ABRX2_MOUSE
ID ABRX2_MOUSE Reviewed; 415 AA.
AC Q3TCJ1; Q3TB08; Q8K0R4;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=BRISC complex subunit Abraxas 2 {ECO:0000312|MGI:MGI:1926116};
DE AltName: Full=Abraxas brother protein 1;
DE AltName: Full=Protein FAM175B;
GN Name=Abraxas2 {ECO:0000312|MGI:MGI:1926116};
GN Synonyms=Abro1 {ECO:0000303|PubMed:21195082}, Fam175b, Kiaa0157;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 70-415.
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY HEART ISCHEMIA.
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 [5]
RP INTERACTION WITH ATF4.
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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 [7]
RP FUNCTION.
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. May act as a central
CC scaffold protein that assembles the various components of the BRISC
CC complex and retains them in the cytoplasm (By similarity). Plays a role
CC in regulating the onset of apoptosis via its role in modulating 'Lys-
CC 63'-linked ubiquitination of target proteins (PubMed:21195082).
CC Required for normal mitotic spindle assembly and microtubule attachment
CC to kinetochores via its role in deubiquitinating NUMA1. Plays a role in
CC interferon signaling via its role in the deubiquitination of the
CC interferon receptor IFNAR1; deubiquitination increases IFNAR1
CC activities by enhancing its stability and cell surface expression
CC (PubMed:24075985, PubMed:26344097). Down-regulates the response to
CC bacterial lipopolysaccharide (LPS) via its role in IFNAR1
CC deubiquitination (PubMed:24075985). Required for normal induction of
CC p53/TP53 in response to DNA damage. Independent of the BRISC complex,
CC promotes interaction between USP7 and p53/TP53, and thereby promotes
CC deubiquitination of p53/TP53, preventing its degradation and resulting
CC in increased p53/TP53-mediated transcription regulation and p53/TP53-
CC dependent apoptosis in response to DNA damage (By similarity).
CC {ECO:0000250|UniProtKB:Q15018, ECO:0000269|PubMed:24075985,
CC ECO:0000269|PubMed:26344097, ECO:0000305|PubMed:21195082}.
CC -!- SUBUNIT: Component of the BRISC complex, at least composed of ABRAXAS2,
CC BRCC3/BRCC36, BABAM2 and BABAM1/NBA1. Interacts with BRCC3/BRCC36; the
CC interaction is direct. Interacts with BABAM1. Does not interact with
CC BRCA1. Interacts with SHMT1 and SHMT2; the interaction is direct.
CC Identified in a complex with SHMT2 and the other subunits of the BRISC
CC complex. The BRISC complex binds monoubiquitin and both 'Lys-48'- and
CC 'Lys-63'-linked polyubiquitin. Identified in complexes with IFNAR1,
CC IFNAR2 and SHMT2. Interacts with THAP5 (By similarity). Interacts with
CC ATF4 (PubMed:22974638). Identified in a complex with p53/TP53 and USP7;
CC interacts directly with both proteins. Interacts with NUMA1. Interacts
CC with microtubule minus ends. Binds polyubiquitin (By similarity).
CC {ECO:0000250|UniProtKB:Q15018, ECO:0000269|PubMed:22974638}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q15018}. Nucleus
CC {ECO:0000250|UniProtKB:Q15018}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250|UniProtKB:Q15018}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q15018}. Note=A minor proportion is detected in
CC the nucleus. Translocates into the nucleus in response to DNA damage.
CC Directly binds to microtubules and is detected at the minus end of K-
CC fibers. Co-localizes with NUMA1 at mitotic spindle poles.
CC {ECO:0000250|UniProtKB:Q15018}.
CC -!- TISSUE SPECIFICITY: Detected in heart (at protein level).
CC {ECO:0000269|PubMed:21195082}.
CC -!- INDUCTION: Up-regulated in heart in response to ischemia and
CC reperfusion (at protein level). {ECO:0000269|PubMed:21195082}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable and fertile, and are protected
CC against toxic shock caused by bacterial lipopolysaccharide (LPS).
