ABRX1_HUMAN
ID ABRX1_HUMAN Reviewed; 409 AA.
AC Q6UWZ7; A5JJ07; Q9H8I1; Q9H9N4;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=BRCA1-A complex subunit Abraxas 1 {ECO:0000312|HGNC:HGNC:25829};
DE AltName: Full=Coiled-coil domain-containing protein 98;
DE AltName: Full=Protein FAM175A;
GN Name=ABRAXAS1 {ECO:0000312|HGNC:HGNC:25829};
GN Synonyms=ABRA1 {ECO:0000312|HGNC:HGNC:25829}, CCDC98,
GN FAM175A {ECO:0000312|HGNC:HGNC:25829}; ORFNames=UNQ496/PRO1013;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP INTERACTION WITH BRCA1 AND UIMC1, PHOSPHORYLATION AT SER-406, AND
RP MUTAGENESIS OF SER-406.
RX PubMed=17525340; DOI=10.1126/science.1139476;
RA Wang B., Matsuoka S., Ballif B.A., Zhang D., Smogorzewska A., Giyi S.,
RA Elledge S.J.;
RT "Abraxas and RAP80 form a BRCA1 protein complex required for the DNA damage
RT response.";
RL Science 316:1194-1198(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASN-373.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT THR-348.
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BRCA1 AND UIMC1,
RP PHOSPHORYLATION AT SER-406, AND MUTAGENESIS OF SER-406.
RX PubMed=17643121; DOI=10.1038/nsmb1279;
RA Liu Z., Wu J., Yu X.;
RT "CCDC98 targets BRCA1 to DNA damage sites.";
RL Nat. Struct. Mol. Biol. 14:716-720(2007).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BRCA1 AND UIMC1,
RP PHOSPHORYLATION AT SER-406, AND MUTAGENESIS OF SER-406.
RX PubMed=17643122; DOI=10.1038/nsmb1277;
RA Kim H., Huang J., Chen J.;
RT "CCDC98 is a BRCA1-BRCT domain-binding protein involved in the DNA damage
RT response.";
RL Nat. Struct. Mol. Biol. 14:710-715(2007).
RN [8]
RP FUNCTION.
RX PubMed=18077395; DOI=10.1073/pnas.0710061104;
RA Wang B., Elledge S.J.;
RT "Ubc13/Rnf8 ubiquitin ligases control foci formation of the
RT Rap80/Abraxas/Brca1/Brcc36 complex in response to DNA damage.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:20759-20763(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386; SER-387; THR-390 AND
RP SER-406, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP IDENTIFICATION IN THE BRCA1-A COMPLEX.
RX PubMed=19261746; DOI=10.1101/gad.1739609;
RA Shao G., Patterson-Fortin J., Messick T.E., Feng D., Shanbhag N., Wang Y.,
RA Greenberg R.A.;
RT "MERIT40 controls BRCA1-Rap80 complex integrity and recruitment to DNA
RT double-strand breaks.";
RL Genes Dev. 23:740-754(2009).
RN [12]
RP IDENTIFICATION IN THE BRCA1-A COMPLEX, DOMAIN MPN-LIKE, INTERACTION WITH
RP UIMC1; BRCC3; BABAM2; BABAM1 AND BRCA1, AND UBIQUITIN-BINDING.
RX PubMed=19261749; DOI=10.1101/gad.1770309;
RA Wang B., Hurov K., Hofmann K., Elledge S.J.;
RT "NBA1, a new player in the Brca1 A complex, is required for DNA damage
RT resistance and checkpoint control.";
RL Genes Dev. 23:729-739(2009).
RN [13]
RP FUNCTION, IDENTIFICATION IN THE BRCA1-A COMPLEX, AND INTERACTION WITH
RP UIMC1; BRCC3; BABAM2 AND BRCA1.
