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Q99PU7

- BAP1_MOUSE

UniProt

Q99PU7 - BAP1_MOUSE

Protein

Ubiquitin carboxyl-terminal hydrolase BAP1

Gene

Bap1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Deubiquitinating enzyme that plays a key role in chromatin by mediating deubiquitination of histone H2A and HCFC1. Catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1). Does not deubiquitinate monoubiquitinated histone H2B. Acts as a regulator of cell growth by mediating deubiquitination of HCFC1 N-terminal and C-terminal chains, with some specificity toward 'Lys-48'-linked polyubiquitin chains compared to 'Lys-63'-linked polyubiquitin chains. Deubiquitination of HCFC1 does not lead to increase stability of HCFC1. Interferes with the BRCA1 and BARD1 heterodimer activity by inhibiting their ability to mediate ubiquitination and autoubiquitination. It however does not mediate deubiquitination of BRCA1 and BARD1. Able to mediate autodeubiquitination via intramolecular interactions to couteract monoubiquitination at the nuclear localization signal (NLS), thereby protecting it from cytoplasmic sequestration. Acts as a tumor suppressor 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 – 911NucleophileCurated
    Active sitei169 – 1691Proton donorBy similarity
    Sitei184 – 1841Important for enzyme activityBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. monoubiquitinated histone H2A deubiquitination Source: UniProtKB
    2. monoubiquitinated protein deubiquitination Source: UniProtKB
    3. negative regulation of cell proliferation Source: MGI
    4. protein deubiquitination Source: UniProtKB
    5. protein K48-linked deubiquitination Source: UniProtKB
    6. regulation of cell cycle Source: UniProtKB
    7. regulation of cell growth Source: UniProtKB
    8. 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
    Ubiquitin C-terminal hydrolase X4
    Short name:
    UCH-X4
    Gene namesi
    Name:Bap1
    Synonyms:Kiaa0272
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 14

    Organism-specific databases

    MGIiMGI:1206586. Bap1.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity
    Note: Mainly nuclear. Binds to chromatin. Localizes to the cytoplasm when monoubiquitinated by the E2/E3 hybrid ubiquitin-protein ligase UBE2O By similarity.By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi91 – 911C → A: Abolishes ability to suppress tumorigenicity when expressed in NCI-H226 cells. 1 Publication
    Mutagenesisi716 – 7216RRKRSR → AAAAAA: Abolishes ability to suppress tumorigenicity when expressed in NCI-H226 cells.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 728728Ubiquitin carboxyl-terminal hydrolase BAP1PRO_0000211070Add
    BLAST

    Post-translational modificationi

    Ubiquitinated: monoubiquitinated at multiple site of its nuclear localization signal (NLS) by UBE2O, leading to cytoplasmic retention. Able to mediate autodeubiquitination via intramolecular interactions to couteract cytoplasmic retention By similarity.By similarity

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    PRIDEiQ99PU7.

    PTM databases

    PhosphoSiteiQ99PU7.

    Expressioni

    Tissue specificityi

    Highly expressed in mammary glands, testis and ovary. Up-regulated in mammary glands during puberty, pregnancy, and as a result of parity.1 Publication

    Gene expression databases

    BgeeiQ99PU7.
    CleanExiMM_BAP1.
    GenevestigatoriQ99PU7.

    Interactioni

    Subunit structurei

    Component of the PR-DUB complex, at least composed of BAP1 and ASXL1. Interacts with BRCA1 (via the RING finger). Interacts (via HBM-like motif) with HCFC1 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi222625. 10 interactions.
    IntActiQ99PU7. 5 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99PU7.
    SMRiQ99PU7. Positions 5-284, 629-690.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni595 – 720126Interaction with BRCA1By similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili629 – 66032Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi363 – 3664HBM-like motifBy similarity
    Motifi716 – 7216Nuclear localization signalBy similarity

    Sequence similaritiesi

    Belongs to the peptidase C12 family. BAP1 subfamily.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG249036.
    GeneTreeiENSGT00510000046560.
    HOGENOMiHOG000013189.
    HOVERGENiHBG054042.
    InParanoidiQ3TCR6.
    KOiK08588.
    OMAiPQQYSDD.
    OrthoDBiEOG7GN2M2.
    PhylomeDBiQ99PU7.
    TreeFamiTF313976.

    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.

