BAP1_XENTR
ID BAP1_XENTR Reviewed; 685 AA.
AC Q66JB6; Q28DW6;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase BAP1;
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:Q92560};
DE AltName: Full=BRCA1-associated protein 1;
GN Name=bap1; ORFNames=TEgg031c22.1;
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=Egg;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Deubiquitinating enzyme that plays a key role in chromatin by
CC mediating deubiquitination of histone H2A. Catalytic component of the
CC PR-DUB complex, a complex that specifically mediates deubiquitination
CC of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1) (By
CC similarity). {ECO:0000250|UniProtKB:Q92560}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:Q92560};
CC -!- SUBUNIT: Component of the PR-DUB complex.
CC {ECO:0000250|UniProtKB:Q92560}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q92560}. Nucleus
CC {ECO:0000250|UniProtKB:Q92560}. Note=Mainly nuclear. Binds to
CC chromatin. {ECO:0000250|UniProtKB:Q92560}.
CC -!- SIMILARITY: Belongs to the peptidase C12 family. BAP1 subfamily.
CC {ECO:0000305}.
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DR EMBL; CR848566; CAJ81966.1; -; mRNA.
DR EMBL; BC080985; AAH80985.1; -; mRNA.
DR RefSeq; NP_001008206.1; NM_001008205.1.
DR AlphaFoldDB; Q66JB6; -.
DR SMR; Q66JB6; -.
DR STRING; 8364.ENSXETP00000000167; -.
DR MEROPS; C12.004; -.
DR PaxDb; Q66JB6; -.
DR DNASU; 493568; -.
DR GeneID; 493568; -.
DR KEGG; xtr:493568; -.
DR CTD; 8314; -.
DR Xenbase; XB-GENE-494978; bap1.
DR eggNOG; KOG2778; Eukaryota.
DR InParanoid; Q66JB6; -.
DR OrthoDB; 1363547at2759; -.
DR Reactome; R-XTR-5689603; UCH proteinases.
DR Proteomes; UP000008143; Chromosome 4.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0035517; C:PR-DUB complex; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR GO; GO:0071108; P:protein K48-linked deubiquitination; ISS:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0001558; P:regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 3.40.532.10; -; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001578; Peptidase_C12_UCH.
DR InterPro; IPR036959; Peptidase_C12_UCH_sf.
DR InterPro; IPR041507; UCH_C.
DR PANTHER; PTHR10589; PTHR10589; 1.
DR Pfam; PF01088; Peptidase_C12; 1.
DR Pfam; PF18031; UCH_C; 1.
DR PRINTS; PR00707; UBCTHYDRLASE.
DR SUPFAM; SSF54001; SSF54001; 1.
PE 2: Evidence at transcript level;
KW Chromatin regulator; Cytoplasm; Hydrolase; Nucleus; Protease;
KW Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..685
FT /note="Ubiquitin carboxyl-terminal hydrolase BAP1"
FT /id="PRO_0000395821"
FT REGION 273..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 673..678
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q92560"
FT COMPBIAS 273..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..423
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..577
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..685
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 91
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q92560"
FT ACT_SITE 169
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P09936"
FT SITE 184
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000250|UniProtKB:P09936"
FT CONFLICT 308
FT /note="N -> S (in Ref. 1; CAJ81966)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 685 AA; 76399 MW; 7A96F850498495FA CRC64;
MNKGWLELES DPGLFTLLVE DFGVKGVQVE EIYDLQSKCP GPVYGFIFLF KWIEERRSRR
KVSTLLDDTS VMEDEVVNNM FFAHQLIPNS CATHALLSVL LNCSGVHLGP TLSRIKEFTK
GFSPESKGYA IGNAPELAKA HNSHARPEPR HLPEKQNGIS AVRTMEAFHF VSYVPIKGRL
FELDGLKVYP IDHGPWAEDE EWTDKARRVI MERIGLATAG EPYHDIRFNL MAVVPDRRLK
YESKLHILKM NRQTVLEALQ QLIRVTQPEL IQAQKPTEGQ STEETKSAAL KAPVSQESHR
AHHGSHRNAT DVGAEPPGAL IRGPVMSAYS KPNSLAQNGG TVAAPASRLP AFLDNHNYAK
SPMQEEEDLA AGVGRSRGVP PPAPDTDEEE EEETENVRRP LTPPGFKRRS SEPLPPPPGP
EPGVLAEKLK ETQRDLCSPL SIKTGAPTAP HSQPSPTPSN ESTDTASEIG SAFNSPLRSP
LRSANPTRPS SPVTLHLSKV LFGEEEPLLR LDCVRYNRAV RELGPHISTG ILHLSKDGYL
CPLSRLETGK VSPKGNKVEE PRESSEPDTE RSRVTEVPQG EKFSPKELLA LLKCVEAEIS
SSEACLREEL EKRKKFKIDD QRRTHNYDEF ICAFISMLAQ EGMLASLVEQ NISVRRRQGV
SIGRLHKQRK PDRRKRSRPY KAKRQ
