ID ABRX2_HUMAN Reviewed; 415 AA. AC Q15018; B4DKR2; Q96H11; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 20-DEC-2005, sequence version 2. DT 28-JAN-2026, entry version 175. DE RecName: Full=BRISC complex subunit Abraxas 2 {ECO:0000312|HGNC:HGNC:28975}; DE AltName: Full=Abraxas brother protein 1 {ECO:0000303|PubMed:22974638}; DE AltName: Full=Protein FAM175B; GN Name=ABRAXAS2 {ECO:0000312|HGNC:HGNC:28975}; GN Synonyms=ABRO1 {ECO:0000303|PubMed:21195082}, FAM175B GN {ECO:0000312|HGNC:HGNC:28975}, KIAA0157 {ECO:0000303|PubMed:8590280}; 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 [LARGE SCALE MRNA]. RC TISSUE=Bone marrow; RX PubMed=8590280; DOI=10.1093/dnares/2.4.167; RA Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.; RT "Prediction of the coding sequences of unidentified human genes. IV. The RT coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of RT cDNA clones from human cell line KG-1."; RL DNA Res. 2:167-174(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Tongue; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta; 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 [4] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=15144186; DOI=10.1021/ac035352d; RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., RA Peters E.C.; RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from RT human T cells using immobilized metal affinity chromatography and tandem RT mass spectrometry."; RL Anal. Chem. 76:2763-2772(2004). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368 AND SER-372, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [6] RP LACK OF INTERACTION WITH BRCA1, AND SUBUNIT. 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280; SER-368; SER-372 AND RP SER-375, 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 [8] RP IDENTIFICATION IN THE BRISC COMPLEX, FUNCTION, AND SUBUNIT. RX PubMed=19214193; DOI=10.1038/emboj.2009.27; RA Cooper E.M., Cutcliffe C., Kristiansen T.Z., Pandey A., Pickart C.M., RA Cohen R.E.; RT "K63-specific deubiquitination by two JAMM/MPN+ complexes: BRISC-associated RT Brcc36 and proteasomal Poh1."; RL EMBO J. 28:621-631(2009). RN [9] RP DOMAIN MPN-LIKE, UBIQUITIN-BINDING, AND SUBUNIT. 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368; SER-372 AND SER-375, 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 [11] RP FUNCTION, SUBUNIT, IDENTIFICATION IN THE BRISC COMPLEX, AND INTERACTION OF RP THE BRISC COMPLEX WITH UBIQUITIN. RX PubMed=20032457; DOI=10.1074/jbc.m109.059667; RA Cooper E.M., Boeke J.D., Cohen R.E.; RT "Specificity of the BRISC deubiquitinating enzyme is not due to selective RT binding to Lys63-linked polyubiquitin."; RL J. Biol. Chem. 285:10344-10352(2010). RN [12] RP FUNCTION, INTERACTION WITH BRCC3, IDENTIFICATION BY MASS SPECTROMETRY, AND RP SUBCELLULAR LOCATION. RX PubMed=20656690; DOI=10.1074/jbc.m110.135392; RA Feng L., Wang J., Chen J.; RT "The Lys63-specific deubiquitinating enzyme BRCC36 is regulated by two RT scaffold proteins localizing in different subcellular compartments."; RL J. Biol. Chem. 285:30982-30988(2010). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, AND IDENTIFICATION BY RP 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 [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH BABAM1, RP IDENTIFICATION IN THE BRISC COMPLEX, LACK OF INTERACTION WITH BRCA1, AND RP SUBCELLULAR LOCATION. RX PubMed=21282113; DOI=10.1074/jbc.m110.200857; RA Hu X., Kim J.A., Castillo A., Huang M., Liu J., Wang B.; RT "NBA1/MERIT40 and BRE interaction is required for the integrity of two RT distinct deubiquitinating enzyme BRCC36-containing complexes."; RL J. Biol. Chem. 286:11734-11745(2011). RN [16] RP INTERACTION WITH THAP5, TISSUE SPECIFICITY, INDUCTION, AND SUBCELLULAR RP LOCATION. RX PubMed=21195082; DOI=10.1016/j.yjmcc.2010.12.015; RA Cilenti L., Balakrishnan M.P., Wang X.L., Ambivero C., Sterlicchi M., RA del Monte F., Ma X.L., Zervos A.S.; RT "Regulation of Abro1/KIAA0157 during myocardial infarction and cell death RT reveals a novel cardioprotective mechanism for Lys63-specific RT deubiquitination."; RL J. Mol. Cell. Cardiol. 50:652-661(2011). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368, AND IDENTIFICATION BY RP 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 [18] RP INTERACTION WITH ATF4, AND SUBCELLULAR LOCATION. RX PubMed=22974638; DOI=10.1016/j.bbamcr.2012.08.020; RA Ambivero C.T., Cilenti L., Zervos A.S.; RT "ATF4 interacts with Abro1/KIAA0157 scaffold protein and participates in a RT cytoprotective pathway."; RL Biochim. Biophys. Acta 1823:2149-2156(2012). RN [19] RP FUNCTION, IDENTIFICATION IN THE BRISC COMPLEX, INTERACTION WITH SHMT1 AND RP SHMT2, IDENTIFICATION IN A COMPLEX WITH SHMT2 AND IFNAR1, IDENTIFICATION BY RP MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF RP 215-ALA--ALA-222. 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 [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274 AND SER-280, 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 [21] RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY DNA DAMAGE, INTERACTION WITH RP USP7 AND TP53, AND IDENTIFICATION IN THE BRISC COMPLEX. RX PubMed=25283148; DOI=10.1038/ncomms6059; RA Zhang J., Cao M., Dong J., Li C., Xu W., Zhan Y., Wang X., Yu M., Ge C., RA Ge Z., Yang X.; RT "ABRO1 suppresses tumourigenesis and regulates the DNA damage response by RT stabilizing p53."; RL Nat. Commun. 5:5059-5059(2014). RN [22] RP FUNCTION, INTERACTION WITH NUMA1, SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=26195665; DOI=10.1083/jcb.201503039; RA Yan K., Li L., Wang X., Hong R., Zhang Y., Yang H., Lin M., Zhang S., RA He Q., Zheng D., Tang J., Yin Y., Shao G.; RT "The deubiquitinating enzyme complex BRISC is required for proper mitotic RT spindle assembly in mammalian cells."; RL J. Cell Biol. 210:209-224(2015). RN [23] RP FUNCTION, IDENTIFICATION IN THE BRISC COMPLEX, INTERACTION WITH BRCC3; RP BABAM2; BABAM1 AND SHMT2, SUBUNIT, AND MUTAGENESIS OF 11-SER-ALA-12; RP VAL-220; GLU-231 AND VAL-241. RX PubMed=26344097; DOI=10.1016/j.molcel.2015.07.028; RA Zeqiraj E., Tian L., Piggott C.A., Pillon M.C., Duffy N.M., RA Ceccarelli D.F., Keszei A.F., Lorenzen K., Kurinov I., Orlicky S., RA Gish G.D., Heck A.J., Guarne A., Greenberg R.A., Sicheri F.; RT "Higher-order assembly of BRCC36-KIAA0157 is required for DUB activity and RT biological function."; RL Mol. Cell 59:970-983(2015). CC -!