RX PubMed=19261748; DOI=10.1101/gad.1770609;
RA Feng L., Huang J., Chen J.;
RT "MERIT40 facilitates BRCA1 localization and DNA damage repair.";
RL Genes Dev. 23:719-728(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-390 AND SER-406, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386; SER-387; THR-390 AND
RP SER-406, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386; SER-387 AND THR-390, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP IDENTIFICATION IN THE ARISC COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=24075985; DOI=10.1016/j.celrep.2013.08.025;
RA Zheng H., Gupta V., Patterson-Fortin J., Bhattacharya S., Katlinski K.,
RA Wu J., Varghese B., Carbone C.J., Aressy B., Fuchs S.Y., Greenberg R.A.;
RT "A BRISC-SHMT complex deubiquitinates IFNAR1 and regulates interferon
RT responses.";
RL Cell Rep. 5:180-193(2013).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-390 AND SER-406, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 399-409 IN COMPLEX WITH BRCA1,
RP AND INTERACTION WITH BRCA1.
RX PubMed=24316840; DOI=10.1107/s1744309113030649;
RA Badgujar D.C., Sawant U., Vikrant X., Yadav L., Hosur M.V., Varma A.K.;
RT "Preliminary crystallographic studies of BRCA1 BRCT-ABRAXAS complex.";
RL Acta Crystallogr. F 69:1401-1404(2013).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 403-409 IN COMPLEX WITH BRCA1,
RP INTERACTION WITH BRCA1, SUBUNIT, FUNCTION, PHOSPHORYLATION AT SER-404 AND
RP SER-406, AND MUTAGENESIS OF PHE-400; GLU-402; TYR-403; SER-404 AND SER-406.
RX PubMed=26778126; DOI=10.1016/j.molcel.2015.12.017;
RA Wu Q., Paul A., Su D., Mehmood S., Foo T.K., Ochi T., Bunting E.L., Xia B.,
RA Robinson C.V., Wang B., Blundell T.L.;
RT "Structure of BRCA1-BRCT/Abraxas complex reveals phosphorylation-dependent
RT BRCT dimerization at DNA damage sites.";
RL Mol. Cell 61:434-448(2016).
RN [21]
RP VARIANTS THR-348 AND ASN-373.
RX PubMed=18695986; DOI=10.1007/s10549-008-0134-y;
RA Novak D.J., Sabbaghian N., Maillet P., Chappuis P.O., Foulkes W.D.,
RA Tischkowitz M.;
RT "Analysis of the genes coding for the BRCA1-interacting proteins, RAP80 and
RT Abraxas (CCDC98), in high-risk, non-BRCA1/2, multiethnic breast cancer
RT cases.";
RL Breast Cancer Res. Treat. 117:453-459(2009).
RN [22]
RP FUNCTION, VARIANTS THR-348 AND ASN-373, VARIANT BC GLN-361, AND
RP CHARACTERIZATION OF VARIANT BC GLN-361.
RX PubMed=22357538; DOI=10.1126/scitranslmed.3003223;
RA Solyom S., Aressy B., Pylkas K., Patterson-Fortin J., Hartikainen J.M.,
RA Kallioniemi A., Kauppila S., Nikkila J., Kosma V.M., Mannermaa A.,
RA Greenberg R.A., Winqvist R.;
RT "Breast cancer-associated Abraxas mutation disrupts nuclear localization
RT and DNA damage response functions.";
RL Sci. Transl. Med. 4:122ra23-122ra23(2012).
RN [23]
RP CHARACTERIZATION OF VARIANT BC GLN-361.
RX PubMed=25105795; DOI=10.1080/07391102.2014.945484;
RA Kumar R.V., Siddiqui Q., Singh N., Waghmare S.K., Varma A.K.;
RT "Mislocalization of BRCA1-complex due to ABRAXAS Arg361Gln mutation.";
RL J. Biomol. Struct. Dyn. 33:1291-1301(2015).
CC -!- FUNCTION: Involved in DNA damage response and double-strand break (DSB)
CC repair. Component of the BRCA1-A complex, acting as a central scaffold
CC protein that assembles the various components of the complex and
CC mediates the recruitment of BRCA1. The BRCA1-A complex specifically
CC recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA
CC lesion sites, leading to target the BRCA1-BARD1 heterodimer to sites of
CC DNA damage at DSBs. This complex also possesses deubiquitinase activity
CC that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and
CC H2AX. {ECO:0000269|PubMed:17525340, ECO:0000269|PubMed:17643121,
CC ECO:0000269|PubMed:17643122, ECO:0000269|PubMed:18077395,
CC ECO:0000269|PubMed:19261748, ECO:0000269|PubMed:22357538,
CC ECO:0000269|PubMed:26778126}.
