatic carcinomas (Peiper, M. et al., Eur. J. Immunol., 27:1115-1123, (1997); Wolfel, T. et al., Int. J. Cancer, 54:636-644, (1993)), squamous tumors of the head and neck (Yasumura, S. et al., Cancer Res., 53:1461-1468, (1993)), and squamous carcinomas of the lung (Slingluff, C. L. Jr et al., Cancer Res., 54:2731-2737, (1994); Yoshino, I. et al., Cancer Res., 54:3387-3390, (1994)). The largest number of reports of human tumor-reactive CTLs have concerned cancers (Boon, T. et al., Ann. Rev. Immunol., 12:337-365, (1994)). The ability of tumor-specific CTLs to mediate tumor regression, in both human (Rosenberg, S. A. et al., N. Engl. J. Med., 319:1676-1680, (1988)) and animal models (Celluzzi, C. M. et al., J. Exp. Med., 183:283-287, (1996); Mayordomo, J. I. et al., Nat. Med., 1:1297-1302, (1995); Zitvogel, L. et al., J. Exp. Med., 183:87-97, (1996)), suggests that methods directed at increasing CTL activity would likely have a beneficial effect with respect to tumor treatment. In order for CTLs to kill or secrete cytokines in response to a cancer cell, the CTL must first recognize that cell as being cancerous. This process involves the interaction of the T cell receptor, located on the surface of the CTL, with what is generically referred to as an MHC-peptide complex which is located on the surface of the cancerous cell. MHC (major histocompatibility-complex)-encoded molecules have been subdivided into two types, and are referred to as class I and class II MHC-encoded molecules. In the human immune system, MHC molecules are referred to as human leukocyte antigens (HLA). Within the MHC, located on chromosome six, are three different genetic loci that encode for class I MHC molecules. MHC molecules encoded at these loci are referred to as HLA-A, HLA-B, and HLA-C. The genes that can be encoded at each of these loci are extremely polymorphic, and thus, different individuals within the population express different class I MHC molecules on the surface of their cells. HLA-A1, HLA-A2, HLA-A3, HLA-B7, and HLA-B8 are examples of different class I MHC molecules that can be expressed from these loci. The present disclosure involves peptides that are associated with the HLA-A1, HLA-A2, or HLA-A11 molecules, HLA-A1 supertypes, HLA-A2 supertypes, and HLA-A11 supertypes and with the gene and protein that gives rise to these peptides. A supertype is a group of HLA molecules that present at least one shared epitope. The peptides that associate with the MHC molecules can either be derived from proteins made within the cell, in which case they typically associate with class I MHC molecules (Rock, K. L. and Golde, U., Ann. Rev. Immunol., 17:739-779, (1999)) or they can be derived from proteins that are acquired from outside of the cell, in which case they typically associate with class II MHC molecules (Watts, C., Ann. Rev. Immunol., 15:821-850, (1997)). Peptides that evoke a cancer-specific CTL response most typically associate with class I MHC molecules. The peptides that associate with a class I MHC molecule are typically nine amino acids in length, but can vary from a minimum length of eight amino acids to a maximum of fourteen amino acids in length. A class I MHC molecule with its bound peptide, or a class II MHC molecule with its bound peptide, is referred to as an MHC-peptide complex. The process by which intact proteins are degraded into peptides is referred to as antigen processing. Two major pathways of antigen processing occur within cells (Rock, K. L. and Golde, U., Ann. Rev. Immunol., 17:739-779, (1999); Watts, C., Ann. Rev. Immunol., 15:821-850, (1997)). One pathway, which is largely restricted to cells that are antigen presenting cells such as dendritic cells, macrophages, and B cells, degrades proteins that are typically phagocytosed or endocytosed into the cell. Peptides derived in this pathway typically bind to class II MHC molecules. A second pathway of antigen processing is present in essentially all cells of the body. This second pathway primarily degrades proteins that are made within the cells, and the peptides derived from this pathway primarily bind to class I MHC molecules. It is the peptides from this second pathway of antigen processing that are referred to herein. Antigen processing by this latter pathway involves polypeptide synthesis and proteolysis in the cytoplasm. The peptides produced are then transported into the endoplasmic reticulum of the cell, associate with newly synthesized class I MHC molecules, and the resulting MHC-peptide complexes are then transported to the cell surface. Peptides derived from membrane and secreted proteins have also been identified. In some cases these peptides correspond to the signal sequence of the proteins that are cleaved from the protein by the signal peptidase. In other cases, it is thought that some fraction of the membrane and secreted proteins are transported from the endoplasmic reticulum into the cytoplasm where processing subsequently occurs. Once bound to the class I MHC molecule and displayed on the surface of a cell, the peptides are recognized by antigen-specific receptors on CTLs. Mere expression of the class I MHC molecule itself is insufficient to trigger the CTL to kill the target cell if the antigenic peptide is not bound to the class I MHC molecule. Several methods have been developed to identify the peptides recognized by CTL, each method relying on the ability of a CTL to recognize and kill only those cells expressing the appropriate class I MHC molecule with the peptide bound to it (Rosenberg, S. A., Immunity, 10:281-287, (1999)). Such peptides can be derived from a non-self source, such as a pathogen (for example, following the infection of a cell by a bacterium or a virus) or from a self-derived protein within a cell, such as a cancerous cell. Examples of sources of self-derived proteins in cancerous cells have been reviewed (Gilboa, E., Immunity, 11:263-270, (1999); Rosenberg, S. A., Immunity, 10:281-287, (1999)) and include: (i) mutated genes; (ii) aberrantly expressed genes such as an alternative open reading frame or through an intron-exon boundary; (iii) normal genes that are selectively expressed in only the tumor and the testis; and (iv) normal differentiation genes that are expressed in the tumor and the normal cellular counterpart. Four different methodologies have typically been used for identifying the peptides that are recognized by CTLs. These are: (i) the genetic method; (2) motif analysis; (3) SErological analysis of REcombinant cDNA expression libraries (SEREX™); and (iv) the analytical chemistry approach or the Direct Identification of Relevant Epitopes for Clinical Therapeutics (DIRECT™). The genetic method is an approach in which progressively smaller subsets of cDNA libraries from tumor cells are transfected into cells that express the appropriate MHC molecule but not the tumor-specific epitope. The molecular clones encoding T cell epitopes are identified by their ability to reconstitute tumor specific T cell recognition of transfected cells. The exact T cell epitope is then identified by a combination of molecular subcloning and the use of synthetic peptides based on the predicted amino acid sequence. Such methods, however, are susceptible to inadvertent identification of cross-reacting peptides, and are not capable of identifying important post-translational modifications. Motif analysis involves scanning a protein for peptides containing known class I MHC binding motifs, followed by synthesis and assay of the predicted peptides for their ability to be recognized by tumor-specific CTL. This approach requires prior knowledge of the protein from which the peptides are derived. This approach is also greatly hampered by the fact that not all of the predicted peptide epitopes are presented on the surface of a cell (Yewdell, J. W. and Bennink, J. R., Ann. Rev. Immunol., 17:51-88, (1999)), thus additional experimentation is required to determine which of the predicted epitopes is useful. The SEREX™ approach relies on using antibodies in the serum of cancer patients to screen cDNA expression libraries for a clone that expresses a protein recognized by the antibody. This methodology presumes that an antibody response will necessarily have developed in the presence of a T cell response, and thus, the identified clone is good candidate to encode a protein that can be recognized by T cells. DIRECT™ involves a combination of cellular immunology and mass spectrometry. This approach involves the actual identification of CTL epitopes by sequencing the naturally occurring peptides associated with class I MHC molecules. In this approach, cells are first lysed in a detergent solution, the peptides associated with the class I MHC molecules are purified, and the peptides fractionated by high performance liquid chromatography (HPLC). The peptides are then used to reconstitute recognition by tumor-specific CTLs on a non-tumor cell expressing the appropriate MHC molecules. Sequencing is readily performed by tandem mass spectrometry (Henderson, R. A. et al., Proc. Natl. Acad. Sci. U.S.A, 90:10275-10279, (1993); Hogan, K. T. et al., Cancer Res., 58:5144-5150, (1998); Hunt, D. F. et al., Science, 255:1261-1263, (1992); Slingluff, C. L. Jr et al., J. Immunol., 150:2955-2963, (1993)). Immunization with cancer-derived, class I MHC-encoded molecule-associated peptides, or with a precursor polypeptide or protein that contains the peptide, or with a gene that encodes a polypeptide or protein containing the peptide, are forms of immunotherapy that can be employed in the treatment of cancer. These forms of immunotherapy require that immunogens be identified so that they can be formulated into an appropriate vaccine. Although a variety of cancer-derived antigens have been identified (Rosenberg, S. A., Immunity, 10:281-287, (1999)), not all of these are appropriate for broad-based immunotherapy as the expression of some peptides is limited to the tumor derived from a specific patient. Furthermore, the number of class I MHC molecules from which tumor-derived peptides have been discovered is largely restricted to HLA-A2. Thus, it would be useful to identify additional peptides that complex with class I MHC molecules other than HLA-A2. Such peptides would be particularly useful in the treatment of cancer patients who do not express the HLA-A2 molecule, HLA-A1 or HLA-A11 antigens, HLA-A1 supertypes, HLA-A2 supertypes and HLA-A11 supertypes, for example. It is also particularly useful to identify antigenic peptides that are derived from different original proteins, even if the derived peptides associate with the same class I MHC molecule. Because an active immune response can result in the outgrowth of tumor cells that have lost the expression of a particular precursor protein for a given antigenic peptide, it is advantageous to stimulate an immune response against peptides derived from more than one protein, as the chances of the tumor cell losing the expression of both proteins is the multiple of the chances of losing each of the individual proteins. SUMMARY OF THE INVENTION The present invention relates to Immunogens comprising polypeptides with amino acid sequences comprising epitopic sequences selected from the sequences of SEQ ID NO: 1-791 and 1514-1533 and which immunogens facilitate a cytotoxic T lymphocyte (CTL)-mediated immune response against cancers. The present invention also relates to nucleic acid molecules that encode for the polypeptides and/or the full length proteins from which the polypeptides are derived, of such immunogens, and which can also be used to facilitate an immune response against cancer. The present invention provides compositions comprising the immunogen described herein, and polynucleotides that direct the synthesis of such polypeptides, whereby the oligopeptides and polypeptides of such immunogens are capable of inducing a CTL response against cells expressing a protein comprising an epitopic sequence of at least one of SEQ ID NO: 1-791 and 1514-1533. The cells are usually cancer cells, preferably carcinoma cells, most preferably ovarian carcinomas expressing such proteins. The present invention further relates to polynucleotides comprising the gene coding for a polypeptide of the immunogens disclosed herein. The present invention also provides methods that comprise contacting a lymphocyte, especially a CTL, with an immunogen of the invention under conditions that induce a CTL response against a tumor cell, and more specifically against a cancer cell. The methods may involve contacting the CTL with the immunogenic peptide in vivo, in which case the peptides, polypeptides, and polynucleotides of the invention are used as vaccines, and will be delivered as a pharmaceutical composition comprising a pharmaceutically acceptable carrier and the immunogen, typically along with an adjuvant or one or more cytokines. Alternatively, the immunogens of the present invention can be used to induce a CTL response in vitro. The generated CTL can then be introduced into a patient with cancer, more specifically cancer, colorectal carcinoma, ovarian carcinoma, breast carcinoma, lung carcinoma, or prostate carcinoma. Alternatively, the ability to generate CTL in vitro could serve as a diagnostic for cancer generally, including colorectal carcinoma, ovarian carcinoma, breast carcinoma, lung carcinoma, or prostate carcinoma. DETAILED DESCRIPTION OF THE INVENTION Definitions As used herein and except as noted otherwise, all terms are defined as given below. The term “peptide” is used herein to designate a series of amino acid residues, connected one to the other typically by peptide bonds between the alpha-amino and carbonyl groups of the adjacent amino acids. The peptides are typically 9 amino acids in length, but can be as short as 8 amino acids in length, and as long as 14 amino acids in length. The term “oligopeptide” is used herein to designate a series of amino acid residues, connected one to the other typically by peptide bonds between the alpha-amino and carbonyl groups of the adjacent amino acids. The length of the oligopeptide is not critical to the invention as long as the correct epitope or epitopes are maintained therein. The oligopeptides are typically less than about 30 amino acid residues in length, and greater than about 14 amino acids in length. The term “polypeptide” designates a series of amino acid residues, connected one to the other typically by peptide bonds between the alpha-amino and carbonyl groups of the adjacent amino acids. The length of the polypeptide is not critical to the invention as long as the correct epitopes are maintained. In contrast to the terms peptide or oligopeptide, the term polypeptide is meant to refer to protein molecules of longer than about 30 residues in length. A peptide, oligopeptide, protein, or polynucleotide coding for such a molecule is “immunogenic” (and thus an “immunogen” within the present invention) if it is capable of inducing an immune response. In the case of the present invention, immunogenicity is more specifically defined as the ability to induce a CTL-mediated response. Thus, an “immunogen” would be a molecule that is capable of inducing an immune response, and in the case of the present invention, a molecule capable of inducing a CTL response. A T cell “epitope” is a short peptide molecule that binds to a class I or II MHC molecule and that is subsequently recognized by a T cell. T cell epitopes that bind to class I MHC molecules are typically 8-14 amino acids in length, and most typically 9 amino acids in length. T cell epitopes that bind to class II MHC molecules are typically 12-20 amino acids in length. In the case of epitopes that bind to class II MHC molecules, the same T cell epitope may share a common core segment, but differ in the length of the carboxy- and amino-terminal flanking sequences due to the fact that ends of the peptide molecule are not buried in the structure of the class II MHC molecule peptide-binding cleft as they are in the class I MHC molecule peptide-binding cleft. There are three different genetic loci that encode for class I MHC molecules: HLA-A, HLA-B, and HLA-C. HLA-A1, HLA-A2, and HLA-A11 are examples of different class I MHC molecules that can be expressed from these loci. The present invention also involves peptides that are associated with HLA-A1 supertypes, HLA-A2 supertypes, and HLA-A11 supertypes. A supertype is a group of HLA molecules that present at least one shared epitope. MHC molecule peptides that have been found to bind to one member of the MHC allele supertype family (A1 for example) are thought to be likely to bind to other members of the same supertype family (A32 for example; see Table 1, below. TABLE 1SupertypeMotifGenotypesA1x[TI(SVLM)]A*0101, A*0102, A*2501, A*2601, A*2604,xxxxxx[WFY]A*3201, A*3601, A*4301, A*8001A2x[LIVMATQ]A*0201, A*0202, A*0203, A*0204, A*0205,xxxxxx[LIVMAT]A*0206, A*0207, A*6802, A*6901A3x[AILMVST]A*0301, A*1101, A*3101, A*3301, A*6801xxxxxx[RK]A24x[YF(WIVLMT)]A*2301, A*2402, A*2403, A*2404, A*3001,xxxxxx[FI(YWLM)]A*3002, A*3003B7x[P]xxxxxxB*0702, B*0703, B*0704, B*0705, B*1508, B*3501,[ALIMVFWY]B*3502, B*3503, B*51, B*5301, B*5401, B*5501,B*5502, B*5601, B*5602, B*6701, B*7801B27x[RKH]xxxxxxB*1401, B*1402, B*1503, B*1509, B*1510, B*1518,[FLY(WMI)]B*2701, B*2702, B*2703, B*2704, B*2705, B*2706,B*2707, B*2708, B*3801, B*3802, B*3901, B*3902,B*3903, B*3904, B*4801, B*4802, B*7301B44x[E(D)]xxxxxxB*18, B*3701, B*4001, B*4006, B*4101, B*4402,[FWYLIMVA]B*4403, B*4501, B*4901, B*5001B58x[AST]xxxxxxB*1516, B*1517, B*5701, B*5702, B*58[FWY(LIV)]B62x[QL(IVMP)]B*1301, B*1302, B*1501, B*1502, B*1506, B*1512,xxxxxx[FWY(MIV)]B*1513, B*1514, B*1519, B*1521, B*4601, B*52 As used herein, reference to a DNA sequence includes both single stranded and double stranded DNA. Thus, the specific sequence, unless the context indicates otherwise, refers to the single strand DNA of such sequence, the duplex of such sequence with its complement (double stranded DNA) and the complement of such sequence. The term “coding region” refers to that portion of a gene which either naturally or normally codes for the expression product of that gene in its natural genomic environment, i.e., the region coding in vivo for the native expression product of the gene. The coding region can be from a normal, mutated or altered gene, or can even be from a DNA sequence, or gene, wholly synthesized in the laboratory using methods well known to those of skill in the art of DNA synthesis. The term “nucleotide sequence” refers to a heteropolymer of deoxyribonucleotides. The nucleotide sequence encoding for a particular peptide, oligopeptide, or polypeptide may be naturally occurring or they may be synthetically constructed. Generally, DNA segments encoding the peptides, polypeptides, and proteins of this invention are assembled from cDNA fragments and short oligonucleotide linkers, or from a series of oligonucleotides, to provide a synthetic gene which is capable of being expressed in a recombinant transcriptional unit comprising regulatory elements derived from a microbial or viral operon. The term “expression product” means that polypeptide or protein that is the natural translation product of the gene and any nucleic acid sequence coding equivalents resulting from genetic code degeneracy and thus coding for the same amino acid(s). The term “fragment,” when referring to a coding sequence, means a portion of DNA comprising less than the complete coding region whose expression product retains essentially the same biological function or activity as the expression product of the complete coding region. The term “DNA segment” refers to a DNA polymer, in the form of a separate fragment or as a component of a larger DNA construct, which has been derived from DNA isolated at least once in substantially pure form, i.e., free of contaminating endogenous materials and in a quantity or concentration enabling identification, manipulation, and recovery of the segment and its component nucleotide sequences by standard biochemical methods, for example, by using a cloning vector. Such segments are provided in the form of an open reading frame uninterrupted by internal nontranslated sequences, or introns, which are typically present in eukaryotic genes. Sequences of non-translated DNA may be present downstream from the open reading frame, where the same do not interfere with manipulation or expression of the coding regions. The term “primer” means a short nucleic acid sequence that is paired with one strand of DNA and provides a free 3′OH end at which a DNA polymerase starts synthesis of a deoxyribonucleotide chain. The term “promoter” means a region of DNA involved in binding of RNA polymerase to initiate transcription. The term “open reading frame (ORF)” means a series of triplets coding for amino acids without any termination codons and is a sequence (potentially) translatable into protein. The term “isolated” means that the material is removed from its original environment (e.g., the natural environment if it is naturally occurring). For example, a naturally-occurring polynucleotide or polypeptide present in a living animal is not isolated, but the same polynucleotide or polypeptide, separated from some or all of the coexisting materials in the natural system, is isolated. Such polynucleotides could be part of a vector and/or such polynucleotides or polypeptides could be part of a composition, and still be isolated in that such vector or composition is not part of its natural environment. The polynucleotides, and recombinant or immunogenic polypeptides, disclosed in accordance with the present invention may also be in “purified” form. The term “purified” does not require absolute purity; rather, it is intended as a relative definition, and can include preparations that are highly purified or preparations that are only partially purified, as those terms are understood by those of skill in the relevant art. For example, individual clones isolated from a cDNA library have been conventionally purified to electrophoretic homogeneity. Purification of starting material or natural material to at least one order of magnitude, preferably two or three orders, and more preferably four or five orders of magnitude is expressly contemplated. Furthermore, the claimed polypeptide which has a purity of preferably 0.001%, or at least 0.01% or 0.1%; and even desirably 1% by weight or greater is expressly contemplated. The nucleic acids and polypeptide expression products disclosed according to the present invention, as well as expression vectors containing such nucleic acids and/or such polypeptides, may be in “enriched form.” As used herein, the term “enriched” means that the concentration of the material is at least about 2, 5, 10, 100, or 1000 times its natural concentration (for example), advantageously 0.01%, by weight, preferably at least about 0.1% by weight. Enriched preparations of about 0.5%, 1%, 5%, 10%, and 20% by weight are also contemplated. The sequences, constructs, vectors, clones, and other materials comprising the present invention can advantageously be in enriched or isolated form. The term “active fragment” means a fragment that generates an immune response (i.e., has immunogenic activity) when administered, alone or optionally with a suitable adjuvant, to an animal, such as a mammal, for example, a rabbit or a mouse, and also including a human, such immune response taking the form of stimulating a CTL response within the recipient animal, such as a human. Alternatively, the “active fragment” may also be used to induce a CTL response in vitro. As used herein, the terms “portion,” “segment,” and “fragment,” when used in relation to polypeptides, refer to a continuous sequence of residues, such as amino acid residues, which sequence forms a subset of a larger sequence. For example, if a polypeptide were subjected to treatment with any of the common endopeptidases, such as trypsin or chymotrypsin, the oligopeptides resulting from such treatment would represent portions, segments or fragments of the starting polypeptide. This means that any such fragment will necessarily contain as part of its amino acid sequence a segment, fragment or portion, that is substantially identical, if not exactly identical, to a sequence of SEQ ID NO: 792-1513, which correspond to the naturally occurring, or “parent” proteins of the SEQ ID NO: 1-791 and 1514-1533. When used in relation to polynucleotides, such terms refer to the products produced by treatment of said polynucleotides with any of the common endonucleases. In accordance with the present invention, the term “percent identity” or “percent identical,” when referring to a sequence, means that a sequence is compared to a claimed or described sequence after alignment of the sequence to be compared (the “Compared Sequence”) with the described or claimed sequence (the “Reference Sequence”). The Percent Identity is then determined according to the following formula: Percent Identity=100[1−( C/R )] wherein C is the number of differences between the Reference Sequence and the Compared Sequence over the length of alignment between the Reference Sequence and the Compared Sequence wherein (i) each base or amino acid in the Reference Sequence that does not have a corresponding aligned base or amino acid in the Compared Sequence and (ii) each gap in the Reference Sequence and (iii) each aligned base or amino acid in the Reference Sequence that is different from an aligned base or amino acid in the Compared Sequence, constitutes a difference; and R is the number of bases or amino acids in the Reference Sequence over the length of the alignment with the Compared Sequence with any gap created in the Reference Sequence also being counted as a base or amino acid. If an alignment exists between the Compared Sequence and the Reference Sequence for which the percent identity as calculated above is about equal to or greater than a specified minimum Percent Identity then the Compared Sequence has the specified minimum percent identity to the Reference Sequence even though alignments may exist in which the herein above calculated Percent Identity is less than the specified Percent Identity. The present invention relates generally to immunogens and immunogenic compositions, and methods of use therefore, for the prevention, treatment, and diagnosis of cancer, especially carcinomas, including ovarian carcinomas. Disclosed according to the invention are immunogens comprising proteins or polypeptides whose amino acid sequences comprises one or more epitopic oligopeptides with sequences selected from the group SEQ ID NO: 1-791 and 1514-1533. In addition, the invention further relates to polynucleotides that can be used to stimulate a CTL response against cancer, and more specifically carcinoma, especially ovarian carcinomas. In accordance with the present invention there are disclosed specific oligopeptide sequences with amino acid sequences shown in SEQ ID NO: 1-791 and 1514-1533, which represent epitopic peptides (i.e. immunogenic oligopeptide sequences) of at least about 8 amino acids in length, preferably about 9 amino acids in length (i.e., nonapeptides), and no longer than about 10 amino acids in length and present as part of a larger structure, such as a polypeptide or full length protein. The polypeptides forming the immunogens of the present invention have amino acid sequences that comprise at least one stretch, possibly two, three, four, or more stretches of about 8 to 10 residues in length and which stretches differ in amino acid sequence from the sequences of SEQ ID NO: 1-791 and 1514-1533 by no more than about 1 amino acid residue, preferably a conservative amino acid residue, especially amino acids of the same general chemical character, such as where they are hydrophobic amino acids. Said polypeptides can be