CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008390
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Breast cancer type 2 susceptibility protein 
Protein Synonyms/Alias
 Fanconi anemia group D1 protein 
Gene Name
 BRCA2 
Gene Synonyms/Alias
 FACD; FANCD1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
241SNHDESLKKNDRFIAubiquitination[1]
242NHDESLKKNDRFIASubiquitination[1]
454PRISSLPKSEKPLNEacetylation[2]
457SSLPKSEKPLNEETVubiquitination[1]
757DTDFQSQKSLLYDHEubiquitination[1, 3]
799YKMSDKLKGNNYESDubiquitination[3]
811ESDVELTKNIPMEKNubiquitination[3]
817TKNIPMEKNQDVCALubiquitination[1, 3]
829CALNENYKNVELLPPubiquitination[1, 3]
838VELLPPEKYMRVASPubiquitination[3]
848RVASPSRKVQFNQNTubiquitination[1]
862TNLRVIQKNQEETTSubiquitination[1, 3]
907NLALGNTKELHETDLubiquitination[3]
985NIDKIPEKNNDYMNKubiquitination[1, 3]
1094TPQMLFSKQDFNSNHubiquitination[1, 3]
1132FEFTQFRKPSYILQKubiquitination[1]
1139KPSYILQKSTFEVPEubiquitination[3]
1153ENQMTILKTTSEECRubiquitination[3]
1202LLKNDCNKSASGYLTubiquitination[1, 3]
1226FYSAHGTKLNVSTEAubiquitination[3]
1236VSTEALQKAVKLFSDubiquitination[1]
1239EALQKAVKLFSDIENubiquitination[3]
1323NTENEDNKYTAASRNubiquitination[1, 3]
1381KEGNTQIKEDLSDLTubiquitination[1, 3]
1406CHGNTSNKEQLTATKubiquitination[1, 3]
1419TKTEQNIKDFETSDTubiquitination[1, 3]
1434FFQTASGKNISVAKEubiquitination[3]
1440GKNISVAKESFNKIVubiquitination[1, 3]
1474HSDIRKNKMDILSYEubiquitination[1, 3]
1549VKNLFDEKEQGTSEIubiquitination[3]
1568HQWAKTLKYREACKDubiquitination[1]
1631TENLKTSKSIFLKVKubiquitination[3]
1678FYTSCSRKTSVSQTSubiquitination[3]
1729STIAENDKNHLSEKQubiquitination[3]
1767SGYLSKNKLDSGIEPubiquitination[1, 3]
1777SGIEPVLKNVEDQKNubiquitination[3]
1783LKNVEDQKNTSFSKVubiquitination[1, 3]
1789QKNTSFSKVISNVKDubiquitination[1, 3]
1863HETIKKVKDIFTDSFubiquitination[1]
1872IFTDSFSKVIKENNEubiquitination[1, 3, 4, 5]
1944SGLEKVSKISPCDVSubiquitination[1, 3]
1959LETSDICKCSIGKLHubiquitination[1, 3]
1984IFSTASGKSVQVSDAubiquitination[1, 3]
2013STKQVFSKVLFKSNEubiquitination[1, 3]
2017VFSKVLFKSNEHSDQubiquitination[1, 3]
2077ESSLHKVKGVLEEFDubiquitination[1, 3]
2104TSRQNVSKILPRVDKubiquitination[1, 3]
2124CVNSEMEKTCSKEFKubiquitination[1, 3]
2150SENNHSIKVSPYLSQubiquitination[1, 3]
2162LSQFQQDKQQLVLGTubiquitination[1, 3]
2191QASPKNVKMEIGKTEubiquitination[3]
2196NVKMEIGKTETFSDVubiquitination[1, 3]
2244DDELTDSKLPSHATHubiquitination[1]
2286LVGEPSIKRNLLNEFubiquitination[1, 3]
2302RIIENQEKSLKASKSubiquitination[1, 3]
2308EKSLKASKSTPDGTIubiquitination[3]
2404ITTGRPTKVFVPPFKubiquitination[1]
2411KVFVPPFKTKSHFHRubiquitination[1]
2448GSDDSKNKINDNEIHubiquitination[3]
2459NEIHQFNKNNSNQAAubiquitination[3]
2472AAAVTFTKCEEEPLDubiquitination[1]
2514PGSLYLAKTSTLPRIubiquitination[1]
2538VPSACSHKQLYTYGVubiquitination[1, 3]
2577KESLWTGKGIQLADGubiquitination[1]
2597SNDGKAGKEEFYRALubiquitination[1, 3]
2657ERVLLQLKYRYDTEIubiquitination[1]
2741PPLLAVLKNGRLTVGubiquitination[1, 3]
2882EHEENTTKPYLPSRAubiquitination[1]
2958AMESAEQKEQGLSRDubiquitination[3]
3032IQLAATKKTQYQQLPubiquitination[1]
3196PKWSTPTKDCTSGPYubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [3] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 
Functional Description
 Involved in double-strand break repair and/or homologous recombination. Binds RAD51 and potentiates recombinational DNA repair by promoting assembly of RAD51 onto single-stranded DNA (ssDNA). Acts by targeting RAD51 to ssDNA over double-stranded DNA, enabling RAD51 to displace replication protein-A (RPA) from ssDNA and stabilizing RAD51-ssDNA filaments by blocking ATP hydrolysis. May participate in S phase checkpoint activation. Binds selectively to ssDNA, and to ssDNA in tailed duplexes and replication fork structures. In concert with NPM1, regulates centrosome duplication. 
