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 13-APR-2016, entry version 50. DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase BAP1; DE EC=3.4.19.12; 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 Cyprinidae; 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., RA Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., RA McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., RA Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T., RA Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., RA Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., RA Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., RA 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., Eliott D., Threadgold G., RA Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., RA Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., RA Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., RA Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., RA Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., RA 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., RA Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., RA Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., RA Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., RA Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., RA Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., RA Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., RA Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., RA Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J., RA Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., RA Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., RA Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., RA Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the RT human 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 CC chromatin by mediating deubiquitination of histone H2A. Catalytic CC component of the PR-DUB complex, a complex that specifically CC mediates deubiquitination of histone H2A monoubiquitinated at CC 'Lys-119' (H2AK119ub1) (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester, CC thioester, amide, peptide and isopeptide bonds formed by the C- CC terminal Gly of ubiquitin (a 76-residue protein attached to CC proteins as an intracellular targeting signal). CC -!- SUBUNIT: Component of the PR-DUB complex. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus CC {ECO:0000250}. Note=Mainly nuclear. Binds to chromatin (By CC similarity). {ECO:0000250}. CC -!- DISRUPTION PHENOTYPE: Neuronal hyperplasia, suggesting a role in CC Notch 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 UniGene; Dr.37720; -. DR STRING; 7955.ENSDARP00000086210; -. DR MEROPS; C12.004; -. DR PaxDb; A1L2G3; -. DR ZFIN; ZDB-GENE-050208-492; bap1. DR eggNOG; KOG2778; Eukaryota. DR eggNOG; ENOG410XP0P; LUCA. DR HOGENOM; HOG000013189; -. DR HOVERGEN; HBG054042; -. DR InParanoid; A1L2G3; -. DR PhylomeDB; A1L2G3; -. DR PRO; PR:A1L2G3; -. DR Proteomes; UP000000437; 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:thiol-dependent ubiquitin-specific protease activity; ISS:UniProtKB. DR GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; 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 Gene3D; 3.40.532.10; -; 1. DR InterPro; IPR001578; Peptidase_C12_UCH. DR PANTHER; PTHR10589; PTHR10589; 1. DR Pfam; PF01088; Peptidase_C12; 1. DR PRINTS; PR00707; UBCTHYDRLASE. PE 2: Evidence at transcript level; KW Chromatin regulator; Complete proteome; Cytoplasm; Hydrolase; Nucleus; KW Protease; Reference proteome; Thiol protease; Ubl conjugation pathway. FT CHAIN 1 755 Ubiquitin carboxyl-terminal hydrolase FT BAP1. FT /FTId=PRO_0000395819. FT ACT_SITE 91 91 Nucleophile. {ECO:0000250}. FT ACT_SITE 169 169 Proton donor. {ECO:0000250}. FT SITE 184 184 Important for enzyme activity. FT {ECO:0000250}. FT CONFLICT 54 54 E -> G (in Ref. 2; AAI29507). FT {ECO:0000305}. FT CONFLICT 111 111 T -> A (in Ref. 2; AAI29507). FT {ECO:0000305}. FT CONFLICT 443 443 G -> D (in Ref. 2; AAI29507). FT {ECO:0000305}. FT CONFLICT 504 504 S -> P (in Ref. 2; AAI29507). FT {ECO:0000305}. FT CONFLICT 617 619 VEM -> AEI (in Ref. 2; AAI29507). FT {ECO:0000305}. FT CONFLICT 627 627 S -> L (in Ref. 2; AAI29507). FT {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 //