CC IFNAR1 'Lys-63'-linked ubiquitination and IFNAR1 internalization are
CC increased. {ECO:0000269|PubMed:24075985}.
CC -!- MISCELLANEOUS: Interaction with THAP5 has been shown in human, but
CC rodents lack a THAP5 homolog. {ECO:0000305}.
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}.
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DR EMBL; AK170704; BAE41965.1; -; mRNA.
DR EMBL; AK171524; BAE42506.1; -; mRNA.
DR EMBL; BC030838; AAH30838.2; -; mRNA.
DR RefSeq; NP_932134.3; NM_198017.3.
DR AlphaFoldDB; Q3TCJ1; -.
DR SMR; Q3TCJ1; -.
DR BioGRID; 224665; 22.
DR STRING; 10090.ENSMUSP00000081541; -.
DR iPTMnet; Q3TCJ1; -.
DR PhosphoSitePlus; Q3TCJ1; -.
DR SwissPalm; Q3TCJ1; -.
DR EPD; Q3TCJ1; -.
DR MaxQB; Q3TCJ1; -.
DR PaxDb; Q3TCJ1; -.
DR PeptideAtlas; Q3TCJ1; -.
DR PRIDE; Q3TCJ1; -.
DR ProteomicsDB; 286020; -.
DR GeneID; 109359; -.
DR KEGG; mmu:109359; -.
DR UCSC; uc009kcr.2; mouse.
DR CTD; 23172; -.
DR MGI; MGI:1926116; Abraxas2.
DR eggNOG; ENOG502QTRN; Eukaryota.
DR InParanoid; Q3TCJ1; -.
DR OrthoDB; 954711at2759; -.
DR PhylomeDB; Q3TCJ1; -.
DR TreeFam; TF331751; -.
DR Reactome; R-MMU-5689901; Metalloprotease DUBs.
DR BioGRID-ORCS; 109359; 3 hits in 68 CRISPR screens.
DR ChiTaRS; Fam175b; mouse.
DR PRO; PR:Q3TCJ1; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q3TCJ1; protein.
DR GO; GO:0070552; C:BRISC complex; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0036449; C:microtubule minus-end; ISO:MGI.
DR GO; GO:0030496; C:midbody; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0031616; C:spindle pole centrosome; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071497; P:cellular response to freezing; IGI:MGI.
DR GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0090307; P:mitotic spindle assembly; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; 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 Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton;
KW Microtubule; Mitosis; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..415
FT /note="BRISC complex subunit Abraxas 2"
FT /id="PRO_0000050726"
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:0000250|UniProtKB:Q15018"
FT REGION 220..241
FT /note="Important for interaction with BBRC36 and other
FT subunits of the BRISC complex"
FT /evidence="ECO:0000250|UniProtKB:Q15018"
FT REGION 249..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 215..266
FT /evidence="ECO:0000255"
FT COMPBIAS 336..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15018"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15018"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15018"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15018"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15018"
SQ SEQUENCE 415 AA; 46943 MW; C9CB374DA089AFA3 CRC64;
MAASISGYTF SAVCFHSANS NADHEGFLLG EVRQEETFSI SDSQISNTEF LQVIEIHNHQ
PCSQLFSFYD YASKVNEESL DRILKDRRKK VIGWYRFRRN TQQQMSYREQ VIHKQLTRIL
GVPDLVFLLF SFISTANNST HALEYVLFRP NRRYNQRISL AIPNLGNTSQ QEYKVSSVPN
TSQSYAKVIK EHGTDFFDKD GVMKDIRAIY QVYNALQEKV QAVCADVEKS ERVVESCQAE
VNKLRRQITQ KKNEKEQERR LQQALLSRQM PSESLEPAFS PRMSYSGFSA EGRSTLAETE
PSDPPPPYSD FHPNNQESTL SHSRMERSVF MPRPQAVGSS SYASTSGGLK FTGSGADLLP
SQSAAGDSGE ESDDSDYENL IDPAESPHSE YSHSKNSRPS THPDEDPRNT QTSQI
