ABRX2_HUMAN
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 03-AUG-2022, entry version 159.
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},
GN FAM175B {ECO:0000312|HGNC:HGNC:28975},
GN 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:26344097,
CC PubMed:26195665). 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; Q96GG9: DCUN1D1; NbExp=3; IntAct=EBI-1056583, EBI-740086;
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};
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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 PDBsum; 6H3C; -.
DR PDBsum; 6R8F; -.
DR AlphaFoldDB; Q15018; -.
DR SMR; Q15018; -.
DR BioGRID; 116784; 87.
DR CORUM; Q15018; -.
DR IntAct; Q15018; 66.
DR MINT; Q15018; -.
DR STRING; 9606.ENSP00000298492; -.
DR BindingDB; Q15018; -.
DR GlyGen; Q15018; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q15018; -.
DR PhosphoSitePlus; Q15018; -.
DR BioMuta; ABRAXAS2; -.
DR DMDM; 84029317; -.
DR EPD; Q15018; -.
DR jPOST; Q15018; -.
DR MassIVE; Q15018; -.
DR MaxQB; Q15018; -.
DR PaxDb; Q15018; -.
DR PeptideAtlas; Q15018; -.
DR PRIDE; Q15018; -.
DR ProteomicsDB; 60367; -.
DR Antibodypedia; 32387; 90 antibodies from 17 providers.
DR DNASU; 23172; -.
DR Ensembl; ENST00000298492.6; ENSP00000298492.5; ENSG00000165660.8.
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 CTD; 23172; -.
DR DisGeNET; 23172; -.
DR GeneCards; ABRAXAS2; -.
DR HGNC; HGNC:28975; ABRAXAS2.
DR HPA; ENSG00000165660; Low tissue specificity.
DR MIM; 611144; gene.
DR neXtProt; NX_Q15018; -.
DR OpenTargets; ENSG00000165660; -.
DR PharmGKB; PA162387331; -.
DR VEuPathDB; HostDB:ENSG00000165660; -.
DR eggNOG; ENOG502QTRN; Eukaryota.
DR GeneTree; ENSGT00530000063424; -.
DR HOGENOM; CLU_040659_0_0_1; -.
DR InParanoid; Q15018; -.
DR OMA; PYSDFNT; -.
DR OrthoDB; 954711at2759; -.
DR PhylomeDB; Q15018; -.
DR TreeFam; TF331751; -.
DR PathwayCommons; Q15018; -.
DR Reactome; R-HSA-5689901; Metalloprotease DUBs.
DR SignaLink; Q15018; -.
DR BioGRID-ORCS; 23172; 22 hits in 1086 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 196 other tissues.
DR Genevisible; Q15018; HS.
DR GO; GO:0070552; C:BRISC complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
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 InterPro; IPR023238; FAM175.
DR InterPro; IPR023240; FAM175_BRISC_cplx_Abro1_su.
DR InterPro; IPR037518; MPN.
DR PANTHER; PTHR31728; PTHR31728; 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 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 389..405
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"
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
