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A1L2G3

- BAP1_DANRE

UniProt

A1L2G3 - BAP1_DANRE

Protein

Ubiquitin carboxyl-terminal hydrolase BAP1

Gene

bap1

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 44 (01 Oct 2014)
      Sequence version 2 (13 Jul 2010)
      Previous versions | rss
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    Functioni

    Deubiquitinating enzyme that plays a key role in chromatin by mediating deubiquitination of histone H2A. Catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1) By similarity.By similarity

    Catalytic activityi

    Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei91 – 911NucleophileBy similarity
    Active sitei169 – 1691Proton donorBy similarity
    Sitei184 – 1841Important for enzyme activityBy similarity

    GO - Molecular functioni

    1. chromatin binding Source: UniProtKB
    2. ubiquitin-specific protease activity Source: UniProtKB
    3. ubiquitin thiolesterase activity Source: UniProtKB

    GO - Biological processi

    1. monoubiquitinated histone H2A deubiquitination Source: UniProtKB
    2. protein deubiquitination Source: UniProtKB
    3. protein K48-linked deubiquitination Source: UniProtKB
    4. regulation of cell cycle Source: UniProtKB
    5. regulation of cell growth Source: UniProtKB
    6. ubiquitin-dependent protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Chromatin regulator, Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Ubl conjugation pathway

    Protein family/group databases

    MEROPSiC12.004.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin carboxyl-terminal hydrolase BAP1 (EC:3.4.19.12)
    Alternative name(s):
    BRCA1-associated protein 1
    Gene namesi
    Name:bap1
    ORF Names:si:dkey-42i9.9
    OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
    Taxonomic identifieri7955 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
    ProteomesiUP000000437: Unplaced

    Organism-specific databases

    ZFINiZDB-GENE-050208-492. bap1.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity
    Note: Mainly nuclear. Binds to chromatin By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nucleus Source: UniProtKB
    3. PR-DUB complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Neuronal hyperplasia, suggesting a role in Notch signaling pathway.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 755755Ubiquitin carboxyl-terminal hydrolase BAP1PRO_0000395819Add
    BLAST

    Interactioni

    Subunit structurei

    Component of the PR-DUB complex.By similarity

    Protein-protein interaction databases

    STRINGi7955.ENSDARP00000086210.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase C12 family. BAP1 subfamily.Curated

    Phylogenomic databases

    eggNOGiNOG249036.
    HOGENOMiHOG000013189.
    HOVERGENiHBG054042.
    PhylomeDBiA1L2G3.

    Family and domain databases

    Gene3Di3.40.532.10. 1 hit.
    InterProiIPR001578. Peptidase_C12_UCH.
    [Graphical view]
    PANTHERiPTHR10589. PTHR10589. 1 hit.
    PfamiPF01088. Peptidase_C12. 1 hit.
    [Graphical view]
    PRINTSiPR00707. UBCTHYDRLASE.

    Sequencei

    Sequence statusi: Complete.