Sequence Annotation
 REPEAT 1002 1036 BRCA2 1.
 REPEAT 1212 1246 BRCA2 2.
 REPEAT 1421 1455 BRCA2 3.
 REPEAT 1517 1551 BRCA2 4.
 REPEAT 1664 1698 BRCA2 5.
 REPEAT 1837 1871 BRCA2 6.
 REPEAT 1971 2005 BRCA2 7.
 REPEAT 2051 2085 BRCA2 8.
 REGION 1 40 Interaction with PALB2.
 REGION 639 1000 Interaction with NPM1.
 REGION 2350 2545 Interaction with FANCD2.
 MOD_RES 755 755 Phosphoserine.
 MOD_RES 3291 3291 Phosphoserine; by CDK1 and CDK2.
 MOD_RES 3387 3387 Phosphothreonine; by CHEK1 and CHEK2.  
Keyword
 3D-structure; Cell cycle; Complete proteome; Disease mutation; DNA damage; DNA recombination; DNA repair; DNA-binding; Fanconi anemia; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Tumor suppressor; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 3418 AA 
Protein Sequence
MPIGSKERPT FFEIFKTRCN KADLGPISLN WFEELSSEAP PYNSEPAEES EHKNNNYEPN 60
LFKTPQRKPS YNQLASTPII FKEQGLTLPL YQSPVKELDK FKLDLGRNVP NSRHKSLRTV 120
KTKMDQADDV SCPLLNSCLS ESPVVLQCTH VTPQRDKSVV CGSLFHTPKF VKGRQTPKHI 180
SESLGAEVDP DMSWSSSLAT PPTLSSTVLI VRNEEASETV FPHDTTANVK SYFSNHDESL 240
KKNDRFIASV TDSENTNQRE AASHGFGKTS GNSFKVNSCK DHIGKSMPNV LEDEVYETVV 300
DTSEEDSFSL CFSKCRTKNL QKVRTSKTRK KIFHEANADE CEKSKNQVKE KYSFVSEVEP 360
NDTDPLDSNV AHQKPFESGS DKISKEVVPS LACEWSQLTL SGLNGAQMEK IPLLHISSCD 420
QNISEKDLLD TENKRKKDFL TSENSLPRIS SLPKSEKPLN EETVVNKRDE EQHLESHTDC 480
ILAVKQAISG TSPVASSFQG IKKSIFRIRE SPKETFNASF SGHMTDPNFK KETEASESGL 540
EIHTVCSQKE DSLCPNLIDN GSWPATTTQN SVALKNAGLI STLKKKTNKF IYAIHDETSY 600
KGKKIPKDQK SELINCSAQF EANAFEAPLT FANADSGLLH SSVKRSCSQN DSEEPTLSLT 660
SSFGTILRKC SRNETCSNNT VISQDLDYKE AKCNKEKLQL FITPEADSLS CLQEGQCEND 720
PKSKKVSDIK EEVLAAACHP VQHSKVEYSD TDFQSQKSLL YDHENASTLI LTPTSKDVLS 780
NLVMISRGKE SYKMSDKLKG NNYESDVELT KNIPMEKNQD VCALNENYKN VELLPPEKYM 840
RVASPSRKVQ FNQNTNLRVI QKNQEETTSI SKITVNPDSE ELFSDNENNF VFQVANERNN 900
LALGNTKELH ETDLTCVNEP IFKNSTMVLY GDTGDKQATQ VSIKKDLVYV LAEENKNSVK 960
QHIKMTLGQD LKSDISLNID KIPEKNNDYM NKWAGLLGPI SNHSFGGSFR TASNKEIKLS 1020
EHNIKKSKMF FKDIEEQYPT SLACVEIVNT LALDNQKKLS KPQSINTVSA HLQSSVVVSD 1080
CKNSHITPQM LFSKQDFNSN HNLTPSQKAE ITELSTILEE SGSQFEFTQF RKPSYILQKS 1140
TFEVPENQMT ILKTTSEECR DADLHVIMNA PSIGQVDSSK QFEGTVEIKR KFAGLLKNDC 1200
NKSASGYLTD ENEVGFRGFY SAHGTKLNVS TEALQKAVKL FSDIENISEE TSAEVHPISL 1260
