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 28-JAN-2026, entry version 157. 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, FAM175A GN {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=16; IntAct=EBI-1263451, EBI-349905; CC Q6UWZ7; P46736: BRCC3; NbExp=4; IntAct=EBI-1263451, EBI-750352; CC Q6UWZ7; P13569: CFTR; NbExp=3; IntAct=EBI-1263451, EBI-349854; CC Q6UWZ7; O00629: KPNA4; NbExp=2; IntAct=EBI-1263451, EBI-396343; 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:17525340, PubMed:17643121, 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_001345962.2. [Q6UWZ7-2] DR RefSeq; NP_620775.2; NM_139076.3. [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; 43. DR ComplexPortal; CPX-4425; BRCA1-A complex. DR CORUM; Q6UWZ7; -. DR DIP; DIP-29615N; -. DR ELM; Q6UWZ7; -. DR FunCoup; Q6UWZ7; 2756. DR IntAct; Q6UWZ7; 19. DR MINT; Q6UWZ7; -. 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 jPOST; Q6UWZ7; -. DR MassIVE; Q6UWZ7; -. DR PaxDb; 9606-ENSP00000369857; -. DR PeptideAtlas; Q6UWZ7; -. DR ProteomicsDB; 67539; -. DR Pumba; Q6UWZ7; -. DR Antibodypedia; 25225; 195 antibodies from 33 providers. DR DNASU; 84142; -. DR Ensembl; ENST00000321945.12; ENSP00000369857.3; ENSG00000163322.15. [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 AGR; HGNC:25829; -. DR ClinPGx; PA162387308; -. 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 OpenTargets; ENSG00000163322; -. DR VEuPathDB; HostDB:ENSG00000163322; -. DR eggNOG; ENOG502QVCD; Eukaryota. DR GeneTree; ENSGT00530000063424; -. DR HOGENOM; CLU_056671_0_1_1; -. DR InParanoid; Q6UWZ7; -. DR OrthoDB; 6358435at2759; -. DR PAN-GO; Q6UWZ7; 6 GO annotations based on evolutionary models. DR PhylomeDB; Q6UWZ7; -. 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 Agora; ENSG00000163322; -. DR BioGRID-ORCS; 84142; 56 hits in 1167 CRISPR screens. DR ChiTaRS; FAM175A; human. DR EvolutionaryTrace; Q6UWZ7; -. 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 primordial germ cell in gonad and 185 other cell types or tissues. DR ExpressionAtlas; Q6UWZ7; baseline and differential. 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:0007095; P:mitotic G2 DNA damage checkpoint signaling; IMP:UniProtKB. DR GO; GO:0044818; P:mitotic G2/M transition checkpoint; NAS: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:0006282; P:regulation of DNA repair; NAS:ComplexPortal. DR GO; GO:0010212; P:response to ionizing radiation; IMP:UniProtKB. DR CDD; cd23523; Abraxas_1; 1. DR InterPro; IPR023239; BRISC_Abraxas1. DR InterPro; IPR023238; FAM175. DR InterPro; IPR037518; MPN. DR PANTHER; PTHR31728; ABRAXAS FAMILY MEMBER; 1. DR PANTHER; PTHR31728:SF2; BRCA1-A COMPLEX SUBUNIT ABRAXAS 1; 1. DR Pfam; PF21125; MPN_2A_DUB_like; 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 Proteomics identification; 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 362..372 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 373..388 FT /note="Polar 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 (in 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 (in 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 //