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Q92560

- BAP1_HUMAN

UniProt

Q92560 - BAP1_HUMAN

Protein

Ubiquitin carboxyl-terminal hydrolase BAP1

Gene

BAP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 2 (01 Nov 1998)
      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 (PubMed:24703950). Acts as a tumor suppressor.8 Publications

    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).1 Publication

    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. peptidase activity Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. ubiquitin-specific protease activity Source: UniProtKB
    5. ubiquitin thiolesterase activity Source: UniProtKB

    GO - Biological processi

    1. cellular protein modification process Source: UniProtKB
    2. monoubiquitinated histone H2A deubiquitination Source: UniProtKB
    3. monoubiquitinated protein deubiquitination Source: UniProtKB
    4. negative regulation of cell proliferation Source: ProtInc
    5. protein deubiquitination Source: UniProtKB
    6. protein K48-linked deubiquitination Source: UniProtKB
    7. regulation of cell cycle Source: UniProtKB
    8. regulation of cell growth Source: UniProtKB
    9. 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
    Cerebral protein 6
    Gene namesi
    Name:BAP1
    Synonyms:KIAA0272
    ORF Names:hucep-6
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:950. BAP1.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: Mainly nuclear. Binds to chromatin. Localizes to the cytoplasm when monoubiquitinated by the E2/E3 hybrid ubiquitin-protein ligase UBE2O (PubMed:24703950).1 Publication

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Mesothelioma, malignant (MESOM) [MIM:156240]: An aggressive neoplasm of the serosal lining of the chest. It appears as broad sheets of cells, with some regions containing spindle-shaped, sarcoma-like cells and other regions showing adenomatous patterns. Pleural mesotheliomas have been linked to exposure to asbestos.2 Publications
    Note: The gene represented in this entry is involved in disease pathogenesis.
    Tumor predisposition syndrome (TPDS) [MIM:614327]: A condition characterized by predisposition to develop a variety of tumors, including benign melanocytic tumors as well as several malignant tumors, including uveal melanoma, cutaneous melanoma, malignant mesothelioma on exposure to asbestos, lung adenocarcinoma and meningioma.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi91 – 911C → A or S: Abolishes enzymatic activity without affecting its ability to interfere with BRCA1 E3 ligase activity. 6 Publications
    Mutagenesisi363 – 3664NHNY → AAAA: Abolishes interaction with HCFC1. 1 Publication
    Mutagenesisi656 – 6616KRKKFK → AAAAAA: Does not affect nuclear localization. 1 Publication
    Mutagenesisi691 – 71121Missing: Abolishes ubiquitination by UBE2O. 2 PublicationsAdd
    BLAST
    Mutagenesisi691 – 6911L → P: Abolishes interaction with BRCA1. 2 Publications
    Mutagenesisi717 – 7226RRKRSR → AAAAAA: Abolishes nuclear localization. 1 Publication

    Organism-specific databases

    MIMi156240. phenotype.
    614327. phenotype.
    Orphaneti289539. BAP1-related tumor predisposition syndrome.
    PharmGKBiPA25254.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 729729Ubiquitin carboxyl-terminal hydrolase BAP1PRO_0000211069Add
    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.1 Publication

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    MaxQBiQ92560.
    PaxDbiQ92560.
    PRIDEiQ92560.

    PTM databases

    PhosphoSiteiQ92560.

    Expressioni

    Tissue specificityi

    Highly expressed in testis, placenta and ovary. Expressed in breast.1 Publication

    Gene expression databases

    ArrayExpressiQ92560.
    BgeeiQ92560.
    CleanExiHS_BAP1.
    GenevestigatoriQ92560.

    Organism-specific databases

    HPAiCAB004322.
    HPA028814.
    HPA055560.