- FUNCTION: Component of the BRISC complex, a multiprotein complex that CC specifically cleaves 'Lys-63'-linked polyubiquitin, leaving the last CC ubiquitin chain attached to its substrates (PubMed:19214193, CC PubMed:20032457, PubMed:20656690, PubMed:24075985). May act as a CC central scaffold protein that assembles the various components of the CC BRISC complex and retains them in the cytoplasm (PubMed:20656690). CC Plays a role in regulating the onset of apoptosis via its role in CC modulating 'Lys-63'-linked ubiquitination of target proteins (By CC similarity). Required for normal mitotic spindle assembly and CC microtubule attachment to kinetochores via its role in deubiquitinating CC NUMA1 (PubMed:26195665). Plays a role in interferon signaling via its CC role in the deubiquitination of the interferon receptor IFNAR1; CC deubiquitination increases IFNAR1 activities by enhancing its stability CC and cell surface expression (PubMed:24075985, PubMed:26344097). Down- CC regulates the response to bacterial lipopolysaccharide (LPS) via its CC role in IFNAR1 deubiquitination (PubMed:24075985). Required for normal CC induction of p53/TP53 in response to DNA damage (PubMed:25283148). CC Independent of the BRISC complex, promotes interaction between USP7 and CC p53/TP53, and thereby promotes deubiquitination of p53/TP53, preventing CC its degradation and resulting in increased p53/TP53-mediated CC transcription regulation and p53/TP53-dependent apoptosis in response CC to DNA damage (PubMed:25283148). {ECO:0000250|UniProtKB:Q3TCJ1, CC ECO:0000269|PubMed:19214193, ECO:0000269|PubMed:20032457, CC ECO:0000269|PubMed:20656690, ECO:0000269|PubMed:24075985, CC ECO:0000269|PubMed:25283148}. CC -!- SUBUNIT: Component of the BRISC complex, at least composed of ABRAXAS2, CC BRCC3/BRCC36, BABAM2 and BABAM1/NBA1 (PubMed:19214193, PubMed:20032457, CC PubMed:21282113, PubMed:24075985, PubMed:25283148, PubMed:26195665, CC PubMed:26344097). Interacts with BRCC3/BRCC36; the interaction is CC direct (PubMed:20032457, PubMed:20656690, PubMed:26344097). Interacts CC with BABAM1 (PubMed:21282113). Does not interact with BRCA1 CC (PubMed:17525340, PubMed:21282113). Interacts with SHMT1 and SHMT2; the CC interaction is direct. Identified in a complex with SHMT2 and the other CC subunits of the BRISC complex (PubMed:24075985). The BRISC complex CC binds monoubiquitin and both 'Lys-48'- and 'Lys-63'-linked CC polyubiquitin (PubMed:20032457). Identified in complexes with IFNAR1, CC IFNAR2 and SHMT2 (PubMed:24075985). Interacts with THAP5 CC (PubMed:21195082). Interacts with ATF4 (PubMed:22974638). Identified in CC a complex with p53/TP53 and USP7; interacts directly with both proteins CC (PubMed:25283148). Interacts with NUMA1 (PubMed:26195665). Interacts CC with microtubule minus ends (PubMed:26195665). Binds polyubiquitin CC (PubMed:19261749). {ECO:0000269|PubMed:17525340, CC ECO:0000269|PubMed:19214193, ECO:0000269|PubMed:19261749, CC ECO:0000269|PubMed:20032457, ECO:0000269|PubMed:20656690, CC ECO:0000269|PubMed:21195082, ECO:0000269|PubMed:21282113, CC ECO:0000269|PubMed:22974638, ECO:0000269|PubMed:24075985, CC ECO:0000269|PubMed:25283148, ECO:0000269|PubMed:26195665, CC ECO:0000269|PubMed:26344097}. CC -!