BAP1_CHICK
ID BAP1_CHICK Reviewed; 700 AA.
AC Q5F3N6;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=RCJMB04_11f19;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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 (By similarity).
CC Binds to chromatin (By similarity). {ECO:0000250|UniProtKB:Q92560}.
CC -!- SIMILARITY: Belongs to the peptidase C12 family. BAP1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AJ851614; CAH65248.1; -; mRNA.
DR RefSeq; NP_001025761.1; NM_001030590.1.
DR AlphaFoldDB; Q5F3N6; -.
DR SMR; Q5F3N6; -.
DR STRING; 9031.ENSGALP00000006954; -.
DR MEROPS; C12.004; -.
DR PaxDb; Q5F3N6; -.
DR GeneID; 415944; -.
DR KEGG; gga:415944; -.
DR CTD; 8314; -.
DR VEuPathDB; HostDB:geneid_415944; -.
DR eggNOG; KOG2778; Eukaryota.
DR InParanoid; Q5F3N6; -.
DR OrthoDB; 1363547at2759; -.
DR PhylomeDB; Q5F3N6; -.
DR PRO; PR:Q5F3N6; -.
DR Proteomes; UP000000539; 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; Coiled coil; Cytoplasm; Hydrolase; Nucleus; Protease;
KW Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..700
FT /note="Ubiquitin carboxyl-terminal hydrolase BAP1"
FT /id="PRO_0000395818"
FT REGION 273..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 598..632
FT /evidence="ECO:0000255"
FT MOTIF 688..693
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q92560"
FT COMPBIAS 273..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..700
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"
SQ SEQUENCE 700 AA; 77704 MW; A279A342674F4DCA CRC64;
MNKGWLELES DPGLFTLLVE DFGVKGVQVE EIYDLQSKCQ GPVYGFIFLF KWIEESRSRR
KVSTLVDETS VIDDDIVNNM FFAHQLIPNS CATHALLSVL LNCNNVDLGP TLSRMKDFTK
GFSPESKGYA IGNAPELAKA RNSHARPEPR HLPEKQNGIS AVRTMEAFHF VSYVPIKGRL
FELDGLKVYP IDHGPWADDE EWTDKARRVI MERIGLATAG EPYHDIRFNL MAVVPDRRMK
YESKLHILKM NRQTVLEALQ QLIRVTQPEL IQSQKSQESQ SPEEAKPANS KTVAPESTHP
DGADEPASQG HTTATQSPPT KSKPVAKASA SSINGVPPAN PNPIVQRLPA FLDNHNYAKS
PMQEEEDLAA GVGRSRVPVR QHQQYSDDED DYDDDEEEEV RNTNSAIRYK RKGQVKQEHA
AGAADGQLSV LQPNTINVLA EKLKESQKDL SIPLSIKTTG GGAAVAIVTH SQPSPTPSNE
STDTASEIGS AFNSPLRSPI RSANPTRPSS PVTSHISKVL FGEEDGLLRI DCLRYNRAVR
DLGPIISSGL LHLTEDGVFC PLAAADGGKS SPPSIKPGEE AQVTIKLDEK EGSEASGSKE
KELLALLKCV EAEIANYEAC LKEEVEKRKK FKIDDQRRTH NYDEFICTFI SMLAQEGMLA
SLVEQNISVR RRQGVSIGRL HKQRKPDRRK RSRPYKAKRQ