SSSKCHDSVV SMFKIENHND KTVSEKNNKC QLILQNNIEM TTGTFVEEIT ENYKRNTENE 1320
DNKYTAASRN SHNLEFDGSD SSKNDTVCIH KDETDLLFTD QHNICLKLSG QFMKEGNTQI 1380
KEDLSDLTFL EVAKAQEACH GNTSNKEQLT ATKTEQNIKD FETSDTFFQT ASGKNISVAK 1440
ESFNKIVNFF DQKPEELHNF SLNSELHSDI RKNKMDILSY EETDIVKHKI LKESVPVGTG 1500
NQLVTFQGQP ERDEKIKEPT LLGFHTASGK KVKIAKESLD KVKNLFDEKE QGTSEITSFS 1560
HQWAKTLKYR EACKDLELAC ETIEITAAPK CKEMQNSLNN DKNLVSIETV VPPKLLSDNL 1620
CRQTENLKTS KSIFLKVKVH ENVEKETAKS PATCYTNQSP YSVIENSALA FYTSCSRKTS 1680
VSQTSLLEAK KWLREGIFDG QPERINTADY VGNYLYENNS NSTIAENDKN HLSEKQDTYL 1740
SNSSMSNSYS YHSDEVYNDS GYLSKNKLDS GIEPVLKNVE DQKNTSFSKV ISNVKDANAY 1800
PQTVNEDICV EELVTSSSPC KNKNAAIKLS ISNSNNFEVG PPAFRIASGK IVCVSHETIK 1860
KVKDIFTDSF SKVIKENNEN KSKICQTKIM AGCYEALDDS EDILHNSLDN DECSTHSHKV 1920
FADIQSEEIL QHNQNMSGLE KVSKISPCDV SLETSDICKC SIGKLHKSVS SANTCGIFST 1980
ASGKSVQVSD ASLQNARQVF SEIEDSTKQV FSKVLFKSNE HSDQLTREEN TAIRTPEHLI 2040
SQKGFSYNVV NSSAFSGFST ASGKQVSILE SSLHKVKGVL EEFDLIRTEH SLHYSPTSRQ 2100
NVSKILPRVD KRNPEHCVNS EMEKTCSKEF KLSNNLNVEG GSSENNHSIK VSPYLSQFQQ 2160
DKQQLVLGTK VSLVENIHVL GKEQASPKNV KMEIGKTETF SDVPVKTNIE VCSTYSKDSE 2220
NYFETEAVEI AKAFMEDDEL TDSKLPSHAT HSLFTCPENE EMVLSNSRIG KRRGEPLILV 2280
GEPSIKRNLL NEFDRIIENQ EKSLKASKST PDGTIKDRRL FMHHVSLEPI TCVPFRTTKE 2340
RQEIQNPNFT APGQEFLSKS HLYEHLTLEK SSSNLAVSGH PFYQVSATRN EKMRHLITTG 2400
RPTKVFVPPF KTKSHFHRVE QCVRNINLEE NRQKQNIDGH GSDDSKNKIN DNEIHQFNKN 2460
NSNQAAAVTF TKCEEEPLDL ITSLQNARDI QDMRIKKKQR QRVFPQPGSL YLAKTSTLPR 2520
ISLKAAVGGQ VPSACSHKQL YTYGVSKHCI KINSKNAESF QFHTEDYFGK ESLWTGKGIQ 2580
LADGGWLIPS NDGKAGKEEF YRALCDTPGV DPKLISRIWV YNHYRWIIWK LAAMECAFPK 2640
EFANRCLSPE RVLLQLKYRY DTEIDRSRRS AIKKIMERDD TAAKTLVLCV SDIISLSANI 2700
SETSSNKTSS ADTQKVAIIE LTDGWYAVKA QLDPPLLAVL KNGRLTVGQK IILHGAELVG 2760
SPDACTPLEA PESLMLKISA NSTRPARWYT KLGFFPDPRP FPLPLSSLFS DGGNVGCVDV 2820
IIQRAYPIQW MEKTSSGLYI FRNEREEEKE AAKYVEAQQK RLEALFTKIQ EEFEEHEENT 2880
TKPYLPSRAL TRQQVRALQD GAELYEAVKN AADPAYLEGY FSEEQLRALN NHRQMLNDKK 2940
QAQIQLEIRK AMESAEQKEQ GLSRDVTTVW KLRIVSYSKK EKDSVILSIW RPSSDLYSLL 3000
TEGKRYRIYH LATSKSKSKS ERANIQLAAT KKTQYQQLPV SDEILFQIYQ PREPLHFSKF 3060
LDPDFQPSCS EVDLIGFVVS VVKKTGLAPF VYLSDECYNL LAIKFWIDLN EDIIKPHMLI 3120
AASNLQWRPE SKSGLLTLFA GDFSVFSASP KEGHFQETFN KMKNTVENID ILCNEAENKL 3180