- INTERACTION: CC Q15018; Q9NXR7: BABAM2; NbExp=3; IntAct=EBI-1056583, EBI-949389; CC Q15018; P46736: BRCC3; NbExp=8; IntAct=EBI-1056583, EBI-750352; CC Q15018; Q96GG9: DCUN1D1; NbExp=3; IntAct=EBI-1056583, EBI-740086; CC Q15018; Q14160: SCRIB; NbExp=2; IntAct=EBI-1056583, EBI-357345; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20656690, CC ECO:0000269|PubMed:21195082, ECO:0000269|PubMed:21282113, CC ECO:0000269|PubMed:22974638, ECO:0000269|PubMed:24075985, CC ECO:0000269|PubMed:25283148}. Nucleus {ECO:0000269|PubMed:21282113, CC ECO:0000269|PubMed:22974638, ECO:0000269|PubMed:24075985, CC ECO:0000269|PubMed:25283148}. Cytoplasm, cytoskeleton, spindle pole CC {ECO:0000269|PubMed:26195665}. Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:26195665}. Note=A minor proportion is detected in CC the nucleus (PubMed:21282113, PubMed:22974638). Translocates into the CC nucleus in response to DNA damage (PubMed:25283148). Directly binds to CC microtubules and is detected at the minus end of K-fibers CC (PubMed:26195665). Co-localizes with NUMA1 at mitotic spindle poles CC (PubMed:26195665). {ECO:0000269|PubMed:21282113, CC ECO:0000269|PubMed:22974638, ECO:0000269|PubMed:25283148, CC ECO:0000269|PubMed:26195665}. CC -!- TISSUE SPECIFICITY: Detected in heart muscle (at protein level). CC Detected in heart and muscle, and at much lower levels in brain CC (PubMed:21195082). {ECO:0000269|PubMed:21195082}. CC -!- INDUCTION: Up-regulated in response to DNA damage (PubMed:25283148). CC Up-regulated in myocardial infarction area (at protein level) CC (PubMed:21195082). {ECO:0000269|PubMed:21195082, CC ECO:0000269|PubMed:25283148}. CC -!- SIMILARITY: Belongs to the FAM175 family. Abro1 subfamily. CC {ECO:0000305}. CC -!- CAUTION: Although strongly related to the ABRAXAS1 protein, lacks the CC C-terminal pSXXF that constitutes a specific recognition motif for the CC BRCT domain of BRCA1. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA09927.1; Type=Erroneous initiation; Note=Extended 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; D63877; BAA09927.1; ALT_INIT; mRNA. DR EMBL; AK296677; BAG59274.1; -; mRNA. DR EMBL; BC008999; AAH08999.2; -; mRNA. DR CCDS; CCDS31308.2; -. DR RefSeq; NP_115558.3; NM_032182.3. DR PDB; 6H3C; EM; 3.90 A; A/F=1-415. DR PDB; 6R8F; EM; 3.80 A; B/D=1-267. DR PDB; 8PVY; EM; 3.02 A; B/D/H/J=1-267. DR PDB; 8PY2; EM; 3.32 A; B/D/H/J=1-267. DR PDBsum; 6H3C; -. DR PDBsum; 6R8F; -. DR PDBsum; 8PVY; -. DR PDBsum; 8PY2; -. DR AlphaFoldDB; Q15018; -. DR EMDB; EMD-0132; -. DR EMDB; EMD-17980; -. DR EMDB; EMD-18009; -. DR EMDB; EMD-4759; -. DR EMDB; EMD-4760; -. DR SMR; Q15018; -. DR BioGRID; 116784; 100. DR ComplexPortal; CPX-9341; BRISC-SHMT2 complex. DR ComplexPortal; CPX-9421; BRISC complex. DR CORUM; Q15018; -. DR FunCoup; Q15018; 2806. DR IntAct; Q15018; 105. DR MINT; Q15018; -. DR STRING; 9606.ENSP00000298492; -. DR BindingDB; Q15018; -. DR GlyGen; Q15018; 3 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (2 sites). DR iPTMnet; Q15018; -. DR PhosphoSitePlus; Q15018; -. DR SwissPalm; Q15018; -. DR BioMuta; ABRAXAS2; -. DR DMDM; 84029317; -. DR jPOST; Q15018; -. DR MassIVE; Q15018; -. DR PaxDb; 9606-ENSP00000298492; -. DR PeptideAtlas; Q15018; -. DR ProteomicsDB; 60367; -. DR Pumba; Q15018; -. DR Antibodypedia; 32387; 88 antibodies from 16 providers. DR DNASU; 23172; -. DR Ensembl; ENST00000298492.6; ENSP00000298492.5; ENSG00000165660.9. DR GeneID; 23172; -. DR KEGG; hsa:23172; -. DR