UniProt Accession

 F175A_HUMAN; Q6UWZ7; A5JJ07; Q9H8I1; Q9H9N4 

Genbank Protein ID

 AY358576; EF531340; CH471057; BC039573; AK022704; AK023676 

Genbank Nucleotide ID

 AAQ88939.1; ABP87396.1; EAX05942.1; AAH39573.1; BAB14189.1; BAB14635.1 

Protein Name

 BRCA1-A complex subunit Abraxas 

Protein Synonyms/Alias

 Coiled-coil domain-containing protein 98; Protein FAM175A 

Gene Name

 FAM175A 

Gene Synonyms/Alias

 ABRA1; CCDC98; UNQ496/PRO1013 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
158	HSLYKPQKGLFHRVP	ubiquitination	[1, 2, 3]
201	AVQTHSSKFFEEDGS	ubiquitination	[1, 2, 3, 4]
210	FEEDGSLKEVHKINE	ubiquitination	[2]
268	QIQAAREKNIQKDPQ	ubiquitination	[2]
272	AREKNIQKDPQENIF	ubiquitination	[2]
302	HSCVMSLKNRHVSKS	ubiquitination	[2]
347	TPQIIKHKALDLDDR	ubiquitination	[1, 2, 3, 4]
358	LDDRWQFKRSRLLDT	ubiquitination	[1, 2, 3]
368	RLLDTQDKRSKADTG	ubiquitination	[2]
384	SNQDKASKMSSPETD	ubiquitination	[2, 4]
396	ETDEEIEKMKGFGEY	ubiquitination	[2, 4]
398	DEEIEKMKGFGEYSR	ubiquitination	[2, 4, 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] 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]
 [3] 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]
 [4] 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]
 [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] 

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 acts as a central scaffold protein that assembles the various components of the BRCA1-A complex and mediates the recruitment of BRCA1. 

Sequence Annotation

 REGION 11 121 MPN-like.
 MOTIF 406 409 pSXXF motif.
 MOD_RES 386 386 Phosphoserine.
 MOD_RES 387 387 Phosphoserine.
 MOD_RES 390 390 Phosphothreonine.
 MOD_RES 406 406 Phosphoserine.  

Keyword

 Chromatin regulator; Coiled coil; Complete proteome; DNA damage; DNA repair; Nucleus; Phosphoprotein; Polymorphism; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 409 AA 

Protein Sequence

Gene Ontology

 GO:0070531; C:BRCA1-A complex; IDA:UniProtKB.
 GO:0031593; F:polyubiquitin binding; 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:0010212; P:response to ionizing radiation; IMP:UniProtKB. 

Interpro

 IPR023238; FAM175.
 IPR023239; FAM175_BRCA1-A_cplx_Abraxas_su. 

Pfam

  

SMART

  

PROSITE

  

PRINTS

 PR02052; ABRAXAS.
 PR02051; PROTEINF175.