CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007826
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Lys-63-specific deubiquitinase BRCC36 
Protein Synonyms/Alias
 BRCA1-A complex subunit BRCC36; BRCA1/BRCA2-containing complex subunit 3; BRCA1/BRCA2-containing complex subunit 36; BRISC complex subunit BRCC36 
Gene Name
 BRCC3 
Gene Synonyms/Alias
 BRCC36; C6.1A; CXorf53 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
51DDTRSDSKFAYTGTEubiquitination[1, 2, 3, 4]
65EMRTVAEKVDAVRIVubiquitination[2, 3]
180FQSIQAQKSSESLHGubiquitination[1, 3]
204HISIEGQKEEERYERubiquitination[3]
226VPHVTIGKVCLESAVubiquitination[3]
237ESAVELPKILCQEEQubiquitination[3]
261THLDSVTKIHNGSVFubiquitination[3, 5]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [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] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094
Functional Description
 Metalloprotease that specifically cleaves 'Lys-63'- linked polyubiquitin chains. Does not have activity toward 'Lys- 48'-linked polyubiquitin chains. Component of the BRCA1-A complex, a complex that specifically recognizes '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). In the BRCA1-A complex, it specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX, antagonizing the RNF8-dependent ubiquitination at double- strand breaks (DSBs). Catalytic subunit of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. Mediates the specific 'Lys-63'- specific deubiquitination associated with the COP9 signalosome complex (CSN), via the interaction of the BRISC complex with the CSN complex. 
Sequence Annotation
 DOMAIN 7 148 MPN.
 MOTIF 122 135 JAMM motif.
 METAL 122 122 Zinc; catalytic (Probable).
 METAL 124 124 Zinc; catalytic (Probable).
 METAL 135 135 Zinc; catalytic (By similarity).
 MOD_RES 2 2 N-acetylalanine.  
Keyword
 Acetylation; Alternative splicing; Chromatin regulator; Chromosomal rearrangement; Complete proteome; Direct protein sequencing; DNA damage; DNA repair; Hydrolase; Metal-binding; Metalloprotease; Nucleus; Polymorphism; Protease; Proto-oncogene; Reference proteome; Ubl conjugation pathway; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 316 AA 
Protein Sequence
MAVQVVQAVQ AVHLESDAFL VCLNHALSTE KEEVMGLCIG ELNDDTRSDS KFAYTGTEMR 60
TVAEKVDAVR IVHIHSVIIL RRSDKRKDRV EISPEQLSAA STEAERLAEL TGRPMRVVGW 120
YHSHPHITVW PSHVDVRTQA MYQMMDQGFV GLIFSCFIED KNTKTGRVLY TCFQSIQAQK 180
SSESLHGPRD FWSSSQHISI EGQKEEERYE RIEIPIHIVP HVTIGKVCLE SAVELPKILC 240
QEEQDAYRRI HSLTHLDSVT KIHNGSVFTK NLCSQMSAVS GPLLQWLEDR LEQNQQHLQE 300
LQQEKEELMQ ELSSLE 316 
Gene Ontology
 GO:0070531; C:BRCA1-A complex; IDA:UniProtKB.
 GO:0070552; C:BRISC complex; IDA:UniProtKB.
 GO:0000152; C:nuclear ubiquitin ligase complex; IDA:UniProtKB.
 GO:0030234; F:enzyme regulator activity; IDA:MGI.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0008237; F:metallopeptidase activity; IMP:UniProtKB.
 GO:0031593; F:polyubiquitin binding; IDA:UniProtKB.
 GO:0004221; F:ubiquitin thiolesterase activity; IMP:UniProtKB.
 GO:0004843; F:ubiquitin-specific protease activity; IMP: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; IDA:UniProtKB.
 GO:0045739; P:positive regulation of DNA repair; IMP:UniProtKB.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
 GO:0010165; P:response to X-ray; IDA:MGI. 
Interpro
 IPR000555; JAB1_Mov34_MPN_PAD1. 
Pfam
 PF01398; JAB 
SMART
 SM00232; JAB_MPN 
PROSITE
  
PRINTS