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BRISC complex subunit Abraxas 2 (Abraxas brother protein 1) (Protein FAM175B)

 ABRX2_HUMAN             Reviewed;         415 AA.
Q15018; B4DKR2; Q96H11;
20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
20-DEC-2005, sequence version 2.
25-OCT-2017, entry version 130.
RecName: Full=BRISC complex subunit Abraxas 2 {ECO:0000312|HGNC:HGNC:28975};
AltName: Full=Abraxas brother protein 1 {ECO:0000303|PubMed:22974638};
AltName: Full=Protein FAM175B;
Name=ABRAXAS2 {ECO:0000312|HGNC:HGNC:28975};
Synonyms=ABRO1 {ECO:0000303|PubMed:21195082},
FAM175B {ECO:0000312|HGNC:HGNC:28975},
KIAA0157 {ECO:0000303|PubMed:8590280};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Bone marrow;
PubMed=8590280; DOI=10.1093/dnares/2.4.167;
Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. IV.
The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by
analysis of cDNA clones from human cell line KG-1.";
DNA Res. 2:167-174(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368 AND SER-372, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[6]
LACK OF INTERACTION WITH BRCA1, AND SUBUNIT.
PubMed=17525340; DOI=10.1126/science.1139476;
Wang B., Matsuoka S., Ballif B.A., Zhang D., Smogorzewska A., Giyi S.,
Elledge S.J.;
"Abraxas and RAP80 form a BRCA1 protein complex required for the DNA
damage response.";
Science 316:1194-1198(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280; SER-368; SER-372
AND SER-375, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[8]
IDENTIFICATION IN THE BRISC COMPLEX, FUNCTION, AND SUBUNIT.
PubMed=19214193; DOI=10.1038/emboj.2009.27;
Cooper E.M., Cutcliffe C., Kristiansen T.Z., Pandey A., Pickart C.M.,
Cohen R.E.;
"K63-specific deubiquitination by two JAMM/MPN+ complexes: BRISC-
associated Brcc36 and proteasomal Poh1.";
EMBO J. 28:621-631(2009).
[9]
DOMAIN MPN-LIKE, UBIQUITIN-BINDING, AND SUBUNIT.
PubMed=19261749; DOI=10.1101/gad.1770309;
Wang B., Hurov K., Hofmann K., Elledge S.J.;
"NBA1, a new player in the Brca1 A complex, is required for DNA damage
resistance and checkpoint control.";
Genes Dev. 23:729-739(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368; SER-372 AND
SER-375, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[11]
FUNCTION, SUBUNIT, IDENTIFICATION IN THE BRISC COMPLEX, AND
INTERACTION OF THE BRISC COMPLEX WITH UBIQUITIN.
PubMed=20032457; DOI=10.1074/jbc.M109.059667;
Cooper E.M., Boeke J.D., Cohen R.E.;
"Specificity of the BRISC deubiquitinating enzyme is not due to
selective binding to Lys63-linked polyubiquitin.";
J. Biol. Chem. 285:10344-10352(2010).
[12]
FUNCTION, INTERACTION WITH BRCC3, IDENTIFICATION BY MASS SPECTROMETRY,
AND SUBCELLULAR LOCATION.
PubMed=20656690; DOI=10.1074/jbc.M110.135392;
Feng L., Wang J., Chen J.;
"The Lys63-specific deubiquitinating enzyme BRCC36 is regulated by two
scaffold proteins localizing in different subcellular compartments.";
J. Biol. Chem. 285:30982-30988(2010).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH BABAM1,
IDENTIFICATION IN THE BRISC COMPLEX, LACK OF INTERACTION WITH BRCA1,
AND SUBCELLULAR LOCATION.
PubMed=21282113; DOI=10.1074/jbc.M110.200857;
Hu X., Kim J.A., Castillo A., Huang M., Liu J., Wang B.;
"NBA1/MERIT40 and BRE interaction is required for the integrity of two
distinct deubiquitinating enzyme BRCC36-containing complexes.";
J. Biol. Chem. 286:11734-11745(2011).
[16]
INTERACTION WITH THAP5, TISSUE SPECIFICITY, INDUCTION, AND SUBCELLULAR
LOCATION.
PubMed=21195082; DOI=10.1016/j.yjmcc.2010.12.015;
Cilenti L., Balakrishnan M.P., Wang X.L., Ambivero C., Sterlicchi M.,
del Monte F., Ma X.L., Zervos A.S.;
"Regulation of Abro1/KIAA0157 during myocardial infarction and cell
death reveals a novel cardioprotective mechanism for Lys63-specific
deubiquitination.";
J. Mol. Cell. Cardiol. 50:652-661(2011).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[18]
INTERACTION WITH ATF4, AND SUBCELLULAR LOCATION.