of any desired length so long as they have immunogenic activity in that they are able, under a given set of desirable conditions, to elicit in vitro or in vivo the activation of cytotoxic T lymphocytes (CTLs) (i.e., a CTL response) against a presentation of a cancer specific protein, especially a carcinoma or sarcoma specific protein, most especially MAGE D, MAGE 4, MFG-E8 or human retinoblastoma-like protein, especially when such proteins are presented along with MHC-1 proteins, such as where said proteins are presented in vitro or in vivo by an antigen presenting cell (APC). The proteins and polypeptides forming the immunogens of the present invention can be naturally occurring or may be synthesized chemically. According to the present invention the polypeptides may comprise at least one of SEQ ID NO: 792-1513. The present invention is also directed to an isolated polypeptide, especially one having immunogenic activity, the sequence of which comprises within it one or more stretches comprising any 2 or more of the sequences of SEQ ID NO: 1-791 and 1514-1533 and in any relative quantities and wherein said sequences may differ by one amino acid residues from the sequences of SEQ ID NO: 1-791 and 1514-1533 in any given stretch of 8 to 10 amino acid residues. Thus, within the present invention, by way of a non-limiting example only, such polypeptide may contain as part of its amino acid sequence, nonapeptide fragments having up to 8 amino acids identical to a sequence of SEQ ID NO: 1-4 such that the polypeptide comprises, in a specific embodiment, 2 segments with at least 8 residues identical to SEQ ID NO: 1 and one segment with at least 8 residues identical to SEQ ID NO: 3. In other embodiments, other combinations and permutations of the epitopic sequences disclosed herein may be part of an immunogen of the present invention or of such a polypeptide so long as any such polypeptide comprises at least 2 such epitopes, whether such epitopes are different or the same. Thus, in a specific embodiment, a polypeptide of the present invention may comprise 2 copies of the sequence of SEQ ID NO: 2 at some point or points within its length. Of course, any combinations and permutations of the epitopes disclosed herein, as long as they are present at least two in number in such polypeptides, are expressly contemplated. All of the epitopic peptides of SEQ ID NO: 1-791 and 1514-1533 are derived from proteins expressed by cancer cells and sequences and were identified through the method of Automated High Through-put Sequencing (HTPS). Accordingly, SEQ ID NO: 792-1513 are polypeptides that comprise at least one of SEQ ID NO: 1-791 and 1514-1533. Oligopeptides as disclosed herein may themselves be prepared by methods well known to those skilled in the art. (Grant, G. A., Synthetic Peptides: A User's Guide, 1992, W. H. Freeman and Company, New York; Coligan, J. E. et al, Current Protocols in Protein Science, 1999, John Wiley & Sons, Inc., New York). Besides the sequences of SEQ ID NO:1-791 and 1514-1533, the proteins and polypeptides forming the immunogens of the present invention may also comprise one or more other immunogenic amino acid stretches known to be associated with cancer, and more specifically with carcinomas and melanomas, including colorectal carcinoma, ovarian carcinoma, breast carcinoma, lung carcinoma, or prostate carcinoma, and which may stimulate a CTL response whereby the immunogenic peptides associate with HLA-A1 or HLA-A11, or HLA-A2, or another class I MHC (i.e., MHC-1) molecule. The immunogens of the present invention can be in the form of a composition of one or more of the different immunogens and wherein each immunogen is present in any desired relative abundance. Such compositions can be homogeneous or heterogeneous with respect to the individual immunogenic peptide components present therein, having only one or more than one of such peptides. The oligopeptides and polypeptides useful in practicing the present invention may be derived by fractionation of naturally occurring proteins by methods such as protease treatment, or they may be produced by recombinant or synthetic methodologies that are well known and clear to the skilled artisan (Ausubel, F. M. et al, Current Protocols in Molecular Biology, 1999, John Wiley & Sons, Inc., New York; Coligan, J. E. et al, Current Protocols in Protein Science, 1999, John Wiley & Sons, Inc., New York; Molecular Cloning: A Laboratory Manual, 1989, Cold Spring Harbor Laboratory Press, Cold Spring Harbor). The polypeptide may comprise a recombinant or synthetic polypeptide that comprises at least one of SEQ ID NO: 1-791 and 1514-1533 which sequences may also be present in multiple copies. Thus, oligopeptides and polypeptides of the present invention may have one, two, three, or more such immunogenic peptides within the amino acid sequence of said oligopeptides and polypeptides, and said immunogenic peptides, or epitopes, may be the same or may be different, or may have any number of such sequences wherein some of them are identical to each other in amino acid sequence while others within the same polypeptide sequence are different from each other and said epitopic sequences may occur in any order within said immunogenic polypeptide sequence. The location of such sequences within the sequence of a polypeptide forming an immunogen of the invention may affect relative immunogenic activity. In addition, immunogens of the present invention may comprise more than one protein comprising the amino acid sequences disclosed herein. Such polypeptides may be part of a single composition or may themselves be covalently or non-covalently linked to each other. The immunogenic peptides disclosed herein may also be linked directly to, or through a spacer or linker to: an immunogenic carrier such as serum albumin, tetanus toxoid, keyhole limpet hemocyanin, dextran, or a recombinant virus particle; an immunogenic peptide known to stimulate a T helper cell type immune response; a cytokine such as interferon gamma or GMCSF; a targeting agent such as an antibody or receptor ligand; a stabilizing agent such as a lipid; or a conjugate of a plurality of epitopes to a branched lysine core structure, such as the so-called “multiple antigenic peptide” described in (Posneft, D. N. et al., J. Biol. Chem., 263:1719-1725, (1988)); a compound such as polyethylene glycol to increase the half life of the peptide; or additional amino acids such as a leader or secretory sequence, or a sequence employed for the purification of the mature sequence. Spacers and linkers are typically comprised of relatively small, neutral molecules, such as amino acids and which are substantially uncharged under physiological conditions. Such spacers are typically selected from the group of nonpolar or neutral polar amino acids, such as glycine, alanine, serine and other similar amino acids. Such optional spacers or linkers need not be comprised of the same residues and thus may be either homo- or hetero-oligomers. When present, such linkers will commonly be of length at least one or two, commonly 3, 4, 5, 6, and possibly as much as 10 or even up to 20 residues (in the case of amino acids). In addition, such linkers need not be composed of amino acids but any oligomeric structures will do as well so long as they provide the correct spacing so as to optimize the desired level of immunogenic activity of the immunogens of the present invention. The immunogen may therefore take any form that is capable of eliciting a CTL response. In addition, the immunogenic peptides of the present invention may be part of an immunogenic structure via attachments other than conventional peptide bonds. Thus, any manner of attaching the peptides of the invention to an immunogen of the invention, such as an immunogenic polypeptide as disclosed herein, could provide an immunogenic structure as claimed herein. Thus, immunogens, such as proteins of the invention, are structures that contain the peptides disclosed according to the present invention but such immunogenic peptides may not necessarily be attached thereto by the conventional means of using ordinary peptide bounds. The immunogens of the present invention simply contain such peptides as part of their makeup, but how such peptides are to be combined to form the final immunogen is left to the talent and imagination of the user and is in no way restricted or limited by the disclosure contained herein. The peptides that are naturally processed and bound to a class I MHC molecule, and which are recognized by a tumor-specific CTL, need not be the optimal peptides for stimulating a CTL response. See, for example, (Parkhurst, M. R. et al., J. Immunol., 157:2539-2548, (1996); Rosenberg, S. A. et al., Nat. Med., 4:321-327, (1998)). Thus, there can be utility in modifying a peptide, such that it more readily induces a CTL response. Generally, peptides may be modified at two types of positions. The peptides may be modified at amino acid residues that are predicted to interact with the class I MHC molecule, in which case the goal is to create a peptide that has a higher affinity for the class I MHC molecule than does the original peptide. The peptides can also be modified at amino acid residues that are predicted to interact with the T cell receptor on the CTL, in which case the goal is to create a peptide that has a higher affinity for the T cell receptor than does the original peptide. Both of these types of modifications can result in a variant peptide that is related to an original peptide, but which is better able to induce a CTL response than is the original peptide. As used herein, the term “original peptide” means an oligopeptide with the amino acid sequence selected from SEQ ID NO: 1-791 and 1514-1533. The original peptides disclosed herein can be modified by the substitution of one or more residues at different, possibly selective, sites within the peptide chain. Such substitutions may be of a conservative nature, for example, where one amino acid is replaced by an amino acid of similar structure and characteristics, such as where a hydrophobic amino acid is replaced by another hydrophobic amino acid. Even more conservative would be replacement of amino acids of the same or similar size and chemical nature, such as where leucine is replaced by isoleucine. In studies of sequence variations in families of naturally occurring homologous proteins, certain amino acid substitutions are more often tolerated than others, and these are often show correlation with similarities in size, charge, polarity, and hydrophobicity between the original amino acid and its replacement, and such is the basis for defining “conservative substitutions.” Conservative substitutions are herein defined as exchanges within one of the following five groups: Group 1—small aliphatic, nonpolar or slightly polar residues (Ala, Ser, Thr, Pro, Gly); Group 2—polar, negatively charged residues and their amides (Asp, Asn, Glu, Gln); Group 3—polar, positively charged residues (His, Arg, Lys); Group 4—large, aliphatic, nonpolar residues (Met, Leu, lie, Val, Cys); and Group 4—large, aromatic residues (Phe, Tyr, Trp). Less conservative substitutions might involve the replacement of one amino acid by another that has similar characteristics but is somewhat different in size, such as replacement of an alanine by an isoleucine residue. Highly nonconservative replacements might involve substituting an acidic amino acid for one that is polar, or even for one that is basic in character. Such radical substitutions cannot, however, be dismissed as potentially ineffective since chemical effects are not totally predictable and radical substitutions might well give rise to serendipitous effects not otherwise predictable from simple chemical principles. Of course, such substitutions may involve structures other than the common L-amino acids. Thus, D-amino acids might be substituted for the L-amino acids commonly found in the antigenic peptides of the invention and yet still be encompassed by the disclosure herein. In addition, amino acids possessing non-standard R groups (i.e., R groups other than those found in the common 20 amino acids of natural proteins) may also be used for substitution purposes to produce immunogens and immunogenic polypeptides according to the present invention. If substitutions at more than one position are found to result in a peptide with substantially equivalent or greater antigenic activity as defined below, then combinations of those substitutions will be tested to determine if the combined substitutions result in additive or syngeneic effects on the antigenicity of the peptide. At most, no more than 4 positions within the peptide would simultaneously be substituted. Based on cytotoxicity assays, an epitope is considered substantially identical to the reference peptide if it has at least 10% of the antigenic activity of the reference peptide as defined by the ability of the substituted peptide to reconstitute the epitope recognized by a CTL in comparison to the reference peptide. Thus, when comparing the lytic activity in the linear portion of the effector:target curves with equimolar concentrations of the reference and substituted peptides, the observed percent specific killing of the target cells incubated with the substituted peptide should be equal to that of the reference peptide at an effector:target ratio that is no greater than 10-fold above the reference peptide effector:target ratio at which the comparison is being made. Preferably, when the CTLs specific for a peptide of SEQ ID NO: 1-791 and 1514-1533 are tested against the substituted peptides, the peptide concentration at which the substituted peptides achieve half the maximal increase in lysis relative to background is no more than about 1 mM, preferably no more than about 1 μM, more preferably no more than about 1 nM, and still more preferably no more than about 100 pM, and most preferably no more than about 10 pM. It is also preferred that the substituted peptide be recognized by CTLs from more than one individual, at least two, and more preferably three individuals. Thus, the epitopes of the present invention may be identical to naturally occurring tumor-associated or tumor-specific epitopes or may include epitopes that differ by no more than 4 residues from the reference peptide, as long as they have substantially identical antigenic activity. It should be appreciated that an immunogen may consist only of a peptide of SEQ ID NO:1-791 or 1514-1533, or comprise a peptide of SEQ ID NO:1-791 or 1514-1533, or comprise a plurality of peptides selected from SEQ ID NO:1-791 and 1514-1533, or comprise a polypeptide that itself comprises one or more of the epitopic peptides of SEQ ID NO: 1-791 and 1514-1533. The immunogenic peptides and polypeptides of the invention can be prepared synthetically, by recombinant DNA technology, or they can be isolated from natural sources such as tumor cells expressing the original protein product. The polypeptides and oligopeptides disclosed herein can be synthesized in solution or on a solid support in accordance with conventional techniques. Various automated peptide synthesizers are commercially available and can be used in accordance with known protocols. See, for example, (Grant, G. A., Synthetic Peptides: A User's Guide, 1992, W. H. Freeman and Company, New York; Coligan, J. E. et al, Current Protocols in Protein Science, 1999, John Wiley & Sons, Inc., New York). Fragments of polypeptides of the invention can also be synthesized as intermediates in the synthesis of a larger polypeptide. Recombinant DNA technology may be employed wherein a nucleotide sequence which encodes an immunogenic peptide or polypeptide of interest is inserted into an expression vector, transformed or transfected into an appropriate host cell, and cultivated under conditions suitable for expression. These procedures are well known in the art to the skilled artisan, as described in (Coligan, J. E. et al, Current Protocols in Immunology, 1999, John Wiley & Sons, Inc., New York; Ausubel, F. M. et al, Current Protocols in Molecular Biology, 1999, John Wiley & Sons, Inc., New York; Molecular Cloning: A Laboratory Manual, 1989, Cold Spring Harbor Laboratory Press, Cold Spring Harbor). Thus, recombinantly produced peptides or polypeptides can be used as the immunogens of the invention. The coding sequences for peptides of the length contemplated herein can be synthesized on commercially available automated DNA synthesizers using protocols that are well know in the art. See for example, (Grant, G. A., Synthetic Peptides: A User's Guide, 1992, W. H. Freeman and Company, New York; Coligan, J. E. et al, Current Protocols in Protein Science, 1999, John Wiley & Sons, Inc., New York). The coding sequences can also be modified such that a peptide or polypeptide will be produced that incorporates a desired amino acid substitution. The coding sequence can be provided with appropriate linkers, be ligated into suitable expression vectors that are commonly available in the art, and the resulting DNA or RNA molecule can be transformed or transfected into suitable hosts to produce the desired fusion protein. A number of such vectors and suitable host systems are available, and their selection is left to the skilled artisan. For expression of the fusion proteins, the coding sequence will be provided with operably linked start and stop codons, promoter and terminator regions, and a replication system to provide an expression vector for expression in the desired host cell. For example, promoter sequences compatible with bacterial hosts are provided in plasmids containing convenient restriction sites for insertion of the desired coding sequence. The resulting expression vectors are transformed into suitable bacterial hosts. Of course, yeast, insect, and mammalian host cells may also be used, employing suitable vectors and control sequences. Host cells are genetically engineered (transduced or transformed or transfected) with the vectors of this invention which may be, for example, a cloning vector or an expression vector. The vector may be, for example, in the form of a plasmid, a viral particle, a phage, etc. The engineered host cells can be cultured in conventional nutrient media modified as appropriate for activating promoters, selecting transformants or amplifying the genes of the present invention. The culture conditions, such as temperature, pH and the like, are those previously used with the host cell selected for expression, and will be apparent to the ordinarily skilled artisan. More particularly, the present invention also includes recombinant constructs comprising one or more of the sequences as broadly described above. The constructs comprise a vector, such as a plasmid or viral vector, into which a sequence of the invention has been inserted, in a forward or reverse orientation. In a preferred aspect of this embodiment, the construct further comprises regulatory sequences, including, for example, a promoter, operably linked to the sequence. Large numbers of suitable vectors and promoters are known to those of skill in the art, and are commercially available. In a further embodiment, the present invention relates to host cells containing the above-described constructs. The host cell can be a higher eukaryotic cell, such as a mammalian cell, or a lower eukaryotic cell, such as a yeast cell, or the host cell can be a prokaryotic cell, such as a bacterial cell. Introduction of the construct into the host cell can be effected by calcium phosphate transfection, DEAE-Dextran mediated transfection, or electroporation (Ausubel, F. M. et al, Current Protocols in Molecular Biology, 1999, John Wiley & Sons, Inc., New York; Molecular Cloning: A Laboratory Manual, 1989, Cold Spring Harbor Laboratory Press, Cold Spring Harbor). Such cells can routinely be utilized for assaying CTL activity by having said genetically engineered, or recombinant, host cells express the immunogenic peptides of the present invention. Various mammalian cell culture systems can also be employed to express recombinant protein. Examples of mammalian expression systems include the COS-7 lines of monkey kidney fibroblasts, described by Gluzman, Cell, 23:175 (1981), and other cell lines capable of expressing a compatible vector, for example, the C127, 3T3, CHO, HeLa and BHK cell lines. Mammalian expression vectors will comprise an origin of replication, a suitable promoter and enhancer, and also any necessary ribosome binding sites, polyadenylation site, splice donor and acceptor sites, transcriptional termination sequences, and 5′ flanking non-transcribed sequences. DNA sequences derived from the SV40 splice, and polyadenylation sites may be used to provide the required nontranscribed genetic elements. The polypeptide can be recovered and purified from recombinant cell cultures by methods including ammonium sulfate or ethanol precipitation, acid extraction, anion or cation exchange chromatography, phosphocellulose chromatography, hydrophobic interaction chromatography, affinity chromatography, hydroxylapatite chromatography and lectin chromatography. Protein refolding steps can be used, as necessary, in completing configuration of the mature protein. High performance liquid chromatography (HPLC) can be employed for final purification steps. The immunogenic peptides of the present invention may be used to elicit CTLs ex vivo from either healthy individuals or from cancer patients with cancer, such as colorectal carcinoma, lung carcinoma, ovarian carcinoma, breast carcinoma, or prostate carcinoma. Such responses are induced by incubating in tissue culture the individual's CTL precursor lymphocytes together with a source of antigen presenting cells and the appropriate immunogenic peptide. Examples of suitable antigen presenting cells include dendritic cells, macrophages, and activated B cells. Typically, the peptide at concentrations between 10 and 40 μg/ml, would be pre-incubated with the antigen presenting cells for periods ranging from 1 to 18 hrs. β 2 -microglobulin (4 μg/ml) can be added during this time period to enhance binding. The antigen presenting cells may also be held at room temperature during the incubation period (Ljunggren, H.-G. et al., Nature, 346:476-480, (1990)) or pretreated with acid (Zeh, H. J., III et al., Hum. Immunol., 39:79-86, (1994)) to promote the generation of denatured class I MHC molecules which can then bind the peptide. The precursor CTLs (responders) are then added to the antigen presenting cells to which the immunogenic peptide has bound (stimulators) at responder to stimulator ratios of between 5:1 and 50:1, and most typically between 10:1 and 20:1. The co-cultivation of the cells is carried out at 37° C. in RPMI 1640, 10% fetal bovine serum, 2 mM L-glutamine, and IL-2 (5-20 Units/ml). Other cytokines, such as IL-1, IL-7, and IL-12 may also be added to the culture. Fresh IL-2-containing media is added to the cultures every 2-4 days, typically by removing one-half the old media and replenishing it with an equal volume of fresh media. After 7-10 days, and every 7-10 days thereafter, the CTL are re-stimulated with antigen presenting cells to which immunogenic peptide has been bound as described above. Fresh IL-2-containing media is added to the cells throughout their culture as described above. Three to four rounds of stimulation, and sometimes as many five to eight rounds of stimulation, are required to generate a CTL response that can then be measured in vitro. The above described protocol is illustrative only and should not be considered limiting. Many in vitro CTL stimulation protocols have been described and the choice of which one to use is well within the knowledge of the skilled artisan. The peptide-specific CTL can be further expanded to large numbers by treatment with anti-CD3 antibody. For example, see (Riddell, S. R. and Greenberg, P. D., J. Immunol. Methods, 128:189-201, (1990); Walter, E. A. et al., N. Engl. J. Med., 333:1038-1044, (1995)). Antigen presenting cells that are to be used to stimulate a CTL response are typically incubated with peptide of an optimal length, most commonly a nonapeptide, that allows for direct binding of the peptide to the class I MHC molecule without additional processing. Larger oligopeptides and polypeptides are generally ineffective in binding to class I MHC molecules as they are not efficiently processed into an appropriately sized peptide in the extracellular milieu. There a variety of approaches that are known in the art, however, that allow oligopeptides and polypeptides to be exogenously acquired by a cell, which then allows for their subsequent processing and presentation by a class I MHC molecule. Representative, but non-limiting examples of such approaches include electroporation of the molecules into the cell (Harding, C. H. III, Eur. J. Immunol., 22:1865-1869, (1992)), encapsulation of the molecules in liposomes which are fused to the cells of interest (Reddy, R. et al., J. Immunol. Methods, 141:157-163, (1991)), or osmotic shock in which the molecules are taken up via pinocytosis (Moore, M. W. et al., Cell, 54:777-785, (1988)). Thus, oligopeptides and polypeptides that comprise one or more of the peptides of the invention can be provided to antigen presenting cells in such a fashion that they are delivered to the cytoplasm of the cell, and are subsequently processed to allow presentation of the peptides. Antigen presenting cells suitable for stimulating an in vitro CTL response that is specific for one or more of the peptides of the invention can also be prepared by introducing polynucleotide vectors encoding the sequences into the cells. These polynucleotides can be designed such that they express only a single peptide of the invention, multiple peptides of the invention, or even a plurality of peptides of the invention. There are a variety of approaches that are known in the art, that allow polynucleotides to be introduced and expressed in a cell, thus providing one or more peptides of the invention to the class I MHC molecule binding pathway. Representative, but non-limiting examples of such approaches include the introduction of plasmid DNA through particle-mediated gene transfer or electroporation (Tuting, T. et al., J. Immunol., 160:1139-1147, (1998)), or the transduction of cells with an adenovirus expressing the polynucleotide of interest (Perez-Diez, A. et al., Cancer Res., 58:5305-5309, (1998)). Thus, oligonucleotides that code for one or more of the peptides of the invention can be provided to antigen presenting cells in such a fashion that the peptides associate with class I MHC molecules and are presented on the surface of the antigen presenting cell, and consequently are available to stimulate a CTL response. By preparing the stimulator cells used to generate an in vitro CTL response in different ways, it is possible to control the peptide specificity of CTL response. For example, the CTLs generated with a particular peptide will necessarily be specific for that peptide. Likewise, CTLs that are generated with a polypeptide or polynucleotide expressing or coding for particular peptides will be limited to specificities that recognize those peptides. More broadly, stimulator cells, and more specifically dendritic cells, can be incubated in the presence of the whole protein. As a further alternative, stimulator cells, and more specifically dendritic cells, can be transduced or transfected with RNA or DNA comprising the polynucleotide sequence encoding the protein. Under these alternative conditions, peptide epitopes that are naturally cleaved out of the protein, and which are generated in addition to peptide epitopes of SEQ ID NO:1-791 and 1514-1533 can associate with an appropriate class I MHC molecule, which may or may not include HLA-A1, -A2, or -A3. The selection