ABRX2_XENTR
ID ABRX2_XENTR Reviewed; 390 AA.
AC Q6P4W0;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=BRISC complex subunit Abraxas 2 {ECO:0000250|UniProtKB:Q15018};
DE AltName: Full=Abraxas brother protein 1;
DE AltName: Full=BRISC complex subunit Abro1;
DE AltName: Full=Protein FAM175B;
GN Name=abraxas2 {ECO:0000250|UniProtKB:Q15018}; Synonyms=abro1, fam175b;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2003) 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 (By similarity).
CC {ECO:0000250|UniProtKB:Q15018, ECO:0000250|UniProtKB:Q3TCJ1}.
CC -!- SUBUNIT: Component of the BRISC complex, at least composed of ABRAXAS2
CC and the catalytic subunit brcc3/brcc36. Interacts with brcc3/brcc36;
CC the interaction is direct. The BRISC complex binds monoubiquitin and
CC 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. {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; BC063225; AAH63225.1; -; mRNA.
DR RefSeq; NP_001192104.1; NM_001205175.1.
DR AlphaFoldDB; Q6P4W0; -.
DR SMR; Q6P4W0; -.
DR STRING; 8364.ENSXETP00000050983; -.
DR PaxDb; Q6P4W0; -.
DR PRIDE; Q6P4W0; -.
DR GeneID; 394764; -.
DR KEGG; xtr:394764; -.
DR CTD; 23172; -.
DR Xenbase; XB-GENE-5771927; abraxas2.
DR eggNOG; ENOG502QTRN; Eukaryota.
DR HOGENOM; CLU_040659_0_0_1; -.
DR InParanoid; Q6P4W0; -.
DR OMA; PYSDFNT; -.
DR OrthoDB; 954711at2759; -.
DR PhylomeDB; Q6P4W0; -.
DR TreeFam; TF331751; -.
DR Reactome; R-XTR-5689901; Metalloprotease DUBs.
DR Proteomes; UP000008143; Chromosome 7.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000023627; Expressed in egg cell and 16 other tissues.
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; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..390
FT /note="BRISC complex subunit Abraxas 2"
FT /id="PRO_0000373943"
FT DOMAIN 3..149
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 288..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 209..248
FT /evidence="ECO:0000255"
FT COMPBIAS 345..369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 390 AA; 44288 MW; 3D15BB218258FBA4 CRC64;
MAASISGYTF SSLCFHSANS CSDHEGFLLG EVRQEETFSI SDSQISNTEL LQVIEIHRHE
PCTNLFSFYD YAGTVNEESL DRILKDRRKN VIGWYRFRRN TQQQMSYREQ ILHKQLTRLL
GAPDLVFLLI TFISTANTST HALEYVLFRP NRRYNQRVSL TIPNLGTTSQ QEYKVSSVPN
TSQNYAKVIK EHGINFFDKD GVMKDIRLIY QVYNALQEKV QAVSEEVEKS ERVVESCQAE
VDKLRTQICR RKAEKEREEN LRHSLQLQTE DTTDCVMTLS STDFIAAASR PQDLHPPAYT
EENADAKDGV DSPPDMPRPQ AVGSSCQLLI EIKDGEPSAC KTSASEETET EESQSDYKKS
RHLSESPDSD MADDQPCQLS TQPDGDLAQQ