PubMed=22974638; DOI=10.1016/j.bbamcr.2012.08.020;
Ambivero C.T., Cilenti L., Zervos A.S.;
"ATF4 interacts with Abro1/KIAA0157 scaffold protein and participates
in a cytoprotective pathway.";
Biochim. Biophys. Acta 1823:2149-2156(2012).
[19]
FUNCTION, IDENTIFICATION IN THE BRISC COMPLEX, INTERACTION WITH SHMT1
AND SHMT2, IDENTIFICATION IN A COMPLEX WITH SHMT2 AND IFNAR1,
IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF 215-ALA--ALA-222.
PubMed=24075985; DOI=10.1016/j.celrep.2013.08.025;
Zheng H., Gupta V., Patterson-Fortin J., Bhattacharya S.,
Katlinski K., Wu J., Varghese B., Carbone C.J., Aressy B., Fuchs S.Y.,
Greenberg R.A.;
"A BRISC-SHMT complex deubiquitinates IFNAR1 and regulates interferon
responses.";
Cell Rep. 5:180-193(2013).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274 AND SER-280, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[21]
FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY DNA DAMAGE, INTERACTION
WITH USP7 AND TP53, AND IDENTIFICATION IN THE BRISC COMPLEX.
PubMed=25283148; DOI=10.1038/ncomms6059;
Zhang J., Cao M., Dong J., Li C., Xu W., Zhan Y., Wang X., Yu M.,
Ge C., Ge Z., Yang X.;
"ABRO1 suppresses tumourigenesis and regulates the DNA damage response
by stabilizing p53.";
Nat. Commun. 5:5059-5059(2014).
[22]
FUNCTION, INTERACTION WITH NUMA1, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=26195665; DOI=10.1083/jcb.201503039;
Yan K., Li L., Wang X., Hong R., Zhang Y., Yang H., Lin M., Zhang S.,
He Q., Zheng D., Tang J., Yin Y., Shao G.;
"The deubiquitinating enzyme complex BRISC is required for proper
mitotic spindle assembly in mammalian cells.";
J. Cell Biol. 210:209-224(2015).
[23]
FUNCTION, IDENTIFICATION IN THE BRISC COMPLEX, INTERACTION WITH BRCC3;
BABAM2; BABAM1 AND SHMT2, SUBUNIT, AND MUTAGENESIS OF 11-SER-ALA-12;
VAL-220; GLU-231 AND VAL-241.
PubMed=26344097; DOI=10.1016/j.molcel.2015.07.028;
Zeqiraj E., Tian L., Piggott C.A., Pillon M.C., Duffy N.M.,
Ceccarelli D.F., Keszei A.F., Lorenzen K., Kurinov I., Orlicky S.,
Gish G.D., Heck A.J., Guarne A., Greenberg R.A., Sicheri F.;
"Higher-order assembly of BRCC36-KIAA0157 is required for DUB activity
and biological function.";
Mol. Cell 59:970-983(2015).
-!- FUNCTION: Component of the BRISC complex, a multiprotein complex
that specifically cleaves 'Lys-63'-linked polyubiquitin, leaving
the last ubiquitin chain attached to its substrates
(PubMed:19214193, PubMed:20032457, PubMed:20656690,
PubMed:24075985). May act as a central scaffold protein that
assembles the various components of the BRISC complex and retains
them in the cytoplasm (PubMed:20656690). Plays a role in
regulating the onset of apoptosis via its role in modulating 'Lys-
63'-linked ubiquitination of target proteins (By similarity).
Required for normal mitotic spindle assembly and microtubule
attachment to kinetochores via its role in deubiquitinating NUMA1
(PubMed:26195665). Plays a role in interferon signaling via its
role in the deubiquitination of the interferon receptor IFNAR1;
deubiquitination increases IFNAR1 activities by enhancing its
stability and cell surface expression (PubMed:24075985,
PubMed:26344097). Down-regulates the response to bacterial
lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination
(PubMed:24075985). Required for normal induction of p53/TP53 in
response to DNA damage (PubMed:25283148). Independent of the BRISC
complex, promotes interaction between USP7 and p53/TP53, and
thereby promotes deubiquitination of p53/TP53, preventing its
degradation and resulting in increased p53/TP53-mediated
transcription regulation and p53/TP53-dependent apoptosis in
response to DNA damage (PubMed:25283148).
{ECO:0000250|UniProtKB:Q3TCJ1, ECO:0000269|PubMed:19214193,
ECO:0000269|PubMed:20032457, ECO:0000269|PubMed:20656690,
ECO:0000269|PubMed:24075985, ECO:0000269|PubMed:25283148}.