of antigen presenting cells and the type of antigen with which to stimulate the CTL, is left to the ordinary skilled artisan. In certain embodiments, the methods of the present invention include a method for inducing a CTL response in vitro that is specific for a tumor cell expressing a molecule from A1, A2, or A3 supertypes (A11 is a member of the A3 supertype), whereby the method comprises contacting a CTL precursor lymphocyte with an antigen presenting cell that has bound an immunogen comprising one or more of the peptides disclosed according to the invention. In specific embodiments, the methods of the present invention include a method for inducing a CTL response in vitro that is specific for a tumor cell expressing a molecule from A1, A2, or A3 supertypes, whereby the method comprises contacting a CTL precursor lymphocyte with an antigen presenting cell that has exogenously acquired an immunogenic oligopeptide or polypeptide that comprises one or more of the peptides disclosed according to the invention. A yet additional embodiment of the present invention is directed to a process for inducing a CTL response in vitro that is specific for a tumor cell expressing a molecule from A1, A2, or A3 supertypes, comprising contacting a CTL precursor lymphocyte with an antigen presenting cell that is expressing a polynucleotide coding for a polypeptide of the invention and wherein said polynucleotide is operably linked to a promoter. In specific embodiments, the methods of the present invention include a method for inducing a CTL response in vitro that is specific for a tumor cell expressing HLA-A1, HLA-A2, or HLA-A11, whereby the method comprises contacting a CTL precursor lymphocyte with an antigen presenting cell that has bound an immunogen comprising one or more of the peptides disclosed according to the invention. In specific embodiments, the methods of the present invention include a method for inducing a CTL response in vitro that is specific for a tumor cell expressing HLA-A1, HLA-A2, or HLA-A11, whereby the method comprises contacting a CTL precursor lymphocyte with an antigen presenting cell that has exogenously acquired an immunogenic oligopeptide or polypeptide that comprises one or more of the peptides disclosed according to the invention. A yet additional embodiment of the present invention is directed to a process for inducing a CTL response in vitro that is specific for a tumor cell expressing HLA-A1, HLA-A2, or HLA-A11, comprising contacting a CTL precursor lymphocyte with an antigen presenting cell that is expressing a polynucleotide coding for a polypeptide of the invention and wherein said polynucleotide is operably linked to a promoter. A variety of techniques exist for assaying the activity of CTL. These techniques include the labeling of target cells with radionuclides such as Na 2 51 Cr0 4 or 3 H-thymidine, and measuring the release or retention of the radionuclides from the target cells as an index of cell death. Such assays are well-known in the art and their selection is left to the skilled artisan. Alternatively, CTL are known to release a variety of cytokines when they are stimulated by an appropriate target cell, such as a tumor cell expressing the relevant class I MHC molecule and the corresponding peptide. Non-limiting examples of such cytokines include IFN-7, TNFα, and GM-CSF. Assays for these cytokines are well known in the art, and their selection is left to the skilled artisan. Methodology for measuring both target cell death and cytokine release as a measure of CTL reactivity are given in (Coligan, J. E. et al, Current Protocols in Immunology, 1999, John Wiley & Sons, Inc., New York). After expansion of the antigen-specific CTLs, the latter are then adoptively transferred back into the patient, where they will destroy their specific target cell. The utility of such adoptive transfer is demonstrated in North, R. J. et al. (Infect. Immun., 67:2010-2012, (1999)) and Riddell, S. R. et al. (Science, 257:238-241, (1992)). In determining the amount of cells to reinfuse, the skilled physician will be guided by the total number of cells available, the activity of the CTL as measured in vitro, and the condition of the patient. Preferably, however, about 1×10 6 to about 1×10 12 , more preferably about 1×10 8 to about 1×10 11 , and even more preferably, about 1×10 9 to about 1×10 10 peptide-specific CTL are infused. Methodology for reinfusing the T cells into a patient are well known and exemplified in U.S. Pat. No. 4,844,893 to Honski, et al., and U.S. Pat. No. 4,690,915 to Rosenberg. The peptide-specific CTL can be purified from the stimulator cells prior to infusion into the patient. For example, monoclonal antibodies directed towards the cell surface protein CD8, present on CTL, can be used in conjunction with a variety of isolation techniques such as antibody panning, flow cytometric sorting, and magnetic bead separation to purify the peptide-specific CTL away from any remaining non-peptide specific lymphocytes or from the stimulator cells. These methods are well known in the art, and are their selection is left to the skilled artisan. It should be appreciated that generation of peptide-specific CTL in this manner, obviates the need for stimulating the CTL in the presence of tumor. Thus, there is no chance of inadvertently reintroducing tumor cells into the patient. Thus, one embodiment of the present invention relates to a process for treating a subject with cancer characterized by tumor cells expressing complexes of a molecule from A1, A2, or A3 supertypes, for example, HLA-A1, HLA-A2, or HLA-A11, whereby CTLs produced in vitro according to the present invention are administered in an amount sufficient to destroy the tumor cells through direct lysis or to effect the destruction of the tumor cells indirectly through the elaboration of cytokines. Another embodiment of the present invention is directed to a process for treating a subject with cancer characterized by tumor cells expressing any class I MHC molecule and an epitope of SEQ ID NO: 1-791 and 1514-1533, whereby the CTLs are produced in vitro and are specific for the epitope or original protein and are administered in an amount sufficient to destroy the tumor cells through direct lysis or to effect the destruction of the tumor cells indirectly through the elaboration of cytokines. In the foregoing embodiments the cancer to be treated may include a colorectal carcinoma, an ovarian carcinoma, a breast carcinoma, a lung carcinoma, and prostate carcinoma, but especially ovarian carcinoma. The ex vivo generated CTL can be used to identify and isolate the T cell receptor molecules specific for the peptide. The genes encoding the alpha and beta chains of the T cell receptor can be cloned into an expression vector system and transferred and expressed in naive T cells from peripheral blood, T cells from lymph nodes, or T lymphocyte progenitor cells from bone marrow. These T cells, which would then be expressing a peptide-specific T cell receptor, would then have anti-tumor reactivity and could be used in adoptive therapy of cancer, and more specifically cancer, colorectal carcinoma, ovarian carcinoma, breast carcinoma, lung carcinoma, and prostate carcinoma. In addition to their use for therapeutic or prophylactic purposes, the immunogenic peptides of the present invention are useful as screening and diagnostic agents. Thus, the immunogenic peptides of the present invention, together with modern techniques of gene screening, make it possible to screen patients for the presence of genes encoding such peptides on cells obtained by biopsy of tumors detected in such patients. The results of such screening may help determine the efficacy of proceeding with the regimen of treatment disclosed herein using the immunogens of the present invention. Alternatively, the immunogenic peptides disclosed herein, as well as functionally similar homologs thereof, may be used to screen a sample for the presence of CTLs that specifically recognize the corresponding epitopes. The lymphocytes to be screened in this assay will normally be obtained from the peripheral blood, but lymphocytes can be obtained from other sources, including lymph nodes, spleen, tumors, and pleural fluid. The peptides of the present invention may then be used as a diagnostic tool to evaluate the efficacy of the immunotherapeutic treatments disclosed herein. Thus, the in vitro generation of CTL as described above would be used to determine if patients are likely to respond to the peptide in vivo. Similarly, the in vitro generation of CTL could be done with samples of lymphocytes obtained from the patient before and after treatment with the peptides. Successful generation of CTL in vivo should then be recognized by a correspondingly easier ability to generate peptide-specific CTL in vitro from lymphocytes obtained following treatment in comparison to those obtained before treatment. The oligopeptides of the invention, such as SEQ ID NO: 1-791 and 1514-1533, can also be used to prepare class I MHC tetramers which can be used in conjunction with flow cytometry to quantitate the frequency of peptide-specific CTL that are present in a sample of lymphocytes from an individual. Specifically, for example, class I MHC molecules comprising peptides of SEQ ID NO: 1-791 and 1514-1533, would be combined to form tetramers as exemplified in U.S. Pat. No. 5,635,363. Said tetramers would find use in monitoring the frequency of CTLs in the peripheral blood, lymph nodes, or tumor mass of an individual undergoing immunotherapy with the peptides, proteins, or polynucleotides of the invention, and it would be expected that successful immunization would lead to an increase in the frequency of the peptide-specific CTL. As stated above, a vaccine in accordance with the present invention may include one or more of the hereinabove described polypeptides or active fragments thereof, or a composition, or pool, of immunogenic peptides disclosed herein. When employing more than one polypeptide or active fragment, two or more polypeptides and/or active fragments may be used as a physical mixture or as a fusion of two or more polypeptides or active fragments. The fusion fragment or fusion polypeptide may be produced, for example, by recombinant techniques or by the use of appropriate linkers for fusing previously prepared polypeptides or active fragments. The immunogenic molecules of the invention, including vaccine compositions, may be utilized according to the present invention for purposes of preventing, suppressing or treating diseases causing the expression of the immunogenic peptides disclosed herein, such as where the antigen is being expressed by tumor cells. As used in accordance with the present invention, the term “prevention” relates to a process of prophylaxis in which an animal, especially a mammal, and most especially a human, is exposed to an immunogen of the present invention prior to the induction or onset of the disease process. This could be done where an individual has a genetic pedigree indicating a predisposition toward occurrence of the disease condition to be prevented. For example, this might be true of an individual whose ancestors show a predisposition toward certain types of cancer. Alternatively, the immunogen could be administered to the general population as is frequently done for infectious diseases. Alternatively, the term “suppression” is often used to describe a condition wherein the disease process has already begun but obvious symptoms of said condition have yet to be realized. Thus, the cells of an individual may have become cancerous but no outside signs of the disease have yet been clinically recognized. In either case, the term prophylaxis can be applied to encompass both prevention and suppression. Conversely, the term “treatment” is often utilized to mean the clinical application of agents to combat an already existing condition whose clinical presentation has already been realized in a patient. This would occur where an individual has already been diagnosed as having a tumor. It is understood that the suitable dosage of an immunogen of the present invention will depend upon the age, sex, health, and weight of the recipient, the kind of concurrent treatment, if any, the frequency of treatment, and the nature of the effect desired. However, the most preferred dosage can be tailored to the individual subject, as determined by the researcher or clinician. The total dose required for any given treatment will commonly be determined with respect to a standard reference dose as set by a manufacturer, such as is commonly done with vaccines, such dose being administered either in a single treatment or in a series of doses, the success of which will depend on the production of a desired immunological result (i.e., successful production of a CTL-mediated response to the antigen, which response gives rise to the prevention and/or treatment desired). Thus, the overall administration schedule must be considered in determining the success of a course of treatment and not whether a single dose, given in isolation, would or would not produce the desired immunologically therapeutic result or effect. The therapeutically effective amount of a composition containing one or more of the immunogens of this invention, is an amount sufficient to induce an effective CTL response to the antigen and to cure or arrest disease progression. Thus, this dose will depend, among other things, on the identity of the immunogens used, the nature of the disease condition, the severity of the disease condition, the extent of any need to prevent such a condition where it has not already been detected, the manner of administration dictated by the situation requiring such administration, the weight and state of health of the individual receiving such administration, and the sound judgment of the clinician or researcher. Thus, for purposes of prophylactic or therapeutic administration, effective amounts would generally lie within the range of from 1.0 μg to about 5,000 μg of peptide for a 70 kg patient, followed by boosting dosages of from about 1.0 μg to about 1,000 μg of peptide pursuant to a boosting regimen over days, weeks or even months, depending on the recipient's response and as necessitated by subsequent monitoring of CTL-mediated activity within the bloodstream. Of course, such dosages are to be considered only a general guide and, in a given situation, may greatly exceed such suggested dosage regimens where the clinician believes that the recipient's condition warrants more a aggressive administration schedule. Needless to say, the efficacy of administering additional doses, and of increasing or decreasing the interval, may be re-evaluated on a continuing basis, in view of the recipient's immunocompetence (for example, the level of CTL activity with respect to tumor-associated or tumor-specific antigens). For such purposes, the immunogenic compositions according to the present invention may be used against a disease condition such as cancer by administration to an individual by a variety of routes. The composition may be administered parenterally or orally, and, if parenterally, either systemically or topically. Parenteral routes include subcutaneous, intravenous, intradermal, intramuscular, intraperitoneal, intranasal, transdermal, or buccal routes. One or more such routes may be employed. Parenteral administration can be, for example, by bolus injection or by gradual perfusion over time. Generally, vaccines are prepared as injectables, in the form of aqueous solutions or suspensions. Vaccines in an oil base are also well known such as for inhaling. Solid forms which are dissolved or suspended prior to use may also be formulated. Pharmaceutical carriers, diluents and excipients are generally added that are compatible with the active ingredients and acceptable for pharmaceutical use. Examples of such carriers include, but are not limited to, water, saline solutions, dextrose, or glycerol. Combinations of carriers may also be used. These compositions may be sterilized by conventional, well known sterilization techniques including sterile filtration. The resulting solutions may be packaged for use as is, or the aqueous solutions may be lyophilized, the lyophilized preparation being combined with sterile water before administration. Vaccine compositions may further incorporate additional substances to stabilize pH, or to function as adjuvants, wetting agents, or emulsifying agents, which can serve to improve the effectiveness of the vaccine. The concentration of the CTL stimulatory peptides of the invention in pharmaceutical formulations are subject to wide variation, including anywhere from less than 0.01% by weight to as much as 50% or more. Factors such as volume and viscosity of the resulting composition must also be considered. The solvents, or diluents, used for such compositions include water, possibly PBS (phosphate buffered saline), or saline itself, or other possible carriers or excipients. The immunogens of the present invention may also be contained in artificially created structures such as liposomes, ISCOMS, slow-releasing particles, and other vehicles which increase the immunogenicity and/or half-life of the peptides or polypeptides in serum. Liposomes include emulsions, foams, micelies, insoluble monolayers, liquid crystals, phospholipid dispersions, lamellar layers and the like. Liposomes for use in the invention are formed from standard vesicle-forming lipids which generally include neutral and negatively charged phospholipids and a sterol, such as cholesterol. The selection of lipids is generally determined by considerations such as liposome size and stability in the blood. A variety of methods are available for preparing liposomes as reviewed, for example, by (Coligan, J. E. et al, Current Protocols in Protein Science, 1999, John Wiley & Sons, Inc., New York) and see also U.S. Pat. Nos. 4,235,871, 4,501,728, 4,837,028, and 5,019,369. Liposomes containing the peptides or polypeptides of the invention can be directed to the site of lymphoid cells where the liposomes then deliver the selected immunogens directly to antigen presenting cells. Targeting can be achieved by incorporating additional molecules such as proteins or polysaccharides into the outer membranes of said structures, thus resulting in the delivery of the structures to particular areas of the body, or to particular cells within a given organ or tissue. Such targeting molecules may a molecule that binds to receptor on antigen presenting cells. For example an antibody that binds to CD80 could be used to direct liposomes to dendritic cells. The immunogens of the present invention may also be administered as solid compositions. Conventional nontoxic solid carriers including pharmaceutical grades of mannitol, lactose, starch, magnesium, cellulose, glucose, sucrose, sodium saccharin, and the like. Such solid compositions will often be administered orally, whereby a pharmaceutically acceptable nontoxic composition is formed by incorporating the peptides and polypeptides of the invention with any of the carriers listed above. Generally, such compositions will contain 10-95% active ingredient, and more preferably 25-75% active ingredient. Aerosol administration is also an alternative, requiring only that the immunogens be properly dispersed within the aerosol propellant. Typical percentages of the peptides or polypeptides of the invention are 0.01%-20% by weight, preferably 1%-10%. The use of a surfactant to properly disperse the immunogen may be required. Representative surfactants include the esters or partial esters of fatty acids containing from 6 to 22 carbon atoms, such as caproic, octanoic, lauric, palmitic, stearic, linoleic, linolenic, olesteric and oleic acids with an aliphatic polyhydric alcohol or its cyclic anhydride. Mixed esters, such as mixed or natural glycerides may be employed. The surfactant may constitute 0.1-20% by weight of the composition, preferably 0.25-5%. Typical propellants for such administration may include esters and similar chemicals but are by no means limited to these. A carrier, such as lecithin for intranasal delivery, may also be included. The peptides and polypeptides of the invention may also be delivered with an adjuvant. Adjuvants include, but are not limited to complete or incomplete Freund's adjuvant, Montanide ISA-51, Lymphocyte Activation Gene-3 (LAG-)3, aluminum phosphate, aluminum hydroxide, alum, and saponin. Adjuvant effects can also be obtained by injecting a variety of cytokines along with the immunogens of the invention. These cytokines include, but are not limited to IL-1, IL-2, IL-7, IL-12, and GM-CSF. The peptides and polypeptides of the invention can also be added to professional antigen presenting cells such as dendritic cells that have been prepared ex vivo. For example, the dendritic cells could be prepared from CD34 positive stem cells from the bone marrow, or they could be prepared from CD14 positive monocytes obtained from the peripheral blood. The dendritic cells are generated ex vivo using cytokines such as GM-CSF, IL-3, IL-4, TNF, and SCF. The cultured DC are then pulsed with peptides at various concentrations using standard methods that are well known in the art. The peptide-pulsed dendritic cells can then be administered either intraveneously, subcutaneously, or intradermally, and the immunization may also include cytokines such as IL-2 or IL-12. The present invention is also directed to a vaccine in which an immunogen of the present invention is delivered or administered in the form of a polynucleotide encoding the a polypeptide or active fragment as disclosed herein, whereby the peptide or polypeptide or active fragment is produced in vivo. The polynucleotide may be included in a suitable expression vector and combined with a pharmaceutically acceptable carrier. For example, the peptides or polypeptides could be expressed in plasmid DNA and nonreplicative viral vectors such as vaccinia, fowlpox, Venezuelan equine encephalitis virus, adenovirus, or other RNA or DNA viruses. These examples are meant to be illustrative only and should not be viewed as self-limiting A wide variety of other vectors are available and are apparent to those skilled in the art from the description given herein. In this approach, a portion of the nucleotide sequence of the viral vector is engineered to express the peptides or polypeptides of the invention. Vaccinia vectors and methods useful in immunization protocols are described in U.S. Pat. No. 4,722,848, the disclosure of which is incorporated herein by reference in its entirety. Regardless of the nature of the composition given, additional therapeutic agents may also accompany the immunogens of the present invention. Thus, for purposes of treating tumors, compositions containing the immunogens disclosed herein may, in addition, contain other antitumor pharmaceuticals. The use of such compositions with multiple active ingredients is left to the discretion of the clinician. In addition, the immunogens of the present invention can be used to stimulate the production of antibodies for use in passive immunotherapy, for use as diagnostic reagents, and for use as reagents in other processes such as affinity chromatography. The present invention also relates to antibodies that react with immunogens, such as a polypeptide comprising one or more of the epitopic peptides of SEQ ID NO: 1-791 and 1514-1533 as disclosed herein. Active fragments of such antibodies are also specifically contemplated. Such antibodies, and active fragments of such antibodies, for example, and Fab structure, may react with, including where it is highly selective or specific for, an immunogenic structure comprising 2, 3, 4 or more of the epitopic peptides of the invention. With the advent of methods of molecular biology and recombinant technology, it is now possible to produce antibody molecules by recombinant means and thereby generate gene sequences that code for specific amino acid sequences found in the polypeptide structure of the antibodies. Such antibodies can be produced by either cloning the gene sequences encoding the polypeptide chains of said antibodies or by direct synthesis of said polypeptide chains, with in vitro assembly of the synthesized chains to form active tetrameric (H 2 L 2 ) structures with affinity for specific epitopes and antigenic determinants. This has permitted the ready production of antibodies having sequences characteristic of neutralizing antibodies from different species and sources. Regardless of the source of the antibodies, or how they are recombinantly constructed, or how they are synthesized, in vitro or in vivo, using transgenic animals, such as cows, goats and sheep, using large cell cultures of laboratory or commercial size, in bioreactors or by direct chemical synthesis employing no living organisms at any stage of the process, all antibodies have a similar overall 3 dimensional structure. This structure is often given as H2L2 and refers to the fact that antibodies commonly comprise 2 light (L) amino acid chains and 2 heavy (H) amino acid chains. Both chains have regions capable of interacting with a structurally complementary antigenic target. The regions interacting with the target are referred to as “variable” or “V” regions and are characterized by differences in amino acid sequence from antibodies of different antigenic specificity. The variable regions of either H or L chains contains the amino acid sequences capable of specifically binding to antigenic targets. Within these sequences are smaller sequences dubbed “hypervariable” because of their extreme variability between antibodies of differing specificity. Such hypervariable regions are also referred to as “complementarity determining regions” or “CDR” regions. These CDR regions account for the basic specificity of the antibody for a particular antigenic determinant structure. The CDRs represent non-contiguous stretches of amino acids within the variable regions but, regardless of species, the positional locations of these critical amino acid sequences within the variable heavy and light chain regions have been found to have similar locations within the amino acid sequences of the variable chains. The variable heavy and light chains of all antibodies each have 3 CDR regions, each non-contiguous with the others (termed L1, L2, L3, H1, H2, H3) for the respective light (L) and heavy (H) chains. The accepted CDR regions have been described in the text and figures of Kabat et al. (J. Biol. Chem. 252:6609-6616 (1977)). In all mammalian species, antibody polypeptides contain constant (i.e., highly conserved) and variable regions, and, within the latter, there are the CDRs and the so-called “framework regions” made up of amino acid sequences within the variable region of the heavy or light chain but outside the CDRs. The antibodies disclosed according to the invention may also be wholly synthetic, wherein the polypeptide chains of the antibodies are synthesized and, possibly, optimized for binding to the polypeptides disclosed herein as being receptors. Such antibodies may be chimeric or humanized antibodies and may be fully tetrameric in structure, or may be dimeric and comprise only a single heavy and a single light chain. Such antibodies may also include fragments, such as Fab and F(ab 2 )′ fragments, capable of reacting with and binding to any of the polypeptides disclosed herein as being receptors. A further embodiment of the present invention relates to a method for inducing a CTL response in a subject comprising administering to subjects that express HLA-A1 antigens an effective (i.e., CTL-stimulating amount) of an immunogen of the invention that does not comprise the entire protein expressing the epitopic peptides disclosed herein (i.e., one that comprises less than the entire protein where the protein is a naturally occurring polypeptide) in an amount sufficient to induce a CTL response to tumor cells expressing at least HLA-A1 or HLA-A2, as the case may be, thereby eliciting a cellular response against said tumor cells. A still further embodiment of the present invention relates to a method for inducing a CTL response in a subject, wherein the immunogen is in the form of a polynucleotide. In one non-limiting example, the method comprises administering to subjects that express HLA-A1 at least one CTL epitope, wherein said epitope or epitopes are selected from a group comprising the peptides disclosed according to the invention, and are coded within a polynucleotide sequence that does not comprise the entire protein coding region, in an amount sufficient to induce a CTL response to tumor cells expressing HLA-A1 or HLA-A2. While the below examples are provided to illustrate the invention, it is to be understood that these methods and examples in no way limit the invention to the embodiments described herein and that other embodiments and uses will no doubt suggest themselves to those skilled in the art. All publications, patents, and patent applications cited herein are hereby incorporated by reference, as are the references cited therein. It is also to be understood that throughout this disclosure where the singular is used, the plural may be inferred and vice versa and use of either is not to be considered limiting. EXAMPLE 1 Cell Lines For HLA-A1 and HLA-A11 studies, ARGOV57, a HLA-A1/11 positive ovarian cell line, was established by culturing tumor cells from an ascitic fluid from an ovarian patient. For HLA-A2 studies, OVCAR3, a HLA-A2 positive ovarian carcinoma cell line, was established by culturing tumor cells from an ascitic fluid from an ovarian patient. SKOV3-A2, a HLA-A2 stably expressing ovarian carcinoma cell line, was established by culturing tumor cells from an ascitic fluid from an ovarian patient and transduced with HLA-A2 gene. EXAMPLE 2 Immunoaffinity Purification ARGOV57 cells were grown in 10-chamber Nunc cell factories (Fisher, Pittsburgh, Pa.). The cells were harvested by treatment with 0.45% trypsin and 0.32 mM EDTA, washed two times in phosphate-buffered saline solution (pH 7.4), and stored as cell pellets at −80° C. Aliquots of 6-8×10 10 cells were solubilized at 5-10×10 6 cells/ml in 20 mM Tris, pH 8.0, 150 mM NaCl, 1% CHAPS, 18.5 μg/ml iodoacetamide, 5 μg/ml aprotonin, 10 μg/ml leupeptin, 10 μg/ml pepstatin A, 5 mM EDTA, 0.2% sodium azide, and 17.4 μg/ml phenylmethylsulfonyl fluoride for 1 h. This and all subsequent steps were performed with ice-cold solutions and at 4° C. The lysates were then centrifuged at 100,000×g, the pellets discarded, and the supernatants passed through a 0.22 μm filter. The supernatants were then passed over a series of columns with the first containing Sepharose, and the second containing the HLA-A1-specific monoclonal antibody, GAP-A1, bound to a protein A-Sepharose matrix. The second column was then sequentially washed with 20 column volumes of 20 mM Tris, pH 8.0, 150 mM NaCl, 20 column volumes of 20 mM Tris, pH 8.0, 1.0 M NaCl, and 20 column volumes of 20 mM Tris, pH 8.0. The peptides were eluted from the column with 5 column volumes of 10% acetic acid. The isolated HLA-A1 molecules were then boiled for 5 min to further dissociate any bound peptide from the heavy chains. The peptides were then separated from the co-purifying class I heavy chain and β 2 -microglobulin by centrifugation on a Ultrafree-CL membrane with a nominal molecular weight cut-off of 5,000 Daltons (Millipore, Bedford, Mass.). For a separate study, OVCAR3 or SKOV3 cells were successfully prepared using the same procedure as just described except that HLA-A2 molecules were prepared using HLA-A2 specific antibodies. EXAMPLE 3 Peptide Fractionation The peptide extracts were fractionated by RP-HPLC (Reversed Phase-High Performance Liquid Chromatography) using an Applied Biosystems (ABI) model 140B system. The extracts were concentrated by vacuum centrifugation from about 20 ml down to 250 μl and injected into either a Brownlee (Norwalk, Conn.) C 18 Aquapore column (2.1 mm×3 cm; 300 Å; 7 μm) or a Higgins (Mountain View, Calif.) C18 Haisil column (2.1 mm×4 cm; 300 Å; 5 μm). The peptides were eluted by first using a gradient of acetonitrile/0.085% TFA (trifluoroacetic acid) in 0.1% TFA/water, with the concentration of acetonitrile increasing from 0-9% (0-5 minutes), 9-36% (5-55 minutes), and 36-60% (55-62 minutes). A second dimension fractionation of combined fractions 17 and 18 from the first dimension (TFA) fraction was accomplished using the same gradient but with the substitution of HFBA (heptafluorobutyric acid) for TFA. The flow rate was 200 μl/min, and fractions were collected at 1 min (Brownlee column) or 40 second (Higgins column) intervals. A third dimension of RP-HPLC was achieved using an Eldex (Napa, Calif.) MicroPro Pump, a homemade C 18 microcapillary column, and an ABI model 785A UV absorbance detector. The column was prepared by packing a 27 cm bed of 10 μm C 18 particles in a section of 285 μm o.d./75 μm i.d. fused silica (Polymicro Technologies, Phoenix, Ariz.). Peptides in combined fractions 26 and 27 of the second dimension fraction were loaded onto this column and eluted with a gradient of acetonitrile/0.67% triethylamine acetate/water in 0.1% triethylamine acetate/water, with the concentration of acetonitrile increasing from 0-60% in 40 minutes. The flow rate was about 300 nl/min, and fractions were collected into 25 μl of water every 30 s. In all RP-HPLC experiments, peptides were detected by monitoring UV absorbance at 214 nm. EXAMPLE 4 Mass Spectrometric Analysis The second dimension HPLC fraction was analyzed using an affluent splitter on the microcapillary HPLC column. In this experiment, the column (360 μm o.d.×100 μm i.d. with a 25 cm C 18 bed) was butt connected with a zero dead volume tee (Valco, Houston, Tex.) to two pieces of fused silica of different lengths (25 μm and 40 μm i.d.). Peptides were eluted with a 34 min gradient of 0-60% acetonitrile. The 25 m capillary deposited one-fifth of the HPLC effluent into the wells of a microtiter plate for use in CTL epitope reconstitution assays, whereas the remaining four-fifths of the effluent was directed into the mass spectrometer. Ions were formed by electrospray ionization, and mass spectra were recorded by scanning between mass to charge ratios (m/z) 300 and 1400 every 1.5 seconds. Peptide sequences were determined by CAD (collision-activated dissociation) tandem mass spectrometry as described in the literature (Hunt, D. F. et al., Proc. Natl. Acad. Sci. U.S.A, 83:6233-6237, (1986)). EXAMPLE 5 Homology Searches of Identified Peptide Sequences Proteins containing peptides corresponding to the masses identified by MS were analyzed with the search algorithm, SEQUEST. Searches were also carried out on the GenBank non-redundant sequence database (http://www.ncbi.nlm.nih.-gov/Entrez/) as well as on our own unique database of 2943 specific sequences compiled from GenBank and EST data-base entries. Upon experimental confirmation of the peptide sequence, a tBLASTn search of the GenBank non-redundant database was performed to identify any genes containing the DNA sequence encoding the peptide. EXAMPLE 6 Peptide Synthesis Peptides were synthesized using a Gilson (Madison, Wis.) AMS 422 multiple peptide synthesizer. Quantities of 10 μMol were synthesized using conventional FMOC amino acids, resins, and chemical techniques. Peptides were purified by RP-HPLC using a 4.6 mm×100 mm POROS (Perseptive Biosystems, Cambridge, Mass.) column and a 10 min, 0-60% acetonitrile in 0.1% TFA gradient. EXAMPLE 7 Generation of Monocyte-Derived DC and Peptide Loading PBMC were purified from HLA-A2 + normal donor blood using lymphocyte separation media (Cappel ICN Biomedical, Aurora, Ohio). PBMC (5.3×10 6 ) were added to individual wells of a 24-well cluster plate (Costar, Corning, N.Y.) in 1.0 ml of serum-free AIM-V medium (Life Technologies) and allowed to adhere for 60 min at 37° C. Non-adherent cells were removed and saved as a source of effector T cells. Adherent PBMC (˜8.3×10 5 /well) were then pulsed with 50 mg/ml synthetic peptides in serum-free AIM-V medium containing 1.5 mg/ml β 2 -microg lobulin (Calbiochem-Novabiochem, San Diego, Calif.) and incubated for 2 h at 37° C. Unbound peptides were aspirated and the wells washed with media. Monocyte-derived DC were generated as follows. PBMC (5.3×10 7 ) were allowed to adhere in T-75 flasks (Corning) in 10 ml of serum-free AIM-V medium for 60 min at 37° C. Non-adherent cells were collected as a source of effector T cells and pooled with the previous collection above. Adherent monocytes in flasks were then exposed to recombinant human granulocyte macrophage colony stimulating factor (GM-CSF, 25 ng/ml; Peprotech) and recombinant human IL-4 (100 ng/ml; Peprotech) in 10 ml of AIM-V medium containing 10% heat-inactivated FBS. DC obtained by this method [immature DC (iDC)] are characterized by expression of low levels of CD83, CD80, CD86, and HLA class I and class II molecules (data not shown). Mature DC (mDC) were obtained by exposing day 5 DC cultures to recombinant soluble CD40 ligand (sCD40L; Peprotech) at 1.5 mg/ml for 24 h in the presence of 25 ng/ml GM-CSF and are characterized by expression of high levels of CD80, CD86, and HLA class I and class II molecules. mDC were harvested, washed, pulsed with 5 mg/ml peptide in serum-free AIM-V medium and irradiated (5000 rad) prior to use as stimulators. EXAMPLE 8 Generation of Peptide-Specific CTL The protocol used here is a modification of the method described by Plebanski et al. (Eur. J. Immunol. 25:1783, (1995)). CTL to peptide were generated by 3±4 cycles of stimulation with peptide-loaded APC. For the first round of stimulation (day 0), T cells or non-adherent PBMC from above (2.3×10 6 /ml or 4.3×10 6 per well) were added in bulk (CD4 + , CD8 + , NK, etc.) to adherent PBMC-loaded peptides in serum-free medium (50 mg/ml), β 2 -microglobulin (1.5 mg/ml) (Calbiochem-Novabiochem), recombinant human IL-7 (5 ng/ml) (Peprotech) and keyhole limpet hemocyanin (5 mg/ml) (Sigma, St Louis, Mo.). Cultures were re-stimulated with iDC every 7 days, pulsed with varying amounts of peptide (second round 25 mg/ml, third round 10 mg/ml) and irradiated (5000 rad) on day 8. At each re-stimulation, the T cells were transferred to new plates by first aspirating 70% of spent media in wells and then transferring the pooled contents to a new plate. Fresh IL-7 was added at each re-stimulation. The responder:stimulator (T cell:DC) ratio was set at 20 for each stimulation. Recombinant human IL-2 (10 U/ml) was added on day 5 after each re-stimulation. Prior to 51 Cr-release assay, the T cells were harvested and CD8 + T cells were purified by positive selection using CD8 + microbeads immunomagnetic cell separation with MACS kit (Miltenyi Biotec, Auburn, Calif.). If a fourth round of stimulation was necessary following CTL analysis, the CTL were pulsed as before, except with 5±10 mg/ml of peptide. EXAMPLE 9 Generation of Allospecific CTL HLA-A2-allospecific CTL were obtained in a mixed lymphocyte reaction by repeated stimulation of HLA-A3 + PBMC (responders) with irradiated HLA-A2 + stimulator PBMC at a ratio of 10:1 in the presence of 10 U/ml IL-2. Stimulation was repeated weekly with PBMC from different HLA-A2 + donors so as to minimize alloresponse to non-HLA-A2 antigens. T cells were assessed for lysis on several HLA-A2 + targets including tumor cells, EBV-B cells and HLA-A3 + targets every week after the third round of stimulation. EXAMPLE 10 CTL Expansion Expansion of large numbers of peptide-specific or HLA-A2-allospecific CTL was achieved by culturing 5.3×10 4 ±1.3×10 5 T cells around day 6 or 7 post peptide- or allostimulation in the presence of 2.5-3.0×10 7 irradiated (5000 rad) allogeneic normal donor PBMC coated with anti-CD3 antibody at 10 ng/ml (BD PharMingen, San Diego, Calif.) and 25 U/ml of recombinant human IL-2 (Peprotech) in a final volume of 30 ml RPMI medium. Media changes with IL-2 addition (50 U/ml) were effected on days 5 and 8. Cells were harvested for cytotoxicity assays on days 10±12 and re-stimulated or frozen for later use. EXAMPLE 11 51Cr-Release Cytotoxicity Assay The standard 4-h Cr-release assay was performed in 96-well V-bottomed microplates. Target cells in suspension (T2, C1R.A2, B-LCL and K562) were labeled with 100 mCi Na 2 51 CrO4 (NEN Life Science, Boston, Mass.) per 1.3×10 6 cells either overnight (˜6±18 h) in 5 ml RPMI 1640 media containing 2±5% FBS or for 60±90 min at 37° C. directly with the cell pellet in the case of adherent cells (tumor cell lines and control lines). Labeling was terminated by washing the targets with cold media containing 5% FBS for a total of three washes. Target cells were resuspended at a concentration of 2-3×10 4 /ml. About 2-3×10 3 targets in 100 ml were delivered to each well containing CTL (effectors) seeded at different E:T ratios. Spontaneous release wells contained targets in media alone, while maximal release wells contained targets in 2% NP-40 detergent (Igepal CA-630; Sigma). HLA restriction of CTL-mediated killing was achieved by preincubation of targets with HLA-specific antibodies prior to incubation with CTL. The plate was gently spun for 1±2 min and incubated at 37° C. for 4 h. For harvesting assay plates, 100 ml of supernatants from the wells was transferred to counting tubes (USA Scientific) and g counts were determined in a g counter (ICN Micromedic Systems, Huntsville, Ala.). Cytolytic activity of T cells was expressed in percent specific lysis as follows: specific lysis={[experimental release (c.p.m.)±spontaneous release (c.p.m.)]/[maximal release (c.p.m.)±spontaneous release (c.p.m.)]}. EXAMPLE 12 Competitive Inhibition Assay Peptide-stimulated CTL were reacted with 51 Cr-labeled Ov2 tumor cells (E:T ratio of 40) in the presence of excess of cold targets in a 4-h Cr-release assay. Cold targets were either empty T2 cells, T2 cells pulsed with 1 mg/ml relevant peptide (used to stimulate CTL) or irrelevant (control) peptides (HER-2/neu 369±377 or MART 127±35), or IFN-γ pre-treated tumor cells (SKOV3.A2 and OVCAR 3) with the cold target in 5-fold excess of the hot target. Results indicate that (i) CTL show specific interaction with the peptide to which they are sensitized to, and (ii) CTL compete for similar epitopes presented on Ov2 as were found in SKOV3.A2 and OVCAR3 cell lines by MS. TABLE 2Description of Fragments, Parent Sequence Iden-tification and Parent SwissProt IdentificationNumber for peptides 1-791 and 1514-1533ParentSwiss-ProtSEQIdenti-IDParent SequenceficationNO:FragmentIdentificationNo.1AEAEFYRQVBCL-6 corepressor longQ6W2J92IYNGDMEKIisoform_E1B_19K/Bcl-2-Q12983interacting proteinNip33KEFDGKSLVSimilar to Heat shockP08238protein HSP 90-beta(HSP 84) (HSP 90)4HIPAGTLVQVCytochrome P450 11B2,P19099mitochondrial precursor5SLAEGLRTV2′-5′oligoadenylateQ2HJ14synthetase 36YLGDGPKLV26S protease regulatoryP62191subunit 4 (P26s4)7YLASLIRSV26S proteasome non-P51665ATPase regulatorysubunit 78FVDDYTVRV26S proteasome non-O00487ATPase regulatorysubunit 149KLLEPVLLL40S ribosomal proteinP62249S1610KLIEVDDERKL40S ribosomal proteinP62753S6 (PhosphoproteinNP33)11RLFEGNALL40S ribosomal proteinP46781S912TLYEAVREV60S ribosomal proteinP62906L10a (CSA-19)13NMVAKVDEV60S ribosomal proteinP62906L10a (CSA-19)14SLIKQIPRI60S ribosomal proteinP62906L10a (CSA-19)15FLSEEGGHVAV6-phosphofructo-2-Q16877kinase/fructose-2,6-biphosphatase 4 (6PF-2-K/Fru-2,6-P2ASE testis-type isozyme)16IETINFHEVCleavage and polyadeny-Q9UKF6lation specificityfactor, 73 kDa subunit(CPSF 73 kDa subunit)17YLNDLIHSVA kinase anchor proteinO4357210, mitochondrialprecursor18RVAPEEHPVLActin, cytoplasmic 1P60709(Beta-actin)19DVLKIPVQLVActivated T-cell markerQ6YHK3CD10920LSDFLKANVActivin receptor typeP270372A precursor (EC2.7.11.30)21DLCFEKVNVADAM19 proteinQ8TBU722KLHDINAQLAP-1 complex subunitQ10567beta-1 (Adapter-relatedprotein complex 1 beta-1 subunit) (Beta-adaptin 1)23GNGAPDVFQTAdaptor-related proteinQ9BYI8NF0101953724IDAIRIPVLLung alpha/beta hydro-Q96SE0lase protein 125FIASKGVKLVAlpha-actinin-3Q0804326HRPDLIDYAlpha-actinin-3Q0804327SPQGLELALPSAnkyrin-2 (BrainQ01484ankyrin) (Ankyrin-B)28KIVKRPSLQFLAnkyrin repeat and SOCSQ8WXJ9box protein 1729TLVTVSAAKTAnti-colorectal carcin-Q65ZQ1oma heavy chain30KVLDGSPIEVAPOBEC1 complementationQ9NQ94factor (APOBEC1-stimulating protein)31FLAEHPNVTLProbable DNA dC->dU-Q96AK3editing enzyme APOBEC-3D (EC 3.5.4.-)32NLVQDSLDLApolipoprotein-L4 pre-Q9BPW4cursor (ApolipoproteinL-IV)33ISENEKLQKApoptosis stimulatingQ96KQ4of p53 protein 134VLAARNPAKVNucleoporin 188 kDaQ5SRE5(arachin)35RYFDGNLEKLProtein ariadne-1 homo-Q9Y4X5log (ARI-1) (Ubiquitin-conjugating enzyme E2-binding protein 1)36TLADVLYHVSet1/Ash2 histoneQ9UBL3methyltransferase com-plex subunit ASH2(ASH2-like protein)37LPSPKPMKMKNATP synthase F0 subunitQ85KZ38 Splice isoform 2 ofQ9H7F038ISSMLVLFFATPase_family_homo-Q9H7F0log_up-regulated_in_senescence_cells_Probable phospholipid-transporting39SPDEGALVRAATPase 1A (EC 3.6.3.1)Q9Y2Q0(Chromaffin granuleATPase II)40ILLITLIPYATP-binding cassetteQ8WWZ4A1041NLEQQETEPATP-binding cassetteQ9BZC7sub-family A member 2(ATP-binding cassettetransporter 2) (ATP-binding cassette 2)42RKVLYVMELAutoantigen RCD8Q6P2E943EAIPARKLKxonemal dynein heavyQ96JB1chain 844SLRLENITVButyrophilin-like pro-Q6UX41tein 8 precursor45SYVLKKAQVUbiquitin carboxyl-Q9Y2K6terminal hydrolase 20(EC 3.1.2.15)46KLIHPKLEYBardet-Biedl syndrome 7Q8IWZ6protein (BBS2-likeprotein 1)47EFDQLDQENLarge proline-rich pro-P48634tein BAT2 (HLA-B-assoc-iated transcript 2)48TVLLRLGDELBcl-2 related ovariankiller49LFEILIEQILipopolysaccharide-P50851responsive and beige-like anchor protein(CDC4-like protein)50KLELDETGQESplice isoform 3 ofP35612-3P3561251LAIGAFTLLLUDP-GlcNAc: betaGalQ9Y2A9beta-1,3-N-acetylgluco-saminyltransferase 3(EC 2.4.1.-)52QILLDETLKCell growth inhibitingQ2TTR2protein 3953DECITNLLVBH3-interacting domainP55957death agonist (BID)54TVVSGSNVILNCD48 antigen precursorP09326(B-lymphocyte activa-tion marker BLAST-1)55SLDERPVAVBone morphogenetic pro-Q13873tein receptor type-2precursor (EC2.7.11.30)56MVDSQQKSPBullous pemphigoid an-Q8WXK8tigen 1, isoform 757SLLLLPEKNBRCA1 associated RINGQ53F80domain 1 variant58VLCVSDIISLBreast cancer type 2P51587susceptibility protein( Fanconi anemia groupD1 protein)59FLPDPSALQNLProtein BRE (Brain andQ9NXR7reproductive organ-expressed protein)(BRCA1/BRCA2-containingcomplex subunit 45)60MLNEHDFEVBreast cancer 1 earlyQ3LRJ0onset61VNTDFSPYLBreast cancer 1 earlyQ3LRJ0onset62EFMLVYKFARBreast and ovarianQ7KYU6cancer susceptibilityprotein63TLWVDPYEVBTG2 protein (NGF-P78543inducible anti-proli-ferative protein PC3)64FLDHIIASVNuclear protein 5qNCAQ7LBC665TLNDREYQLCAD protein [Includes:P27708Glutamine-dependentcarbamoyl-phosphatesynthase (EC 6.3.5.5);Aspartate carbamoyl-transferase (EC2.1.3.2); Dihydrooro-tase (EC 3.5.2.3)]66VEVMVNDVNCadherin EGF LAG seven-Q9NYQ7pass G-type receptor 3precursor (Flamingohomolog 1) (hFmi 1)(Multiple epidermalgrowth factor-like do-mains 2) (Epidermalgrowth factor-like 1)67LSIYLSIYLCadherin FIB3Q6UW7068SLSMVNHRLIntegrin alpha-3 pre-P26006cursor (GalactoproteinB3)69RVDFPGFVRCalcineurin B homolo-O43745gous protein 2 (Hepato-cellular carcinoma-as-sociated antigen 520)70MTDKAPPGVCalcium/calmodulin-Q7Z7J9dependent protein ki-nase II inhibitor alpha(CaMKIINalpha)71WTNPQFKICalpain-11 (ECQ9UMQ63.4.22.-)72IMAQLPQEQKAAlpha-1 catenin (Cad-P35221herin-associated pro-tein) (Alpha E-catenin)73KIDPLEVEENeural cell adhesionQ59FY0molecule variant74KLPEKWESVRibosomal L1 domain-O76021containing protein 1(Cellular senescence-inhibited gene protein)75LIEKEKVLNCENP-F kinetochore pro-P49454tein (Centromere pro-tein F) (Mitosin)76FEVKEDQVKCentaurin-delta 1 (Cnt-Q8WZ64d1) (Arf-GAP, Rho-GAP,ankyrin repeat andpleckstrin homology do-main-containing protein2)77DTEAEKSQVCentrosomal protein 2Q9BV73(Centrosomal Nek2-as-sociated protein 1) (C-NAP1)78FLKEHMDEVPericentriol material 1Q1515479KLLGELHTLPericentriol material 1Q1515480TLVEAFPTLCervical cancer sup-Q8NFX8pressor gene 581QSNKGFVVINT-complex protein 1Q92526subunit zeta-282LADGALIYRChemokine-like factorQ9UBR5(C32)83GLGAEIEIRVacuolar proteinQ96RL7sorting 13A84GKLILLDKLChromodomain-helicase-O14647DNA-binding protein 2(EC 3.6.1.-)85PQTICRKPFERM domain-containingQ96NE9protein 686RSYYLNEIPutative proteinQ9H0A9C21orf5687TTITVSPFYAdiponutrin (iPLA2-Q9NST1epsilon)88RLPDDDPTAVCoatomer subunit gamma-Q9UBF2289LVAISTVSFSISodium/potassium/Q9UI40calcium exchanger 2precursor90VLIDYQRNVExportin-1 (ChromosomeO14980region maintenance 1protein homolog)91SILNEGGIKCUB and sushi domain-Q7Z407containing protein 3precursor92YMADRLLGVCullin-7 (CUL-7)Q1499993YLKDLIEEVCyclic AMP-dependentP18848transcription factorATF-494YLDIKGLLDS-phase kinase-associ-P63208ated protein 1A (CyclinA/CDK2-associatedprotein p19)95PCLSELHKACyclin-A1P7839696TVLDFGVLASICyclin M3, isoform 1Q8NE0197MPSETPQAECystathionine beta-Q58H57synthase human homologof Cynomolgus monkeygene product98FLLEALRKTCytochrome P450 2E1 (ECP051811.14.14.1)99KMLETKWSLKeratin, type II cyto-P05787skeletal 8100QPLLKQSPWCPEB2 proteinQ3B8N6101YLLPAIVHIProbable ATP-dependentP17844RNA helicase DDX5 (EC3.6.1.-)102KLLPGDIHQIDedicator of cytokine-Q14185sis protein 1103SLLKGDLKGVDevelopment and differ-O43150entiation-enhancingfactor 2104NAEVLLVSEIProbable ubiquitinO00507carboxyl-terminal hy-drolase FAF-Y (EC3.1.2.15)105RLWGEPVNLProbable ubiquitin car-O00507boxyl-terminal hy-drolase FAF-Y (EC3.1.2.15)106QLIDLSSPLIG2 and S phase ex-Q9NYZ3pressed protein 1107YIDYTGAAYAHUMAN CDNA FLJ30829Q96NI3fis, cloneFEBRA2001790, highlysimilar to Xenopuslaevis RRM-containingprotein SEB-4 mRNA108VIENKSDEKVIKIAA1799 proteinQ96B95109PSPQLWTVPeroxisomal prolifera-Q9BYK8tor-activated receptorA-interacting complex285 kDa protein (EC3.6.1.-) (ATP-dependenthelicase PRIC285)110EGRGGLPAGLPVHUMAN KIAA1922Q96PW6111NMYGKVVTVTranscription elonga-O00267tion factor SPT5 (DLC-1)(deleted in livercancer-1)112RLYDGLFKVDNA damage-binding pro-Q16531tein 1 (Damage-specificDNA-binding protein 1)113QNFVDSKEVDNA excision repairQ03468protein ERCC-6114ALIEKLVELDNA polymerase alphaQ14181subunit B (DNA poly-merase alpha 70 kDasubunit)115VIEDDVNMAIRDNA replication licens-P49736ing factor MCM2 (Mini-chromosome maintenanceprotein 2 homolog)116SQDEIKQEVDNA2-like homolog (ECP515303.6.1.-) (DNA replica-tion ATP-dependent hel-icase-like homolog)117HLNGSCHLLIEstrogen response ele-Q77798ment binding protein(cotton-top Tarmarin),DNA2-like homolog(human)118ALIDRMVNLDNA damage-inducibleP35638transcript 3 (DDIT-3)(Growth arrest and DNA-damage-inducible pro-tein GADD153)119SQKIQEAVKADNA-directed RNA poly-O95602merase I largest sub-unit (EC 2.7.7.6)120LFDLVEEVQDnaJ homolog subfamilyQ96KC8C member 1121LLAALLLDPSplice isoform 2 ofP35462-2P35462122FLDESRSTQYMRuvB-like 2 (ECQ9Y2303.6.1.-) (48-kDa TATAbox-binding protein-interacting protein)123VLLGKVYVVDRE1_proteinQ9NXT9124TIDELKEQVDynactin-1 (150 kDaQ14203dynein-associatedpolypeptide)125NLAYENVKEDynein heavy chain,Q14204cytosolic (DYHC)126SEVEQYVKYDynein heavy chain,Q14204cytosolic (DYHC)127ETQLTYRREchinoderm microtubuleQ6UYC9associated protein-like5128IKDDLEDLIECT2 protein (Epithel-Q9H8V3ial cell-transformingsequence 2 oncogene)129QVLGKIERAEndothelial differenti-O60869ation-related factor 1(EDF-1)130IQINLQRKMDevelopmentally-regu-O43854lated endothelial celllocus 1 protein)131KLIEKLDIKLElongation factor 2P13639(EF-2)132YLNEIKDSVElongation factor 2P13639(EF-2)133YLAEKYEWDVElongation factor 2P13639(EF-2)134VFEESQVAGTElongation factor 2P13639(EF-2)135DAQKEIVRAQKJ domain proteinQ9NX36C21orf55136DLEETVFTASJ domain proteinQ9NX36C21orf55137AMLEGGVDGLLEMILIN-3 precursorQ9NT22(EMILIN-5) (Elastin mi-crofibril interface-located protein 5)138RKADEKRIRSynaptotagmin-like pro-Q96C24tein 4 (Exophilin-2)139ALQEMVHQVEnhancer of filamenta-Q14511tion 1 (HEF1)140ILAINKPQNKEnhancer of filamenta-Q14511tion 1 (HEF1)141SMYGVDLHHABand 4.1-like protein 3Q9Y2J2(4.1B) (Differentiallyexpressed in adenocar-cinoma of the lung pro-tein 1) (DAL-1)142SEDITRYYLBand 4.1-like protein 3Q9Y2J2(4.1B) (Differentiallyexpressed in adenocar-cinoma of the lung pro-tein 1) (DAL-1)143NQQEQEDLEEpidermal growth factorP42566receptor substrate 15144SKEEDPENVEpidermal growth factorP42566receptor substrate 15145FLDKQGFYVEpidermal growth factorP42566receptor substrate 15(Protein Eps15) (AF-1pprotein)146TGALIYAIHAEpithelial membraneP54852protein 3 (EMP-3) (YMPprotein)147AVQVLMVLSLEpithelial membraneP54852protein 3 (EMP-3) (YMPprotein)148TLKEVEELEQLZyxin (Zyxin-2)Q15942149VLMTEDIKLEukaryotic translationQ04637initiation factor 4gamma 1150EEKKQKEMDEukaryotic translationQ04637initiation factor 4gamma 1151ELQALYALQALEukaryotic translationQ04637initiation factor 4gamma 1152WSNKYDPPLF-actin capping proteinP47756beta subunit153NLSDLIDLVF-actin capping proteinP47756beta subunit154FLSHKLDIKProtocadherin Fat 2Q9NYQ8precursor (hFat2) (Mul-tiple epidermal growthfactor-like domains 1)155VEPALRKPPProtocadherin Fat 2Q9NYQ8precursor (hFat2) (Mul-tiple epidermal growthfactor-like domains 1)156QVVYSLPDSAProtocadherin Fat 2Q9NYQ8precursor (hFat2) (Mul-tiple epidermal growthfactor-like domains 1)157EKISSYQLKProtocadherin Fat 2precursor (hFat2) (Mul-Q9NYQ8tiple epidermal growthfactor-like domains 1)158EMDPQKMPYLKIAA1752 proteinQ9C0B1159VTNRARASKDFc alpha/mu receptorQ8WWV6160SMNLTISAGPFc alpha/mu receptorQ8WWV6161VTYLQNGKGRLow affinity immuno-P08637globulin gamma Fc re-gion receptor III-Aprecursor (IgG Fc re-ceptor III-2)162ELLKTARSSKFYVE, RhoGEF and PH do-Q7Z6J4main-containing protein2 (Zinc finger FYVE do-main-containing protein4)163LKEYIQKLPFYVE, RhoGEF and PH do-Q7Z6J4main-containing protein2 (Zinc finger FYVE do-main-containing protein4)164YLNKLLITRFibroblast growth fac-Q8N441tor receptor-like 1precursor (FGF recep-tor-like protein 1)165IARPVGSSVRFibroblast growth fac-Q8N441tor receptor-like 1precursor (FGF recep-tor-like protein 1)166QCPVEGDPPPLFibroblast growth fac-Q8N441tor receptor-like 1precursor (FGF recep-tor-like protein 1)167TEDNVMKIAFibroblast growth fac-P22455tor receptor 4 precur-sor (EC 2.7.10.1)168YLLDVLERSFibroblast growth fac-P22455tor receptor 4 precur-sor (EC 2.7.10.1)169TASPDYLEIFibroblast growth fac-P21802tor receptor 2 precur-sor (EC 2.7.10.1)(FGFR-2)170TENNVMKIAFibroblast growth fac-P21802tor receptor 2 precur-sor (EC 2.7.10.1)(FGFR-2)171ETFKQIDMDNDFK506-binding protein 7Q9Y680precursor (EC 5.2.1.8)172GLLELIEEPGlomulin (FKBP-associa-Q92990ted protein) (FK506-binding protein-assoc-iated protein)173FVEEVIDNKGlomulin (FKBP-associa-Q92990ted protein) (FK506-binding protein-assoc-iated protein)174LQLYINKLDGlomulin (FKBP-associa-Q92990ted protein) (FK506-binding protein-assoc-iated protein)175EQSLETTKVFKSG73Q9BWW1176VFNDELPASIFlavin containing mono-Q53FW5oxygenase 3 isoform 2variant177SLFPGKLEVProtein flightless-1Q13045homolog178QKKLVDTIEGuanylate-binding pro-Q96PP9tein 4179DVGKDQEFTVFilamin-A (Alpha-P21333filamin) (Filamin-1)(Endothelial actin-binding protein)180YLLKDKGEYTLFilamin-A (Alpha-P21333filamin) (Filamin-1)(Endothelial actin-binding protein)181KTTDDIVKVFLJ10101 proteinQ8WU94182IEQERLERCDNA FLJ14503 fis,Q96T17clone NT2RM1000252,weakly similar to H.sapiens E- MAP-115 mRNA183KINSAPSSPIKE2F8 proteinQ5BKY4184NNDICLDEVHuman HypotheticalQ2VPJ3protein185VFAEVGCSPCHUMAN CDNA FLJ34154Q8NB70fis, clone FCBBF3013058186NIVETVLDLHypothetical proteinQ6ZUJ4FLJ43654 (Hypotheticalprotein C3orf62)187IYIDGVQEVFHUMAN CDNA FLJ46180Q6ZRQ5fis, clone TESTI4004031188KIMTEKELLAVFlotillin-2 (EpidermalQ14254surface antigen) (ESA)189VEAQEILRFlotillin-2 (EpidermalQ14254surface antigen) (ESA)190MLLDFIQHISerine/threonine-pro-Q13535tein kinase ATR (EC2.7.11.1) ( Ataxia tel-angiectasia and Rad3-related protein) (FRAP-related protein 1)191SLLESVQKLSerine/threonine-pro-Q13535tein kinase ATR (EC2.7.11.1) ( Ataxia tel-angiectasia and Rad3-related protein) (FRAP-related protein 1)192YLQPKLLGISerine/threonine-pro-Q13535tein kinase ATR (EC2.7.11.1) ( Ataxia tel-angiectasia and Rad3-related protein) (FRAP-related protein 1)193YLLVGTLFLLFrizzled 5 precursorQ13467(Frizzled-5)194MAAGDYPEAFrizzled 5 precursorQ13467(Frizzled-5)195LYLLVGTLFLFrizzled 5 precursorQ13467(Frizzled-5)196ALSDHHVYLFructose-bisphosphateP09972aldolase C (EC4.1.2.13)197YLAPHVRTLG protein pathway sup-Q53HS2pressor 1 isoform 1variant198YLQNWSHVLG protein pathway sup-Q53HS2pressor 1 isoform 1variant199FAALMLLGLVKiSS-1 receptor (KiSS-Q969F81R) (Kisspeptins recep-tor) (Metastin recep-tor) (G-protein coupledreceptor 54)200MINLAVFDLProbable G-proteinQ9Y2T6coupled receptor 55201EASALAVAPSAKProbable G-proteinQ9HC97coupled receptor 35202TFVLTIILVG-protein coupled re-Q9NQ84ceptor family C group 5member C precursor(Retinoic acid-inducedgene 3 protein)203FLLDFEEDLLeucine-rich repeat-O75473containing G-proteincoupled receptor 5 pre-cursor (Orphan G-pro-tein coupled receptorHG38) (G-proteincoupled receptor 49)(G-protein coupled re-ceptor 67)204FAMDSYGTSNProbable G-proteinQ6QNK2coupled receptor 133precursor (G-proteincoupled receptor PGR25)205MELSEPIVENG1 to S phase transi-P15170tion protein 1 homolog(GTP-binding proteinGST1- HS)206WLENALGKLGamma-aminobutyric-acidQ16445receptor alpha-6 sub-unit precursor (GABA(A)receptor)207KILEHDDVSYLGanglioside-inducedQ96MZ0differentiation-assoc-iated protein 1-like 1(GDAP1-L1)208SQQNTDNLVGap junction alpha-5P36382protein (Connexin-40)(Cx40)209SKLCEETPIGEM-interacting proteinQ9P107(GMIP)210QLVVELKDIGolgin subfamily BQ14789member 1 (Giantin)211VFDIFQFAKUDP-N-acetylhexosamineQ16222pyrophosphorylase(Antigen X)212NIANHFFTVUDP-N-acetylhexosamineQ16222pyrophosphorylase(Antigen X)213HLIHEVTKVNeutral alpha-glucosi-Q14697dase AB precursor (EC3.2.1.84)214FLDPNNIPKAProbable dolichyl pyro-Q9BVK2phosphateGlc1Man9GlcNAc2 alpha-1,3-glucosyltransferase(EC 2.4.1.