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Q92560

- BAP1_HUMAN

UniProt

Q92560 - BAP1_HUMAN

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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

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. ubiquitin-specific protease activity Source: UniProtKB
  4. 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
Complete GO annotation...

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
Complete GO annotation...

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. 5 Publications
Mutagenesisi363 – 3664NHNY → AAAA: Abolishes interaction with HCFC1. 2 Publications
Mutagenesisi656 – 6616KRKKFK → AAAAAA: Does not affect nuclear localization. 1 Publication
Mutagenesisi691 – 71121Missing: Abolishes ubiquitination by UBE2O. 1 PublicationAdd
BLAST
Mutagenesisi691 – 6911L → P: Abolishes interaction with BRCA1. 1 Publication
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

BgeeiQ92560.
CleanExiHS_BAP1.
ExpressionAtlasiQ92560. baseline and differential.
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.
GeneTreeiENSGT00510000046560.
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

        10         20         30         40         50
MNKGWLELES DPGLFTLLVE DFGVKGVQVE EIYDLQSKCQ GPVYGFIFLF
60 70 80 90 100
KWIEERRSRR KVSTLVDDTS VIDDDIVNNM FFAHQLIPNS CATHALLSVL
110 120 130 140 150
LNCSSVDLGP TLSRMKDFTK GFSPESKGYA IGNAPELAKA HNSHARPEPR
160 170 180 190 200
HLPEKQNGLS AVRTMEAFHF VSYVPITGRL FELDGLKVYP IDHGPWGEDE
210 220 230 240 250
EWTDKARRVI MERIGLATAG EPYHDIRFNL MAVVPDRRIK YEARLHVLKV
260 270 280 290 300
NRQTVLEALQ QLIRVTQPEL IQTHKSQESQ LPEESKSASN KSPLVLEANR
310 320 330 340 350
APAASEGNHT DGAEEAAGSC AQAPSHSPPN KPKLVVKPPG SSLNGVHPNP
360 370 380 390 400
TPIVQRLPAF LDNHNYAKSP MQEEEDLAAG VGRSRVPVRP PQQYSDDEDD
410 420 430 440 450
YEDDEEDDVQ NTNSALRYKG KGTGKPGALS GSADGQLSVL QPNTINVLAE
460 470 480 490 500
KLKESQKDLS IPLSIKTSSG AGSPAVAVPT HSQPSPTPSN ESTDTASEIG
510 520 530 540 550
SAFNSPLRSP IRSANPTRPS SPVTSHISKV LFGEDDSLLR VDCIRYNRAV
560 570 580 590 600
RDLGPVISTG LLHLAEDGVL SPLALTEGGK GSSPSIRPIQ GSQGSSSPVE
610 620 630 640 650
KEVVEATDSR EKTGMVRPGE PLSGEKYSPK ELLALLKCVE AEIANYEACL
660 670 680 690 700
KEEVEKRKKF KIDDQRRTHN YDEFICTFIS MLAQEGMLAN LVEQNISVRR
710 720
RQGVSIGRLH KQRKPDRRKR SRPYKAKRQ
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.
GeneTreei ENSGT00510000046560.
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

Bgeei Q92560.
CleanExi HS_BAP1.
ExpressionAtlasi Q92560. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 121 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