-!- SUBUNIT: Component of the BRISC complex, at least composed of
ABRAXAS2, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1 (PubMed:19214193,
PubMed:20032457, PubMed:21282113, PubMed:24075985,
PubMed:25283148, PubMed:26344097, PubMed:26195665). Interacts with
BRCC3/BRCC36; the interaction is direct (PubMed:20032457,
PubMed:20656690, PubMed:26344097). Interacts with BABAM1
(PubMed:21282113). Does not interact with BRCA1 (PubMed:17525340,
PubMed:21282113). Interacts with SHMT1 and SHMT2; the interaction
is direct. Identified in a complex with SHMT2 and the other
subunits of the BRISC complex (PubMed:24075985). The BRISC complex
binds monoubiquitin and both 'Lys-48'- and 'Lys-63'-linked
polyubiquitin (PubMed:20032457). Identified in complexes with
IFNAR1, IFNAR2 and SHMT2 (PubMed:24075985). Interacts with THAP5
(PubMed:21195082). Interacts with ATF4 (PubMed:22974638).
Identified in a complex with p53/TP53 and USP7; interacts directly
with both proteins (PubMed:25283148). Interacts with NUMA1
(PubMed:26195665). Interacts with microtubule minus ends
(PubMed:26195665). Binds polyubiquitin (PubMed:19261749).
{ECO:0000269|PubMed:17525340, ECO:0000269|PubMed:19214193,
ECO:0000269|PubMed:19261749, ECO:0000269|PubMed:20032457,
ECO:0000269|PubMed:20656690, ECO:0000269|PubMed:21195082,
ECO:0000269|PubMed:21282113, ECO:0000269|PubMed:22974638,
ECO:0000269|PubMed:24075985, ECO:0000269|PubMed:25283148,
ECO:0000269|PubMed:26195665, ECO:0000269|PubMed:26344097}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20656690,
ECO:0000269|PubMed:21195082, ECO:0000269|PubMed:21282113,
ECO:0000269|PubMed:22974638, ECO:0000269|PubMed:24075985,
ECO:0000269|PubMed:25283148}. Nucleus
{ECO:0000269|PubMed:21282113, ECO:0000269|PubMed:22974638,
ECO:0000269|PubMed:24075985, ECO:0000269|PubMed:25283148}.
Cytoplasm, cytoskeleton, spindle pole
{ECO:0000269|PubMed:26195665}. Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:26195665}. Note=A minor proportion is detected
in the nucleus (PubMed:21282113, PubMed:22974638). Translocates
into the nucleus in response to DNA damage (PubMed:25283148).
Directly binds to microtubules and is detected at the minus end of
K-fibers (PubMed:26195665). Co-localizes with NUMA1 at mitotic
spindle poles (PubMed:26195665). {ECO:0000269|PubMed:21282113,
ECO:0000269|PubMed:22974638, ECO:0000269|PubMed:25283148,
ECO:0000269|PubMed:26195665}.
-!- TISSUE SPECIFICITY: Detected in heart muscle (at protein level).
Detected in heart and muscle, and at much lower levels in brain
(PubMed:21195082). {ECO:0000269|PubMed:21195082}.
-!- INDUCTION: Up-regulated in response to DNA damage
(PubMed:25283148). Up-regulated in myocardial infarction area (at
protein level) (PubMed:21195082). {ECO:0000269|PubMed:21195082,
ECO:0000269|PubMed:25283148}.
-!- SIMILARITY: Belongs to the FAM175 family. Abro1 subfamily.
{ECO:0000305}.
-!- CAUTION: Although strongly related to the ABRAXAS1 protein, lacks
the C-terminal pSXXF that constitutes a specific recognition motif
for the BRCT domain of BRCA1. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA09927.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; D63877; BAA09927.1; ALT_INIT; mRNA.
EMBL; AK296677; BAG59274.1; -; mRNA.
EMBL; BC008999; AAH08999.2; -; mRNA.
CCDS; CCDS31308.2; -.
RefSeq; NP_115558.3; NM_032182.3.
UniGene; Hs.280695; -.
ProteinModelPortal; Q15018; -.
SMR; Q15018; -.
BioGrid; 116784; 49.
IntAct; Q15018; 40.
MINT; MINT-1181536; -.
STRING; 9606.ENSP00000298492; -.
BindingDB; Q15018; -.
iPTMnet; Q15018; -.
PhosphoSitePlus; Q15018; -.
BioMuta; FAM175B; -.
DMDM; 84029317; -.
EPD; Q15018; -.
MaxQB; Q15018; -.
PaxDb; Q15018; -.
