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BRCA1-A complex subunit Abraxas 1 (Coiled-coil domain-containing protein 98) (Protein FAM175A)

 ABRX1_HUMAN             Reviewed;         409 AA.
Q6UWZ7; A5JJ07; Q9H8I1; Q9H9N4;
20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
20-FEB-2007, sequence version 2.
20-JUN-2018, entry version 119.
RecName: Full=BRCA1-A complex subunit Abraxas 1 {ECO:0000312|HGNC:HGNC:25829};
AltName: Full=Coiled-coil domain-containing protein 98;
AltName: Full=Protein FAM175A;
Name=ABRAXAS1 {ECO:0000312|HGNC:HGNC:25829};
Synonyms=ABRA1 {ECO:0000312|HGNC:HGNC:25829}, CCDC98,
FAM175A {ECO:0000312|HGNC:HGNC:25829}; ORFNames=UNQ496/PRO1013;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, INTERACTION WITH BRCA1 AND UIMC1, PHOSPHORYLATION AT
SER-406, AND MUTAGENESIS OF SER-406.
PubMed=17525340; DOI=10.1126/science.1139476;
Wang B., Matsuoka S., Ballif B.A., Zhang D., Smogorzewska A., Giyi S.,
Elledge S.J.;
"Abraxas and RAP80 form a BRCA1 protein complex required for the DNA
damage response.";
Science 316:1194-1198(2007).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ASN-373.
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
THR-348.
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BRCA1 AND UIMC1,
PHOSPHORYLATION AT SER-406, AND MUTAGENESIS OF SER-406.
PubMed=17643121; DOI=10.1038/nsmb1279;
Liu Z., Wu J., Yu X.;
"CCDC98 targets BRCA1 to DNA damage sites.";
Nat. Struct. Mol. Biol. 14:716-720(2007).
[7]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BRCA1 AND UIMC1,
PHOSPHORYLATION AT SER-406, AND MUTAGENESIS OF SER-406.
PubMed=17643122; DOI=10.1038/nsmb1277;
Kim H., Huang J., Chen J.;
"CCDC98 is a BRCA1-BRCT domain-binding protein involved in the DNA
damage response.";
Nat. Struct. Mol. Biol. 14:710-715(2007).
[8]
FUNCTION.
PubMed=18077395; DOI=10.1073/pnas.0710061104;
Wang B., Elledge S.J.;
"Ubc13/Rnf8 ubiquitin ligases control foci formation of the
Rap80/Abraxas/Brca1/Brcc36 complex in response to DNA damage.";
Proc. Natl. Acad. Sci. U.S.A. 104:20759-20763(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386; SER-387; THR-390
AND SER-406, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[11]
IDENTIFICATION IN THE BRCA1-A COMPLEX.
PubMed=19261746; DOI=10.1101/gad.1739609;
Shao G., Patterson-Fortin J., Messick T.E., Feng D., Shanbhag N.,
Wang Y., Greenberg R.A.;
"MERIT40 controls BRCA1-Rap80 complex integrity and recruitment to DNA
double-strand breaks.";
Genes Dev. 23:740-754(2009).
[12]
IDENTIFICATION IN THE BRCA1-A COMPLEX, DOMAIN MPN-LIKE, INTERACTION
WITH UIMC1; BRCC3; BABAM2; BABAM1 AND BRCA1, AND UBIQUITIN-BINDING.
PubMed=19261749; DOI=10.1101/gad.1770309;
Wang B., Hurov K., Hofmann K., Elledge S.J.;
"NBA1, a new player in the Brca1 A complex, is required for DNA damage
resistance and checkpoint control.";
Genes Dev. 23:729-739(2009).
[13]
FUNCTION, IDENTIFICATION IN THE BRCA1-A COMPLEX, AND INTERACTION WITH
UIMC1; BRCC3; BABAM2 AND BRCA1.