CC -!- SUBUNIT: Component of the ARISC complex, at least composed of
CC UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1
CC (PubMed:24075985). Component of the BRCA1-A complex, at least composed
CC of BRCA1, BARD1, UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36, BABAM2 and
CC BABAM1/NBA1. In the complex, interacts directly with UIMC1/RAP80,
CC BRCC3/BRCC36 and BABAM2. Interacts directly (when phosphorylated at
CC Ser-406) with BRCA1. Homodimer. The homodimer interacts directly (when
CC phosphorylated at Ser-404 and Ser-406) with two BRCA1 chains, giving
CC rise to a heterotetramer. Binds polyubiquitin.
CC {ECO:0000269|PubMed:17525340, ECO:0000269|PubMed:17643121,
CC ECO:0000269|PubMed:17643122, ECO:0000269|PubMed:19261746,
CC ECO:0000269|PubMed:19261748, ECO:0000269|PubMed:19261749,
CC ECO:0000269|PubMed:24075985, ECO:0000269|PubMed:24316840,
CC ECO:0000269|PubMed:26778126}.
CC -!- INTERACTION:
CC Q6UWZ7; P38398: BRCA1; NbExp=15; IntAct=EBI-1263451, EBI-349905;
CC Q6UWZ7; P46736: BRCC3; NbExp=4; IntAct=EBI-1263451, EBI-750352;
CC Q6UWZ7; Q96RL1: UIMC1; NbExp=9; IntAct=EBI-1263451, EBI-725300;
CC Q6UWZ7; Q96RL1-1: UIMC1; NbExp=4; IntAct=EBI-1263451, EBI-9640371;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17525340,
CC ECO:0000269|PubMed:17643121, ECO:0000269|PubMed:17643122}.
CC Note=Localizes at sites of DNA damage at double-strand breaks (DSBs).
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6UWZ7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6UWZ7-2; Sequence=VSP_058196;
CC -!- PTM: Phosphorylation of Ser-406 of the pSXXF motif by ATM or ATR
CC constitutes a specific recognition motif for the BRCT domain of BRCA1
CC (PubMed:17643121, PubMed:17525340, PubMed:17643122). Ionizing radiation
CC promotes rapid phosphorylation at Ser-404 and Ser-406 by ATM; this
CC promotes recruitment of BRCA1 to sites of DNA damage (PubMed:26778126).
CC {ECO:0000269|PubMed:17525340, ECO:0000269|PubMed:17643121,
CC ECO:0000269|PubMed:17643122, ECO:0000269|PubMed:26778126}.
CC -!- DISEASE: Breast cancer (BC) [MIM:114480]: A common malignancy
CC originating from breast epithelial tissue. Breast neoplasms can be
CC distinguished by their histologic pattern. Invasive ductal carcinoma is
CC by far the most common type. Breast cancer is etiologically and
CC genetically heterogeneous. Important genetic factors have been
CC indicated by familial occurrence and bilateral involvement. Mutations
CC at more than one locus can be involved in different families or even in
CC the same case. {ECO:0000269|PubMed:22357538,
CC ECO:0000269|PubMed:25105795}. Note=Disease susceptibility is associated
CC with variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the FAM175 family. Abraxas subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH39573.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY358576; AAQ88939.1; -; mRNA.
DR EMBL; EF531340; ABP87396.1; -; mRNA.
DR EMBL; CH471057; EAX05942.1; -; Genomic_DNA.
DR EMBL; BC039573; AAH39573.1; ALT_INIT; mRNA.
DR EMBL; AK022704; BAB14189.1; -; mRNA.
DR EMBL; AK023676; BAB14635.1; -; mRNA.
DR CCDS; CCDS3605.2; -. [Q6UWZ7-1]
DR RefSeq; NP_001332891.1; NM_001345962.1. [Q6UWZ7-2]
DR RefSeq; NP_620775.2; NM_139076.2. [Q6UWZ7-1]
DR PDB; 4JLU; X-ray; 3.50 A; B=399-409.
DR PDB; 4U4A; X-ray; 3.51 A; D/E/F=399-409.
DR PDB; 4Y18; X-ray; 3.50 A; I/J/K/L/M/N/O/P=399-409.