    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 HCFC1.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ASXL1Q8IXJ94EBI-1791447,EBI-1646500
    BRCA1P383983EBI-1791447,EBI-349905
    BRCA1P38398-52EBI-1791447,EBI-2015072
    HCFC1P516103EBI-1791447,EBI-396176

    Protein-protein interaction databases

    BioGridi113911. 42 interactions.
    DIPiDIP-47004N.
    IntActiQ92560. 23 interactions.
    STRINGi9606.ENSP00000417132.

    Structurei

    3D structure databases

    ProteinModelPortaliQ92560.
    SMRiQ92560. Positions 5-284, 630-691.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni596 – 721126Interaction with BRCA1Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili630 – 66132Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi363 – 3664HBM-like motif
    Motifi717 – 7226Nuclear localization signal2 Publications

    Sequence similaritiesi

    Belongs to the peptidase C12 family. BAP1 subfamily.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG249036.
    HOGENOMiHOG000013189.
    HOVERGENiHBG054042.
    InParanoidiQ92560.
    KOiK08588.
    OMAiPQQYSDD.
    OrthoDBiEOG7GN2M2.
    PhylomeDBiQ92560.
    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.

    Q92560-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNKGWLELES DPGLFTLLVE DFGVKGVQVE EIYDLQSKCQ GPVYGFIFLF    50
    KWIEERRSRR KVSTLVDDTS VIDDDIVNNM FFAHQLIPNS CATHALLSVL 100
    LNCSSVDLGP TLSRMKDFTK GFSPESKGYA IGNAPELAKA HNSHARPEPR 150
    HLPEKQNGLS AVRTMEAFHF VSYVPITGRL FELDGLKVYP IDHGPWGEDE 200
    EWTDKARRVI MERIGLATAG EPYHDIRFNL MAVVPDRRIK YEARLHVLKV 250
    NRQTVLEALQ QLIRVTQPEL IQTHKSQESQ LPEESKSASN KSPLVLEANR 300
    APAASEGNHT DGAEEAAGSC AQAPSHSPPN KPKLVVKPPG SSLNGVHPNP 350
    TPIVQRLPAF LDNHNYAKSP MQEEEDLAAG VGRSRVPVRP PQQYSDDEDD 400
    YEDDEEDDVQ NTNSALRYKG KGTGKPGALS GSADGQLSVL QPNTINVLAE 450
    KLKESQKDLS IPLSIKTSSG AGSPAVAVPT HSQPSPTPSN ESTDTASEIG 500
    SAFNSPLRSP IRSANPTRPS SPVTSHISKV LFGEDDSLLR VDCIRYNRAV 550
    RDLGPVISTG LLHLAEDGVL SPLALTEGGK GSSPSIRPIQ GSQGSSSPVE 600
    KEVVEATDSR EKTGMVRPGE PLSGEKYSPK ELLALLKCVE AEIANYEACL 650
    KEEVEKRKKF KIDDQRRTHN YDEFICTFIS MLAQEGMLAN LVEQNISVRR 700
    RQGVSIGRLH KQRKPDRRKR SRPYKAKRQ 729
    Length:729
    Mass (Da):80,362
    Last modified:November 1, 1998 - v2
    Checksum:i031DA03AE1841D85
    GO

    Sequence cautioni

    The sequence BAA13401.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti63 – 631S → C Found in a malignant pleural mesothelioma sample; somatic mutation. 1 Publication
    VAR_065976
    Natural varianti81 – 811F → V Found in a malignant pleural mesothelioma sample; somatic mutation. 1 Publication
    VAR_065977
    Natural varianti91 – 911C → W Found in a malignant pleural mesothelioma sample. 1 Publication
    VAR_065978
    Natural varianti95 – 951A → D in a lung cancer sample; also found in a malignant pleural mesothelioma cell line; impairs deubiquitinase activity. 2 Publications
    VAR_063498
    Natural varianti178 – 1781G → V in a lung cancer sample; impairs deubiquitinase activity. 1 Publication
    VAR_063499
    Natural varianti315 – 3151E → A Found in a malignant pleural mesothelioma sample. 1 Publication
    Corresponds to variant rs149974450 [ dbSNP | Ensembl ].
    VAR_065979
    Natural varianti616 – 6161V → E.
    Corresponds to variant rs35353781 [ dbSNP | Ensembl ].
    VAR_051517
    Natural varianti685 – 6851E → V Found in a malignant pleural mesothelioma cell line. 1 Publication
    VAR_065980

