CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019777
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 BRCA1-associated RING domain protein 1 
Protein Synonyms/Alias
 BARD-1 
Gene Name
 BARD1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
110SMIQLCSKLRNLLHDubiquitination[1]
124DNELSDLKEDKPRKSacetylation[2]
160KVRYVVSKASVQTQPubiquitination[3, 4]
171QTQPAIKKDASAQQDubiquitination[1]
371SPPSCKRKVGGTSGRacetylation[2]
423LLPNMAVKRNHRGETubiquitination[4, 5]
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] 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]
 [4] 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]
 [5] Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry.
 Denis NJ, Vasilescu J, Lambert JP, Smith JC, Figeys D.
 Proteomics. 2007 Mar;7(6):868-74. [PMID: 17370265] 
Functional Description
 Probable E3 ubiquitin-protein ligase. The BRCA1-BARD1 heterodimer specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Plays a central role in the control of the cell cycle in response to DNA damage. Acts by mediating ubiquitin E3 ligase activity that is required for its tumor suppressor function. Also forms a heterodimer with CSTF1/CSTF-50 to modulate mRNA processing and RNAP II stability by inhibiting pre-mRNA 3' cleavage. 
Sequence Annotation
 REPEAT 427 459 ANK 1.
 REPEAT 460 492 ANK 2.
 REPEAT 493 525 ANK 3.
 REPEAT 526 546 ANK 4; degenerate.
 DOMAIN 560 653 BRCT 1.
 DOMAIN 667 777 BRCT 2.
 ZN_FING 50 87 RING-type.
 REGION 26 119 Interaction with BRCA1.
 REGION 554 558 Flexible linker.
 MOD_RES 391 391 Phosphoserine.
 MOD_RES 394 394 Phosphothreonine.
 CROSSLNK 423 423 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; ANK repeat; Complete proteome; DNA damage; DNA repair; Isopeptide bond; Ligase; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 777 AA 
Protein Sequence
MPDNRQPRNR QPRIRSGNEP RSAPAMEPDG RGAWAHSRAA LDRLEKLLRC SRCTNILREP 60
VCLGGCEHIF CSNCVSDCIG TGCPVCYTPA WIQDLKINRQ LDSMIQLCSK LRNLLHDNEL 120
SDLKEDKPRK SLFNDAGNKK NSIKMWFSPR SKKVRYVVSK ASVQTQPAIK KDASAQQDSY 180
EFVSPSPPAD VSERAKKASA RSGKKQKKKT LAEINQKWNL EAEKEDGEFD SKEESKQKLV 240
SFCSQPSVIS SPQINGEIDL LASGSLTESE CFGSLTEVSL PLAEQIESPD TKSRNEVVTP 300
EKVCKNYLTS KKSLPLENNG KRGHHNRLSS PISKRCRTSI LSTSGDFVKQ TVPSENIPLP 360
ECSSPPSCKR KVGGTSGRKN SNMSDEFISL SPGTPPSTLS SSSYRRVMSS PSAMKLLPNM 420
AVKRNHRGET LLHIASIKGD IPSVEYLLQN GSDPNVKDHA GWTPLHEACN HGHLKVVELL 480
LQHKALVNTT GYQNDSPLHD AAKNGHVDIV KLLLSYGASR NAVNIFGLRP VDYTDDESMK 540
SLLLLPEKNE SSSASHCSVM NTGQRRDGPL VLIGSGLSSE QQKMLSELAV ILKAKKYTEF 600
DSTVTHVVVP GDAVQSTLKC MLGILNGCWI LKFEWVKACL RRKVCEQEEK YEIPEGPRRS 660
RLNREQLLPK LFDGCYFYLW GTFKHHPKDN LIKLVTAGGG QILSRKPKPD SDVTQTINTV 720
AYHARPDSDQ RFCTQYIIYE DLCNYHPERV RQGKVWKAPS SWFIDCVMSF ELLPLDS 777 
Gene Ontology
 GO:0070531; C:BRCA1-A complex; IDA:UniProtKB.
 GO:0031436; C:BRCA1-BARD1 complex; IDA:UniProtKB.
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0019900; F:kinase binding; NAS:UniProtKB.
 GO:0003723; F:RNA binding; IDA:MGI.
 GO:0004842; F:ubiquitin-protein ligase activity; NAS:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0007050; P:cell cycle arrest; NAS:UniProtKB.
 GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
 GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
 GO:0031441; P:negative regulation of mRNA 3'-end processing; NAS:UniProtKB.
 GO:0046826; P:negative regulation of protein export from nucleus; IDA:UniProtKB.
 GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
 GO:0045732; P:positive regulation of protein catabolic process; NAS:UniProtKB.
 GO:0085020; P:protein K6-linked ubiquitination; IDA:UniProtKB.
 GO:0042325; P:regulation of phosphorylation; IMP:UniProtKB.
 GO:0006974; P:response to DNA damage stimulus; NAS:UniProtKB.
 GO:0001894; P:tissue homeostasis; TAS:UniProtKB. 
Interpro
 IPR002110; Ankyrin_rpt.
 IPR020683; Ankyrin_rpt-contain_dom.
 IPR001357; BRCT_dom.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD.
 IPR017907; Znf_RING_CS. 
Pfam
 PF00023; Ank
 PF00533; BRCT 
SMART
 SM00248; ANK
 SM00292; BRCT
 SM00184; RING 
PROSITE
 PS50297; ANK_REP_REGION
 PS50088; ANK_REPEAT
 PS50172; BRCT
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS
 PR01415; ANKYRIN.