MANE-Select; ENST00000298492.6; ENSP00000298492.5; NM_032182.4; NP_115558.3. DR UCSC; uc001lib.4; human. DR AGR; HGNC:28975; -. DR ClinPGx; PA162387331; -. DR CTD; 23172; -. DR DisGeNET; 23172; -. DR GeneCards; ABRAXAS2; -. DR HGNC; HGNC:28975; ABRAXAS2. DR HPA; ENSG00000165660; Low tissue specificity. DR MIM; 611144; gene. DR OpenTargets; ENSG00000165660; -. DR VEuPathDB; HostDB:ENSG00000165660; -. DR eggNOG; ENOG502QTRN; Eukaryota. DR GeneTree; ENSGT00530000063424; -. DR HOGENOM; CLU_040659_0_0_1; -. DR InParanoid; Q15018; -. DR OMA; CPPRGMM; -. DR OrthoDB; 6358435at2759; -. DR PAN-GO; Q15018; 6 GO annotations based on evolutionary models. DR PhylomeDB; Q15018; -. DR PathwayCommons; Q15018; -. DR Reactome; R-HSA-5689901; Metalloprotease DUBs. DR SignaLink; Q15018; -. DR Agora; ENSG00000165660; -. DR BioGRID-ORCS; 23172; 24 hits in 1165 CRISPR screens. DR ChiTaRS; ABRAXAS2; human. DR GeneWiki; KIAA0157; -. DR GenomeRNAi; 23172; -. DR Pharos; Q15018; Tbio. DR PRO; PR:Q15018; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; Q15018; protein. DR Bgee; ENSG00000165660; Expressed in secondary oocyte and 198 other cell types or tissues. DR GO; GO:0070552; C:BRISC complex; IDA:UniProtKB. DR GO; GO:0036064; C:ciliary basal body; IDA:HPA. DR GO; GO:0035869; C:ciliary transition zone; IDA:HPA. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell. DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB. DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IDA:UniProtKB. DR GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; IMP:UniProtKB. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB. DR GO; GO:0000278; P:mitotic cell cycle; IMP:UniProtKB. DR GO; GO:0090307; P:mitotic spindle assembly; IMP:UniProtKB. DR GO; GO:0070536; P:protein K63-linked deubiquitination; IMP:UniProtKB. DR GO; GO:0002931; P:response to ischemia; IMP:UniProtKB. DR CDD; cd23524; Abraxas_2; 1. DR InterPro; IPR023240; BRISC_Abraxas2. DR InterPro; IPR023238; FAM175. DR InterPro; IPR037518; MPN. DR PANTHER; PTHR31728; ABRAXAS FAMILY MEMBER; 1. DR PANTHER; PTHR31728:SF1; BRISC COMPLEX SUBUNIT ABRAXAS 2; 1. DR Pfam; PF21125; MPN_2A_DUB_like; 1. DR PRINTS; PR02053; BRISCABRO1. DR PRINTS; PR02051; PROTEINF175. DR PROSITE; PS50249; MPN; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell cycle; Cell division; Coiled coil; Cytoplasm; KW Cytoskeleton; Microtubule; Mitosis; Nucleus; Phosphoprotein; KW Proteomics identification; Reference proteome; Ubl conjugation pathway. FT CHAIN 1..415 FT /note="BRISC complex subunit Abraxas 2" FT /id="PRO_0000050725" FT DOMAIN 3..149 FT /note="MPN" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182" FT REGION 215..222 FT /note="Important for interaction with SHMT2" FT /evidence="ECO:0000269|PubMed:24075985" FT REGION 220..241 FT /note="Important for interaction with BBRC36 and other FT subunits of the BRISC complex" FT /evidence="ECO:0000269|PubMed:26344097" FT REGION 250..323 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 335..415 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 215..266 FT /evidence="ECO:0000255" FT COMPBIAS 251..261 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 312..322 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 337..347 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 368..379 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 