-)215KINEAVECLLSLBifunctional aminoacyl-P07814tRNA synthetase [In-cludes: Glutamyl-tRNAsynthetase (EC6.1.1.17) (Glutamate--tRNA ligase); Prolyl-tRNA synthetase (EC6.1.1.15) (Proline--tRNA ligase)]216LLQTPKLLLGlycoprotein nmb-likeQ8IXJ5protein217VLLYSVVVVProlactin-releasingP49683peptide receptor (PrRPreceptor) (PrRPR) (G-protein coupled recep-tor 10)218KFKQCKLLQG protein-coupled re-Q5EGP2ceptor 112219DVLSTSSAISLG protein-coupled re-Q5EGP2ceptor 112220YIDDHSWTLGrowth factor receptor-Q14449bound protein 14 (GRB14adapter protein)221SLYEENNKLGRIP and coiled-coilQ8IWJ2domain-containing pro-tein 2 (Golgi coiledcoil protein GCC185)(CTCL tumor antigense1-1)222KLLEVQILEGRIP and coiled-coilQ8IWJ2domain-containing pro-tein 2 (Golgi coiledcoil protein GCC185)(CTCL tumor antigense1-1)223KPLLEQKELGRIP and coiled-coilQ8IWJ2domain-containing pro-tein 2 (Golgi coiledcoil protein GCC185)(CTCL tumor antigense1-1)224FPWELDPDWSGROS1-L proteinQ9HC86225YLSAAINPILGrowth hormone secreta-Q92847gogue receptor type 1(GHS-R)226QLSLADVILLGlutathione S-transfer-O15217ase A4-4 (EC 2.5.1.18)227QSFLVGNQLGlutathione S-transfer-O15217ase A4-4 (EC 2.5.1.18)228LKNKTKEAAEGTP-binding proteinQ96D21Rhes (Ras homolog en-riched in striatum)(Tumor endothelialmarker 2)229EDFHRKVYNIGTP-binding proteinQ96D21Rhes (Ras homolog en-riched in striatum)(Tumor endothelialmarker 2)230YIDDVFHALGTP-binding proteinQ92963Rit1 (Ras-like proteinexpressed in manytissues)231EQLAELRQEFVGFG2573Q6UY45232GLLERVKELHypothetical proteinQ53QU2HDLBP233DAILRIVGEHypothetical proteinQ53QU2HDLBP234RHKLVSDGQHeat shock protein 75Q12931kDa, mitochondrial pre-cursor (HSP 75) (Tumornecrosis factor type 1receptor-associatedprotein)235IQLVMKVIEHeat shock proteinQ53ZP9apg-1236MTREELVKNTumor rejection antigenQ5CAQ5(Gp96) 1237ALKDKIEKATumor rejection antigenQ5CAQ5(Gp96) 1238KIILRHLIEHeat-shock proteinQ12988beta-3 (HspB3) (Heatshock 17 kDa protein)239TLGKLFWVLow-density lipoproteinO75197receptor-related pro-tein S precursor240KGQGGAGGQFLRegulator of telomereQ9NZ71elongation helicase 1(EC 3.6.1.-) (Helicase-like protein NHL)241KEFLVVASVHematopoietic protein 1Q52LW0242KIAQKALDLHeme oxygenase 1 (ECP096011.14.99.3) (HO-1)243ITEPLPELQLHeparan sulfate gluco-Q8IZT8samine 3-O-sulfotrans-ferase 5 (EC 2.8.2.23)244KLRKEKEEFHepatocellular carcin-Q9NYH9oma-associated antigen66245EDVFPNILNMelanoma-associated an-Q8TD90tigen E2 (MAGE-E2 an-tigen) (Hepatocellularcarcinoma-associatedprotein 3)246IAVMLLEGGAN26S proteasome non-O75832ATPase regulatory sub-unit 10 (26S proteasomeregulatory subunit p28)247VDLFPGTFEVHepatocellular carcin-Q5JUU1oma-associated proteinp28-II Hephaestin248MVCGSPDIPLHECT domain and RCC1-O95714like domain-containingprotein 2 (HERC2)249DAPHSEGDMHLLHECT domain and RCC1-O95714like domain-containingprotein 2 (HERC2)250DTIEIITDRHeterogeneous nuclearP22626ribonucleoproteins A2/B1 (hnRNP A2/hnRNP B1)251RLFVGSIPKHeterogeneous nuclearO43390ribonucleoprotein R(hnRNP R)252FLSEYQHQPHEXIM1 protein (HMBA-O94992inducible)253LALMISMISADHistatin-1 precursorHis-(Histidine-rich proteintatin-11)precur-sor(Histi-dine-richprotein1)254RMLPHAPGVHistone deacetylase 1Q13547(HD1)255THNLLLNYGLHistone deacetylase 1Q13547(HD1)256SPNMNAVISLHistone deacetylase 9Q9UKV0(HD9) (HD7B) (HD7)257EFIDLLKKMHomeodomain-interactingQ9H2X6protein kinase 2 (EC2.7.11.1)258KMINHDSEKEDCullin-2 (CUL-2)Q13617259AVDEDRKMYLCullin-2 (CUL-2)Q13617260LFELLEKEISWI/SNF-related matrix-O60264associated actin-de-pendent regulator ofchromatin subfamily Amember 5 (EC 3.6.1.-)261FISEFEHRVHUMAN HSPC027 26S pro-Q9Y6E3teasome non-ATPaseregulatory subunit 13Synonyms 26S proteasomeregulatory subunit S1126S proteasome regula-tory subunit p40.5262AMFDHIPVGVHypothetical proteinQ9Y310(Novel protein HSPC117)(DJ149A16.6 protein)(Hypothetical proteinHSPC117)263WSFCLACVClaudin domain-contain-Q9NY35ing protein 1 (Membraneprotein GENX-3745)Q9NY35264NLLFPIIYLLarge neutral aminoQ9UHI5acids transporter smallsubunit 2 (L-type aminoacid transporter 2)(hLAT2)265SLLENLEKIHeterogeneous nuclearO60812ribonucleoprotein C-like 1 (hnRNP coreprotein C-like 1)266ILDQKINEVOrnithine decarboxylaseP11926(EC 4.1.1.17) (ODC)267DQINIETKNRegulator of nonsenseQ9HAU5transcripts 2 (NonsensemRNA reducing factor 2)(Up-frameshift suppres-sor 2 homolog) (hUpf2)268PFQNLLKEYRegulator of nonsenseQ9HAU5transcripts 2 (NonsensemRNA reducing factor 2)(Up-frameshift suppres-sor 2 homolog) (hUpf2)269LELELENLEIRegulator of nonsenseQ9HAU5transcripts 2 (NonsensemRNA reducing factor 2)(Up-frameshift suppres-sor 2 homolog) (hUpf2)270GLADASLLKKVATX10_HUMAN Ataxin-10Q9UBB4271GQILEAAVSVKIAA1833 proteinQ569G6272RVVSVSFRVHUMAN UDP-GalNAc:Q8NCR0betaGlcNAc beta 1,3-galactosaminyltransfer-ase, polypeptide 2(Beta 1,3-N-acetylgal-actosaminyltransferase-II) (MGC39558)273TQKRLDVYLHypothetical proteinQ2M389KIAA1033274AMLTVLHEIActivating signal coin-Q8N3C0tegrator 1 complex sub-unit 3 (EC 3.6.1.-)275ARLAALVQRDelta-interacting pro-Q15834tein A (Hepatitis deltaantigen-interactingprotein A) (Coiled-coildomain-containing pro-tein 85B)276FAVHFYRSHypothetical proteinQ96BP7FLJ14466277FNITYLDIDInterferon-inducibleO75569double stranded RNA-dependent proteinkinase activator A278GLAKRVWSLHypothetical proteinQ9BUH6C9orf142279HLDATKLLLTetratricopeptide re-Q96AE7peat protein 17280IGSFHGVLSLCDNA FLJ14058 fis,Q9H7Z0clone HEMBB1000554281ILDLIDDAWAnaphase promoting com-Q9BS18plex subunit 13282KLLEMVREDHypothetical proteinQ8IWA6CCDC60283LSYLPATVEPSphingosine kinase 2Q9NRA0(EC 2.7.1.-)284QLAQFVHEVProbable ATP-dependentQ96FC9RNA helicase DDX11 (EC3.6.1.-) (DEAD/H boxprotein 11) (CHL1 homo-log) (Keratinocytegrowth factor-regulatedgene 2 protein) (KRG-2)285SYDESDEEEProtein KIAA0182Q14687286SYSDEFGPSRas GTPase-activatingQ96PV0protein SynGAP (Synap-tic Ras-GTPase-activat-ing protein 1) (Synap-tic Ras-GAP 1) (Neuro-nal RasGAP)287TVERADSSHLSIFibrinogen C domainQ8N539containing 1288VTENELAVITMGC39581 proteinQ86XM0289VTYLEDYSABcl-2-like 13 proteinQ9BXK5(Mill protein)(Bcl-rambo)290YLLEKTRVAMyosin head domain con-Q96H55taining 1291TLKILDLMEWD-repeat protein 51AQ8NBT0292EDLIKELIKKIF27AQ86VH2(OTTHUMP00000021559)293LSLENLEKIInositol polyphosphate-Q2T9J45-phosphatase F,isoform 1294FLNKAADFIEMyopalladinQ96KF5295GLDIDGIYRVRho GTPase activatingQ5T2Y2protein 12296QNNNLQTQIHypothetical proteinQ7Z3C5DKFZp686D0630297FLDDVVHSLJumonji domain-contain-Q15652ing protein 1C (Thyroidreceptor-interactingprotein 8) (TRIP-8)298NMVDLNDYCoatomer subunit betaP53618(Beta-coat protein)(Beta-COP)299YLLKEDMAGIFLJ10462 fis, cloneQ9NVW8NT2RP1001494, weaklysimilar to MALESTERILITY PROTEIN 2300KLFEKVKEVFLJ10462 fis, cloneQ9NVW8NT2RP1001494, weaklysimilar to MALESTERILITY PROTEIN 2301TVMDEIHTVCell-cycle and apopto-Q6X935sis regulatoryprotein 1302KLISELQKLTelomere-associatedQ5UIP0protein RIF1 (Rap1-in-teracting factor 1 hom-olog)303KVIDEIYRVF-box only protein 28Q9NVF7304SSLSDGLLLECDNA FLJ10901 fis,Q9NV65clone NT2RP5003524305EEIVKVTFEAcetoacetyl-CoA synthe-Q86V21tase (EC 6.2.1.16)306ELLENIIKNPutative cell cycleQ9NXZ0control protein (DEPdomain containing 1)307ELLSLVQNLSynaptopodin 2-likeQ68A20308PQQERDFYCDNA FLJ36560 fis,Q8N9T8clone TRACH2009340309GRGGKDPPLEPCDNA FLJ13330 fis,Q9H8Q0clone OVARC1001802310LADISLHDPVATP-dependent RNA heli-Q9H8H2case DDX31 (EC 3.6.1.-)(DEAD box protein 31)(Helicain)311PSNMGIAIPLProtein C14orf161Q9H7T0312FMMPQSLGVCysteine protease ATG4BQ9Y4P1(EC 3.4.22.-) (Auto-phagy-related protein4 homolog B)313IMVATAVVAICDNA FLJ14526 fis,Q96T08clone NT2RM1001139314MTKRYEALEHypothetical proteinQ9BR77CCDC77 (CDNA FLJ14732fis, cloneNT2RP3001969, weaklysimilar toTRICHOHYALIN)315SLDAKEIYLCDNA FLJ14790 fis,Q96K38clone NT2RP4000973,weakly similar toPROBABLE PROTEIN DI-SULFIDE ISOMERASE P5(EC 5.3.4.1)316QLLDIKTRLKeratin 24Q2M215317FLTDYLNDLBCoR protein (BCL-6Q6W2J9corepressor)318ANQGGFENGEHypothetical proteinQ61Q21FLJ20582319ILGLLLLHLEHypothetical proteinQ9BT04FLJ22688320VYQKEGVLASHypothetical proteinQ9H5W3FLJ22944321YLNDFTHEIZinc finger protein,Q8TBE5subfamily 1 A, 5-322SPPLQGEISLeucine-rich repeatsQ8IW35and IQ motif containing2323LFFEPVTTPHypothetical proteinQ8TEA0FLJ23749http://www.expasy.org/spr324WISVPVVTHypothetical proteinot/userFLJ25336man.html-AC —lineQ96LP1325NMEIMPEGSLHypothetical proteinQ8N7G6FLJ25660326QDQLSALQLCDNA FLJ30058 fis,Q96NU6clone ADRGL2000074,weakly similar toRHO-GIPASE- ACTIVATINGPROTEIN 6327MEADPDLSRCDNA FLJ30106 fis,Q96A82clone BNGH41000190,weakly similar toRattus norvegicusschlafen-4 (SLFN-4) mRNA.328LYLPATTPYWhirlinQ9P202329SEIEKNKKVCDNA FLJ31846 fis,Q96MV0clone NT2RP7000425,weakly similar toMYOSIN HEAVY CHAIN,NONMUSCLE TYPE B330SLVQIVTTLFLJ32833 fis, cloneQ96M43TESTI2003228331KILDIRKNVGuanine nucleotide-P38405binding proteinG(olf), alpha subunit(Adenylate cyclase-stimulating G alphaprotein, olfactorytype)332QSLELLLLPVCDNA FLJ33811 fis,Q8N279clone CTONG2002095333ALLNNIIEITransmembrane proteinQ9BYT916C334FNQSSSLIIHZinc finger protein 31P17040(Zinc finger proteinKOX29) (Zinc finger andSCAN domain-containingprotein 20) (Zincfinger protein 360)335LSLSALPVSYTransmembrane 6Q9BZW4superfamily member 2336YLDLTPNQECDNA FLJ90251 fis,Q8NCH3clone NT2RM4000115337YLFERIKELCDNA FLJ90251 fis,Q8NCH3clone NT2RM4000115338FILDVLLPEACDNA FLJ90760 fis,Q8N2I4clone THYRO1000061339EFIPEFEKTubulin--tyrosineQ14166ligase-like protein 12340DVFPATPGSQNKIAA0303 proteinO15021341FIFDVHVHEVPlexin-B2 precursorO15031(MM1)342ILEVTNNLEZinc finger and BTBO15062domain-containingprotein 5343ILSKKDLPLCentrosome-associatedQ8WY20protein 350344HEPPKAVDKpiccolo (Aczonin)Q9Y6V0345ILDDSHLLVKIAA0560 proteinO60306346YLDNVVNKQKIAA0676 proteinQ96H49347KLLPYVGLLQHuman homolog of MusQ810B7SLIT and NTRK-likeprotein 5 precursor348QLKSLIQIDHuman homolog of MusQ810B7SLIT and NTRK-likeprotein 5 precursor349SLLNNPLSINischarinQ6PIB4350SSLSDALVLEFERM domain-containingQ9P2Q2protein 4A351DELQQLFNLLeucine-rich repeatsQ6UXK5neuronal protein 1 pre-cursor (Neuronal leu-cine-rich repeat pro-tein 1) (NLRR-1)352QILSGRKPELKIAA1512 proteinQ9P216353KLVEVIEEVKIAA1598 proteinQ9HCH4354QTLLKNPLYhosphatidylinositol-3Q96QU2phosphate 3-phosphataseadaptor subunit355SLLDDLHSAKIAA1730 proteinQ9C0D3356HILDSSIYSKIAA1786 proteinQ96JN9357QSSPPPPPPSHypothetical proteinQ96EK3MGC20470358LMCYAIMVTOACT1 proteinQ86XC2359FLSEEGGHVAV6-phosphofructo-2-ki-Q16877nase/fructose-2,6-bi-phosphatase 4 (6PF-2-K/Fru-2,6-P2ASE testis-type isozyme)360SPDQELVLLIkappaB kinase complex-O95163associated protein (IKKcomplex-associated pro-tein) (p150)361FLLVVLLKLImmune receptor ex-Q7Z7I3pressed on myeloidcells 2362QIIEANYHSHigh-affinity cAMP-O60658specific and IBMX-in-sensitive 3,5-cyclicphosphodiesterase 8A(EC 3.1.4.17)363ILIDKSGKLELBone specific CMF608Q6WRI0364TVMDSKIVQVImportin alpha-7 sub-O60684unit (Karyopherinalpha-6)365VMDSKIVQVImportin alpha-7 sub-O60684unit (Karyopherinalpha-6)366YQDPLDPTRSVInaD-like proteinQ8NI35(Inadl protein)(hINADL) (Pals1-assoc-iated tight junctionprotein) (Protein as-sociated to tightjunctions)367HEFLTPRLInaD-like proteinQ8NI35(Inadl protein)(hINADL) (Pals1-assoc-iated tight junctionprotein) (Protein as-sociated to tightjunctions)368GLFPWTPKLInaD-like proteinQ8NI35(Inadl protein)(hINADL) (Pals1-assoc-iated tight junctionprotein) (Protein as-sociated to tightjunctions)369CDVQRYNINitric oxide synthase,P35228inducible (EC1.14.13.39)370NMYGKVVTVTranscription elonga-O00267tion factor SPT5(hSPT5)371QNVQVNQKVInositol-trisphosphateP279873-kinase B (EC2.7.1.127) (Inositol1,4,5-trisphosphate 3-kinase B)372SLINQMTQVType I inositol-3,4-Q96PE3bisphosphate 4-phospha-tase (EC 3.1.3.66)(Inositol polyphosphate4-phosphatase type I)373NVTVAVPTVInsulin receptor betaQ9UCB7subunit374LGLENLCHLInsulin-like growthQ8TAY0factor binding protein,acid labile subunit375YYEKLHTYFIntegrin beta-4 precur-P16144sor (GP150) (CD104antigen)376LLAALLLDPSplice isoform 2 ofP35462-2P35462377RRDFGFPQInterferon alpha 2Q16055protein378SLLGFVYKLInterferon-induced pro-P09914tein with tetratrico-peptide repeats 1(IFIT-1)) (Interferon-induced 56 kDa protein)(IFI-56K)379LDRVFKNYInterleukin-20 precur-Q9NYY1sor (IL-20) (Four alphahelix cytokine Zcyto10)380LMVDHVTEVSteroid receptor RNAQ9HD15activator isoform 1381KMDQQEFSIIntersectin-2 (SH3 do-Q9NZM3main-containing protein1B) (SH3P18) (SH3P18-like WASP-associatedprotein)382SLLLLPEELITI-like protein (In-Q6UXX5ter-alpha (Globulin)inhibitor H5-like)383SQQNTDNLVGap junction alpha-5P36382protein (Connexin-40)384WLDETLAQVKelch-like protein 8Q9P2G9385VNLGGSKSISISKeratin, type II cyto-P04264skeletal 1 (Cytokera-tin-1)386ANYLDSMYIADAM 9 precursor (ECQ134433.4.24.-) (A disinte-grin and metallopro-teinase domain 9) (Met-alloprotease/disinte-grin/cysteine-rich pro-tein 9) (Myeloma cellmetalloproteinase)387HLWNSIHGLNext to BRCA1 gene 1Q14596protein (Neighbor ofBRCA1 gene 1 protein)(Membrane component,chromosome 17, surfacemarker 2) (1A1-3B)388SLADLMPRVHypothetical proteinQ6MZZ8DKFZp686K2075389IDLSASLVLNKIAA0100 proteinQ14667390HLTYLNVYLPre-mRNA-splicing fac-Q92620tor ATP-dependent RNAhelicase PRP16 (EC3.6.1.-) (ATP-dependentRNA helicase DHX38)(DEAH box protein 38)391QLVACIESKLKIAA0251 proteinQ8TBS5392EGKLVVQDIEHUMAN KIAA0342 proteinO15050393QALEAGAVVLIKIAA0357 proteinO15064394VLSCSQALKIHypothetical proteinQ6PGP7KIAA0372395LSIEGEQELKIAA0377 splice variantQ86TE72396EFQDLNQEVKIAA0386 proteinQ9Y4F9397RTKLTDIQIHUMAN CTCL tumor anti-Q548S1gen HD-CL-04398RECKYDLPPImportin-13 (Imp13)O94829(Ran-binding protein13)399QLTKIQTELKIAA0769 proteinO94868400LVNAAQSVFVHypothetical proteinQ61Q32KIAA0863401VKAEDKARVZinc finger proteinQ96KM6KIAA1196-402VLHDRIVSVCRSP complex subunit 3Q9ULK4(Cofactor required forSp1 transcriptionalactivation subunit 3)(Transcriptional co-activator CRSP130)(Vitamin D3 receptor-interacting proteincomplex403RNSIATLQGGR130 kDa componentQ9P2J9[Pyruvate dehydrogenase[lipoamide]]-phospha-tase 2, mitochondrialprecursor (EC 3.1.3.43)404TVNILIVDQNProtocadherin-10Q9P2E7precursor405YLFDLPLKVLeucine-rich repeatsQ5VUJ6and calponin homology(CH) domain containing2406NLAKDNEVLAnkyrin repeat domainQ5W0G218B407SGDKLKLDQTKin17 protein (HsKin17O60870protein) (KIN, antigen-ic determinant of recAprotein homolog)408KLTDYQVTLKinesin-like proteinQ9H1H9KIF13A (Kinesin-likeprotein RBKIN)409KIQEILTQVPutative RNA bindingO00425protein KOC410YLDEQIKKVHUMAN Kinesin-like pro-Q9H1H9tein KIF13A (Kinesin-like protein RBKIN)411SSIWEVDSLHHUMAN Kinesin-like pro-Q9H1H9tein KIF13A (Kinesin-like protein RBKIN)412RLASYLDRVKeratin, type I cyto-P05783skeletal 18(Cytokeratin-18)413ALLNIKVKLKeratin, type I cyto-P05783skeletal 18(Cytokeratin-18)414FNIVKNKTEKv3.2d voltage-gatedQ86W09potassium channel415KAITAPVSLLethal(3)malignantQ9Y468brain tumor-like pro-tein (L(3)mbt-like)(L(3)mbt proteinhomolog)416HEYLKAFKVLactadherin precursorQ08431(Milk fat globule-EGFfactor 8) (MFG-E8)(HMFG) (Breast epithe-lial antigen BA46)(MFGM)417LKAFKVAYSLactadherin precursorQ08431(Milk fat globule-EGFfactor 8) (MFG-E8)(HMFG) (Breast epithe-lial antigen BA46)(MFGM)418RLAVYIDRVLamin-A/C (70 kDaP02545lamin)419YLLGNSSPRTLamin-A/C (70 kDaP02545lamin)420EMKVSDLDRLaminin gamma-1 chainP11047precursor (Laminin B2chain)421VRLVDAGGVKLLow-density lipoproteinO75197receptor-related pro-ein 5 precursor422KPETFEHLFLeptin receptor precur-P48357sor (LEP-R) (OBreceptor)423EITDDGNLKLeptin receptor precur-P48357sor (LEP-R) (OBreceptor)424ECHHRYAELLeptin receptor precur-P48357sor (LEP-R) (OBreceptor)425PSTCPDGFKIMitogen-activated pro-O43283tein kinase kinase ki-nase 13 (EC 2.7.11.25)426RKGIIDVNLLeukemia virus receptorQ083572427LIQERDVKKLeukemia-associatedQ8NFU7protein with a CXXCdomain428LTLEQVVAIELeukemia-associatedQ8NFU7protein with a CXXCdomain429RDTPHSDFRGRNA-binding protein 6P78332(RNA-binding motif pro-tein 6) (RNA-bindingprotein DEF-3) (Lungcancer antigen NY-LU-12)430HRVLLHLFLung cancer oncogene 5Q7Z5Q7431LLFDRPMHVHeterogeneous nuclearP52272ribonucleoprotein M(hnRNP M)432FLSELTQQLMacrophage migrationP14174inhibitory factor (MIF)(Phenylpyruvate tauto-merase) (EC 5.3.2.1)433SLLSHVEQLMitotic spindle assem-Q9UI95bly checkpoint proteinMAD2B (MAD2-like 2)(hREV7)434KLILRLHKLMitogen-activated pro-Q9Y6R4tein kinase kinase ki-nase 4 (EC 2.7.11.25)(MAPK/ERK kinase kinase4)435RLTHHPVYISerine/threonine/tyro-Q9Y6J8sine-interacting-likeprotein 1 (Dual-speci-ficity protein phospha-tase 24) (Map kinasephosphatase-like pro-tein MK-STYX)436QDNLEKLLQMicrotubule-associatedQ6P0Q8serine/threonine-pro-tein kinase 2 (EC2.7.11.1)437MKRLLLLFMatrix metalloproteaseQ9H306MMP-27438DPQDILEVKMCM10 proteinQ7L590439FLFGEVHKAMCM10 proteinQ7L590440KVIVLVNKVLLInterferon-induced hel-Q9BYX4icase C domain-contain-ing protein 1 (EC3.6.1.-) (Melanoma dif-ferentiation-associatedprotein 5)441QILSLEEKIMelanoma ubiquitousQ2TAK8mutated protein442MLKDIIKEYMelanoma antigen familyQ5BJF3D, 2443KTWGQYWQVMelanocyte protein PmelP4096717 precursor (Melano-cyte lineage-specificantigen GP100)444LLDGTATLRLMelanocyte protein PmelP4096717 precursor (Melano-cyte lineage-specificantigen GP100)445VLKEIVERVGPI-anchored proteinQ14444p137 (p137GPI) (Mem-brane component chromo-some 11 surface marker1) Cytoplasmic activa-tion/proliferation-associated protein 1446SLLDEFYKLGPI-anchored proteinQ14444p137 (p137GPI) (Mem-brane component chromo-some 11 surface marker1) Cytoplasmic activa-tion/proliferation-associated protein 1447TLNQNGYTLVHepatocyte growth fac-P08581tor receptor precursor(EC 2.7.10.1) (HGF re-ceptor) (Scatter factorreceptor) (SF receptor)(HGF/SF receptor) (Metproto-oncogene tyrosinekinase)448QMPKMNFANMitogen-activated pro-Q16539tein kinase 14 (EC2.7.11.24)449KLADFGVSGEMitogen-activated pro-Q12851tein kinase kinase ki-nase kinase 2 (EC2.7.11.1) (MAPK/ERKkinase kinase kinase 2)450SIKDYEQANMitotic kinesin-relatedQ96Q89protein451EDLMEDEDLMitotic kinesin-relatedQ96Q89protein452VLISKELISLSperm-associated anti-Q96R06gen 5 (Astrin) (Mitoticspindle-associated pro-tein p126)453LIEKVQEARMyeloid/lymphoid orQ9UMN6mixed-lineage leukemiaprotein 4 (Trithoraxhomolog 2)454SRVRMKTPTMyeloid/lymphoid orQ9UMN6mixed-lineage leukemiaprotein 4 (Trithoraxhomolog 2)455GLDDIKDLKVPutative helicase MOV-Q9HCE110 (EC 3.6.1.-) (Molo-ney leukemia virus 10protein)456VLAETLTQVMOZ/CBP proteinQ712H6457DTNADKQLSCalgranulin B (Migra-P06702tion inhibitory factor-related protein 14)(MRP-14) (P14)458GRWVCKDLPCPMUC2_HUMAN Mucin-2 pre-Q02817cursor (Intestinalmucin 2)459FGNMQKINQMUC2_HUMAN Mucin-2 pre-Q02817cursor (Intestinalmucin 2)460FPNWTLAQVMucin-5B precursorQ9HC84(Mucin 5 subtype B,tracheobronchial)461ATPSSTPETVMucin-5B precursorQ9HC84(Mucin 5 subtype B,tracheobronchial)462FVNDVNLENMultiple PDZ domainO75970protein (Multi PDZ do-main protein 1) (Multi-PDZ-domain protein 1)463SENKLILMKRUFY2 (Run and FYVE do-Q81W33main-containing proteinRabip4464TFCVQPGEKVMultidrug resistance-Q8NHX7associated protein 7465YLNDGLWHMMultiple copies in aQ9ULC4T-cell malignancies(Malignant T cell am-plified sequence 1)(MCT1)466GTTLRNLEIDNA mismatch repairP20585protein Msh3467SPPTLNGAPSPProtein CBFA2T2 (MTG8-O43439like protein) (MTG8-related protein 1)(Myeloid translocation-related protein 1)468NEAAIKNVYLMyomesin-1 (190 kDaP52179titin-associated pro-tein) (190 kDa connec-tin-associated protein469FIDFGMDLQMyosin heavy chain,P12883cardiac muscle betaisoform (MyHC-beta)470LLEAKVKELMyosin-13 (Myosin heavyQ9UKX3chain, skeletal muscle,extraocular) (MyHC-eo)471LLAEKVEQLTumor suppressor candi-Q13454date 3 (N33 protein)472LANARGLGLQNebulin-related anchor-Q8TCH0ing protein473VNRIGQESLENeural cell adhesionP13592molecule 1, 1474YLEIQGITRNeurotrimin precursorQ9P121475EALENNKELNineinQ8N4C6476NSMVVERQQLNineinQ8N4C6477HLLERVDQVNineinQ8N4C6478PERTQLLYLNotch homolog 2QSVTD0479NGGTCEDGINNeurogenic locus notchP46531homolog protein 1 pre-cursor (Notch 1) (hN1)(Translocation-associa-ted notch protein TAN-1) [Contains: Notch 1extracellular trunca-tion; Notch 1 intracel-lular domain]480QSAADYLGALNeurogenic locus notchQ9UM47homolog protein 3 pre-cursor (Notch 3) [Con-tains: Notch 3 extra-cellular truncation;Notch 3 intracellulardomain]481ALLVVLSPPALNeurogenic locus notchQ99466homolog protein 4 pre-cursor (Notch 4)(hNotch4) [Contains:Notch 4 extracellulartruncation; Notch 4intracellular domain]-482LRLDXLFKLPlexin-A1 precursorQ9UIW2(Semaphorin receptorNOV)483WLIEDGKVVHUMAN NPD011Q9H2R7484SQPQEPENKNuclear autoantigen Sp-P23497100 (Speckled 100 kDa)(Nuclear dot-associatedSp100 protein)485LLREKVEFLNuclear factor eryth-Q14494roid 2-related factor 1(NF-E2-related factor1) (NFE2-related factor1) (Nuclear factor,erythroid derived 2,like 1) (Transcriptionfactor 11) (Transcrip-tion factor HBZ17)(Transcription factorLCR-F1) (Locus controlregion-factor 1)486YLDDVNEIINuclear factor of acti-O95644vated T-cells, cyto-plasmic 1 (NFAT trans-cription complex cyto-solic component) (NF-ATc1)487ALLDQLYLANuclear receptor co-Q15596activator 2 (NCoA-2)(Transcriptional in-termediary factor 2)488TLFDYEVRLUbiquitin-like PHD andQ96T88RING finger domain-con-taining protein 1 (EC6.3.2.-)489SILKVVINNNucleic acid helicaseQ8IWW2DDXx490LLYGGDLHSANucleic acid helicaseQ8IWW2DDXx491KLAENIDAQLNucleoporin 62 kDaQ6GTM2(NUP62 protein)492SLLTDEEDVDNuclear pore complexP52948protein Nup98-Nup96precursor [Contains:Nuclear pore complexprotein Nup98 (Nucleo-porin Nup98) (98 kDanucleoporin);493VDITQEPVLNuclear pore complexP52948protein Nup98-Nup96precursor [Contains:Nuclear pore complexprotein Nup98 (Nucleo-porin Nup98) (98 kDanucleoporin);494QLEKKLMENucleoprotein TPRP12270495GLDPLGYEIQNuclear pore complexP57740protein Nup107496ALLDRIVSVNuclear pore complexQ92621protein Nup205497KILDLETQLODF2 proteinQ6PJQ8498VTWLKETEVTrophoblast glycopro-Q6PJQ8tein precursor (5T4oncofetal trophoblastglycoprotein)499VDLPGVINTVDynamin-like 120 kDaO60313protein, mitochondrialprecursor (Opticatrophy 1 gene protein)500TITCLPATLVOrexin receptor type 2O43614(Ox2r) (Hypocretinreceptor type 2)501LLGPRLVLATransmembrane emp24 do-P49755main-containing protein10 precursor (Transmem-brane protein Tmp21)502LTTPDAAGVNQOrphan nuclear receptorP13056TR2 (Testicularreceptor 2)503FLDGHDLQLMKL/myocardin-like pro-Q969V6tein 1 (Myocardin-re-lated transcriptionfactor A) (MRTF-A)(Megakaryoblasticleukemia 1 protein)(Megacaryocytic acuteleukemia protein)504KTTEVLDASAOvarian cancer relatedQ8WXI7tumor marker CA125-505TSPTVPWTTSIFOvarian cancer relatedQ8WXI7tumor marker CA125-506WTITDTTEHOvarian cancer relatedQ8WXI7tumor marker CA125-507TITNLQYGEOvarian cancer relatedQ8WXI7tumor marker CA125-508ARLTFLNRGOxysterol-binding pro-Q9BZF1tein-related protein 8(OSBP-related protein8)509KIDALSSEKLCentrosomal protein ofQ8NHQ170 kDa (Cep70 protein)(p10-binding protein)510LLAEAVLTYLLeucine carboxylO60294methyltransferase 2 (EC2.1.1.-) (p21WAF1/CIP1promoter-interactingprotein)511SLFEKGLKNVF-box/LRR-repeat pro-Q9UKA1tein 5 (F-box and leu-cine-rich repeat pro-tein 5) (F-box proteinFBL4/FBL5)512LDTPSQPVNNInhibitor of growthQ9NXR8protein 3513VLDELKNMKCP53 inducible proteinQ9UN29514PQDYPDKKSLPDNA polymerase alphaP09884catalytic subunit (EC2.7.7.7)515NLLPKLHIVChloride intracellularQ9Y696channel protein 4 (In-tracellular chlorideion channel proteinp64H1516LAAAGGPGQGWAPaired mesoderm homeo-Q99453box protein 2B (Paired-like homeobox 2B)(PHOX2B homeodomainprotein) (NeuroblastomaPhox)517GTPPPPGKPEPRB3 proteinP81489518SQGAVGLAGVProtein patched homologQ136351 (PTC1) (PTC)519ELKKINYQVProtein patched homologQ136351 (PTC1) (PTC)520KLFQDLQDLRap guanine nucleotideQ9Y4G8exchange factor 2(Neural RAP guanine nu-cleotide exchange pro-tein) (nRap GEP) (PDZdomain-containing gua-nine nucleotide ex-change factor 1) (PDZ-GEF1)521EAIVSHEKNPecanex-like protein 1Q96RV3(Pecanex homolog)522GLLPQVNTFVPecanex-like protein 1Q96RV3(Pecanex homolog)-523KAYDVERELGC-1-related estrogenQ8TDE4receptor alpha coacti-vator short isoform524DVLESWLDFPHD fingerQ86U89525TMLVLVIRGHypothetical proteinQ6N038DKFZp686C07187526DVAQLQALLQPhosphatidylinositol-P423384,5-bisphosphate 3-ki-nase catalytic subunitbeta isoform (EC2.7.1.153) (P13-kinasep110 subunit beta)(PtdIns-3-kinase p110)527QIIEANYHSPhosphodiesterase 8A,Q6P9H3isoform 1528YVTDVLYRVSerine/threonine-pro-Q96Q15tein kinase SMG1 (EC2.7.11.1) (SMG-1)(hSMG-1) (Lambda/iotaprotein kinase C-in-teracting protein)(Lambda-interactingprotein) (529FLDDEVIELPiggyBac transposableQ8N328element derived 3530VICILPNDDKPIWIL3 proteinQ7Z3Z3531IQNSQLQLQHomeobox protein PKNOX1P55347(PBX/knotted homeobox1)532FAYLLTYMATransmembrane proteinQ12893115 (Protein PL6)533GLIDSLVHYVPlakophilin-2Q99959534REDHPARPPlectin 6Q6S380535FLLDPVKGERLPlectin 1 (PLTN) (PCN)Q15149(Hemidesmosomal protein1) (HD1)536RGQNLDVVQPlexin B1; plexin 5;O43157semaphorin receptor537SLTGHISTVPleiotropic regulator 1O43660538EPLRVPPDLBlood vessel epicardialQ8NE79substance (hBVES) (Pop-eye domain-containingprotein 1) (Popeyeprotein 1)539EIPVLNELPVCarboxypeptidase-likeQ8N436protein X2 precursor540LYIPAMAFIYIF1B proteinYIF1Bprotein541SLLQHLIGLMelanoma antigen pre-P78395ferentially expressedin tumors (Pr4eferen-tially expressed anti-gen of melanoma) (OPA-interacting protein 4)542ISSMLVLFFSplice isoform 2 ofQ9H7F0-2Q9H7F0543ENHSSQTDNIP2Y purinoceptor 13Q9BPV8(P2Y13) (G-proteincoupled receptor 86)(G-protein coupledreceptor 94)544ILMGVLKEVPutative pre-mRNA-O43143splicing factor ATP-dependent RNA helicaseDHX15 (EC 3.6.1.