    A1L2G3-1 [UniParc]FASTAAdd to Basket

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    MNKGWLELES DPGLFTLLVE DFGVKGVQVE EIYDLQSKCQ SPVYGFIFLF    50
    KWIEERRSRR KVSTLVDETS VIDDDIVNDM FFAHQLIPNS CATHALLSVL 100
    LNCSGVELGM TLSRMKAFTK GFNPESKGYA IGNAPELAKA HNSHARPEPR 150
    HLPEKQNGIS AVRTMEAFHF VSYVPIKDRL FELDGLKAYP IDHGPWGEDE 200
    EWTDKARRVI MERIGLATAG EPYHDIRFNL MAVVPDRRIK YESKLDILKR 250
    NRQIILEGLQ QIREKKVIRM TQQESGQDRK QQDSSSSEDT PPVVKKEEVQ 300
    ETPIPSGAEQ ATPTEAQEGA ASLPSPAGKV RSMAKPALPA GGAPPPAPLP 350
    APSTNTIVQR LPAFLDNHNY AKSPMQEEED LAAGVGRSRP PQPPYSDDED 400
    DYDDEEEECS TAGVTNSRVR RKLGLRTRTM SRTAVGGVAA MEGQLALSVL 450
    AEKLKKEVQR KDALATTGST PLNVRTEGRT GGISITSACQ PSPTPSNEST 500
    DTASEIGSAF NSPLRSPARS QATTRPSSPV ASHVGRVLFG EEEGLPRLDA 550
    RHNRAVRDLG VLVSSTQLQL QEDGVIFALP PTEALEGLKK VGGVDKKKKE 600
    EASGPGGEEE VKEGPSVEMK AEDVKESVDV KPEKENLPTT DVENSTKPPG 650
    EKYTPKELLA LLKYVEADIA NYEVYLKEEV EKRKKYKIDD QRRTHNYDEF 700
    ICTFISMLAQ EGMLASLVEQ NISVRRRQGV SIGRLHKQRK PDRRKRSRPY 750
    KAKRQ 755
    Length:755
    Mass (Da):83,777
    Last modified:July 13, 2010 - v2
    Checksum:i6DE37B40D438B535
    GO

    Sequence cautioni

    The sequence AAI29507.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence CAK11034.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti54 – 541E → G in AAI29507. 1 PublicationCurated
    Sequence conflicti111 – 1111T → A in AAI29507. 1 PublicationCurated
    Sequence conflicti443 – 4431G → D in AAI29507. 1 PublicationCurated
    Sequence conflicti504 – 5041S → P in AAI29507. 1 PublicationCurated
    Sequence conflicti617 – 6193VEM → AEI in AAI29507. 1 PublicationCurated
    Sequence conflicti627 – 6271S → L in AAI29507. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX465868 Genomic DNA. Translation: CAK11034.1. Sequence problems.
    BC129506 mRNA. Translation: AAI29507.1. Sequence problems.
    UniGeneiDr.37720.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX465868 Genomic DNA. Translation: CAK11034.1 . Sequence problems.
    BC129506 mRNA. Translation: AAI29507.1 . Sequence problems.
    UniGenei Dr.37720.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 7955.ENSDARP00000086210.

    Protein family/group databases

    MEROPSi C12.004.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    ZFINi ZDB-GENE-050208-492. bap1.

    Phylogenomic databases

    eggNOGi NOG249036.
    HOGENOMi HOG000013189.
    HOVERGENi HBG054042.
    PhylomeDBi A1L2G3.

    Miscellaneous databases

    PROi A1L2G3.

    Family and domain databases

    Gene3Di 3.40.532.10. 1 hit.
    InterProi IPR001578. Peptidase_C12_UCH.
    [Graphical view ]
    PANTHERi PTHR10589. PTHR10589. 1 hit.
    Pfami PF01088. Peptidase_C12. 1 hit.
    [Graphical view ]
    PRINTSi PR00707. UBCTHYDRLASE.
    ProtoNeti Search...

    Publicationsi

    1. "The zebrafish reference genome sequence and its relationship to the human genome."
      Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.
      , White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G., Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.
      Nature 496:498-503(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Tuebingen.
    2. NIH - Zebrafish Gene Collection (ZGC) project
      Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-682.
      Tissue: Olfactory epithelium.
    3. "Genome-wide loss-of-function analysis of deubiquitylating enzymes for zebrafish development."
      Tse W.K., Eisenhaber B., Ho S.H., Ng Q., Eisenhaber F., Jiang Y.J.
      BMC Genomics 10:637-637(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiBAP1_DANRE
    AccessioniPrimary (citable) accession number: A1L2G3
    Secondary accession number(s): Q1LXB5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 13, 2010
    Last sequence update: July 13, 2010
    Last modified: October 1, 2014
    This is version 44 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3