DR PDB; 4Y2G; X-ray; 2.50 A; B=403-409.
DR PDBsum; 4JLU; -.
DR PDBsum; 4U4A; -.
DR PDBsum; 4Y18; -.
DR PDBsum; 4Y2G; -.
DR AlphaFoldDB; Q6UWZ7; -.
DR SMR; Q6UWZ7; -.
DR BioGRID; 123911; 37.
DR ComplexPortal; CPX-4425; BRCA1-A complex.
DR CORUM; Q6UWZ7; -.
DR DIP; DIP-29615N; -.
DR ELM; Q6UWZ7; -.
DR IntAct; Q6UWZ7; 16.
DR STRING; 9606.ENSP00000369857; -.
DR GlyGen; Q6UWZ7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6UWZ7; -.
DR PhosphoSitePlus; Q6UWZ7; -.
DR BioMuta; ABRAXAS1; -.
DR DMDM; 126215684; -.
DR EPD; Q6UWZ7; -.
DR jPOST; Q6UWZ7; -.
DR MassIVE; Q6UWZ7; -.
DR MaxQB; Q6UWZ7; -.
DR PaxDb; Q6UWZ7; -.
DR PeptideAtlas; Q6UWZ7; -.
DR PRIDE; Q6UWZ7; -.
DR ProteomicsDB; 67539; -.
DR Antibodypedia; 25225; 182 antibodies from 33 providers.
DR DNASU; 84142; -.
DR Ensembl; ENST00000321945.12; ENSP00000369857.3; ENSG00000163322.14. [Q6UWZ7-1]
DR GeneID; 84142; -.
DR KEGG; hsa:84142; -.
DR MANE-Select; ENST00000321945.12; ENSP00000369857.3; NM_139076.3; NP_620775.2.
DR UCSC; uc003hou.3; human. [Q6UWZ7-1]
DR CTD; 84142; -.
DR DisGeNET; 84142; -.
DR GeneCards; ABRAXAS1; -.
DR HGNC; HGNC:25829; ABRAXAS1.
DR HPA; ENSG00000163322; Low tissue specificity.
DR MalaCards; ABRAXAS1; -.
DR MIM; 114480; phenotype.
DR MIM; 611143; gene.
DR neXtProt; NX_Q6UWZ7; -.
DR OpenTargets; ENSG00000163322; -.
DR PharmGKB; PA162387308; -.
DR VEuPathDB; HostDB:ENSG00000163322; -.
DR eggNOG; ENOG502QVCD; Eukaryota.
DR GeneTree; ENSGT00530000063424; -.
DR HOGENOM; CLU_056671_0_1_1; -.
DR InParanoid; Q6UWZ7; -.
DR OMA; QESVIGW; -.
DR OrthoDB; 954711at2759; -.
DR PhylomeDB; Q6UWZ7; -.
DR TreeFam; TF331751; -.
DR PathwayCommons; Q6UWZ7; -.
DR Reactome; R-HSA-5689901; Metalloprotease DUBs.
DR Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-HSA-5693571; Nonhomologous End-Joining (NHEJ).
DR Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
DR SignaLink; Q6UWZ7; -.
DR SIGNOR; Q6UWZ7; -.
DR BioGRID-ORCS; 84142; 54 hits in 1080 CRISPR screens.
DR ChiTaRS; FAM175A; human.
DR GenomeRNAi; 84142; -.
DR Pharos; Q6UWZ7; Tbio.
DR PRO; PR:Q6UWZ7; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q6UWZ7; protein.
DR Bgee; ENSG00000163322; Expressed in calcaneal tendon and 184 other tissues.
DR ExpressionAtlas; Q6UWZ7; baseline and differential.
DR Genevisible; Q6UWZ7; HS.
DR GO; GO:0070531; C:BRCA1-A complex; IDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
DR GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006302; P:double-strand break repair; IMP:UniProtKB.
DR GO; GO:0070537; P:histone H2A K63-linked deubiquitination; IC:ComplexPortal.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IMP:UniProtKB.
DR GO; GO:0044818; P:mitotic G2/M transition checkpoint; IC:ComplexPortal.
DR GO; GO:0090307; P:mitotic spindle assembly; IBA:GO_Central.
DR GO; GO:0045739; P:positive regulation of DNA repair; IMP:UniProtKB.