PubMed=19261748; DOI=10.1101/gad.1770609;
Feng L., Huang J., Chen J.;
"MERIT40 facilitates BRCA1 localization and DNA damage repair.";
Genes Dev. 23:719-728(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-390 AND SER-406, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386; SER-387; THR-390
AND SER-406, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386; SER-387 AND
THR-390, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[17]
IDENTIFICATION IN THE ARISC COMPLEX, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=24075985; DOI=10.1016/j.celrep.2013.08.025;
Zheng H., Gupta V., Patterson-Fortin J., Bhattacharya S.,
Katlinski K., Wu J., Varghese B., Carbone C.J., Aressy B., Fuchs S.Y.,
Greenberg R.A.;
"A BRISC-SHMT complex deubiquitinates IFNAR1 and regulates interferon
responses.";
Cell Rep. 5:180-193(2013).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-390 AND SER-406, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 399-409 IN COMPLEX WITH
BRCA1, AND INTERACTION WITH BRCA1.
PubMed=24316840; DOI=10.1107/S1744309113030649;
Badgujar D.C., Sawant U., Vikrant X., Yadav L., Hosur M.V.,
Varma A.K.;
"Preliminary crystallographic studies of BRCA1 BRCT-ABRAXAS complex.";
Acta Crystallogr. F 69:1401-1404(2013).
[20]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 403-409 IN COMPLEX WITH
BRCA1, INTERACTION WITH BRCA1, SUBUNIT, FUNCTION, PHOSPHORYLATION AT
SER-404 AND SER-406, AND MUTAGENESIS OF PHE-400; GLU-402; TYR-403;
SER-404 AND SER-406.
PubMed=26778126; DOI=10.1016/j.molcel.2015.12.017;
Wu Q., Paul A., Su D., Mehmood S., Foo T.K., Ochi T., Bunting E.L.,
Xia B., Robinson C.V., Wang B., Blundell T.L.;
"Structure of BRCA1-BRCT/Abraxas complex reveals phosphorylation-
dependent BRCT dimerization at DNA damage sites.";
Mol. Cell 61:434-448(2016).
[21]
VARIANTS THR-348 AND ASN-373.
PubMed=18695986; DOI=10.1007/s10549-008-0134-y;
Novak D.J., Sabbaghian N., Maillet P., Chappuis P.O., Foulkes W.D.,
Tischkowitz M.;
"Analysis of the genes coding for the BRCA1-interacting proteins,
RAP80 and Abraxas (CCDC98), in high-risk, non-BRCA1/2, multiethnic
breast cancer cases.";
Breast Cancer Res. Treat. 117:453-459(2009).
[22]
FUNCTION, VARIANTS THR-348 AND ASN-373, VARIANT BC GLN-361, AND
CHARACTERIZATION OF VARIANT BC GLN-361.
PubMed=22357538; DOI=10.1126/scitranslmed.3003223;
Solyom S., Aressy B., Pylkas K., Patterson-Fortin J.,
Hartikainen J.M., Kallioniemi A., Kauppila S., Nikkila J., Kosma V.M.,
Mannermaa A., Greenberg R.A., Winqvist R.;
"Breast cancer-associated Abraxas mutation disrupts nuclear
localization and DNA damage response functions.";
Sci. Transl. Med. 4:122ra23-122ra23(2012).
[23]
CHARACTERIZATION OF VARIANT BC GLN-361.
PubMed=25105795; DOI=10.1080/07391102.2014.945484;
Kumar R.V., Siddiqui Q., Singh N., Waghmare S.K., Varma A.K.;
"Mislocalization of BRCA1-complex due to ABRAXAS Arg361Gln mutation.";
J. Biomol. Struct. Dyn. 33:1291-1301(2015).
-!- FUNCTION: Involved in DNA damage response and double-strand break
(DSB) repair. Component of the BRCA1-A complex, acting as a
central scaffold protein that assembles the various components of
the complex and mediates the recruitment of BRCA1. The BRCA1-A
complex specifically recognizes 'Lys-63'-linked ubiquitinated
histones H2A and H2AX at DNA lesion sites, leading to target the
BRCA1-BARD1 heterodimer to sites of DNA damage at DSBs. This
complex also possesses deubiquitinase activity that specifically
removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX.
