CPLM-022285

Genbank Nucleotide ID

BRISC and BRCA1-A complex member 1

Protein Synonyms/Alias

Mediator of RAP80 interactions and targeting subunit of 40 kDa; New component of the BRCA1-A complex

C19orf62; MERIT40; NBA1; HSPC142

Homo sapiens (Human)

Position	Peptide	Type	References
117	LESFNGSKTNALNVS	ubiquitination	[1, 2, 3, 4, 5, 6]
126	NALNVSQKMIEMFVR	ubiquitination	[1, 4, 6]
234	SLTEPMKKMFQCPYF	ubiquitination	[6]

[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] 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]
[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] 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]
[5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
[6] 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]

Functional Description

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). The BRCA1-A complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. In the BRCA1-A complex, it is required for the complex integrity and its localization at DSBs. Probably also plays a role as a component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin. In these 2 complexes, it is probably required to maintain the stability of BRE/BRCC45 and help the 'Lys-63'-linked deubiquitinase activity mediated by BRCC3/BRCC36 component.

REGION 95 298 VWFA-like.
MOD_RES 1 1 N-acetylmethionine.
MOD_RES 29 29 Phosphoserine.
MOD_RES 49 49 Phosphoserine.
MOD_RES 62 62 Phosphoserine.
MOD_RES 65 65 Phosphothreonine.
MOD_RES 66 66 Phosphoserine.

Acetylation; Alternative splicing; Chromatin regulator; Complete proteome; Cytoplasm; DNA damage; DNA repair; Nucleus; Phosphoprotein; Reference proteome.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0070531; C:BRCA1-A complex; IDA:UniProtKB.
GO:0070552; C:BRISC complex; IDA:UniProtKB.
GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
GO:0006302; P:double-strand break repair; IMP:UniProtKB.
GO:0031572; P:G2 DNA damage checkpoint; IMP:UniProtKB.
GO:0045739; P:positive regulation of DNA repair; IMP:UniProtKB.
GO:0070536; P:protein K63-linked deubiquitination; IMP:UniProtKB.
GO:0010212; P:response to ionizing radiation; IMP:UniProtKB.