-)(DEAH box protein 15)(ATP-dependent RNAhelicase #46)545VLFENTDSVHLHUMAN RNA-binding pro-P42696tein 34 (RNA-bindingmotif protein 34)546INMRIQDLProlyl 4-hydroxylaseP13674alpha-1 subunit precur-sor (EC 1.14.11.2) (4-PH alpha-1) (Procolla-gen-proline,2-oxoglu-tarate-4-dioxygenasealpha-1 subunit)547KTDKTLVLLProfilin-1P07737548GLIEILKKVProgrammed cell deathO14737protein 5 (TFAR19 pro-tein) (IF-1 cell apop-tosis-related gene 19protein)549NMVDIIHSVPropionyl-CoA carboxy-P05166lase beta chain, mito-chondrial precursor (EC6.4.1.3)550ILDAGGHNVTI26S proteasome non-Q99460ATPase regulatory sub-unit 1 (26S proteasomeregulatory subunitRPN2) (26S proteasomeregulatory subunit S1)(26S proteasome subunitp1112)551YMNLEKPDFI26S proteasome non-Q99460ATPase regulatory sub-unit 1 (26S proteasomeregulatory subunitRPN2) (26S proteasomeregulatory subunit S1)(26S proteasome subunitp112)552SLADIAQKL26S proteasome non-O43242ATPase regulatory sub-unit 3 (26S proteasomeregulatory subunitS3) (Proteasome subunitp58)553QLVDIIEKVProteasome activatorP61289complex subunit 3 (Pro-teasome activator 28-gamma subunit)(PA28gamma) (PA28g)(Activator of multi-catalytic protease sub-unit 3) (11S regulatorcomplex gamma subunit)(REG-gamma) (Ki nuclearautoantigen)554SLLKVDQEVProteasome activatorP61289complex subunit 3 (Pro-teasome activator 28-gamma subunit)(PA28gamma) (PA28g)(Activator of multi-catalytic protease sub-unit 3) (11S regulatorcomplex gamma subunit)(REG-gamma) (Ki nuclearautoantigen)555QILRLLHIEProtein C14orf166Q9Y224556EMGGGENNLKProtein KIAA1219Q86X10557NLAEKLIGVProtein KIAA1219Q86X10558EKSVSVQTNLProtein KIAA1688Q9COH5559GLLDSLTGILNProtein Plunc precursorQ9NP55(Palate lung and nasalepithelium clone pro-tein) (Lung-specificprotein X) (Nasopharyn-geal carcinoma-relatedprotein) (Tracheal epi-thelium-enriched pro-tein) (Secretory pro-tein in upper respira-tory tracts)560SLLPPDALVGLProtein transport pro-Q15437tein Sec23B561LEEKNTLIQELLiprin-alpha-2 (ProteinO75334tyrosine phosphatasereceptor type f poly-peptide-interactingprotein alpha-2)(PTPRF-interactingprotein alpha-2)562LLSESNERLLiprin-alpha-2 (ProteinO75334tyrosine phosphatasereceptor type f poly-peptide-interactingprotein alpha-2)(PTPRF-interactingprotein alpha-2)563LADLGSLESPProtocadherin gamma A12O60330precursor (PCDH-gamma-A12) (Cadherin-21)(Fibroblast cadherin 3)564QLLKFQLNKProtocadherin gamma A10Q9Y5H3precursor (PCDH-gamma-A10)565LLAEAVLTYLLeucine carboxylO60294methyltransferase 2(EC 2.1.1.-) (p21WAF1/CIP1 promoter-interact-ing protein)566QLLREPHLQKIAA1636 proteinQ9HCD6567TIPNLEQIEProbable G-proteinQ9UJ42coupled receptor 160568KLWEAESKLProtein C21orf45Q9NYP9569IFHLHELPEPeriodic tryptophanQ15269protein 2 homolog570KLFNDAIRLRab-like protein 2BQ9UNT1571FENQEVQAICell cycle checkpointO75943protein RAD17 (hRad17)(RF-C/activator 1homolog)572EYVEKFYRIDNA repair proteinQ92878RAD50 (EC 3.6.-.-)(hRAD50)573QIDEIRDKDNA repair proteinQ92878RAD50 (EC 3.6.-.-)(hRAD50)574FLHEKLESLRas GTPase-activatingP20936protein 1 (GTPase-acti-vating protein) (GAP)(Ras p21 protein acti-vator) (p120GAP)(RasGAP)575FELNNELKMRas guanine nucleotideQ9UK56exchange factor 2576LLSNNNQALRas-GTPase-activatingQ13283protein-binding protein1 (EC 3.6.1.-) (ATP-dependent DNA helicaseVIII) (GAP SH3-domain-binding protein 1)(G3BP-1) (HDH-VIII)577VLCGNKSDLERas-related proteinP51159Rab-27A (Rab-27) (GTP-binding protein Ram)578LLMYDIANRas-related proteinO95716Rab-3D579SQVNILSKIVSRNuclear pore complexP57740protein Nup107 (Nucleo-porin Nup107) (107 kDanucleoporin)580VMFNGKVYLReceptor-interactingQ86XS4factor 1581LEVEVIEARRegulating synapticQ9UJD0membrane exocytosisprotein 3 (Nim3) (Rab-3interacting molecule 3)(RIM 3) (RIM3 gamma)582TLLRGIEWRegulator of G proteinQ86UV0signaling protein (Reg-ulator of G-proteinsignalling like 1)583PDFTELDLQMHC class II regulatoryP22670factor RFX1 (RFX) (En-hancer factor C) (EF-C)584DVLFALFSKLRetinoblastoma-associa-P06400ted protein (PP110)(P105-RB)585RSGERKAVQARoundabout homolog 3Q96MS0precursor (Roundabout-like protein 3)586GLNEEIARVRetinoblastoma-associa-O14777ted protein HEC (Kine-tochore associated 2)587FLFQEPRSIRetinoblastoma-associa-Q9UK61ted protein RAP140588FLFQEPRSIVTRetinoblastoma-associa-Q9UK61ted protein RAP140589KEVDILNLPAT-rich interactive do-P29374main-containing protein4A (ARID domain-con-taining protein 4A)(Retinoblastoma-bindingprotein 1)590YKLPMEDLKJumonji/ARID domain-P29375containing protein 1A(Retinoblastoma-bindingprotein 2) (RBBP-2)591TMVDRIEEVJumonji/ARID domain-P29375containing protein 1A(Retinoblastoma-bindingprotein 2) (RBBP-2)592VEGLLTLSDFDLRhoGTPase regulatingQ6RJU5protein variantARHGAP20-lad593WMLDKLTGV405 ribosomal proteinQ8TD47S4, Y isoform 2594LLKHLLLLLRNA binding motifQ13380595ALLSRLEQIRNA binding proteinQ2M365(Autoantigenic, hnRNP-associated with lethalyellow), long isoform-596DVYEDELVPRNA-binding proteinQ8NI52597VMLGGRNIKVRo ribonucleoprotein-Q9UHX1binding protein 1(SIAHBP1 protein)598RLDELGGVYLHUMANQSJYR6OTTHUMP00000030902599FEDKLIEDLRyanodine receptor 2Q92736(Cardiac muscle-typeryanodine receptor)(RyR2) (RYR-2) (Cardiacmuscle ryanodine recep-tor-calcium releasechannel) (hRYR-2)600QLIDKVWQLSEC14-like protein 1Q92503601FLLEPQMKVSecreted and transmem-Q8WVN6brane protein 1 pre-cursor (Protein K12)602ILNEDGSPNLNeudesin precursorQ9UMX5(Neuron-derived neuro-trophic factor)603LLAILILALP-selectin glycoproteinQ14242ligand 1 precursor(PSGL-1) (Selectin Pligand) (CD162 antigen)604SMNRGGYMPSemaphorin-6D precursorQ8NFY4605EFIDGSLQMSerine/threonine/tyro-Q8WUJ0sine-interacting pro-tein (Protein tyrosinephosphatase-likeprotein)606ILVVYVIGLOlfactory receptor 8G5Q8NG78(Olfactory receptorOR11-298)607TLSERLWLGShb-like adapterQ7M4L6protein, Shf608VLWDRTFSLSignal transducer andP42224activator of transcrip-tion 1 -alpha/beta(Transcription factorISGF-3 componentsp91/p84) STAT1609NVNFFTKPPSignal transducer andP40763activator of transcrip-tion 3 (Acute-phaseresponse factor)610ETFSGVYKK40S ribosomal proteinP62081S7611QLDDLKVEL60S ribosomal proteinP42766L35612MEDLIHEI60S ribosomal proteinP18124L7613QTDVDNDLVThrombospondin-2P35442precursor614LLIDPPRYIC3 and PZP-like alpha-Q8IZJ32-macroglobulin domaincontaining 8615PSIPTSAQHVC3 and PZP-like alpha-Q8IZJ32-macroglobulin domaincontaining 8616FLDEPTNHLATP-binding cassetteQ9UG63sub-family F member 2(Iron-inhibited ABCtransporter 2)617KMDDPDYWRTVRibosome biogenesisQ14137protein BOP1 (Block ofproliferation 1protein)618LANVQQVQICDNA FLJ13765 fis,Q9H8C5clone PLACE4000128,weakly similar, to Musmusculus putativetranscription factormRNA619SLFVVILVTGD200 cell surfaceQ6Q8B3glycoprotein receptorisoform 2 variant 2620ARTIKIRNILRRC58 proteinQ96CX6621LVLTSGIVFVClaudin-6 (Skullin 2)P56747622VISFDKLKLT-box transcriptionO95935factor TBX18 (T-boxprotein 18)623DLMELYKVINTS7 proteinQ8WUH5624LQRRKPTGAFFRAS1-related extracel-Q5SZK8lular matrix protein 2precursor (ECM3homolog)625KVNNEKFRTZinc finger protein 318Q5VUA4(Endocrine regulatoryprotein)626SLDQPTQTVEukaryotic translationQ99613initiation factor 3subunit 8 (eIF3 p110)(eIF3c)627SVTSEGIKAVHUMAN LOC196394 proteinQ81Y45628ISLSEPAKPGHypothetical proteinQ8NDZ2FLJ44216629ILDKKVEKVHeat shock protein HSPP0823890-beta (HSP 84)(HSP 90)630KLSAEVESLKSarcoma antigen NY-SAR-Q5T9S541 (NY-SAR-41)631VTWDAALYIProtein FAM86AQ96G04632YLLPKDIKLRas-like family 11Q6T310member A(OTTHUMP00000018162)633RLLEDGEDFNLKeratin, type I cyto-P05783skeletal 18 (Cytokera-tin-18) (CK-18)634RVLPYPFTHU3 small nucleolar RNA-Q9BVJ6associated protein 14homolog A (Antigen NY-CO-16)635QNQERLERHypothetical proteinQ68DM0DKFZp781D1722636QDNIKELELChromosome-associatedO95239kinesin KIF4A(Chromokinesin)637ILKQRDNEIKinesin-like proteinQ6ZMV9KIF6638QNELDNVSTLMyosin-10 (Myosin heavyP35580chain, nonmuscle IIb)(Nonmuscle myosin heavychain IIb)639NIDLLDDGSNHypothetical proteinQ8IY85C17orf57640VLQSNIQHVSimilar to peptide N-Q9BVR8glycanase homolog( S.cerevisiae )641VFFDIAVDGEPLPeptidyl-prolyl cis-P62937trans isomerase A (EC5.2.1.8)642DFHFPKFSISerpin A13 precursorQ6UXR4643SYVNLPTIAL40S ribosomal proteinP08865SA (p40) (34/67 kDalaminin receptor)(Colon carcinomalaminin-binding pro-tein) (NEM/1CHD4) (Mul-tidrug resistance-as-sociated protein MGr1-Ag)644SNLEHLGHEN-acetylglucosamine-1-Q9UJJ9phosphotransferase sub-unit gamma precursor645LKLKLTAVEKLiprin-beta-1 (ProteinQ86W92tyrosine phosphatasereceptor type f poly-peptide-interactingprotein-binding protein1)646GLKGRVFEV40S ribosomal proteinP61247S3a647SLADLQNDEV40S ribosomal proteinP61247S3a648NNLPHLQVVL0C124512 proteinQ86XA0(Fragment)649ISFGGSVQLHypothetical proteinQ96KX1MGC26744650SILDQILQHypothetical proteinQ96KW9L0C122258651TLSDLRVYLSulfiredoxin-1 (ECQ9BYN01.8.98.2)652EAFVNSKNBasalinQ5QJ38653VTWDAALYLProtein FAM86AQ96G04654VLDDKLVFVTransmembrane proteinQ4KMQ216F655YLLDLHSYLTEB4 proteinO14670656FLALAVIQLSLC10A5Q5PT55657TLAEVSTRLSerine/threonine-pro-P57059tein kinase SNF1-likekinase 1 (EC 2.7.11.1)658VIEVYQEQIL0C391257 proteinQ6P094659RLWEEAVKAZinc finger protein 161Q14119(Putative transcriptionfactor DB1)660SLKTLMLRSlit homolog 2 proteinO94813precursor(Slit-2)661EIKKKFKLFYN-binding proteinO15117(FYN-T-binding protein)662VHKEMFIMVJumonji/ARID domain-P41229containing protein 1C(SmcX protein) (Xe169protein)663VHKEMFIMVJumonji/ARID domain-Q9BY66containing protein 1D(SmcY protein) (Histo-compatibility Yantigen)664LAGSEVALAGVMonocarboxylate trans-O95907porter 3 (MCT 3)665IPHDLFTELSolute carrier family 4Q6U841sodium bicarbonatecotransporter-likemember 10-666FLADPDTVNHLLSorting nexin 14, iso-Q6NUI7form a667RVADRLYGVSorting nexin-4O95219668HRPDLLDYSpectrin beta chain,Q9NRC6brain 4 (Spectrin, non-erythroid beta chain 4)669TLDENHPSISpermatogenesis-assoc-Q9P0W8iated protein 7 (Sperm-atogenesis-associatedprotein HSD3)670TLAEIAKVELNon-POU domain-contain-Q15233ing octamer-bindingprotein (NonO protein)(54 kDa nuclear RNA-and DNA-binding pro-tein) (p54(nrb))(p54nrb) (55 kDanuclear protein)671DVAVEAIRLCohesin subunit SA-1Q8WVM7(Stromal antigen 1)(SCC3 homolog 1)672LMVDHVTEVSteroid receptor RNAQ9HD15activator isoform 1673SLYEMVSRVStructure-specificQ08945recognition protein 1(SSRP1) (Recombinationsignal sequence recog-nition protein) (T160)(Chromatin-specifictranscription elonga-tion factor 80 kDasubunit)674SINPKRAKLSuppressor of hairyQ86YH2wing homolog 2(5′OY11.1) (Zinc fingerprotein 632)675NMYGKVVTVTranscription elonga-O00267tion factor SPT5(hSPT5) (DRB sensitiv-ity-inducing factorlarge subunit) (DSIFlarge subunit) (DSIFp160) (Tat-cotransacti-vator 1 protein) (Tat-CT1 protein)-676SLFATEQLSynaptogyrin-3O43761677RLQEGDKILSVSynaptojanin-2-bindingP57105protein (Mitochondrialouter membrane protein25)678AMFDKKVQLSyneminQ8TE61679ALNELLQHVTalin-1Q9Y490680RVVSMAALAMTAR RNA loop bindingvprotein (TAR (HIV) RNAbinding protein 1)681GIIMQIIDVTaste receptor type 2Q9NYW6member 3 (T2R3)682IFNAIALFLTaste receptor type 2P59535member 40 (T2R40)(T2R58) (G-proteincoupled receptor 60)683LEQGLFSKVOxidoreductase HTATIP2Q9BUP3(EC 1.1.1.-) (HIV-1TAT-interactive protein2)684KFMHMGKRQKTranscription initia-P49848tion factor TFIID sub-unit 6 (Transcriptioninitiation factor TFIID70 kDa subunit)(TAF(II)70) (TAFII-70)(TAFII-80) (TAFII80)685SNFGNEKLTRA@ proteinQ6PIP7686FLLDKKIGVT-complex protein 1P78371subunit beta (TCP-1-beta) (CCT-beta)687RSLAASNPILTelomerase-bindingQ86U58protein EST1A (Evershorter telomeres 1A)(Telomerase subunitEST1A) (EST1-like pro-tein A) (hSmg5/7a)688EMESLTGHQTumor endothelial mar-Q96PE0ker 6 (Hypotheticalprotein TEM6)689LDFQEELEVRas GTPase-activating-Q13576like protein IQGAP2690SPNSEGDAGDLTetratricopeptide re-Q8WVT3peat protein 15 (TPRrepeat protein 15)691LVYLNESSVLHMyosin-18A (MyosinQ92614XVIIIa) (Myosin con-taining PDZ domain)(Molecule associatedwith JAK3 N-terminus)(MAJN)692VAGIKVNQVKPolycystic kidney andQ8TCZ9hepatic disease 1 pre-cursor (Fibrocystin)693ILYELQVELTMC4 proteinQ7Z5M3694EVLDELYRVMDC-3.13 isoform 1Q9UER5(TNFAIP8 protein)695TNIEDGVFETToll-like receptor 8Toll-precursorlikereceptor8 pre-cursor696EIRKNEGQITolloid-like protein 1O43897precursor (EC 3.4.24.-)697IAAKILSYNDNA topoisomerase I,Q969P6mitochondrial precursor(EC 5.99.1.2) (TOP1mt)698LYGRHFNYLPAP associated domain-Q8NDF8containing protein 5(EC 2.7.7.-)(Topoisomerase-relatedfunction protein 4-2)(TRF4-2)699NLFNKYPALPlastin-3 (T-plastin)P13797700YLDEIVKEVTranslocated promoterQ5SWY0region (To activatedMET oncogene)701ENHSSQTDNIP2Y purinoceptor 13Q9BPV8(P2Y13) (G-proteincoupled receptor 86)(G-protein coupled re-ceptor 94)702RTHMLSSLTranscript Y 5Q9BXH6703QATIAPVTVTranscription factorQ02446Sp4 (SPR-1)704NLFRAPIYLTranscription initia-P21675tion factor TFIID sub-unit 1 (EC 2.7.11.1)(Transcription initia-tion factor TFIID 250kDa subunit)(TAF(II)250) (TAFII-250) (TAFII250) (TBP-associated factor 250kDa) (p250) (Cell cyclegene 1 protein)705KLEEEQEKNQLTranscriptional repres-Q8NI51sor CTCFL (CCCTC-bind-ing factor) (Brother ofthe regulator of im-printed sites) (Zincfinger protein CTCF-T)(CTCF paralog706LNVDTPFPLTransducer of regulatedQ6UUV7CREB protein 3707ILYELKVELTransmembrane channel-Q7Z404like protein 4708KFMHMGKRQKTranscription initia-P49848tion factor TFIID sub-unit 6 (Transcriptioninitiation factor TFIID70 kDa subunit)(TAF(II)70) (TAFII-70)(TAFII-80) (TAFII80)709HSDEGGVASLTrophinin-associatedQ12815protein (Tastin) (Tro-phinin-assistingprotein)710AMLTGELKKATryptophanyl-tRNA syn-P23381thetase (EC 6.1.1.2)(Tryptophan--tRNAligase) (TrpRS) (IFP53)(hWRS)711VFPTHVFPTTubulin, gamma complexQ5T9Y2associated protein 3712KELAELRESTSTumor necrosis factorP48023ligand superfamilymember 6 (Fas antigenligand) (Fas ligand)(CD178 antigen) (CD95Lprotein) (Apoptosisantigen ligand) (APTL)[Contains: Tumor necro-sis factor ligandsuperfamily member 6,membrane form713LTDKEGWILTumor necrosis factor,Q13829alpha-induced protein1, endothelial (B12protein)714VVTYKNENINetrin receptor DCCP43146precursor (Tumor sup-pressor protein DCC)(Colorectal cancersuppressor)715TVAEGLIEDAdipocyte-derived leu-Q9NZ08cine aminopeptidaseprecursor (EC 3.4.11.-)(A-LAP) (ARTS-1)(Aminopeptidase PILS)(Puromycin-insensitiveleucyl-specific amino-peptidase) (PILS-AP)(Type 1 tumor necrosisfactor receptorshedding aminopeptidase716NEKIKKDELU1 small nuclear ribo-P09012nucleoprotein A (U1snRNP protein A) (U1Aprotein) (U1-A717ILDESHERVU6 snRNA-associatedO95777Sm-like protein LSm8718NLYSDYILNUbiquitin-proteinQ05086ligase E3A (EC 6.3.2.-)(E6AP ubiquitin-proteinligase) (Oncogenic pro-tein-associated proteinE6-AP) (Human papillo-mavirus E6-associatedprotein)719RYVNGHAKUbiquitin carboxyl-Q9Y6I4terminal hydrolase 3(EC 3.1.2.15) (Ubiqui-tin thioesterase 3)(Ubiquitin-specific-processing protease 3)(Deubiquitinating en-zyme 3)720KLLDLELAPSUBX domain-containingQ92575protein 2721YLYDLNHTLUNC93 homolog B1 (UNC-Q9H1C493B protein) (hUNC93B1)722FFFWLMELSplice isoform 5 ofQ9H171-5Q9H171723ELSSLKETHICDNA FLJ46282 fis,Q6ZRK6clone TESTI4031066724KLGSVPVTVCCDC73 proteinQ6P5Q7725ALWERIEGVCaspase recruitment do-Q9BWT7main-containing protein10 (CARD-containingMAGUK protein 3)(Carma 3)726VKAQEILRCaspase recruitment do-Q9BWT7main-containing protein10 (CARD-containingMAGUK protein 3)(Carma 3)727ANVDAIVVSVChromatin-specificQ9Y5B9transcription elonga-tion factor FACT 140kDa subunit728CKDGEDSIIRBeta-defensin 120Q8N689precursor729DNTKKSDKTAlpha-catulin (CateninQ9UBT7alpha-like protein 1)(Alpha-catenin-relatedprotein)730EFLGDSIMQRibonuclease III (ECQ9NRR43.1.26.3) (RNase III)731EFLQEGLEKSeizure related 6Q53EL9homolog732FLLKCLEQVGranulocyte colony-P09919stimulating factorprecursor (G-CSF)(Pluripoietin) (Fil-grastim) (Lenograstim)733FLTDSNNIKEVLysyl-tRNA synthetaseQ9HB23734GGVQELLNQQProtein C6orf130Q9Y530735GKPRRKSNLMelanophilin (Exo-Q9BV36philin-3) (Synaptotag-min-like protein 2a)(Slp homolog lackingC2 domains a)736HIKEELMHGNovel protein (PossibleQ5VTR6ortholog of mouse phos-phoinositide-3-kinaseadaptor protein 1(Pik3ap1)737HIPFFLHNAER61 glycosyltrans-Q6P985ferase738ILEKKVEKVHeat shock protein HSPP0790090-alpha (HSP 86)739ILMEHIHKL60S ribosomal proteinP84098L19740KASQLGIFISKVPDZ domain-containingQ5EBL8protein 11741KILEVMHTKDedicator of cytokine-Q5JSL3sis 11-; Cdc42-associa-ted guanine nucleotideexchange factorACG/DOCK11742LAVGTSPVLAHypothetical proteinQ6ZNX6FLJ26930743LLAEEARKLLaminin gamma-1 chainP11047precursor (Laminin B2chain)744LLGICFCIAATP-binding cassetteQ96J66transporter sub-familyC member 11 (Multidrugresistance-associatedprotein 8)745LMAEMGVHSVUridine/cytidineQ9NWZ5kinase-like 1746ISRLENITVButyrophilin-like pro-Q6UX41tein 8 precursor747MISLPGPLVTNEndothelial cell-Q96AP7selective adhesionmolecule precursor748MLLDVMHTVPoly(A)-specific ribo-O95453nuclease PARN (EC3.1.13.4) (Polyadenyl-ate-specific ribonucle-ase) (Deadenylating nu-clease) (Deadenylationnuclease)749NVMNLIDFVVoltage-gated potassiumQ96RP8channel KCNA7750NVTMKDNKIF-box protein 11Q52ZP1751PRSNIDVNIrythrocyte membraneQ7Z5S1protein band 4.1 like 5752PSAQPLLSLCDNA FLJ45015 fis,Q6ZT30clone BRAWH3014639753QLKESKLKIFAM13A1_v2 proteinQ24JP0754RDAPHLPDGHypothetical proteinQ6ZP70FLJ26432755RLPPEGILHNVVPS13D-1A proteinQ709C5756SEGAEYDDQTCoagulation factor VIIIP00451precursor (Procoagulantcomponent) (Antihemo-philic factor) (AHF)757SLFERLVKVNFX1-type zinc finger-Q9P2E3containing protein 1758SLLDKIIGAPolymerase I and trans-Q6NZI2cript release factor(PTRF protein)759SMMDVDHQIT-complex protein 1P48643subunit epsilon (TCP-1-epsilon) (CCT-epsilon)760TLDEKIEKVProbable ATP-dependentQ96GQ7RNA helicase DDX27 (EC3.6.1.-) (DEAD boxprotein 27)761TLLEDGTFKVHSCARGQ9HBL8762TVLKTKFSSCDNA FLJ43956 fis,Q6ZU72clone TESTI4015681763VIFEDVGRQVLMitochondrial-process-Q10713ing peptidase alphasubunit, mitochondrialprecursor (EC3.4.24.64) (Alpha-MPP)764YILDINPLLCDNA FLJ45287 fis,Q6ZSR0clone BRHIP3002124765YKTFSTSMMLLHypothetical proteinQ96I36C12orf62766RLPPEGILHNVVPS13D-2A proteinQ709C4767LLGPRVLSPCDNA FLJ32009 fis,Q96DN2clone NT2RP7009498,weakly similar toFIBULIN-1, ISOFORM A768FIILLVTYITransient receptor po-Q9HBA0tential cation channelsubfamily V member 4(TrpV4) (osm-9-like TRPchannel 4) (OTRPC4)(Vanilloid receptor-like channel 2)(Vanilloid receptor-like protein 2) (VRL-2)769FYDIEILKVascular endothelialO43915growth factor D precur-sor (VEGF-D) (c-fos-induced growth factor)(FIGF)770WMAPESIFDKIVascular endothelialP17948growth factor receptor1 precursor (EC2.7.10.1) (VEGFR-1)(Vascular permeabilityfactor receptor) (Tyro-sine-protein kinase re-ceptor FLT) (Flt-1)(Tyrosine-proteinkinase FRT) (Fms-liketyrosine kinase 1)771LLDQQNPDEProto-oncogene C-crkP46108(P38) (Adapter moleculecrk)772VMFKKIKSFEVVDUP1 protein (Thiore-Q9H3M7doxin interactingprotein)773KLLEGEESRISLVimentinP08670774KLLEGEESRISLHUMAN CTCL tumor anti-Q548L2gen HD-CL-06 (Vimentinvariant)775RILGAVAKVVinculin (Metavinculin)P18206776SLSMVNHRLIntegrin alpha-3 pre-P26006cursor (GalactoproteinB3) (GAPB3) (VLA-3alpha chain) (FRP-2)(CD49c antigen) [Con-tains: Integrin alpha-3heavy chain; Integrinalpha-3 light chain]777VGQADGGLSVLRVoltage-dependent T-O95180type calcium channelalpha-1H subunit (Vol-tage-gated calciumchannel alpha subunitCav3.2) (Low-voltage-activated calciumchannel alphal 3.2subunit)778DVATILSRRWiskott-Aldrich syn-Q8IV90drome protein familymember 4 (WASP-familyprotein member 4)779PKFEVIEKPQAATP synthase couplingP18859factor 6, mitochondrialprecursor (EC 3.6.3.14)(ATPase subunit F6)780NCTTIDDSLAIProto-oncogene proteinP56703Wnt-3 precursor781ILPIVILANmyloid beta A4 precur-Q99767sor protein-bindingfamily A member 2(Neuron-specific X11Lprotein) (NeuronalMunc 18-1-interactingprotein 2) (Mint-2)(Adapter protein X11beta)782EFLELSAAQEZinc finger CCHC do-Q8N8U3main-containing protein5783SLTDKVQEAMyeloidl/ymphoid orQ59FF2mixed-lineage leukemia(Trithorax homolog,Drosophila) variant784SKNSALEYQLZinc finger proteinQ86YF9DZIP1 (DAZ-interactingprotein 1/2)785LQDVEEVEIHypothetical proteinQ69YS5DKFZp761O1618786FLDEPTNHLATP-binding cassetteQ9UG63sub-family F member 2(Iron-inhibited ABCtransporter 2)787KMDDPDYWRTVRibosome biogenesisQ14137protein BOP1 (Block ofproliferation 1protein)788LANVQQVQICDNA FLJ13765 fis,Q9H8C5clone PLACE4000128789KLDPTKTTLNDRG1 protein (N-mycQ92597downstream regulatedgene 1 protein)790HLTYLNVYLPre-mRNA splicingQ92620factor ATP-dependentRNA helicase PRP16791ALWDKLFNLNesprin 2 (Nuclear en-Q9NU50velope spectrin repeatprotein 2)1514KIMDQVQQAAdenomatous polyposisP25054coli1515RLQEDPPAGVUbiquitin conjugatingP49459enzyme E21516KLDVGNAEVB cell receptor-P5572associated proteinBAP31 (CDM protein)6c6-AG1517FLYDDNQRVTopoisomerase Il-alphaP113881518FLYDDNQRVTopoisomerase II betaQ028801519ALMEQQHYVIntegrin beta8 subunitP26012precursor1520YLMDTSGKVReplication Protein AP276941521ILDDIGHGVAbl Binding protein 3U310891522LLDRFLATVCyclin IQ140941523LLIDDKGTIKLCell Division ControlP06493Protein 2 (CDC2)1524RLYPWGVVEVSeptin 2 (NEDD5)Q150191525KLQELNYNLSTAT1 alpha/betaP422241526ILIEHLYGLLDL Receptor-relatedQ07954protein (LRP)1527YLIELIDRVTACE (ADAM17)NP-0686041528NLMEQPIKVJunction plakoglobinP14923(gamma catenin)1529FLAEDALNTVEDDR1 (rtk6), h-RYKQ083451530TLLNVIKSVIP3 receptor type IIQ145711531MLKDIIKEYMelanoma-associatedQ9UNF1antigen D2 (MAGE-D2antigen) (MAGE-D)(Breast cancer-associ-ated gene 1 protein)(BCG-1) (11B6) (Hepato-cellular carcinoma-as-sociated protein JCL-1)1532TSYVKVLEHMelanoma-associatedP43358antigen 4 (MAGE-4 antigen) (MAGE-X2)(MAGE-41)1533HEYLKAFKVHUMAN Retinoblastoma-Q08999like protein 2 (130kDa retinoblastoma-associated protein)(PRB2) (P130) (RBR-2) TABLE 3SEQ ID NO, Parent Protein Identification and SwissProt IdentificationNumber for full-length sequences 792-1513ParentSEQSwissProtIDIdentificationNO:Parent Sequence IdentificationNo.792BCL-6 corepressor long isoform —Q6W2J9793E1B_19K/Bcl-2-interacting protein Nip3Q12983794Similar to Heat shock protein HSP 90-beta (HSP 84) (HSPP0823890)795Cytochrome P450 11B2, mitochondrial precursorP190997962′-5′oligoadenylate synthetase 3Q2HJ1479726S protease regulatory subunit 4 (P26s4)P6219179826S proteasome non-ATPase regulatory subunit 7P5166579926S proteasome non-ATPase regulatory subunit 14O0048780040S ribosomal protein S16P6224980140S ribosomal protein S6 (Phosphoprotein NP33)P6275380240S ribosomal protein S9P4678180360S ribosomal protein L10a (CSA-19)P629068046-phosphofructo-2-kinase/fructose-2,6-biphosphatase 4Q16877(6PF-2-K/Fru-2,6-P2ASE testis-type isozyme)805Cleavage and polyadenylation specificity factor, 73 kDaQ9UKF6subunit (CPSF 73 kDa subunit)806A kinase anchor protein 10, mitochondrial precursorO43572807Actin, cytoplasmic 1 (Beta-actin)P60709808Activated T-cell marker CD109Q6YHK3809Activin receptor type 2A precursor (EC 2.7.11.30)P27037810ADAM19 proteinQ8TBU7811AP-1 complex subunit beta-1 (Adapter-related proteinQ10567complex 1 beta-1 subunit) (Beta-adaptin 1)812Adaptor-related protein NF01019537Q9BYI8813Lung alpha/beta hydrolase protein 1Q96SE0814Alpha-actinin-3Q08043815Ankyrin-2 (Brain ankyrin) (Ankyrin-B)Q01484816Ankyrin repeat and SOCS box protein 17Q8WXJ9817Anti-colorectal carcinoma heavy chainQ65ZQ1818APOBEC1 complementation factor (APOBEC1-Q9NQ94stimulating protein)819Probable DNA dC->dU-editing enzyme APOBEC-3D (ECQ96AK33.5.4.—)820Apolipoprotein-L4 precursor (Apolipoprotein L-IV)Q9BPW4821Apoptosis stimulating of p53 protein 1Q96KQ4822Nucleoporin 188 kDa (arachin)Q5SRE5823Protein ariadne-1 homolog (ARI-1) (Ubiquitin-conjugatingQ9Y4X5enzyme E2-binding protein 1)824Set1/Ash2 histone methyltransferase complex subunitQ9UBL3ASH2 (ASH2-like protein)825ATP synthase F0 subunit 8Q85KZ3826Splice isoform 2 of Q9H7F0 ATPase_family_homolog_up-Q9H7F0regulated_in_senescence_cells —827Probable phospholipid-transporting ATPase IA (ECQ9Y2Q03.6.3.1) (Chromaffin granule ATPase II)828ATP-binding cassette A10Q8WWZ4829ATP-binding cassette sub-family A member 2 (ATP-Q9BZC7binding cassette transporter 2) (ATP-binding cassette 2)830Autoantigen RCD8Q6P2E9831xonemal dynein heavy chain 8Q96JB1832Butyrophilin-like protein 8 precursorQ6UX41833Ubiquitin carboxyl-terminal hydrolase 20 (EC 3.1.2.15)Q9Y2K6834Bardet-Biedl syndrome 7 protein (BBS2-like protein 1)Q8IWZ6835Large proline-rich protein BAT2 (HLA-B-associatedP48634transcript 2)836Bcl-2 related ovarian killerQ9UL32837Lipopolysaccharide-responsive and beige-like anchorP50851protein (CDC4-like protein)838Splice isoform 3 of P35612P35612-3839UDP-GlcNAc:betaGal beta-1,3-N-Q9Y2A9acetylglucosaminyltransferase 3 (EC 2.4.1.—)840Cell growth inhibiting protein 39Q2TTR2841BH3-interacting domain death agonist (BID)P55957842CD48 antigen precursor (B-lymphocyte activation markerP09326BLAST-1)843Bone morphogenetic protein receptor type-2 precursor (ECQ138732.7.11.30)844Bullous pemphigoid antigen 1, isoform 7Q8WXK8845BRCA1 associated RING domain 1 variantQ53F80846Breast cancer type 2 susceptibility protein (Fanconi anemiaP51587group D1 protein)847Protein BRE (Brain and reproductive organ-expressedQ9NXR7protein) (BRCA1/BRCA2-containing complex subunit 45)848Breast cancer 1 early onsetQ3LRJ0849Breast and ovarian cancer susceptibility proteinQ7KYU6850BTG2 protein (NGF-inducible anti-proliferative proteinP78543PC3)851Nuclear protein 5qNCAQ7LBC6852CAD protein [Includes: Glutamine-dependent carbamoyl-P27708phosphate synthase (EC 6.3.5.5); Aspartatecarbamoyltransferase (EC 2.1.3.2); Dihydroorotase (EC3.5.2.3)]853Cadherin EGF LAG seven-pass G-type receptor 3Q9NYQ7precursor (Flamingo homolog 1) (hFmi1) (Multipleepidermal growth factor-like domains 2) (Epidermalgrowth factor-like 1)854Cadherin FIB3Q6UW70855Integrin alpha-3 precursor (Galactoprotein B3)P26006856Calcineurin B homologous protein 2 (HepatocellularO43745carcinoma-associated antigen 520)857Calcium/calmodulin-dependent protein kinase II inhibitorQ7Z7J9alpha (CaMKIINalpha)858Calpain-11 (EC 3.4.22.—)Q9UMQ6859Alpha-1 catenin (Cadherin-associated protein) (Alpha E-P35221catenin)860Neural cell adhesion molecule variantQ59FY0861Ribosomal L1 domain-containing protein 1 (CellularO76021senescence-inhibited gene protein)862CENP-F kinetochore protein (Centromere protein F)P49454(Mitosin)863Centaurin-delta 1 (Cnt-d1) (Arf-GAP, Rho-GAP, ankyrinQ8WZ64repeat and pleckstrin homology domain-containing protein2)864Centrosomal protein 2 (Centrosomal Nek2-associatedQ9BV73protein 1) (C-NAP1)865Pericentriol material 1Q15154866Cervical cancer suppressor gene 5Q8NFX8867T-complex protein 1 subunit zeta-2Q92526868Chemokine-like factor (C32)Q9UBR5869Vacuolar protein sorting 13AQ96RL7870Chromodomain-helicase-DNA-binding protein 2 (ECO146473.6.1.—)871FERM domain-containing protein 6Q96NE9872Putative protein C21orf56Q9H0A9873Adiponutrin (iPLA2-epsilon)Q9NST1884Coatomer subunit gamma-2Q9UBF2875Sodium/potassium/calcium exchanger 2 precursorQ9UI40876Exportin-1 (Chromosome region maintenance 1 proteinO14980homolog)877CUB and sushi domain-containing protein 3 precursorQ7Z407878Cullin-7 (CUL-7)Q14999879Cyclic AMP-dependent transcription factor ATF-4P18848880S-phase kinase-associated protein 1A (Cyclin A/CDK2-P63208associated protein p19)881Cyclin-A1P78396882Cyclin M3, isoform 1Q8NE01883Cystathionine beta-synthase human homolog ofQ58H57Cynomolgus monkey gene product884Cytochrome P450 2E1 (EC 1.14.14.1)P05181885Keratin, type II cytoskeletal 8P05787886CPEB2 proteinQ3B8N6887Probable ATP-dependent RNA helicase DDX5 (EC 3.6.1.—)P17844888Dedicator of cytokinesis protein 1Q14185889Development and differentiation-enhancing factor 2O43150890Probable ubiquitin carboxyl-terminal hydrolase FAF-Y (ECO005073.1.2.15)891G2 and S phase expressed protein 1Q9NYZ3892HUMAN CDNA FLJ30829 fis, clone FEBRA2001790,Q96NI3highly similar to Xenopus laevis RRM-containing proteinSEB-4 mRNA893KIAA1799 proteinQ96B95894Peroxisomal proliferator-activated receptor A-interactingQ9BYK8complex 285 kDa protein (EC 3.6.1.—) (ATP-dependenthelicase PRIC285)895HUMAN KIAA1922Q96PW6896Transcription elongation factor SPT5 (DLC-1)(deleted inO00267liver cancer-1)897DNA damage-binding protein 1 (Damage-specific DNA-Q16531binding protein 1)898DNA excision repair protein ERCC-6Q03468899DNA polymerase alpha subunit B (DNA polymerase alphaQ1418170 kDa subunit)900DNA replication licensing factor MCM2P49736(Minichromosome maintenance protein 2 homolog)901DNA2-like homolog (EC 3.6.1.—) (DNA replication ATP-P51530dependent helicase-like homolog)902Estrogen response element binding protein (cotton-topO77798Tarmarin), DNA2-like homolog (human)903DNA damage-inducible transcript 3 (DDIT-3) (GrowthP35638arrest and DNA-damage-inducible protein GADD153)904DNA-directed RNA polymerase I largest subunit (ECO956022.7.7.6)905DnaJ homolog subfamily C member 1Q96KC8906Splice isoform 2 of P35462P35462-2907RuvB-like 2 (EC 3.6.1.