{ECO:0000269|PubMed:17525340, ECO:0000269|PubMed:17643121,
ECO:0000269|PubMed:17643122, ECO:0000269|PubMed:18077395,
ECO:0000269|PubMed:19261748, ECO:0000269|PubMed:22357538,
ECO:0000269|PubMed:26778126}.
-!- SUBUNIT: Component of the ARISC complex, at least composed of
UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1
(PubMed:24075985). Component of the BRCA1-A complex, at least
composed of BRCA1, BARD1, UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36,
BABAM2 and BABAM1/NBA1. In the complex, interacts directly with
UIMC1/RAP80, BRCC3/BRCC36 and BABAM2. Interacts directly (when
phosphorylated at Ser-406) with BRCA1. Homodimer. The homodimer
interacts directly (when phosphorylated at Ser-404 and Ser-406)
with two BRCA1 chains, giving rise to a heterotetramer. Binds
polyubiquitin. {ECO:0000269|PubMed:17525340,
ECO:0000269|PubMed:17643121, ECO:0000269|PubMed:17643122,
ECO:0000269|PubMed:19261746, ECO:0000269|PubMed:19261748,
ECO:0000269|PubMed:19261749, ECO:0000269|PubMed:24075985,
ECO:0000269|PubMed:24316840, ECO:0000269|PubMed:26778126}.
-!- INTERACTION:
P38398:BRCA1; NbExp=14; IntAct=EBI-1263451, EBI-349905;
P46736:BRCC3; NbExp=4; IntAct=EBI-1263451, EBI-750352;
Q96RL1:UIMC1; NbExp=9; IntAct=EBI-1263451, EBI-725300;
Q96RL1-1:UIMC1; NbExp=4; IntAct=EBI-1263451, EBI-9640371;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17525340,
ECO:0000269|PubMed:17643121, ECO:0000269|PubMed:17643122}.
Note=Localizes at sites of DNA damage at double-strand breaks
(DSBs). {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q6UWZ7-1; Sequence=Displayed;
Name=2;
IsoId=Q6UWZ7-2; Sequence=VSP_058196;
-!- PTM: Phosphorylation of Ser-406 of the pSXXF motif by ATM or ATR
constitutes a specific recognition motif for the BRCT domain of
BRCA1 (PubMed:17643121, PubMed:17525340, PubMed:17643122).
Ionizing radiation promotes rapid phosphorylation at Ser-404 and
Ser-406 by ATM; this promotes recruitment of BRCA1 to sites of DNA
damage (PubMed:26778126). {ECO:0000269|PubMed:17525340,
ECO:0000269|PubMed:17643121, ECO:0000269|PubMed:17643122,
ECO:0000269|PubMed:26778126}.
-!- DISEASE: Breast cancer (BC) [MIM:114480]: A common malignancy
originating from breast epithelial tissue. Breast neoplasms can be
distinguished by their histologic pattern. Invasive ductal
carcinoma is by far the most common type. Breast cancer is
etiologically and genetically heterogeneous. Important genetic
factors have been indicated by familial occurrence and bilateral
involvement. Mutations at more than one locus can be involved in
different families or even in the same case.
{ECO:0000269|PubMed:22357538, ECO:0000269|PubMed:25105795}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the FAM175 family. Abraxas subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH39573.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AY358576; AAQ88939.1; -; mRNA.
EMBL; EF531340; ABP87396.1; -; mRNA.
EMBL; CH471057; EAX05942.1; -; Genomic_DNA.
EMBL; BC039573; AAH39573.1; ALT_INIT; mRNA.
EMBL; AK022704; BAB14189.1; -; mRNA.
EMBL; AK023676; BAB14635.1; -; mRNA.
CCDS; CCDS3605.2; -. [Q6UWZ7-1]
RefSeq; NP_001332891.1; NM_001345962.1. [Q6UWZ7-2]
RefSeq; NP_620775.2; NM_139076.2. [Q6UWZ7-1]
UniGene; Hs.334772; -.
PDB; 4JLU; X-ray; 3.50 A; B=399-409.
PDB; 4U4A; X-ray; 3.51 A; D/E/F=399-409.