392..408 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 274 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 280 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 368 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:21406692" FT MOD_RES 372 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332" FT MOD_RES 375 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332" FT MUTAGEN 11..12 FT /note="SA->RR: Slightly reduces interaction with BBRC36. FT Abolishes interaction with SHMT2. Strongly reduces FT interactions with BABAM2 and BABAM1." FT /evidence="ECO:0000269|PubMed:26344097" FT MUTAGEN 215..222 FT /note="Missing: Reduces interaction with SHMT2, but has no FT effect on interaction with BRCC3." FT /evidence="ECO:0000269|PubMed:24075985" FT MUTAGEN 220 FT /note="V->R: Strongly reduces interaction with BBRC3; FT SHMT2; BABAM2 and BABAM1; when associated with Y-231. FT Abolishes interaction with BRCC3 and strongly reduces FT interaction with SHMT2; BABAM2 and BABAM1; when associated FT with Y-231 and Y-241." FT /evidence="ECO:0000269|PubMed:26344097" FT MUTAGEN 231 FT /note="E->Y: Strongly reduces interaction with BBRC3; FT SHMT2; BABAM2 and BABAM1; when associated with R-220. FT Abolishes interaction with BRCC3 and strongly reduces FT interaction with SHMT2; BABAM2 and BABAM1; when associated FT with R-220 and Y-241." FT /evidence="ECO:0000269|PubMed:26344097" FT MUTAGEN 241 FT /note="V->R: Abolishes interaction with BRCC3 and strongly FT reduces interaction with SHMT2; BABAM2 and BABAM1; when FT associated with R-220 and Y-231." FT /evidence="ECO:0000269|PubMed:26344097" FT CONFLICT 55..57 FT /note="EIH -> QIY (in Ref. 1; BAA09927)" FT /evidence="ECO:0000305" FT CONFLICT 230 FT /note="S -> G (in Ref. 2; BAG59274)" FT /evidence="ECO:0000305" FT STRAND 2..5 FT /evidence="ECO:0007829|PDB:8PVY" FT HELIX 7..18 FT /evidence="ECO:0007829|PDB:8PVY" FT STRAND 24..34 FT /evidence="ECO:0007829|PDB:8PVY" FT STRAND 52..61 FT /evidence="ECO:0007829|PDB:8PVY" FT STRAND 63..66 FT /evidence="ECO:0007829|PDB:8PVY" FT HELIX 77..83 FT /evidence="ECO:0007829|PDB:8PVY" FT STRAND 84..86 FT /evidence="ECO:0007829|PDB:8PVY" FT HELIX 87..89 FT /evidence="ECO:0007829|PDB:8PVY" FT STRAND 91..100 FT /evidence="ECO:0007829|PDB:8PVY" FT HELIX 107..120 FT /evidence="ECO:0007829|PDB:8PVY" FT STRAND 126..133 FT /evidence="ECO:0007829|PDB:8PVY" FT STRAND 141..148 FT /evidence="ECO:0007829|PDB:8PVY" FT STRAND 152..154 FT /evidence="ECO:0007829|PDB:8PVY" FT HELIX 165..167 FT /evidence="ECO:0007829|PDB:8PVY" FT HELIX 183..192 FT /evidence="ECO:0007829|PDB:8PVY" FT TURN 193..195 FT /evidence="ECO:0007829|PDB:8PVY" FT STRAND 199..203 FT /evidence="ECO:0007829|PDB:8PVY" FT HELIX 204..251 FT /evidence="ECO:0007829|PDB:8PVY" SQ SEQUENCE 415 AA; 46901 MW; EDA67ACB10C66C51 CRC64; MAASISGYTF SAVCFHSANS NADHEGFLLG EVRQEETFSI SDSQISNTEF LQVIEIHNHQ PCSKLFSFYD YASKVNEESL DRILKDRRKK VIGWYRFRRN TQQQMSYREQ VLHKQLTRIL GVPDLVFLLF SFISTANNST HALEYVLFRP NRRYNQRISL AIPNLGNTSQ QEYKVSSVPN TSQSYAKVIK EHGTDFFDKD GVMKDIRAIY QVYNALQEKV QAVCADVEKS ERVVESCQAE VNKLRRQITQ RKNEKEQERR LQQAVLSRQM PSESLDPAFS PRMPSSGFAA EGRSTLGDAE ASDPPPPYSD FHPNNQESTL SHSRMERSVF MPRPQAVGSS NYASTSAGLK YPGSGADLPP PQRAAGDSGE DSDDSDYENL IDPTEPSNSE YSHSKDSRPM AHPDEDPRNT QTSQI //