—) (48-kDa TATA box-bindingQ9Y230protein-interacting protein)908DRE1_proteinQ9NXT9909Dynactin-1 (150 kDa dynein-associated polypeptide)Q14203910Dynein heavy chain, cytosolic (DYHC)Q14204911Echinoderm microtubule associated protein-like 5Q6UYC9912ECT2 protein (Epithelial cell-transforming sequence 2Q9H8V3oncogene)913Endothelial differentiation-related factor 1 (EDF-1)O60869914Developmentally-regulated endothelial cell locus 1 protein)O43854915Elongation factor 2 (EF-2)P13639916J domain protein C21orf55Q9NX36917EMILIN-3 precursor (EMILIN-5) (Elastin microfibrilQ9NT22interface-located protein 5)918Synaptotagmin-like protein 4 (Exophilin-2)Q96C24919Enhancer of filamentation 1 (HEF1)Q14511920Band 4.1-like protein 3 (4.1B) (Differentially expressed inQ9Y2J2adenocarcinoma of the lung protein 1) (DAL-1)921Epidermal growth factor receptor substrate 15P42566922Epithelial membrane protein 3 (EMP-3) (YMP protein)P54852923Zyxin (Zyxin-2)Q15942924Eukaryotic translation initiation factor 4 gamma 1Q04637925F-actin capping protein beta subunitP47756926Protocadherin Fat 2 precursor (hFat2) (Multiple epidermalQ9NYQ8growth factor-like domains 1)927KIAA1752 proteinQ9C0B1928Fc alpha/mu receptorQ8WWV6929Low affinity immunoglobulin gamma Fc region receptorP08637III-A precursor (IgG Fc receptor III-2)930FYVE, RhoGEF and PH domain-containing protein 2 (ZincQ7Z6J4finger FYVE domain-containing protein 4)931Fibroblast growth factor receptor-like 1 precursor (FGFQ8N441receptor-like protein 1)932Fibroblast growth factor receptor 4 precursor (EC 2.7.10.1)P22455933Fibroblast growth factor receptor 2 precursor (EC 2.7.10.1)P21802(FGFR-2)934FK506-binding protein 7 precursor (EC 5.2.1.8)Q9Y680935Glomulin (FKBP-associated protein) (FK506-bindingQ92990protein-associated protein)936FKSG73Q9BWW1937Flavin containing monooxygenase 3 isoform 2 variantQ53FW5938Protein flightless-1 homologQ13045939Guanylate-binding protein 4Q96PP9940Filamin-A (Alpha-filamin) (Filamin-1) (Endothelial actin-P21333binding protein)941FLJ10101 proteinQ8WU94942CDNA FLJ14503 fis, clone NT2RM1000252, weaklyQ96T17similar to H. sapiens E-MAP-115 mRNA943E2F8 proteinQ5BKY4944Human Hypothetical proteinQ2VPJ3945HUMAN CDNA FLJ34154 fis, clone FCBBF3013058Q8NB70946Hypothetical protein FLJ43654 (Hypothetical proteinQ6ZUJ4C3orf62)947HUMAN CDNA FLJ46180 fis, clone TESTI4004031Q6ZRQ5948Flotillin-2 (Epidermal surface antigen) (ESA)Q14254949Serine/threonine-protein kinase ATR (EC 2.7.11.1) (AtaxiaQ13535telangiectasia and Rad3-related protein) (FRAP-relatedprotein 1)950Frizzled 5 precursor (Frizzled-5)Q13467951Fructose-bisphosphate aldolase C (EC 4.1.2.13)P09972952G protein pathway suppressor 1 isoform 1 variantQ53HS2953KiSS-1 receptor (KiSS-1R) (Kisspeptins receptor)Q969F8(Metastin receptor) (G-protein coupled receptor 54)954Probable G-protein coupled receptor 55Q9Y2T6955Probable G-protein coupled receptor 35Q9HC97956G-protein coupled receptor family C group 5 member CQ9NQ84precursor (Retinoic acid-induced gene 3 protein)957Leucine-rich repeat-containing G-protein coupled receptorO754735 precursor (Orphan G-protein coupled receptor HG38) (G-protein coupled receptor 49) (G-protein coupled receptor67)958Probable G-protein coupled receptor 133 precursor (G-Q6QNK2protein coupled receptor PGR25)959G1 to S phase transition protein 1 homolog (GTP-bindingP15170protein GST1-HS)960Gamma-aminobutyric-acid receptor alpha-6 subunitQ16445precursor (GABA(A) receptor)961Ganglioside-induced differentiation-associated protein 1-Q96MZ0like 1 (GDAP1-L1)962Gap junction alpha-5 protein (Connexin-40) (Cx40)P36382963GEM-interacting protein (GMIP)Q9P107964Golgin subfamily B member 1 (Giantin)Q14789965UDP-N-acetylhexosamine pyrophosphorylase (Antigen X)Q16222966Neutral alpha-glucosidase AB precursor (EC 3.2.1.84)Q14697967Probable dolichyl pyrophosphate Glc1Man9GlcNAc2Q9BVK2alpha-1,3-glucosyltransferase (EC 2.4.1.—)968Bifunctional aminoacyl-tRNA synthetase [Includes:P07814Glutamyl-tRNA synthetase (EC 6.1.1.17) (Glutamate--tRNA ligase); Prolyl-tRNA synthetase (EC 6.1.1.15)(Proline--tRNA ligase)]969Glycoprotein nmb-like proteinQ8IXJ5970Prolactin-releasing peptide receptor (PrRP receptor)P49683(PrRPR) (G-protein coupled receptor 10)971G protein-coupled receptor 112Q5EGP2972Growth factor receptor-bound protein 14 (GRB14 adapterQ14449protein)973GRIP and coiled-coil domain-containing protein 2 (GolgiQ8IWJ2coiled coil protein GCC185) (CTCL tumor antigen se1-1)974GROS1-L proteinQ9HC86975Growth hormone secretagogue receptor type 1 (GHS-R)Q92847976Glutathione S-transferase A4-4 (EC 2.5.1.18)O15217977GTP-binding protein Rhes (Ras homolog enriched inQ96D21striatum) (Tumor endothelial marker 2)978GTP-binding protein Rit1 (Ras-like protein expressed inQ92963many tissues)979VGFG2573Q6UY45980Hypothetical protein HDLBPQ53QU2981Heat shock protein 75 kDa, mitochondrial precursor (HSPQ1293175) (Tumor necrosis factor type 1 receptor-associatedprotein)982Heat shock protein apg-1Q53ZP9983Tumor rejection antigen (Gp96) 1Q5CAQ5984Heat-shock protein beta-3 (HspB3) (Heat shock 17 kDaQ12988protein)985Low-density lipoprotein receptor-related protein 5O75197precursor986Regulator of telomere elongation helicase 1 (EC 3.6.1.—)Q9NZ71(Helicase-like protein NHL)987Hematopoietic protein 1Q52LW0988Heme oxygenase 1 (EC 1.14.99.3) (HO-1)P09601989Heparan sulfate glucosamine 3-O-sulfotransferase 5 (ECQ8IZT82.8.2.23)990Hepatocellular carcinoma-associated antigen 66Q9NYH9991Melanoma-associated antigen E2 (MAGE-E2 antigen)Q8TD90(Hepatocellular carcinoma-associated protein 3)99226S proteasome non-ATPase regulatory subunit 10 (26SO75832proteasome regulatory subunit p28) Hepatocellularcarcinoma-associated protein p28-II993HephaestinQ5JUU1994HECT domain and RCC1-like domain-containing protein 2O95714(HERC2)995Heterogeneous nuclear ribonucleoproteins A2/B1 (hnRNPP22626A2/hnRNP B1)996Heterogeneous nuclear ribonucleoprotein R (hnRNP R)O43390997HEXIM1 protein (HMBA-inducible)O94992998Histatin-1 precursor (Histidine-rich protein 1)P15515999Histone deacetylase 1 (HD1)Q135471000Histone deacetylase 9 (HD9) (HD7B) (HD7)Q9UKV01001Homeodomain-interacting protein kinase 2 (EC 2.7.11.1)Q9H2X61002Cullin-2 (CUL-2)Q136171003SWI/SNF-related matrix-associated actin-dependentO60264regulator of chromatin subfamily A member 5 (EC 3.6.1.—)1004HUMAN HSPC027 26S proteasome non-ATPaseQ9Y6E3regulatory subunit 13 Synonyms 26S proteasomeregulatory subunit S1126S proteasome regulatory subunit p40.51005Hypothetical protein (Novel protein HSPC117)Q9Y3I0(DJ149A16.6 protein) (Hypothetical protein HSPC117)1006Claudin domain-containing protein 1 (Membrane proteinQ9NY35GENX-3745) Q9NY351007Large neutral amino acids transporter small subunit 2 (L-Q9UHI5type amino acid transporter 2) (hLAT2)1008Heterogeneous nuclear ribonucleoprotein C-like 1 (hnRNPO60812core protein C-like 1)1009Ornithine decarboxylase (EC 4.1.1.17) (ODC)P119261010Regulator of nonsense transcripts 2 (Nonsense mRNAQ9HAU5reducing factor 2) (Up-frameshift suppressor 2 homolog)(hUpf2)1011ATX10_HUMAN Ataxin-10Q9UBB41012KIAA1833 proteinQ569G61013HUMAN UDP-GalNAc:betaGlcNAc beta 1,3-Q8NCR0galactosaminyltransferase, polypeptide 2 (Beta 1,3-N-acetylgalactosaminyltransferase-II) (MGC39558)1014Hypothetical protein KIAA1033Q2M3891015Activating signal cointegrator 1 complex subunit 3 (ECQ8N3C03.6.1.—)1016Delta-interacting protein A (Hepatitis delta antigen-Q15834interacting protein A) (Coiled-coil domain-containingprotein 85B)1017Hypothetical protein FLJ14466Q96BP71018Interferon-inducible double stranded RNA-dependentO75569protein kinase activator A1019Hypothetical protein C9orf142Q9BUH61020Tetratricopeptide repeat protein 17Q96AE71021CDNA FLJ14058 fis, clone HEMBB1000554Q9H7Z01022Anaphase promoting complex subunit 13Q9BS181023Hypothetical protein CCDC60Q8IWA61024Sphingosine kinase 2 (EC 2.7.1.—)Q9NRA01025Probable ATP-dependent RNA helicase DDX11 (ECQ96FC93.6.1.—) (DEAD/H box protein 11) (CHL1 homolog)(Keratinocyte growth factor-regulated gene 2 protein)(KRG-2)1026Protein KIAA0182Q146871027Ras GTPase-activating protein SynGAP (Synaptic Ras-Q96PV0GTPase-activating protein 1) (Synaptic Ras-GAP 1)(Neuronal RasGAP)1028Fibrinogen C domain containing 1Q8N5391029MGC39581 proteinQ86XM01030Bcl-2-like 13 protein (Mil1 protein) (Bcl-rambo)Q9BXK51031Myosin head domain containing 1Q96H551032WD-repeat protein 51AQ8NBT01033KIF27A (OTTHUMP00000021559)Q86VH21034Inositol polyphosphate-5-phosphatase F, isoform 1Q2T9J41035MyopalladinQ96KF51036Rho GTPase activating protein 12Q5T2Y21037Hypothetical protein DKFZp686D0630Q7Z3C51038Jumonji domain-containing protein 1C (Thyroid receptor-Q15652interacting protein 8) (TRIP-8)1039Coatomer subunit beta (Beta-coat protein) (Beta-COP)P536181040FLJ10462 fis, clone NT2RP1001494, weakly similar toQ9NVW8MALE STERILITY PROTEIN 21041Cell-cycle and apoptosis regulatory protein 1Q6X9351042Telomere-associated protein RIF1 (Rap1-interacting factorQ5UIP01 homolog)1043F-box only protein 28Q9NVF71044CDNA FLJ10901 fis, clone NT2RP5003524Q9NV651045Acetoacetyl-CoA synthetase (EC 6.2.1.16)Q86V211046Putative cell cycle control protein (DEP domain containingQ9NXZ01)1047Synaptopodin 2-likeQ68A201048CDNA FLJ36560 fis, clone TRACH2009340Q8N9T81049CDNA FLJ13330 fis, clone OVARC1001802Q9H8Q01050ATP-dependent RNA helicase DDX31 (EC 3.6.1.—) (DEADQ9H8H2box protein 31) (Helicain)1051Protein C14orf161Q9H7T01052Cysteine protease ATG4B (EC 3.4.22.—) (Autophagy-Q9Y4P1related protein 4 homolog B)1053CDNA FLJ14526 fis, clone NT2RM1001139Q96T081054Hypothetical protein CCDC77 (CDNA FLJ14732 fis, cloneQ9BR77NT2RP3001969, weakly similar to TRICHOHYALIN)1055CDNA FLJ14790 fis, clone NT2RP4000973, weaklyQ96K38similar to PROBABLE PROTEIN DISULFIDEISOMERASE P5 (EC 5.3.4.1)1056Keratin 24Q2M2I51057BCoR protein (BCL-6 corepressor)Q6W2J91058Hypothetical protein FLJ20582Q6IQ211059Hypothetical protein FLJ22688Q9BT041060Hypothetical protein FLJ22944Q9H5W31061Zinc finger protein, subfamily 1A, 5-Q8TBE51062Leucine-rich repeats and IQ motif containing 2Q8IW351063Hypothetical protein FLJ23749Q8TEA01064Hypothetical protein FLJ25336http://www.expasy.org/sprot/userman.htmlAC lineQ96LP11065Hypothetical protein FLJ25660Q8N7G61066CDNA FLJ30058 fis, clone ADRGL2000074, weaklyQ96NU6similar to RHO-GTPASE-ACTIVATING PROTEIN 61067CDNA FLJ30106 fis, clone BNGH41000190, weaklyQ96A82similar to Rattus norvegicus schlafen-4 (SLFN-4) mRNA.1068WhirlinQ9P2021069CDNA FLJ31846 fis, clone NT2RP7000425, weaklyQ96MV0similar to MYOSIN HEAVY CHAIN, NONMUSCLETYPE B1070FLJ32833 fis, clone TESTI2003228Q96M431071Guanine nucleotide-binding protein G(olf), alpha subunitP38405(Adenylate cyclase-stimulating G alpha protein, olfactorytype)1072CDNA FLJ33811 fis, clone CTONG2002095Q8N2791073Transmembrane protein 16CQ9BYT91074Zinc finger protein 31 (Zinc finger protein KOX29) (ZincP17040finger and SCAN domain-containing protein 20) (Zincfinger protein 360)1075Transmembrane 6 superfamily member 2Q9BZW41076CDNA FLJ90251 fis, clone NT2RM4000115Q8NCH31077CDNA FLJ90760 fis, clone THYRO1000061Q8N2I41078Tubulin--tyrosine ligase-like protein 12Q141661079KIAA0303 proteinO150211080Plexin-B2 precursor (MM1)O150311081Zinc finger and BTB domain-containing protein 5O150621082Centrosome-associated protein 350Q8WY201083piccolo (Aczonin)Q9Y6V01084KIAA0560 proteinO603061085KIAA0676 proteinQ96H491086Human homolog of Mus SLIT and NTRK-like protein 5Q810B7precursor1087NischarinQ6PIB41088FERM domain-containing protein 4AQ9P2Q21089Leucine-rich repeats neuronal protein 1 precursorQ6UXK5(Neuronal leucine-rich repeat protein 1) (NLRR-1)1090KIAA1512 proteinQ9P2161091KIAA1598 proteinQ9HCH41092Phosphatidylinositol-3 phosphate 3-phosphatase adaptorQ96QU2subunit1093KIAA1730 proteinQ9C0D31094KIAA1786 proteinQ96JN91095Hypothetical protein MGC20470Q96EK31096OACT1 proteinQ86XC210976-phosphofructo-2-kinase/fructose-2,6-biphosphatase 4Q16877(6PF-2-K/Fru-2,6-P2ASE testis-type isozyme)1098IkappaB kinase complex-associated protein (IKK complex-O95163associated protein) (p150)1099Immune receptor expressed on myeloid cells 2Q7Z7I31100High-affinity cAMP-specific and IBMX-insensitive 3′,5′-O60658cyclic phosphodiesterase 8A (EC 3.1.4.17)1101Bone specific CMF608Q6WRI01102Importin alpha-7 subunit (Karyopherin alpha-6)O606841103InaD-like protein (Inadl protein) (hINADL) (Pals1-Q8NI35associated tight junction protein) (Protein associated totight junctions)1104Nitric oxide synthase, inducible (EC 1.14.13.39)P352281105Transcription elongation factor SPT5 (hSPT5)O002671106Inositol-trisphosphate 3-kinase B (EC 2.7.1.127) (InositolP279871,4,5-trisphosphate 3-kinase B)1107Type I inositol-3,4-bisphosphate 4-phosphatase (ECQ96PE33.1.3.66) (Inositol polyphosphate 4-phosphatase type I)1108Insulin receptor beta subunitQ9UCB71109Insulin-like growth factor binding protein, acid labileQ8TAY0subunit1110Integrin beta-4 precursor (GP150) (CD104 antigen)P161441111Splice isoform 2 of P35462P35462-21112Interferon alpha 2 proteinQ160551113Interferon-induced protein with tetratricopeptide repeats 1P09914(IFIT-1)) (Interferon-induced 56 kDa protein) (IFI-56K)1114Interleukin-20 precursor (IL-20) (Four alpha helix cytokineQ9NYY1Zcyto10)1115Steroid receptor RNA activator isoform 1Q9HD151116Intersectin-2 (SH3 domain-containing protein 1B)Q9NZM3(SH3P18) (SH3P18-like WASP-associated protein)11117ITI-like protein (Inter-alpha (Globulin) inhibitor H5-like)Q6UXX51118Gap junction alpha-5 protein (Connexin-40)P363821119Kelch-like protein 8Q9P2G91120Keratin, type II cytoskeletal 1 (Cytokeratin-1)P042641121ADAM 9 precursor (EC 3.4.24.—) (A disintegrin andQ13443metalloproteinase domain 9)(Metalloprotease/disintegrin/cysteine-rich protein 9)(Myeloma cell metalloproteinase)1122Next to BRCA1 gene 1 protein (Neighbor of BRCA1 geneQ145961 protein) (Membrane component, chromosome 17, surfacemarker 2) (1A1-3B)1123Hypothetical protein DKFZp686K2075Q6MZZ81124KIAA0100 proteinQ146671125Pre-mRNA-splicing factor ATP-dependent RNA helicaseQ92620PRP16 (EC 3.6.1.—) (ATP-dependent RNA helicaseDHX38) (DEAH box protein 38)1126KIAA0251 proteinQ8TBS51127HUMAN KIAA0342 proteinO150501128KIAA0357 proteinO150641129Hypothetical protein KIAA0372Q6PGP71130KIAA0377 splice variant 2Q86TE71131KIAA0386 proteinQ9Y4F91132HUMAN CTCL tumor antigen HD-CL-04Q548S11133Importin-13 (Imp13) (Ran-binding protein 13)O948291134KIAA0769 proteinO948681135Hypothetical protein KIAA0863Q6IQ321136Zinc finger protein KIAA1196 -Q96KM61137CRSP complex subunit 3 (Cofactor required for Sp1Q9ULK4transcriptional activation subunit 3) (Transcriptionalcoactivator CRSP130) (Vitamin D3 receptor-interactingprotein complex 130 kDa component1138[Pyruvate dehydrogenase [lipoamide]]-phosphatase 2,Q9P2J9mitochondrial precursor (EC 3.1.3.43)1139Protocadherin-10 precursorQ9P2E71140Leucine-rich repeats and calponin homology (CH) domainQ5VUJ6containing 21141Ankyrin repeat domain 18BQ5W0G21142Kin17 protein (HsKin17 protein) (KIN, antigenicO60870determinant of recA protein homolog)1143Kinesin-like protein KIF13A (Kinesin-like protein RBKIN)Q9H1H91144Putative RNA binding protein KOCO004251145Keratin, type I cytoskeletal 18 (Cytokeratin-18)P057831146Kv3.2d voltage-gated potassium channelQ86W091147Lethal(3)malignant brain tumor-like protein (L(3)mbt-like)Q9Y468(L(3)mbt protein homolog)1148Lactadherin precursor (Milk fat globule-EGF factor 8)Q08431(MFG-E8) (HMFG) (Breast epithelial antigen BA46)(MFGM)1149Lamin-A/C (70 kDa lamin)P025451150Laminin gamma-1 chain precursor (Laminin B2 chain)P110471151Low-density lipoprotein receptor-related protein 5O75197precursor1152Leptin receptor precursor (LEP-R) (OB receptor)P483571153Mitogen-activated protein kinase kinase kinase 13 (ECO432832.7.11.25)1154Leukemia virus receptor 2Q083571155Leukemia-associated protein with a CXXC domainQ8NFU71156RNA-binding protein 6 (RNA-binding motif protein 6)P78332(RNA-binding protein DEF-3) (Lung cancer antigen NY-LU-12)1157Lung cancer oncogene 5Q7Z5Q71158Heterogeneous nuclear ribonucleoprotein M (hnRNP M)P522721159Macrophage migration inhibitory factor (MIF)P14174(Phenylpyruvate tautomerase) (EC 5.3.2.1)1160Mitotic spindle assembly checkpoint protein MAD2BQ9UI95(MAD2-like 2) (hREV7)1161Mitogen-activated protein kinase kinase kinase 4 (ECQ9Y6R42.7.11.25) (MAPK/ERK kinase kinase 4)1162Serine/threonine/tyrosine-interacting-like protein 1 (Dual-Q9Y6J8specificity protein phosphatase 24) (Map kinasephosphatase-like protein MK-STYX)1163Microtubule-associated serine/threonine-protein kinase 2Q6P0Q8(EC 2.7.11.1)1164Matrix metalloprotease MMP-27Q9H3061165MCM10 proteinQ7L5901166Interferon-induced helicase C domain-containing protein 1Q9BYX4(EC 3.6.1.—) (Melanoma differentiation-associated protein5)1167Melanoma ubiquitous mutated proteinQ2TAK81168Melanoma antigen family D, 2Q5BJF31169Melanocyte protein Pmel 17 precursor (MelanocyteP40967lineage-specific antigen GP100)1170GPI-anchored protein p137 (p137GPI) (MembraneQ14444component chromosome 11 surface marker 1) Cytoplasmicactivation/proliferation-associated protein 11171Hepatocyte growth factor receptor precursor (EC 2.7.10.1)P08581(HGF receptor) (Scatter factor receptor) (SF receptor)(HGF/SF receptor) (Met proto-oncogene tyrosine kinase)1172Mitogen-activated protein kinase 14 (EC 2.7.11.24)Q165391173Mitogen-activated protein kinase kinase kinase kinase 2Q12851(EC 2.7.11.1) (MAPK/ERK kinase kinase kinase 2)1174Mitotic kinesin-related proteinQ96Q891175Sperm-associated antigen 5 (Astrin) (Mitotic spindle-Q96R06associated protein p126)1176Myeloid/lymphoid or mixed-lineage leukemia protein 4Q9UMN6(Trithorax homolog 2)1177Putative helicase MOV-10 (EC 3.6.1.—) (Moloney leukemiaQ9HCE1virus 10 protein)1178MOZ/CBP proteinQ712H61179Calgranulin B (Migration inhibitory factor-related proteinP0670214) (MRP-14) (P14)1180MUC2_HUMAN Mucin-2 precursor (Intestinal mucin 2)Q028171181Mucin-5B precursor (Mucin 5 subtype B, tracheobronchial)Q9HC841182Multiple PDZ domain protein (Multi PDZ domain proteinO759701) (Multi-PDZ-domain protein 1)1183RUFY2 (Run and FYVE domain-containing protein Rabip4Q8IW331184Multidrug resistance-associated protein 7Q8NHX71185Multiple copies in a T-cell malignancies (Malignant T cellQ9ULC4amplified sequence 1) (MCT1)1186DNA mismatch repair protein Msh3P205851187Protein CBFA2T2 (MTG8-like protein) (MTG8-relatedO43439protein 1) (Myeloid translocation-related protein 1)1188Myomesin-1 (190 kDa titin-associated protein) (190 kDaP52179connectin-associated protein1189Myosin heavy chain, cardiac muscle beta isoform (MyHC-P12883beta)1190Myosin-13 (Myosin heavy chain, skeletal muscle,Q9UKX3extraocular) (MyHC-eo)1191Tumor suppressor candidate 3 (N33 protein)Q134541192Nebulin-related anchoring proteinQ8TCH01193Neural cell adhesion molecule 1, 1P135921194Neurotrimin precursorQ9P1211195NineinQ8N4C61196Notch homolog 2Q5VTD01197Neurogenic locus notch homolog protein 1 precursorP46531(Notch 1) (hN1) (Translocation-associated notch proteinTAN-1) [Contains: Notch 1 extracellular truncation; Notch1 intracellular domain]1198Neurogenic locus notch homolog protein 3 precursorQ9UM47(Notch 3) [Contains: Notch 3 extracellular truncation;Notch 3 intracellular domain]1199Neurogenic locus notch homolog protein 4 precursorQ99466(Notch 4) (hNotch4) [Contains: Notch 4 extracellulartruncation; Notch 4 intracellular domain] -1200Plexin-A1 precursor (Semaphorin receptor NOV)Q9UIW21201HUMAN NPD011Q9H2R71202Nuclear autoantigen Sp-100 (Speckled 100 kDa) (NuclearP23497dot-associated Sp100 protein)1203Nuclear factor erythroid 2-related factor 1 (NF-E2-relatedQ14494factor 1) (NFE2-related factor 1) (Nuclear factor, erythroidderived 2, like 1) (Transcription factor 11) (Transcriptionfactor HBZ17) (Transcription factor LCR-F1) (Locuscontrol region-factor 1)1204Nuclear factor of activated T-cells, cytoplasmic 1 (NFATO95644transcription complex cytosolic component) (NF-ATc1)1205Nuclear receptor coactivator 2 (NCoA-2) (TranscriptionalQ15596intermediary factor 2)1206Ubiquitin-like PHD and RING finger domain-containingQ96T88protein 1 (EC 6.3.2.—)1207Nucleic acid helicase DDXxQ8IWW21208Nucleoporin 62 kDa (NUP62 protein)Q6GTM21209Nuclear pore complex protein Nup98-Nup96 precursorP52948[Contains: Nuclear pore complex protein Nup98(Nucleoporin Nup98) (98 kDa nucleoporin);1210Nucleoprotein TPRP122701211Nuclear pore complex protein Nup107P577401212Nuclear pore complex protein Nup205Q926211213ODF2 proteinQ6PJQ81214Trophoblast glycoprotein precursor (5T4 oncofetalQ13641trophoblast glycoprotein)1215Dynamin-like 120 kDa protein, mitochondrial precursorO60313(Optic atrophy 1 gene protein)1216Orexin receptor type 2 (Ox2r) (Hypocretin receptor type 2)O436141217Transmembrane emp24 domain-containing protein 10P49755precursor (Transmembrane protein Tmp21)1218Orphan nuclear receptor TR2 (Testicular receptor 2)P130561219MKL/myocardin-like protein 1 (Myocardin-relatedQ969V6transcription factor A) (MRTF-A) (Megakaryoblasticleukemia 1 protein) (Megacaryocytic acute leukemiaprotein)1220Ovarian cancer related tumor marker CA125 -Q8WXI71221Oxysterol-binding protein-related protein 8 (OSBP-relatedQ9BZF1protein 8)1222Centrosomal protein of 70 kDa (Cep70 protein) (p10-Q8NHQ1binding protein)1223Leucine carboxyl methyltransferase 2 (EC 2.1.1.—)O60294(p21WAF1/CIP1 promoter-interacting protein)1224F-box/LRR-repeat protein 5 (F-box and leucine-rich repeatQ9UKA1protein 5) (F-box protein FBL4/FBL5)1225Inhibitor of growth protein 3Q9NXR81226P53 inducible proteinQ9UN291227DNA polymerase alpha catalytic subunit (EC 2.7.7.7)P098841228Chloride intracellular channel protein 4 (IntracellularQ9Y696chloride ion channel protein p64H11229Paired mesoderm homeobox protein 2B (Paired-likeQ99453homeobox 2B) (PHOX2B homeodomain protein)(Neuroblastoma Phox)1230PRB3 proteinP814891231Protein patched homolog 1 (PTC1) (PTC)Q136351232Rap guanine nucleotide exchange factor 2 (Neural RAPQ9Y4G8guanine nucleotide exchange protein) (nRap GEP) (PDZdomain-containing guanine nucleotide exchange factor 1)(PDZ-GEF1)1233Pecanex-like protein 1 (Pecanex homolog) -Q96RV31234GC-1-related estrogen receptor alpha coactivator shortQ8TDE4isoform1235PHD fingerQ86U891236Hypothetical protein DKFZp686C07187Q6N0381237Phosphatidylinositol-4,5-bisphosphate 3-kinase catalyticP42338subunit beta isoform (EC 2.7.1.153) (PI3-kinase p110subunit beta) (PtdIns-3-kinase p110)1238Phosphodiesterase 8A, isoform 1Q6P9H31239Serine/threonine-protein kinase SMG1 (EC 2.7.11.1)Q96Q15(SMG-1) (hSMG-1) (Lambda/iota protein kinase C-interacting protein) (Lambda-interacting protein) (1240PiggyBac transposable element derived 3Q8N3281241PIWIL3 proteinQ7Z3Z31242Homeobox protein PKNOX1 (PBX/knotted homeobox 1)P553471243Transmembrane protein 115 (Protein PL6)Q128931244Plakophilin-2Q999591245Plectin 6Q6S3801246Plectin 1 (PLTN) (PCN) (Hemidesmosomal protein 1)Q15149(HD1)1247Plexin B1; plexin 5; semaphorin receptorO431571248Pleiotropic regulator 1O436601249Blood vessel epicardial substance (hBVES) (PopeyeQ8NE79domain-containing protein 1) (Popeye protein 1)1250Carboxypeptidase-like protein X2 precursorQ8N4361251YIF1B proteinQ5BJH71252Melanoma antigen preferentially expressed in tumorsP78395(Pr4eferentially expressed antigen of melanoma) (OPA-interacting protein 4)1253Splice isoform 2 of Q9H7F0Q9H7F0-21254P2Y purinoceptor 13 (P2Y13) (G-protein coupled receptorQ9BPV886) (G-protein coupled receptor 94)1255Putative pre-mRNA-splicing factor ATP-dependent RNAO43143helicase DHX15 (EC 3.6.1.—) (DEAH box protein 15)(ATP-dependent RNA helicase #46)1256HUMAN RNA-binding protein 34 (RNA-binding motifP42696protein 34)1257Prolyl 4-hydroxylase alpha-1 subunit precursor (ECP136741.14.11.2) (4-PH alpha-1) (Procollagen-proline, 2-oxoglutarate-4-dioxygenase alpha-1 subunit)1258Profilin-1P077371259Programmed cell death protein 5 (TFAR19 protein) (TF-1O14737cell apoptosis-related gene 19 protein)1260Propionyl-CoA carboxylase beta chain, mitochondrialP05166precursor (EC 6.4.1.3)126126S proteasome non-ATPase regulatory subunit 1 (26SQ99460proteasome regulatory subunit RPN2) (26S proteasomeregulatory subunit S1) (26S proteasome subunit p112)126226S proteasome non-ATPase regulatory subunit 3 (26SO43242proteasome regulatory subunit S3) (Proteasome subunitp58)1263Proteasome activator complex subunit 3 (ProteasomeP61289activator 28-gamma subunit) (PA28gamma) (PA28g)(Activator of multicatalytic protease subunit 3) (11Sregulator complex gamma subunit) (REG-gamma) (Kinuclear autoantigen)1264Protein C14orf166Q9Y2241265Protein KIAA1219Q86X101266Protein KIAA1688Q9C0H51267Protein Plunc precursor (Palate lung and nasal epitheliumQ9NP55clone protein) (Lung-specific protein X) (Nasopharyngealcarcinoma-related protein) (Tracheal epithelium-enrichedprotein) (Secretory protein in upper respiratory tracts)1268Protein transport protein Sec23BQ154371269Liprin-alpha-2 (Protein tyrosine phosphatase receptor type fO75334polypeptide-interacting protein alpha-2) (PTPRF-interacting protein alpha-2)1270Protocadherin gamma A12 precursor (PCDH-gamma-A12)O60330(Cadherin-21) (Fibroblast cadherin 3)1271Protocadherin gamma A10 precursor (PCDH-gamma-A10)Q9Y5H31272Leucine carboxyl methyltransferase 2 (EC 2.1.1.—)O60294(p21WAF1/CIP1 promoter-interacting protein)1273KIAA1636 proteinQ9HCD61274Probable G-protein coupled receptor 160Q9UJ421275Protein C21orf45Q9NYP91276Periodic tryptophan protein 2 homologQ152691277Rab-like protein 2BQ9UNT11278Cell cycle checkpoint protein RAD17 (hRad17) (RF-O75943C/activator 1 homolog)1279DNA repair protein RAD50 (EC 3.6.—.—) (hRAD50)Q928781280Ras GTPase-activating protein 1 (GTPase-activatingP20936protein) (GAP) (Ras p21 protein activator) (p120GAP)(RasGAP)1281Ras guanine nucleotide exchange factor 2Q9UK561282Ras-GTPase-activating protein-binding protein 1 (ECQ132833.6.1.