ABRX2_BOVIN
ID ABRX2_BOVIN Reviewed; 409 AA.
AC A6QLR3;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=BRISC complex subunit Abraxas 2 {ECO:0000250|UniProtKB:Q15018};
DE AltName: Full=Abraxas brother protein 1;
DE AltName: Full=Protein FAM175B;
GN Name=ABRAXAS2 {ECO:0000250|UniProtKB:Q15018}; Synonyms=ABRO1, FAM175B;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). Required
CC for normal mitotic spindle assembly and microtubule attachment to
CC 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 Down-regulates the response to bacterial lipopolysaccharide (LPS) via
CC its role in IFNAR1 deubiquitination. 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:0000250|UniProtKB:Q3TCJ1}.
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. Interacts with ATF4. Identified
CC in a complex with p53/TP53 and USP7; interacts directly with both
CC proteins. Interacts with NUMA1. Interacts with microtubule minus ends.
CC Binds polyubiquitin. {ECO:0000250|UniProtKB:Q15018}.
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 -!- 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; EE228209; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC148057; AAI48058.1; -; mRNA.
DR RefSeq; NP_001160059.1; NM_001166587.1.
DR AlphaFoldDB; A6QLR3; -.
DR SMR; A6QLR3; -.
DR STRING; 9913.ENSBTAP00000032663; -.
DR PaxDb; A6QLR3; -.
DR GeneID; 510233; -.
DR KEGG; bta:510233; -.
DR CTD; 23172; -.
DR eggNOG; ENOG502QTRN; Eukaryota.
DR InParanoid; A6QLR3; -.
DR OrthoDB; 954711at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0070552; C:BRISC complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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; 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: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:0070536; P:protein K63-linked deubiquitination; ISS:UniProtKB.
DR GO; GO:0002931; P:response to ischemia; ISS: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 2: Evidence at transcript level;
KW Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton;
KW Microtubule; Mitosis; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..409
FT /note="BRISC complex subunit Abraxas 2"
FT /id="PRO_0000373942"
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 248..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 215..264
FT /evidence="ECO:0000255"
FT COMPBIAS 248..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..348
FT /note="Polar 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 409 AA; 46138 MW; 69DBF50D831BCB44 CRC64;
MAASISGYTF SAVCFHSANS NADHEGFLLG EVRQEETFSI SDSQISSTEF LQVIEIHNHQ
PCSKLFSFYD YASKVNEESL DRILKDRRKK VIGWYRFRRN TQQQMSYREQ VIHKQLTRIL
GVPDLVFLLF SFISTANNST HALEYVLFRP NRRYNQRISL AIPNLGNTSQ QEYKVSSVPN
TSQSYAKVIK EHGADFFDKD GVMKDIRAIY QVYNALQEKV QAVCADVEKS ERVVESCQAE
VNKLRRQITQ RKNEKEQERR LQQAMVSRQM PSESVDPTFS PRMPYPGFTA EGRSTLGDTE
ASDPPPPYSD LHPNNQESTL SHSRMESSVF MPRPQAVGSS SYASTSAGLK YPGSGADAPP
SHRAAGDSAE ESDDSDYENL IDPTEPPNSE YSRSRDSRPM THPDGGSQI