PDB; 4Y18; X-ray; 3.50 A; I/J/K/L/M/N/O/P=399-409.
PDB; 4Y2G; X-ray; 2.50 A; B=403-409.
PDBsum; 4JLU; -.
PDBsum; 4U4A; -.
PDBsum; 4Y18; -.
PDBsum; 4Y2G; -.
ProteinModelPortal; Q6UWZ7; -.
SMR; Q6UWZ7; -.
BioGrid; 123911; 20.
CORUM; Q6UWZ7; -.
DIP; DIP-29615N; -.
ELM; Q6UWZ7; -.
IntAct; Q6UWZ7; 8.
STRING; 9606.ENSP00000369857; -.
iPTMnet; Q6UWZ7; -.
PhosphoSitePlus; Q6UWZ7; -.
BioMuta; FAM175A; -.
DMDM; 126215684; -.
EPD; Q6UWZ7; -.
MaxQB; Q6UWZ7; -.
PaxDb; Q6UWZ7; -.
PeptideAtlas; Q6UWZ7; -.
PRIDE; Q6UWZ7; -.
ProteomicsDB; 67539; -.
DNASU; 84142; -.
Ensembl; ENST00000321945; ENSP00000369857; ENSG00000163322. [Q6UWZ7-1]
GeneID; 84142; -.
KEGG; hsa:84142; -.
UCSC; uc003hou.3; human. [Q6UWZ7-1]
CTD; 84142; -.
DisGeNET; 84142; -.
EuPathDB; HostDB:ENSG00000163322.13; -.
GeneCards; ABRAXAS1; -.
HGNC; HGNC:25829; ABRAXAS1.
HPA; HPA037654; -.
MalaCards; ABRAXAS1; -.
MIM; 114480; phenotype.
MIM; 611143; gene.
neXtProt; NX_Q6UWZ7; -.
OpenTargets; ENSG00000163322; -.
PharmGKB; PA162387308; -.
eggNOG; ENOG410IG59; Eukaryota.
eggNOG; ENOG4110D5E; LUCA.
GeneTree; ENSGT00530000063424; -.
HOGENOM; HOG000112448; -.
HOVERGEN; HBG095943; -.
InParanoid; Q6UWZ7; -.
KO; K20774; -.
OrthoDB; EOG091G07ID; -.
PhylomeDB; Q6UWZ7; -.
TreeFam; TF331751; -.
Reactome; R-HSA-5689901; Metalloprotease DUBs.
Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-HSA-5693571; Nonhomologous End-Joining (NHEJ).
Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
SIGNOR; Q6UWZ7; -.
GenomeRNAi; 84142; -.
PRO; PR:Q6UWZ7; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000163322; -.
CleanEx; HS_FAM175A; -.
ExpressionAtlas; Q6UWZ7; baseline and differential.
Genevisible; Q6UWZ7; HS.
GO; GO:0070531; C:BRCA1-A complex; IDA:UniProtKB.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
GO; GO:0006302; P:double-strand break repair; IMP:UniProtKB.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; TAS:Reactome.
GO; GO:0045739; P:positive regulation of DNA repair; IMP:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0010212; P:response to ionizing radiation; IMP:UniProtKB.
GO; GO:0072425; P:signal transduction involved in G2 DNA damage checkpoint; IMP:UniProtKB.
InterPro; IPR023238; FAM175.
InterPro; IPR023239; FAM175_Abraxas1.
InterPro; IPR037518; MPN.
PANTHER; PTHR31728; PTHR31728; 1.
PRINTS; PR02052; ABRAXAS.
PRINTS; PR02051; PROTEINF175.
PROSITE; PS50249; MPN; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chromatin regulator; Coiled coil;
Complete proteome; Disease mutation; DNA damage; DNA repair; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome.
CHAIN 1 409 BRCA1-A complex subunit Abraxas 1.
/FTId=PRO_0000278575.
DOMAIN 7 160 MPN. {ECO:0000255|PROSITE-
ProRule:PRU01182}.
COILED 206 260 {ECO:0000255}.
MOTIF 406 409 pSXXF motif. {ECO:0000305}.