PeptideAtlas; Q15018; -.
PRIDE; Q15018; -.
Ensembl; ENST00000298492; ENSP00000298492; ENSG00000165660.
GeneID; 23172; -.
KEGG; hsa:23172; -.
UCSC; uc001lib.4; human.
CTD; 23172; -.
DisGeNET; 23172; -.
EuPathDB; HostDB:ENSG00000165660.7; -.
GeneCards; ABRAXAS2; -.
H-InvDB; HIX0009288; -.
HGNC; HGNC:28975; ABRAXAS2.
HPA; HPA037591; -.
HPA; HPA037592; -.
HPA; HPA074089; -.
neXtProt; NX_Q15018; -.
OpenTargets; ENSG00000165660; -.
PharmGKB; PA162387331; -.
eggNOG; ENOG410IPEG; Eukaryota.
eggNOG; ENOG410ZUYJ; LUCA.
GeneTree; ENSGT00530000063424; -.
HOGENOM; HOG000112450; -.
HOVERGEN; HBG081817; -.
InParanoid; Q15018; -.
KO; K20799; -.
OMA; REQVLHK; -.
OrthoDB; EOG091G07ID; -.
PhylomeDB; Q15018; -.
TreeFam; TF331751; -.
Reactome; R-HSA-5689901; Metalloprotease DUBs.
GeneWiki; KIAA0157; -.
GenomeRNAi; 23172; -.
PRO; PR:Q15018; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000165660; -.
CleanEx; HS_FAM175B; -.
Genevisible; Q15018; HS.
GO; GO:0070552; C:BRISC complex; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; IMP:UniProtKB.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB.
GO; GO:0000278; P:mitotic cell cycle; IMP:UniProtKB.
GO; GO:0090307; P:mitotic spindle assembly; IMP:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0070536; P:protein K63-linked deubiquitination; IMP:UniProtKB.
GO; GO:0002931; P:response to ischemia; IMP:UniProtKB.
InterPro; IPR023238; FAM175.
InterPro; IPR023240; FAM175_BRISC_cplx_Abro1_su.
PRINTS; PR02053; BRISCABRO1.
PRINTS; PR02051; PROTEINF175.
PROSITE; PS50249; MPN; 1.
1: Evidence at protein level;
Cell cycle; Cell division; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Microtubule; Mitosis; Nucleus; Phosphoprotein;
Reference proteome; Ubl conjugation pathway.
CHAIN 1 415 BRISC complex subunit Abraxas 2.
/FTId=PRO_0000050725.
DOMAIN 3 149 MPN. {ECO:0000255|PROSITE-
ProRule:PRU01182}.
REGION 215 222 Important for interaction with SHMT2.
{ECO:0000269|PubMed:24075985}.
REGION 220 241 Important for interaction with BBRC36 and
other subunits of the BRISC complex.
{ECO:0000269|PubMed:26344097}.
COILED 215 266 {ECO:0000255}.
MOD_RES 274 274 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 280 280 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 368 368 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692}.
MOD_RES 372 372 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 375 375 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MUTAGEN 11 12 SA->RR: Slighly reduces interaction with
BBRC36. Abolishes interaction with SHMT2.
Strongly reduces interactions with BABAM2
and BABAM1.
{ECO:0000269|PubMed:26344097}.
MUTAGEN 215 222 Missing: Reduces interaction with SHMT2,
but has no effect on interaction with
BRCC3. {ECO:0000269|PubMed:24075985}.
MUTAGEN 220 220 V->R: Strongly reduces interaction with
BBRC3; SHMT2; BABAM2 and BABAM1; when
associated with Y-231. Abolishes
interaction with BRCC3 and strongly
reduces interaction with SHMT2; BABAM2
and BABAM1; when associated with Y-231
and Y-241. {ECO:0000269|PubMed:26344097}.
MUTAGEN 231 231 E->Y: Strongly reduces interaction with
BBRC3; SHMT2; BABAM2 and BABAM1; when
associated with R-220. Abolishes
interaction with BRCC3 and strongly
reduces interaction with SHMT2; BABAM2
and BABAM1; when associated with R-220
and Y-241. {ECO:0000269|PubMed:26344097}.
MUTAGEN 241 241 V->R: Abolishes interaction with BRCC3
and strongly reduces interaction with
SHMT2; BABAM2 and BABAM1; when associated
with R-220 and Y-231.
{ECO:0000269|PubMed:26344097}.
CONFLICT 55 57 EIH -> QIY (in Ref. 1; BAA09927).
{ECO:0000305}.
CONFLICT 230 230 S -> G (in Ref. 2; BAG59274).
{ECO:0000305}.
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


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