ID BAP1_DANRE Reviewed; 755 AA. AC A1L2G3; Q1LXB5; DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot. DT 13-JUL-2010, sequence version 2. DT 03-MAY-2023, entry version 73. 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=si:dkey-42i9.9; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Danionidae; Danioninae; Danio. OX NCBI_TaxID=7955; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen; RX PubMed=23594743; DOI=10.1038/nature12111; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J., RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G., RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P., RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the human RT genome."; RL Nature 496:498-503(2013). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-682. RC TISSUE=Olfactory epithelium; RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. RN [3] RP DISRUPTION PHENOTYPE. RX PubMed=20040115; DOI=10.1186/1471-2164-10-637; RA Tse W.K., Eisenhaber B., Ho S.H., Ng Q., Eisenhaber F., Jiang Y.J.; RT "Genome-wide loss-of-function analysis of deubiquitylating enzymes for RT zebrafish development."; RL BMC Genomics 10:637-637(2009). 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 -!- DISRUPTION PHENOTYPE: Neuronal hyperplasia, suggesting a role in Notch CC signaling pathway. {ECO:0000269|PubMed:20040115}. CC -!- SIMILARITY: Belongs to the peptidase C12 family. BAP1 subfamily. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAI29507.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC Sequence=CAK11034.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BX465868; CAK11034.1; ALT_SEQ; Genomic_DNA. DR EMBL; BC129506; AAI29507.1; ALT_SEQ; mRNA. DR AlphaFoldDB; A1L2G3; -. DR SMR; A1L2G3; -. DR STRING; 7955.ENSDARP00000086210; -. DR MEROPS; C12.004; -. DR PaxDb; A1L2G3; -. DR PeptideAtlas; A1L2G3; -. DR ZFIN; ZDB-GENE-050208-492; bap1. DR eggNOG; KOG2778; Eukaryota. DR InParanoid; A1L2G3; -. DR PhylomeDB; A1L2G3; -. DR Reactome; R-DRE-5689603; UCH proteinases. DR PRO; PR:A1L2G3; -. DR Proteomes; UP000000437; Genome assembly. 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:1904888; P:cranial skeletal system development; IMP:ZFIN. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:0007219; P:Notch signaling pathway; IMP:ZFIN. 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 CDD; cd09617; Peptidase_C12_UCH37_BAP1; 1. DR Gene3D; 1.20.58.860; -; 1. DR Gene3D; 3.40.532.10; Peptidase C12, ubiquitin carboxyl-terminal hydrolase; 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; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1. DR PANTHER; PTHR10589:SF28; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE BAP1; 1. DR Pfam; PF01088; Peptidase_C12; 1. DR Pfam; PF18031; UCH_C; 1. DR PRINTS; PR00707; UBCTHYDRLASE. DR SUPFAM; SSF54001; Cysteine proteinases; 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..755 FT /note="Ubiquitin carboxyl-terminal hydrolase BAP1" FT /id="PRO_0000395819" FT REGION 270..354 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 368..415 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 469..535 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 593..652 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 729..755 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 743..748 FT /note="Nuclear localization signal" FT /evidence="ECO:0000250|UniProtKB:Q92560" FT COMPBIAS 281..296 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 305..319 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 469..530 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 593..640 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 730..755 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 54 FT /note="E -> G (in Ref. 2; AAI29507)" FT /evidence="ECO:0000305" FT CONFLICT 111 FT /note="T -> A (in Ref. 2; AAI29507)" FT /evidence="ECO:0000305" FT CONFLICT 443 FT /note="G -> D (in Ref. 2; AAI29507)" FT /evidence="ECO:0000305" FT CONFLICT 504 FT /note="S -> P (in Ref. 2; AAI29507)" FT /evidence="ECO:0000305" FT CONFLICT 617..619 FT /note="VEM -> AEI (in Ref. 2; AAI29507)" FT /evidence="ECO:0000305" FT CONFLICT 627 FT /note="S -> L (in Ref. 2; AAI29507)" FT /evidence="ECO:0000305" SQ SEQUENCE 755 AA; 83777 MW; 6DE37B40D438B535 CRC64; MNKGWLELES DPGLFTLLVE DFGVKGVQVE EIYDLQSKCQ SPVYGFIFLF KWIEERRSRR KVSTLVDETS VIDDDIVNDM FFAHQLIPNS CATHALLSVL LNCSGVELGM TLSRMKAFTK GFNPESKGYA IGNAPELAKA HNSHARPEPR HLPEKQNGIS AVRTMEAFHF VSYVPIKDRL FELDGLKAYP IDHGPWGEDE EWTDKARRVI MERIGLATAG EPYHDIRFNL MAVVPDRRIK YESKLDILKR NRQIILEGLQ QIREKKVIRM TQQESGQDRK QQDSSSSEDT PPVVKKEEVQ ETPIPSGAEQ ATPTEAQEGA ASLPSPAGKV RSMAKPALPA GGAPPPAPLP APSTNTIVQR LPAFLDNHNY AKSPMQEEED LAAGVGRSRP PQPPYSDDED DYDDEEEECS TAGVTNSRVR RKLGLRTRTM SRTAVGGVAA MEGQLALSVL AEKLKKEVQR KDALATTGST PLNVRTEGRT GGISITSACQ PSPTPSNEST DTASEIGSAF NSPLRSPARS QATTRPSSPV ASHVGRVLFG EEEGLPRLDA RHNRAVRDLG VLVSSTQLQL QEDGVIFALP PTEALEGLKK VGGVDKKKKE EASGPGGEEE VKEGPSVEMK AEDVKESVDV KPEKENLPTT DVENSTKPPG EKYTPKELLA LLKYVEADIA NYEVYLKEEV EKRKKYKIDD QRRTHNYDEF ICTFISMLAQ EGMLASLVEQ NISVRRRQGV SIGRLHKQRK PDRRKRSRPY KAKRQ //