MOD_RES 48 48 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BPZ8}.
MOD_RES 386 386 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 387 387 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 390 390 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 404 404 Phosphoserine.
{ECO:0000269|PubMed:26778126}.
MOD_RES 406 406 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:17525340,
ECO:0000269|PubMed:17643121,
ECO:0000269|PubMed:17643122,
ECO:0000269|PubMed:26778126}.
VAR_SEQ 1 109 Missing (in isoform 2).
/FTId=VSP_058196.
VARIANT 239 239 A -> T (in dbSNP:rs12642536).
/FTId=VAR_030790.
VARIANT 348 348 A -> T (common polymorphism not
associated with susceptibility to breast
cancer; dbSNP:rs12642536).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:18695986,
ECO:0000269|PubMed:22357538}.
/FTId=VAR_054054.
VARIANT 361 361 R -> Q (in BC; results in reduced DSB
repair efficiency; primarily localizes to
the cytoplasm and has reduced nuclear
localization; does not affect interaction
with BRCA1; results in highly reduced
interaction with UIMC1/RAP80;
dbSNP:rs201627097).
{ECO:0000269|PubMed:22357538,
ECO:0000269|PubMed:25105795}.
/FTId=VAR_071865.
VARIANT 373 373 D -> N (common polymorphism not
associated with susceptibility to breast
cancer; dbSNP:rs13125836).
{ECO:0000269|PubMed:12975309,
ECO:0000269|PubMed:18695986,
ECO:0000269|PubMed:22357538}.
/FTId=VAR_054055.
MUTAGEN 400 400 F->D: No effect on formation of a
heterotetramer with BRCA1.
{ECO:0000269|PubMed:26778126}.
MUTAGEN 402 402 E->R: Decreases formation of a
heterotetramer with BRCA1.
{ECO:0000269|PubMed:26778126}.
MUTAGEN 403 403 Y->A: No effect on formation of a
heterotetramer with BRCA1.
{ECO:0000269|PubMed:26778126}.
MUTAGEN 404 404 S->A: No effect on homodimerization.
Mildly decreased recruitment of BRCA1 to
sites of DNA damage.
{ECO:0000269|PubMed:26778126}.
MUTAGEN 404 404 S->D: Permits formation of a
heterotetramer with BRCA1.
{ECO:0000269|PubMed:26778126}.
MUTAGEN 404 404 S->P: Abolishes formation of a
heterotetramer with BRCA1. Does not
affect interaction with a first BRCA1
chain. {ECO:0000269|PubMed:26778126}.
MUTAGEN 406 406 S->A: Abolishes phosphorylation of the
pSXXF motif and the interaction with
BRCA1 but does not affect the interaction
with UIMC1/RAP80. Strongly decreases
recruitment of BRCA1 to sites of DNA
damage. No effect on homodimerization.
{ECO:0000269|PubMed:17525340,
ECO:0000269|PubMed:17643121,
ECO:0000269|PubMed:17643122,
ECO:0000269|PubMed:26778126}.
SEQUENCE 409 AA; 46663 MW; A1ACA4F759BD1AEE CRC64;
MEGESTSAVL SGFVLGALAF QHLNTDSDTE GFLLGEVKGE AKNSITDSQM DDVEVVYTID
IQKYIPCYQL FSFYNSSGEV NEQALKKILS NVKKNVVGWY KFRRHSDQIM TFRERLLHKN
LQEHFSNQDL VFLLLTPSII TESCSTHRLE HSLYKPQKGL FHRVPLVVAN LGMSEQLGYK
TVSGSCMSTG FSRAVQTHSS KFFEEDGSLK EVHKINEMYA SLQEELKSIC KKVEDSEQAV
DKLVKDVNRL KREIEKRRGA QIQAAREKNI QKDPQENIFL CQALRTFFPN SEFLHSCVMS
LKNRHVSKSS CNYNHHLDVV DNLTLMVEHT DIPEASPAST PQIIKHKALD LDDRWQFKRS
RLLDTQDKRS KADTGSSNQD KASKMSSPET DEEIEKMKGF GEYSRSPTF


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