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Q99PU7

- BAP1_MOUSE

UniProt

Q99PU7 - BAP1_MOUSE

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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

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. ubiquitin-specific protease activity Source: UniProtKB
  3. 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
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
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. nucleus Source: UniProtKB
  3. PR-DUB complex Source: UniProtKB
Complete GO annotation...

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. 1 Publication

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

MaxQBiQ99PU7.
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.
InParanoidiQ99PU7.
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

        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
LNCSNVDLGP TLSRMKDFTK GFSPESKGYA IGNAPELAKA HNSHARPEPR
160 170 180 190 200
HLPEKQNGLS AVRTMEAFHF VSYVPITGRL FELDGLKVYP IDHGPWGEDE
210 220 230 240 250
EWTDKARRVI MERIGLATAG EPYHDIRFNL MAVVPDRRIK YETRLHVLKV
260 270 280 290 300
NRQTVLEALQ QLIRVTQPEL IQTHKSQESQ LPEESKPASS KSPLGLEAGR
310 320 330 340 350
TPVASECTQT DGAEEVAGSC PQTTTHSPPS KCKLVVKPPG SSLNGVPPNP
360 370 380 390 400
APIVQRLPAF LDNHNYAKSP MQEEEDLAAG VGRSRVPVRA PQQYSEDEDD
410 420 430 440 450
YEDEDEDVQN TNPAIRYKRK GTGKPGSLSN SSDGQLSVLQ PNTINVLTEK
460 470 480 490 500
LQESQKDLSV PLSIKTSSGA GSPAVAVPTH SQPSPTPSNE STDTASEIGS
510 520 530 540 550
AFNSPLRSPI RSANPTRPSS PVTSHISKVL FGEDDSLLRV DCIRYNRAVR
560 570 580 590 600
DLGPVISTGL LHLAEDGVLS PLALTEGGKG SSPSTRSSQG SQGSSGLEEK
610 620 630 640 650
EVVEVTESRD KPGLNRSSEP LSGEKYSPKE LLALLKCVEA EIANYEACLK
660 670 680 690 700
EEVEKRKKFK IDDQRRTHNY DEFICTFISM LAQEGMLANL VEQNISVRRR
710 720
QGVSIGRLHK QRKPDRRKRS RPYKAKRQ
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.Curated

Experimental Info

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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

MaxQBi Q99PU7.
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 Q99PU7.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 101 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