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF045581 mRNA. Translation: AAC15970.1.
    D88812 mRNA. Translation: BAB46921.1.
    D87462 mRNA. Translation: BAA13401.2. Different initiation.
    AK292608 mRNA. Translation: BAF85297.1.
    CH471055 Genomic DNA. Translation: EAW65220.1.
    BC001596 mRNA. Translation: AAH01596.1.
    AY130008 mRNA. Translation: AAN05092.1.
    CCDSiCCDS2853.1.
    RefSeqiNP_004647.1. NM_004656.3.
    UniGeneiHs.106674.

    Genome annotation databases

    EnsembliENST00000460680; ENSP00000417132; ENSG00000163930.
    GeneIDi8314.
    KEGGihsa:8314.
    UCSCiuc003ddx.4. human.

    Polymorphism databases

    DMDMi68565074.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF045581 mRNA. Translation: AAC15970.1 .
    D88812 mRNA. Translation: BAB46921.1 .
    D87462 mRNA. Translation: BAA13401.2 . Different initiation.
    AK292608 mRNA. Translation: BAF85297.1 .
    CH471055 Genomic DNA. Translation: EAW65220.1 .
    BC001596 mRNA. Translation: AAH01596.1 .
    AY130008 mRNA. Translation: AAN05092.1 .
    CCDSi CCDS2853.1.
    RefSeqi NP_004647.1. NM_004656.3.
    UniGenei Hs.106674.

    3D structure databases

    ProteinModelPortali Q92560.
    SMRi Q92560. Positions 5-284, 630-691.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113911. 42 interactions.
    DIPi DIP-47004N.
    IntActi Q92560. 23 interactions.
    STRINGi 9606.ENSP00000417132.

    Chemistry

    BindingDBi Q92560.
    ChEMBLi CHEMBL1293314.

    Protein family/group databases

    MEROPSi C12.004.

    PTM databases

    PhosphoSitei Q92560.

    Polymorphism databases

    DMDMi 68565074.

    Proteomic databases

    MaxQBi Q92560.
    PaxDbi Q92560.
    PRIDEi Q92560.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000460680 ; ENSP00000417132 ; ENSG00000163930 .
    GeneIDi 8314.
    KEGGi hsa:8314.
    UCSCi uc003ddx.4. human.

    Organism-specific databases

    CTDi 8314.
    GeneCardsi GC03M052410.
    HGNCi HGNC:950. BAP1.
    HPAi CAB004322.
    HPA028814.
    HPA055560.
    MIMi 156240. phenotype.
    603089. gene.
    614327. phenotype.
    neXtProti NX_Q92560.
    Orphaneti 289539. BAP1-related tumor predisposition syndrome.
    PharmGKBi PA25254.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG249036.
    HOGENOMi HOG000013189.
    HOVERGENi HBG054042.
    InParanoidi Q92560.
    KOi K08588.
    OMAi PQQYSDD.
    OrthoDBi EOG7GN2M2.
    PhylomeDBi Q92560.
    TreeFami TF313976.

    Miscellaneous databases

    ChiTaRSi BAP1. human.
    GeneWikii BAP1.
    GenomeRNAii 8314.
    NextBioi 31137.
    PROi Q92560.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q92560.
    Bgeei Q92560.
    CleanExi HS_BAP1.
    Genevestigatori Q92560.