    Q99PU7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNKGWLELES DPGLFTLLVE DFGVKGVQVE EIYDLQSKCQ GPVYGFIFLF    50
    KWIEERRSRR KVSTLVDDTS VIDDDIVNNM FFAHQLIPNS CATHALLSVL 100
    LNCSNVDLGP TLSRMKDFTK GFSPESKGYA IGNAPELAKA HNSHARPEPR 150
    HLPEKQNGLS AVRTMEAFHF VSYVPITGRL FELDGLKVYP IDHGPWGEDE 200
    EWTDKARRVI MERIGLATAG EPYHDIRFNL MAVVPDRRIK YETRLHVLKV 250
    NRQTVLEALQ QLIRVTQPEL IQTHKSQESQ LPEESKPASS KSPLGLEAGR 300
    TPVASECTQT DGAEEVAGSC PQTTTHSPPS KCKLVVKPPG SSLNGVPPNP 350
    APIVQRLPAF LDNHNYAKSP MQEEEDLAAG VGRSRVPVRA PQQYSEDEDD 400
    YEDEDEDVQN TNPAIRYKRK GTGKPGSLSN SSDGQLSVLQ PNTINVLTEK 450
    LQESQKDLSV PLSIKTSSGA GSPAVAVPTH SQPSPTPSNE STDTASEIGS 500
    AFNSPLRSPI RSANPTRPSS PVTSHISKVL FGEDDSLLRV DCIRYNRAVR 550
    DLGPVISTGL LHLAEDGVLS PLALTEGGKG SSPSTRSSQG SQGSSGLEEK 600
    EVVEVTESRD KPGLNRSSEP LSGEKYSPKE LLALLKCVEA EIANYEACLK 650
    EEVEKRKKFK IDDQRRTHNY DEFICTFISM LAQEGMLANL VEQNISVRRR 700
    QGVSIGRLHK QRKPDRRKRS RPYKAKRQ 728
    Length:728
    Mass (Da):80,492
    Last modified:June 1, 2001 - v1
    Checksum:i2BDEAFB09CD276DB
    GO

    Sequence cautioni

    The sequence BAC97918.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti725 – 7251A → V in BAC97918. (PubMed:14621295)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB047820 mRNA. Translation: BAB32976.1.
    AK129108 mRNA. Translation: BAC97918.1. Different initiation.
    AK170576 mRNA. Translation: BAE41889.1.
    BC050901 mRNA. Translation: AAH50901.1.
    CCDSiCCDS26910.1.
    RefSeqiNP_081364.1. NM_027088.2.
    UniGeneiMm.3779.

    Genome annotation databases

    EnsembliENSMUST00000022458; ENSMUSP00000022458; ENSMUSG00000021901.
    GeneIDi104416.
    KEGGimmu:104416.
    UCSCiuc007sxh.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB047820 mRNA. Translation: BAB32976.1 .
    AK129108 mRNA. Translation: BAC97918.1 . Different initiation.
    AK170576 mRNA. Translation: BAE41889.1 .
    BC050901 mRNA. Translation: AAH50901.1 .
    CCDSi CCDS26910.1.
    RefSeqi NP_081364.1. NM_027088.2.
    UniGenei Mm.3779.

    3D structure databases

    ProteinModelPortali Q99PU7.
    SMRi Q99PU7. Positions 5-284, 629-690.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 222625. 10 interactions.
    IntActi Q99PU7. 5 interactions.

    Protein family/group databases

    MEROPSi C12.004.

    PTM databases

    PhosphoSitei Q99PU7.

    Proteomic databases

    PRIDEi Q99PU7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000022458 ; ENSMUSP00000022458 ; ENSMUSG00000021901 .
    GeneIDi 104416.
    KEGGi mmu:104416.
    UCSCi uc007sxh.1. mouse.

    Organism-specific databases

    CTDi 8314.
    MGIi MGI:1206586. Bap1.
    Rougei Search...

    Phylogenomic databases

    eggNOGi NOG249036.
    GeneTreei ENSGT00510000046560.
    HOGENOMi HOG000013189.
    HOVERGENi HBG054042.
    InParanoidi Q3TCR6.
    KOi K08588.
    OMAi PQQYSDD.
    OrthoDBi EOG7GN2M2.
    PhylomeDBi Q99PU7.
    TreeFami TF313976.

    Miscellaneous databases

    ChiTaRSi BAP1. mouse.
    NextBioi 357097.
    PROi Q99PU7.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q99PU7.
    CleanExi MM_BAP1.
    Genevestigatori Q99PU7.

    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. "Ubiquitin C-terminal hydrolase."
      Mizuta R.
      Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
      DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: NOD.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6.
      Tissue: Fetal brain.
    5. Cited for: TISSUE SPECIFICITY.
    6. "BRCA1-associated protein-1 is a tumor suppressor that requires deubiquitinating activity and nuclear localization."
      Ventii K.H., Devi N.S., Friedrich K.L., Chernova T.A., Tighiouart M., Van Meir E.G., Wilkinson K.D.
      Cancer Res. 68:6953-6962(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-91 AND 716-ARG--ARG-721.
    7. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiBAP1_MOUSE
    AccessioniPrimary (citable) accession number: Q99PU7
    Secondary accession number(s): Q3TCR6, Q6ZQE6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2005
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 99 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Has the ability to ability to suppress tumorigenicity when expressed in NCI-H226 cells.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3