DR GO; GO:0070536; P:protein K63-linked deubiquitination; IBA:GO_Central.
DR GO; GO:0006282; P:regulation of DNA repair; IC:ComplexPortal.
DR GO; GO:0010212; P:response to ionizing radiation; IMP:UniProtKB.
DR InterPro; IPR023238; FAM175.
DR InterPro; IPR023239; FAM175_Abraxas1.
DR InterPro; IPR037518; MPN.
DR PANTHER; PTHR31728; PTHR31728; 1.
DR PRINTS; PR02052; ABRAXAS.
DR PRINTS; PR02051; PROTEINF175.
DR PROSITE; PS50249; MPN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromatin regulator; Coiled coil;
KW Disease variant; DNA damage; DNA repair; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..409
FT /note="BRCA1-A complex subunit Abraxas 1"
FT /id="PRO_0000278575"
FT DOMAIN 7..160
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 362..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 206..260
FT /evidence="ECO:0000255"
FT MOTIF 406..409
FT /note="pSXXF motif"
FT /evidence="ECO:0000305"
FT COMPBIAS 385..400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BPZ8"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 390
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 404
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26778126"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17525340,
FT ECO:0000269|PubMed:17643121, ECO:0000269|PubMed:17643122,
FT ECO:0000269|PubMed:26778126, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..109
FT /note="Missing (in isoform 2)"
FT /id="VSP_058196"
FT VARIANT 239
FT /note="A -> T (in dbSNP:rs752929794)"
FT /id="VAR_030790"
FT VARIANT 348
FT /note="A -> T (not associated with susceptibility to breast
FT cancer; dbSNP:rs12642536)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:18695986, ECO:0000269|PubMed:22357538"
FT /id="VAR_054054"
FT VARIANT 361
FT /note="R -> Q (in BC; results in reduced DSB repair
FT efficiency; primarily localizes to the cytoplasm and has
FT reduced nuclear localization; does not affect interaction
FT with BRCA1; results in highly reduced interaction with
FT UIMC1/RAP80; dbSNP:rs201627097)"
FT /evidence="ECO:0000269|PubMed:22357538,
FT ECO:0000269|PubMed:25105795"
FT /id="VAR_071865"
FT VARIANT 373
FT /note="D -> N (not associated with susceptibility to breast
FT cancer; dbSNP:rs13125836)"
FT /evidence="ECO:0000269|PubMed:12975309,
FT ECO:0000269|PubMed:18695986, ECO:0000269|PubMed:22357538"
FT /id="VAR_054055"
FT MUTAGEN 400
FT /note="F->D: No effect on formation of a heterotetramer
FT with BRCA1."
FT /evidence="ECO:0000269|PubMed:26778126"
FT MUTAGEN 402
FT /note="E->R: Decreases formation of a heterotetramer with
FT BRCA1."
FT /evidence="ECO:0000269|PubMed:26778126"
FT MUTAGEN 403
FT /note="Y->A: No effect on formation of a heterotetramer
FT with BRCA1."
FT /evidence="ECO:0000269|PubMed:26778126"
FT MUTAGEN 404
FT /note="S->A: No effect on homodimerization. Mildly
FT decreased recruitment of BRCA1 to sites of DNA damage."
FT /evidence="ECO:0000269|PubMed:26778126"
FT MUTAGEN 404
FT /note="S->D: Permits formation of a heterotetramer with
FT BRCA1."
FT /evidence="ECO:0000269|PubMed:26778126"
FT MUTAGEN 404
FT /note="S->P: Abolishes formation of a heterotetramer with
FT BRCA1. Does not affect interaction with a first BRCA1
FT chain."
FT /evidence="ECO:0000269|PubMed:26778126"
FT MUTAGEN 406
FT /note="S->A: Abolishes phosphorylation of the pSXXF motif
FT and the interaction with BRCA1 but does not affect the
FT interaction with UIMC1/RAP80. Strongly decreases
FT recruitment of BRCA1 to sites of DNA damage. No effect on
FT homodimerization."
FT /evidence="ECO:0000269|PubMed:17525340,
FT ECO:0000269|PubMed:17643121, ECO:0000269|PubMed:17643122,
FT ECO:0000269|PubMed:26778126"
SQ 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