    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. Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, FUNCTION, MUTAGENESIS OF CYS-91 AND LEU-691, INTERACTION WITH BRCA1, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
      Tissue: B-cell.
    2. "Biological functions of a novel human gene, hucep-6, which is specifically expressed in the central nervous system."
      Yoshimoto M., Yazaki M., Takayama K., Matsumoto K.
      Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    3. "Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain."
      Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N.
      DNA Res. 3:321-329(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    4. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Testis.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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].
      Tissue: Skin.
    8. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 164-729.
      Tissue: Medulloblastoma.
    9. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. "The nuclear deubiquitinase BAP1 is commonly inactivated by somatic mutations and 3p21.1 losses in malignant pleural mesothelioma."
      Bott M., Brevet M., Taylor B.S., Shimizu S., Ito T., Wang L., Creaney J., Lake R.A., Zakowski M.F., Reva B., Sander C., Delsite R., Powell S., Zhou Q., Shen R., Olshen A., Rusch V., Ladanyi M.
      Nat. Genet. 43:668-672(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN MESOM, VARIANTS CYS-63; VAL-81; TRP-91; ASP-95; ALA-315 AND VAL-685.
    14. Cited for: INVOLVEMENT IN TPDS.
    15. Cited for: INVOLVEMENT IN TPDS AND MESOM.
    16. "Defining biochemical functions for the BRCA1 tumor suppressor protein: analysis of the BRCA1 binding protein BAP1."
      Jensen D.E., Rauscher F.J. III
      Cancer Lett. 143:S13-S17(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ASP-95 AND VAL-178.
    17. "Activation of the E3 ligase function of the BRCA1/BARD1 complex by polyubiquitin chains."
      Mallery D.L., Vandenberg C.J., Hiom K.
      EMBO J. 21:6755-6762(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    18. "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: FUNCTION, SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, MUTAGENESIS OF CYS-91; 656-LYS--ARG-661 AND 717-ARG--ARG-722, CHARACTERIZATION OF VARIANTS ASP-95 AND VAL-178.
    19. "BRCA1-associated protein 1 interferes with BRCA1/BARD1 RING heterodimer activity."
      Nishikawa H., Wu W., Koike A., Kojima R., Gomi H., Fukuda M., Ohta T.
      Cancer Res. 69:111-119(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH BARD1 AND BRCA1, MUTAGENESIS OF CYS-91.
    20. "The deubiquitinating enzyme BAP1 regulates cell growth via interaction with HCF-1."
      Machida Y.J., Machida Y., Vashisht A.A., Wohlschlegel J.A., Dutta A.
      J. Biol. Chem. 284:34179-34188(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HCFC1, MUTAGENESIS OF CYS-91 AND 363-ASN--TYR-366.
    21. "Association of C-terminal ubiquitin hydrolase BRCA1-associated protein 1 with cell cycle regulator host cell factor 1."
      Misaghi S., Ottosen S., Izrael-Tomasevic A., Arnott D., Lamkanfi M., Lee J., Liu J., O'Rourke K., Dixit V.M., Wilson A.C.
      Mol. Cell. Biol. 29:2181-2192(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HCFC1, MUTAGENESIS OF CYS-91 AND 363-ASN--TYR-366.
    22. "Histone H2A deubiquitinase activity of the Polycomb repressive complex PR-DUB."
      Scheuermann J.C., de Ayala Alonso A.G., Oktaba K., Ly-Hartig N., McGinty R.K., Fraterman S., Wilm M., Muir T.W., Muller J.
      Nature 465:243-247(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE PR-DUB COMPLEX, INTERACTION WITH ASXL1.
    23. "Autodeubiquitination protects the tumor suppressor BAP1 from cytoplasmic sequestration mediated by the atypical ubiquitin ligase UBE2O."
      Mashtalir N., Daou S., Barbour H., Sen N.N., Gagnon J., Hammond-Martel I., Dar H.H., Therrien M., Affar E.B.
      Mol. Cell 54:392-406(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, UBIQUITINATION, NUCLEAR LOCALIZATION SIGNAL, MUTAGENESIS OF 691-LEU--LYS-711.

    Entry informationi

    Entry nameiBAP1_HUMAN
    AccessioniPrimary (citable) accession number: Q92560
    Secondary accession number(s): A8K993, Q6LEM0, Q7Z5E8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2005
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 120 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3