MHILHANDPK WSTPTKDCTS GPYTAQIIPG TGNKLLMSSP NCEIYYQSPL SLCMAKRKSV 3240
STPVSAQMTS KSCKGEKEID DQKNCKKRRA LDFLSRLPLP PPVSPICTFV SPAAQKAFQP 3300
PRSCGTKYET PIKKKELNSP QMTPFKKFNE ISLLESNSIA DEELALINTQ ALLSGSTGEK 3360
QFISVSESTR TAPTSSEDYL RLKRRCTTSL IKEQESSQAS TEECEKNKQD TITTKKYI 3418 
Gene Ontology
 GO:0033593; C:BRCA2-MAGE-D1 complex; IDA:UniProtKB.
 GO:0005813; C:centrosome; IDA:UniProtKB.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0030141; C:secretory granule; IDA:UniProtKB.
 GO:0010484; F:H3 histone acetyltransferase activity; IDA:UniProtKB.
 GO:0010485; F:H4 histone acetyltransferase activity; IDA:UniProtKB.
 GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
 GO:0007420; P:brain development; IEA:Compara.
 GO:0007569; P:cell aging; IEA:Compara.
 GO:0051298; P:centrosome duplication; IMP:UniProtKB.
 GO:0000910; P:cytokinesis; IDA:UniProtKB.
 GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; IEA:Compara.
 GO:0000724; P:double-strand break repair via homologous recombination; IDA:UniProtKB.
 GO:0008585; P:female gonad development; IEA:Compara.
 GO:0030097; P:hemopoiesis; IEA:Compara.
 GO:0001833; P:inner cell mass cell proliferation; IEA:Compara.
 GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IEA:Compara.
 GO:0007141; P:male meiosis I; IEA:Compara.
 GO:0033600; P:negative regulation of mammary gland epithelial cell proliferation; IDA:UniProtKB.
 GO:0006289; P:nucleotide-excision repair; IMP:UniProtKB.
 GO:0001556; P:oocyte maturation; IEA:Compara.
 GO:0045931; P:positive regulation of mitotic cell cycle; IEA:Compara.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:UniProtKB.
 GO:0032465; P:regulation of cytokinesis; IEA:Compara.
 GO:0048478; P:replication fork protection; IEA:Compara.
 GO:0010332; P:response to gamma radiation; IEA:Compara.
 GO:0010225; P:response to UV-C; IEA:Compara.
 GO:0010165; P:response to X-ray; IEA:Compara.
 GO:0007283; P:spermatogenesis; IEA:Compara. 
Interpro
 IPR015525; BRCA2.
 IPR015187; BRCA2_OB_1.
 IPR015188; BRCA2_OB_3.
 IPR002093; BRCA2_repeat.
 IPR015252; DNA_recomb/repair_BRCA2_hlx.
 IPR012340; NA-bd_OB-fold.
 IPR015205; Tower. 
Pfam
 PF09169; BRCA-2_helical
 PF09103; BRCA-2_OB1
 PF09104; BRCA-2_OB3
 PF00634; BRCA2
 PF09121; Tower 
SMART
  
PROSITE
 PS50138; BRCA2_REPEAT 
PRINTS