CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019586
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 BRCA1-A complex subunit RAP80 
Protein Synonyms/Alias
 Receptor-associated protein 80; Retinoid X receptor-interacting protein 110; Ubiquitin interaction motif-containing protein 1 
Gene Name
 UIMC1 
Gene Synonyms/Alias
 RAP80; RXRIP110 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
20ESRNLEKKDVETTSSubiquitination[1]
31TTSSVSVKRKRRLEDubiquitination[1, 2, 3, 4]
90EQFALALKMSEQEARubiquitination[4]
245GRGSAFLKAVQGSGDubiquitination[1, 2, 3, 4]
265LPTLADAKGLQDTGGubiquitination[1]
374SDWHSKTKDFQESSIubiquitination[1, 4]
382DFQESSIKSLKEKLLubiquitination[2, 3, 4]
387SIKSLKEKLLLEEEPubiquitination[4]
428SVAALTSKRSLVLMPubiquitination[4]
480VRIIMADKEVGNKEDubiquitination[5]
485ADKEVGNKEDAEKEVubiquitination[4, 5]
544RQKEAKTKSDSGTAAubiquitination[1, 3, 4, 5]
559QTSLDIDKNEKCYLCubiquitination[5]
567NEKCYLCKSLVPFREubiquitination[1]
587DSCLQLAKADQGDGPubiquitination[3, 4, 5]
607ACSTVEGKWQQRLKNubiquitination[1]
642KTSDADIKSSETGAFubiquitination[5]
Reference
 [1] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [2] 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]
 [3] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [5] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983] 
Functional Description
 Ubiquitin-binding protein that specifically recognizes and binds 'Lys-63'-linked ubiquitin. Plays a central role in the BRCA1-A complex by specifically binding 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). The BRCA1-A complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. Also weakly binds monoubiquitin but with much less affinity than 'Lys-63'-linked ubiquitin. May interact with monoubiquitinated histones H2A and H2B; the relevance of such results is however unclear in vivo. Does not bind Lys-48'-linked ubiquitin. May indirectly act as a transcriptional repressor by inhibiting the interaction of NR6A1 with the corepressor NCOR1. 
Sequence Annotation
 REPEAT 79 96 UIM 1.
 REPEAT 104 124 UIM 2.
 REGION 1 101 Necessary for transcriptional repression.
 REGION 97 103 UIM-linker.
 REGION 100 200 Necessary for interaction with NR6A1 N-
 REGION 270 400 AIR.
 REGION 400 500 Necessary for interaction with NR6A1 C-
 REGION 505 582 Zinc-finger-like region.
 MOTIF 60 78 LR motif.
 MOD_RES 44 44 Phosphoserine.
 MOD_RES 46 46 Phosphoserine.
 MOD_RES 101 101 Phosphoserine.
 MOD_RES 140 140 Phosphoserine.
 MOD_RES 205 205 Phosphoserine.
 MOD_RES 402 402 Phosphoserine.
 MOD_RES 419 419 Phosphoserine.
 MOD_RES 627 627 Phosphoserine.
 MOD_RES 653 653 Phosphoserine.
 MOD_RES 677 677 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; Chromatin regulator; Complete proteome; DNA damage; DNA repair; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Transcription; Transcription regulation; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 719 AA 
Protein Sequence
MPRRKKKVKE VSESRNLEKK DVETTSSVSV KRKRRLEDAF IVISDSDGEE PKEENGLQKT 60
KTKQSNRAKC LAKRKIAQMT EEEQFALALK MSEQEAREVN SQEEEEEELL RKAIAESLNS 120
CRPSDASATR SRPLATGPSS QSHQEKTTDS GLTEGIWQLV PPSLFKGSHI SQGNEAEERE 180
EPWDHTEKTE EEPVSGSSGS WDQSSQPVFE NVNVKSFDRC TGHSAEHTQC GKPQESTGRG 240
SAFLKAVQGS GDTSRHCLPT LADAKGLQDT GGTVNYFWGI PFCPDGVDPN QYTKVILCQL 300
EVYQKSLKMA QRQLLNKKGF GEPVLPRPPS LIQNECGQGE QASEKNECIS EDMGDEDKEE 360
RQESRASDWH SKTKDFQESS IKSLKEKLLL EEEPTTSHGQ SSQGIVEETS EEGNSVPASQ 420
SVAALTSKRS LVLMPESSAE EITVCPETQL SSSETFDLER EVSPGSRDIL DGVRIIMADK 480
EVGNKEDAEK EVAISTFSSS NQVSCPLCDQ CFPPTKIERH AMYCNGLMEE DTVLTRRQKE 540
AKTKSDSGTA AQTSLDIDKN EKCYLCKSLV PFREYQCHVD SCLQLAKADQ GDGPEGSGRA 600
CSTVEGKWQQ RLKNPKEKGH SEGRLLSFLE QSEHKTSDAD IKSSETGAFR VPSPGMEEAG 660
CSREMQSSFT RRDLNESPVK SFVSISEATD CLVDFKKQVT VQPGSRTRTK AGRGRRRKF 719 
Gene Ontology
 GO:0070531; C:BRCA1-A complex; IDA:UniProtKB.
 GO:0042393; F:histone binding; IDA:UniProtKB.
 GO:0070530; F:K63-linked polyubiquitin binding; IDA:UniProtKB.
 GO:0006302; P:double-strand break repair; IMP:UniProtKB.
 GO:0031572; P:G2 DNA damage checkpoint; IMP:UniProtKB.
 GO:0070537; P:histone H2A K63-linked deubiquitination; IMP:UniProtKB.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:HGNC.
 GO:0045739; P:positive regulation of DNA repair; IMP:UniProtKB.
 GO:0010212; P:response to ionizing radiation; IMP:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR003903; Ubiquitin-int_motif. 
Pfam
  
SMART
 SM00726; UIM 
PROSITE
 PS50330; UIM 
PRINTS