—) (ATP-dependent DNA helicase VIII) (GAP SH3-domain-binding protein 1) (G3BP-1) (HDH-VIII)1283Ras-related protein Rab-27A (Rab-27) (GTP-bindingP51159protein Ram)1284Ras-related protein Rab-3DO957161285Nuclear pore complex protein Nup107 (NucleoporinP57740Nup107) (107 kDa nucleoporin)1286Receptor-interacting factor 1Q86XS41287Regulating synaptic membrane exocytosis protein 3 (Nim3)Q9UJD0(Rab-3 interacting molecule 3) (RIM 3) (RIM3 gamma)1288Regulator of G protein signaling protein (Regulator of G-Q86UV0protein signalling like 1)1289MHC class II regulatory factor RFX1 (RFX) (EnhancerP22670factor C) (EF-C)1290Retinoblastoma-associated protein (PP110) (P105-RB)P064001291Roundabout homolog 3 precursor (Roundabout-like proteinQ96MS03)1292Retinoblastoma-associated protein HEC (KinetochoreO14777associated 2)1293Retinoblastoma-associated protein RAP140Q9UK611294AT-rich interactive domain-containing protein 4A (ARIDP29374domain-containing protein 4A) (Retinoblastoma-bindingprotein 1)1295Jumonji/ARID domain-containing protein 1AP29375(Retinoblastoma-binding protein 2) (RBBP-2)1296RhoGTPase regulating protein variant ARHGAP20-1adQ6RJU5129740S ribosomal protein S4, Y isoform 2Q8TD471298RNA binding motifQ133801299RNA binding protein (Autoantigenic, hnRNP-associatedQ2M365with lethal yellow), long isoform -1300RNA-binding proteinQ8NI521301Ro ribonucleoprotein-binding protein 1 (SIAHBP1 protein)Q9UHX11302HUMAN OTTHUMP00000030902Q5JYR61303Ryanodine receptor 2 (Cardiac muscle-type ryanodineQ92736receptor) (RyR2) (RYR-2) (Cardiac muscle ryanodinereceptor-calcium release channel) (hRYR-2)1304SEC14-like protein 1Q925031305Secreted and transmembrane protein 1 precursor (ProteinQ8WVN6K12)1306Neudesin precursor (Neuron-derived neurotrophic factor)Q9UMX51307P-selectin glycoprotein ligand 1 precursor (PSGL-1)Q14242(Selectin P ligand) (CD162 antigen)1308Semaphorin-6D precursorQ8NFY41309Serine/threonine/tyrosine-interacting protein (ProteinQ8WUJ0tyrosine phosphatase-like protein)1310Olfactory receptor 8G5 (Olfactory receptor OR11-298)Q8NG781311Shb-like adapter protein, ShfQ7M4L61312Signal transducer and activator of transcription 1-alpha/betaP42224(Transcription factor ISGF-3 components p91/p84) STAT11313Signal transducer and activator of transcription 3 (Acute-P40763phase response factor)131440S ribosomal protein S7P62081131560S ribosomal protein L35P42766131660S ribosomal protein L7P181241317Thrombospondin-2 precursorP354421318C3 and PZP-like alpha-2-macroglobulin domain containing 8Q8IZJ31319ATP-binding cassette sub-family F member 2 (Iron-Q9UG63inhibited ABC transporter 2)1320Ribosome biogenesis protein BOP1 (Block of proliferationQ141371 protein)1321CDNA FLJ13765 fis, clone PLACE4000128, weaklyQ9H8C5similar to Mus musculus putative transcription factormRNA1322CD200 cell surface glycoprotein receptor isoform 2 variant 2Q6Q8B31323LRRC58 proteinQ96CX61324Claudin-6 (Skullin 2)P567471325T-box transcription factor TBX18 (T-box protein 18)O959351326INTS7 proteinQ8WUH51327FRAS1-related extracellular matrix protein 2 precursorQ5SZK8(ECM3 homolog)1328Zinc finger protein 318 (Endocrine regulatory protein)Q5VUA41329Eukaryotic translation initiation factor 3 subunit 8 (eIF3Q99613p110) (eIF3c)1330HUMAN LOC196394 proteinQ8IY451331Hypothetical protein FLJ44216Q8NDZ21332Heat shock protein HSP 90-beta (HSP 84) (HSP 90)P082381333Sarcoma antigen NY-SAR-41 (NY-SAR-41)Q5T9S51334Protein FAM86AQ96G041335Ras-like family 11 member A (OTTHUMP00000018162)Q6T3101336Keratin, type I cytoskeletal 18 (Cytokeratin-18) (CK-18)P057831337U3 small nucleolar RNA-associated protein 14 homolog AQ9BVJ6(Antigen NY-CO-16)1338Hypothetical protein DKFZp781D1722Q68DM01339Chromosome-associated kinesin KIF4A (Chromokinesin)O952391340Kinesin-like protein KIF6Q6ZMV91341Myosin-10 (Myosin heavy chain, nonmuscle IIb)P35580(Nonmuscle myosin heavy chain IIb)1342Hypothetical protein C17orf57Q8IY851343Similar to peptide N-glycanase homolog ( S. cerevisiae )Q9BVR81344Peptidyl-prolyl cis-trans isomerase A (EC 5.2.1.8)P629371345Serpin A13 precursorQ6UXR4134640S ribosomal protein SA (p40) (34/67 kDa lamininP08865receptor) (Colon carcinoma laminin-binding protein)(NEM/1CHD4) (Multidrug resistance-associated proteinMGr1-Ag)1347N-acetylglucosamine-1-phosphotransferase subunit gammaQ9UJJ9precursor1348Liprin-beta-1 (Protein tyrosine phosphatase receptor type fQ86W92polypeptide-interacting protein-binding protein 1)134940S ribosomal protein S3aP61247135040S ribosomal protein S3aP612471351LOC124512 protein (Fragment)Q86XA01532Hypothetical protein MGC26744Q96KX11535Hypothetical protein LOC122258Q96KW91354Sulfiredoxin-1 (EC 1.8.98.2)Q9BYN01355BasalinQ5QJ381356Protein FAM86AQ96G041357Transmembrane protein 16FQ4KMQ21358TEB4 proteinO146701359SLC10A5Q5PT551360Serine/threonine-protein kinase SNF1-like kinase 1 (ECP570592.7.11.1)1361LOC391257 proteinQ6P0941362Zinc finger protein 161 (Putative transcription factor DB1)Q141191363Slit homolog 2 protein precursor (Slit-2)O948131364FYN-binding protein (FYN-T-binding protein)O151171365Jumonji/ARID domain-containing protein 1C (SmcXP41229protein) (Xe169 protein)1366Jumonji/ARID domain-containing protein 1D (SmcYQ9BY66protein) (Histocompatibility Y antigen)1367Monocarboxylate transporter 3 (MCT 3)O959071368Solute carrier family 4 sodium bicarbonate cotransporter-Q6U841like member 10 -1369Sorting nexin 14, isoform aQ6NUI71370Sorting nexin-4O952191371Spectrin beta chain, brain 4 (Spectrin, non-erythroid betaQ9NRC6chain 4)1372Spermatogenesis-associated protein 7 (Spermatogenesis-Q9P0W8associated protein HSD3)1373Non-POU domain-containing octamer-binding proteinQ15233(NonO protein) (54 kDa nuclear RNA- and DNA-bindingprotein) (p54(nrb)) (p54nrb) (55 kDa nuclear protein)1374Cohesin subunit SA-1 (Stromal antigen 1) (SCC3 homologQ8WVM71)1375Steroid receptor RNA activator isoform 1Q9HD151376Structure-specific recognition protein 1 (SSRP1)Q08945(Recombination signal sequence recognition protein)(T160) (Chromatin-specific transcription elongation factor80 kDa subunit)1377Suppressor of hairy wing homolog 2 (5′OY11.1) (ZincQ86YH2finger protein 632)1378Transcription elongation factor SPT5 (hSPT5) (DRBO00267sensitivity-inducing factor large subunit) (DSIF largesubunit) (DSIF p160) (Tat-cotransactivator 1 protein) (Tat-CT1 protein) -1379Synaptogyrin-3O437611380Synaptojanin-2-binding protein (Mitochondrial outerP57105membrane protein 25)1381SyneminQ8TE611382Talin-1Q9Y4901383TAR RNA loop binding protein (TAR (HIV) RNA bindingQ13395protein 1)1384Taste receptor type 2 member 3 (T2R3)Q9NYW61385Taste receptor type 2 member 40 (T2R40) (T2R58) (G-P59535protein coupled receptor 60)1386Oxidoreductase HTATIP2 (EC 1.1.1.—) (HIV-1 TAT-Q9BUP3interactive protein 2)1387Transcription initiation factor TFIID subunit 6P49848(Transcription initiation factor TFIID 70 kDa subunit)(TAF(II)70) (TAFII-70) (TAFII-80) (TAFII80)1388TRA@ proteinQ6PIP71389T-complex protein 1 subunit beta (TCP-1-beta) (CCT-beta)P783711390Telomerase-binding protein EST1A (Ever shorterQ86US8telomeres 1A) (Telomerase subunit EST1A) (EST1-likeprotein A) (hSmg5/7a)1391Tumor endothelial marker 6 (Hypothetical protein TEM6)Q96PE01392Ras GTPase-activating-like protein IQGAP2Q135761393Tetratricopeptide repeat protein 15 (TPR repeat protein 15)Q8WVT31394Myosin-18A (Myosin XVIIIa) (Myosin containing PDZQ92614domain) (Molecule associated with JAK3 N-terminus)(MAJN)1395Polycystic kidney and hepatic disease 1 precursorQ8TCZ9(Fibrocystin)1396TMC4 proteinQ7Z5M31397MDC-3.13 isoform 1 (TNFAIP8 protein)Q9UER51398Toll-like receptor 8 precursorQ9NR971399Tolloid-like protein 1 precursor (EC 3.4.24.—)O438971400DNA topoisomerase I, mitochondrial precursor (ECQ969P65.99.1.2) (TOP1mt)1401PAP associated domain-containing protein 5 (EC 2.7.7.—)Q8NDF8(Topoisomerase-related function protein 4-2) (TRF4-2)1402Plastin-3 (T-plastin)P137971403Translocated promoter region (To activated METQ5SWY0oncogene)1404P2Y purinoceptor 13 (P2Y13) (G-protein coupled receptorQ9BPV886) (G-protein coupled receptor 94)1405Transcript Y 5Q9BXH61406Transcription factor Sp4 (SPR-1)Q024461407Transcription initiation factor TFIID subunit 1 (ECP216752.7.11.1) (Transcription initiation factor TFIID 250 kDasubunit) (TAF(II)250) (TAFII-250) (TAFII250) (TBP-associated factor 250 kDa) (p250) (Cell cycle gene 1protein)1408Transcriptional repressor CTCFL (CCCTC-binding factor)Q8NI51(Brother of the regulator of imprinted sites) (Zinc fingerprotein CTCF-T) (CTCF paralog1409Transducer of regulated CREB protein 3Q6UUV71410Transmembrane channel-like protein 4Q7Z4041411Transcription initiation factor TFIID subunit 6P49848(Transcription initiation factor TFIID 70 kDa subunit)(TAF(II)70) (TAFII-70) (TAFII-80) (TAFII80)1412Trophinin-associated protein (Tastin) (Trophinin-assistingQ12815protein)1413Tryptophanyl-tRNA synthetase (EC 6.1.1.2) (Tryptophan--P23381tRNA ligase) (TrpRS) (IFP53) (hWRS)1414Tubulin, gamma complex associated protein 3Q5T9Y21415Tumor necrosis factor ligand superfamily member 6 (FasP48023antigen ligand) (Fas ligand) (CD178 antigen) (CD95Lprotein) (Apoptosis antigen ligand) (APTL) [Contains:Tumor necrosis factor ligand superfamily member 6,membrane form1416Tumor necrosis factor, alpha-induced protein 1, endothelialQ13829(B12 protein)1417Netrin receptor DCC precursor (Tumor suppressor proteinP43146DCC) (Colorectal cancer suppressor)1418Adipocyte-derived leucine aminopeptidase precursor (ECQ9NZ083.4.11.—) (A-LAP) (ARTS-1) (Aminopeptidase PILS)(Puromycin-insensitive leucyl-specific aminopeptidase)(PILS-AP) (Type 1 tumor necrosis factor receptor sheddingaminopeptidase1419U1 small nuclear ribonucleoprotein A (U1 snRNP proteinP09012A) (U1A protein) (U1-A1420U6 snRNA-associated Sm-like protein LSm8O957771421Ubiquitin-protein ligase E3A (EC 6.3.2.—) (E6AP ubiquitin-Q05086protein ligase) (Oncogenic protein-associated protein E6-AP) (Human papillomavirus E6-associated protein)1422Ubiquitin carboxyl-terminal hydrolase 3 (EC 3.1.2.15)Q9Y6I4(Ubiquitin thioesterase 3) (Ubiquitin-specific-processingprotease 3) (Deubiquitinating enzyme 3)1423UBX domain-containing protein 2Q925751424UNC93 homolog B1 (UNC-93B protein) (hUNC93B1)Q9H1C41425Splice isoform 5 of Q9H171Q9H171-51426CDNA FLJ46282 fis, clone TESTI4031066Q6ZRK61427CCDC73 proteinQ6P5Q71428Caspase recruitment domain-containing protein 10 (CARD-Q9BWT7containing MAGUK protein 3) (Carma 3)1429Chromatin-specific transcription elongation factor FACTQ9Y5B9140 kDa subunit1430Beta-defensin 120 precursorQ8N6891431Alpha-catulin (Catenin alpha-like protein 1) (Alpha-Q9UBT7catenin-related protein)1432Ribonuclease III (EC 3.1.26.3) (RNase III)Q9NRR41433Seizure related 6 homologQ53EL91434Granulocyte colony-stimulating factor precursor (G-CSF)P09919(Pluripoietin) (Filgrastim) (Lenograstim)1435Lysyl-tRNA synthetaseQ9HB231436Protein C6orf130Q9Y5301437Melanophilin (Exophilin-3) (Synaptotagmin-like proteinQ9BV362a) (Slp homolog lacking C2 domains a)1438Novel protein (Possible ortholog of mouseQ5VTR6phosphoinositide-3-kinase adaptor protein 1 (Pik3ap1)1439AER61 glycosyltransferaseQ6P9851440Heat shock protein HSP 90-alpha (HSP 86)P07900144160S ribosomal protein L19P840981442PDZ domain-containing protein 11Q5EBL81443Dedicator of cytokinesis 11-; Cdc42-associated guanineQ5JSL3nucleotide exchange factor ACG/DOCK111444Hypothetical protein FLJ26930Q6ZNX61445Laminin gamma-1 chain precursor (Laminin B2 chain)P110471446ATP-binding cassette transporter sub-family C member 11Q96J66(Multidrug resistance-associated protein 8)1447Uridine/cytidine kinase-like 1Q9NWZ51448Butyrophilin-like protein 8 precursorQ6UX411449Endothelial cell-selective adhesion molecule precursorQ96AP71450Poly(A)-specific ribonuclease PARN (EC 3.1.13.4)O95453(Polyadenylate-specific ribonuclease) (Deadenylatingnuclease) (Deadenylation nuclease)1451Voltage-gated potassium channel KCNA7Q96RP81452F-box protein 11Q52ZP11453rythrocyte membrane protein band 4.1 like 5Q7Z5S11454CDNA FLJ45015 fis, clone BRAWH3014639Q6ZT301455FAM13A1_v2 proteinQ24JP01456Hypothetical protein FLJ26432Q6ZP701457VPS13D-1A proteinQ709C51458Coagulation factor VIII precursor (ProcoagulantP00451component) (Antihemophilic factor) (AHF)1459NFX1-type zinc finger-containing protein 1Q9P2E31460Polymerase I and transcript release factor (PTRF protein)Q6NZI21461T-complex protein 1 subunit epsilon (TCP-1-epsilon)P48643(CCT-epsilon)1462Probable ATP-dependent RNA helicase DDX27 (ECQ96GQ73.6.1.—) (DEAD box protein 27)1463HSCARGQ9HBL81464CDNA FLJ43956 fis, clone TESTI4015681Q6ZU721465Mitochondrial-processing peptidase alpha subunit,Q10713mitochondrial precursor (EC 3.4.24.64) (Alpha-MPP)1466CDNA FLJ45287 fis, clone BRHIP3002124Q6ZSR01467Hypothetical protein C12orf62Q96I361468VPS13D-2A proteinQ709C41469CDNA FLJ32009 fis, clone NT2RP7009498, weaklyQ96DN2similar to FIBULIN-1, ISOFORM A1470Transient receptor potential cation channel subfamily VQ9HBA0member 4 (TrpV4) (osm-9-like TRP channel 4) (OTRPC4)(Vanilloid receptor-like channel 2) (Vanilloid receptor-likeprotein 2) (VRL-2)1471Vascular endothelial growth factor D precursor (VEGF-D)O43915(c-fos-induced growth factor) (FIGF)1472Vascular endothelial growth factor receptor 1 precursorP17948(EC 2.7.10.1) (VEGFR-1) (Vascular permeability factorreceptor) (Tyrosine-protein kinase receptor FLT) (Flt-1)(Tyrosine-protein kinase FRT) (Fms-like tyrosine kinase 1)1473Proto-oncogene C-crk (P38) (Adapter molecule crk)P461081474VDUP1 protein (Thioredoxin interacting protein)Q9H3M71475VimentinP086701476HUMAN CTCL tumor antigen HD-CL-06 (VimentinQ548L2variant)1477Vinculin (Metavinculin)P182061478Integrin alpha-3 precursor (Galactoprotein B3) (GAPB3)P26006(VLA-3 alpha chain) (FRP-2) (CD49c antigen) [Contains:Integrin alpha-3 heavy chain; Integrin alpha-3 light chain]1479Voltage-dependent T-type calcium channel alpha-1HO95180subunit (Voltage-gated calcium channel alpha subunitCav3.2) (Low-voltage-activated calcium channel alpha13.2 subunit)1480Wiskott-Aldrich syndrome protein family member 4Q8IV90(WASP-family protein member 4)1481ATP synthase coupling factor 6, mitochondrial precursorP18859(EC 3.6.3.14) (ATPase subunit F6)1482Proto-oncogene protein Wnt-3 precursorP567031483Amyloid beta A4 precursor protein-binding family AQ99767member 2 (Neuron-specific X11L protein) (NeuronalMunc18-1-interacting protein 2) (Mint-2) (Adapter proteinX11beta)1484Zinc finger CCHC domain-containing protein 5Q8N8U31485Myeloid/lymphoid or mixed-lineage leukemia (TrithoraxQ59FF2homolog, Drosophila) variant1486Zinc finger protein DZIP1 (DAZ-interacting protein 1/2)Q86YF91487Hypothetical protein DKFZp761O1618Q69YS51488ATP-binding cassette sub-family F member 2 (Iron-Q9UG63inhibited ABC transporter 2)1489Ribosome biogenesis protein BOP1 (Block of proliferationQ141371 protein)1490CDNA FLJ13765 fis, clone PLACE4000128Q9H8C51491NDRG1 protein (N-myc downstream regulated gene 1Q92597protein)1492Pre-mRNA splicing factor ATP-dependent RNA helicaseQ92620PRP161493Nesprin 2 (Nuclear envelope spectrin repeat protein 2)Q9NU501494Adenomatous polyposis coliP250541495Ubiquitin conjugating enzyme E2P494591496B cell receptor-associated protein BAP31 (CDM protein)P55726c6-AG1497Topoisomerase II-alphaP113881498Topoisomerase II betaQ028801499Integrin beta8 subunit precursorP260121500Replication Protein AP276941501Abl Binding protein 3U310891502Cyclin IQ140941503Cell Division Control Protein 2 (CDC2)P064931504Septin 2 (NEDD5)Q150191505STAT1 alpha/betaP422241506LDL Receptor-related protein (LRP)Q079541507TACE (ADAM17)NP-0686041508Junction plakoglobin (gamma catenin)P149231509EDDR1 (rtk6), h-RYKQ083451510IP3 receptor type IIQ145711511Melanoma-associated antigen D2 (MAGE-D2 antigen)Q9UNF1(MAGE-D) (Breast cancer-associated gene 1 protein)(BCG-1) (11B6) (Hepatocellular carcinoma-associatedprotein JCL-1)1512Melanoma-associated antigen 4 (MAGE-4 antigen)P43358(MAGE-X2) (MAGE-41)1513HUMAN Retinoblastoma-like protein 2 (130 kDaQ08999retinoblastoma-associated protein) (PRB2) (P130) (RBR-2)","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"}},"description_lang":["en"],"has_description":true,"has_docdb":true,"has_inpadoc":true,"has_full_text":true,"biblio_lang":"en"},"jurisdiction":"US","collections":[],"usersTags":[],"lensId":"125-560-489-712-087","publicationKey":"US_2008_0207497_A1","displayKey":"US 2008/0207497 A1","docAssets":{"lensId":"125-560-489-712-087","pdfUrl":"https://www.lens.org/images/patent/US/20080207497/A1/US_2008_0207497_A1.pdf","images":[{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000001.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000001.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000002.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000002.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000003.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000003.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000004.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000004.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000005.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000005.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000006.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000006.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000007.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000007.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000008.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000008.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000009.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000009.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000010.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000010.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000011.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000011.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000012.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000012.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000013.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000013.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000014.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000014.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000015.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000015.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000016.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000016.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000017.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000017.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000018.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000018.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000019.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000019.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000020.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000020.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000021.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000021.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000022.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000022.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000023.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000023.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000024.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000024.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000025.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000025.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000026.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000026.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000027.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000027.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000028.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000028.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000029.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000029.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000030.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000030.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000031.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000031.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000032.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000032.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000033.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000033.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000034.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000034.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000035.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000035.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000036.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000036.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000037.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000037.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000038.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000038.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000039.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000039.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000040.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000040.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000041.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000041.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000042.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000042.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000043.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000043.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000044.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000044.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000045.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000045.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000046.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000046.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000047.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000047.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000048.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000048.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000049.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000049.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000050.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000050.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000051.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000051.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000052.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000052.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000053.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000053.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000054.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000054.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000055.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000055.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000056.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000056.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000057.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000057.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000058.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000058.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000059.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000059.png"},{"thumb":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/10pc/00000060.png","full":"https://s3-us-west-2.amazonaws.com/lens-resource/patent/US/A1/20080207/20080207497/image/page/full/00000060.png"}],"fallover":false},"countryName":"USA","inventorModel":{"inventors":[{"name":{"value":"RAMAKRISHNA VENKY","valueNormalised":"Ramakrishna Venky"},"inventorship":null},{"name":{"value":"ROSS MARK M","valueNormalised":"Ross Mark M"},"inventorship":null},{"name":{"value":"PHILIP RAMILA","valueNormalised":"Philip Ramila"},"inventorship":null},{"name":{"value":"KELLER LORRAINE H","valueNormalised":"Keller Lorraine H"},"inventorship":null}],"inventorships":[],"unmatchedInventorships":[],"activeUserHasInventorship":false},"simpleFamilyId":192478061,"citesPatentCount":20,"countrySpec":{"countryName":"USA","description":"FIRST PUBLISHED PATENT APPLICATION [FROM 2001 ONWARDS]","rule":"pubdate:AFTER:15-03-2001","docType":"PATENT_APPLICATION"},"pageTitle":"US 2008/0207497 A1 - Cytotoxic T-Lymphocyte-Inducing Immunogens For Prevention, Treatment, And Diagnosis Of Cancer","documentTitle":"Cytotoxic T-Lymphocyte-Inducing Immunogens For Prevention, Treatment, And Diagnosis Of Cancer"},"claims":{"source":"xml_claims","claims":[{"lines":["A method for treating a subject with cancer, said cancer characterized by tumor cells expressing any class I MHC molecule, comprising administering to said subject a composition comprising\n
at least one polypeptide comprising an epitopic peptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 1 to 791 and 1514 to 1533 in an amount sufficient to induce a CTL response to said tumor cells; or\n
at least one polypeptide comprising an epitopic peptide having at least one amino acid difference from an amino acid sequence selected from the group consisting of SEQ ID NO: 1 to 791 and 1514 to 1533 in an amount sufficient to induce a CTL response to said tumor cells."],"number":1,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 1, wherein said amino acid difference from an amino acid sequence selected from the group consisting of SEQ ID NO: 1 to 791 and 1514 to 1533 is the result of a conservative amino acid substitution."],"number":2,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 1, wherein said amino acid difference from an amino acid sequence selected from the group consisting of SEQ ID NO: 1 to 791 and 1514 to 1533 is the result of a substitution of one hydrophobic amino acid with another hydrophobic amino acid."],"number":3,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 1, wherein said amino acid difference from an amino acid sequence selected from the group consisting of SEQ ID NO: 1 to 791 and 1514 to 1533 is the result of an addition or deletion of one amino acid to or from said epitopic peptide."],"number":4,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 1, wherein said composition further comprises an adjuvant."],"number":5,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 5, wherein said adjuvant is selected from the group consisting of complete Freund's adjuvant, incomplete Freund's adjuvant, Montanide ISA-51, LAG-3, aluminum phosphate, aluminum hydroxide, alum, and saponin."],"number":6,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 1, wherein said composition further comprises a cytokine."],"number":7,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 5, wherein said cytokine is selected from the group consisting of IL-1, IL-2, IL-7, IL-12, IL-15, TNF, SCF and GM-CSF."],"number":8,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 1, where in said composition further comprises a vehicle."],"number":9,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 9, where said vehicle is selected from the group consisting of a liposome, an immunostimulating complex (ISCOM), and slow-releasing particles."],"number":10,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 10, where in said liposome comprises an emulsion, a foam, a micel, an insoluble monolayer, a liquid crystal, a phospholipid dispersion, or a lamellar layer."],"number":11,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 1, wherein said polypeptide consists of\n
an amino acid sequence selected from the group consisting of SEQ ID NO: 1 to 791 and 1514 to 1533; or\n
an amino acid sequence having at least one amino acid difference from an amino acid sequence selected from the group consisting of SEQ ID NO: 1 to 791 and 1514 to 1533."],"number":12,"annotation":false,"title":false,"claim":true},{"lines":["A method for treating a subject with cancer, said cancer characterized by tumor cells expressing any class I MHC molecule, said method comprising administering to said subject a composition comprising a polynucleotide comprising a nucleic acid sequence encoding\n
at least one polypeptide comprising an epitopic peptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 1 to 791 and 1514 to 1533 in an amount sufficient to induce a CTL response to said tumor cells; or\n
at least one polypeptide comprising an epitopic peptide comprising one amino acid difference from an amino acid sequence selected from the group consisting of SEQ ID NO: 1 to 791 and 1514 to 1533 in an amount sufficient to induce a CTL response to said tumor cells."],"number":13,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 13, wherein said polynucleotide further comprises an expression vector."],"number":14,"annotation":false,"title":false,"claim":true},{"lines":["15-23. (canceled)"],"number":-1,"annotation":false,"title":false,"claim":true},{"lines":["A method for treating a subject with cancer, said cancer characterized by tumor cells expressing any class I MHC molecule and a gene coding for an epitopic sequence of at least one of SEQ ID NO: 792 to 1513, whereby the CTLs of claim 20 are administered in an amount sufficient to destroy the tumor cells through direct lysis or to effect the destruction of the tumor cells indirectly through the elaboration of cytokines."],"number":24,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 1 wherein said cancer is carcinoma."],"number":25,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 1 wherein said cancer is ovarian carcinoma."],"number":26,"annotation":false,"title":false,"claim":true},{"lines":["27-30. (canceled)"],"number":-1,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 1 wherein said polypeptide comprises at least two epitopic peptides."],"number":31,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 31 wherein said polypeptide comprises at least three epitopic peptides."],"number":32,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 31, said polypeptide comprising a first epitopic peptide and a second epitopic peptide, wherein said first epitopic peptide comprises the amino acid sequence of SEQ ID NO: 1 to 791 and 1514 to 1533 and said second epitopic peptide comprises an amino acid sequence selected from the group consisting of SEQ ID NOS: 1 to 791 and 1514 to 1533."],"number":33,"annotation":false,"title":false,"claim":true}]}},"filters":{"npl":[],"notNpl":[],"applicant":[],"notApplicant":[],"inventor":[],"notInventor":[],"owner":[],"notOwner":[],"tags":[],"dates":[],"types":[],"notTypes":[],"j":[],"notJ":[],"fj":[],"notFj":[],"classIpcr":[],"notClassIpcr":[],"classNat":[],"notClassNat":[],"classCpc":[],"notClassCpc":[],"so":[],"notSo":[],"sat":[]},"sequenceFilters":{"s":"SEQIDNO","d":"ASCENDING","p":0,"n":10,"sp":[],"si":[],"len":[],"t":[],"loc":[]}}