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Q99PU7 (BAP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Bap1
Synonyms:Kiaa0272
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length728 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

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).

Subunit structure

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.

Subcellular location

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.

Tissue specificity

Highly expressed in mammary glands, testis and ovary. Up-regulated in mammary glands during puberty, pregnancy, and as a result of parity. Ref.5

Post-translational modification

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.

Miscellaneous

Has the ability to ability to suppress tumorigenicity when expressed in NCI-H226 cells (Ref.6).

Sequence similarities

Belongs to the peptidase C12 family. BAP1 subfamily.

Sequence caution

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

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   DomainCoiled coil
   Molecular functionChromatin regulator
Hydrolase
Protease
Thiol protease
   PTMUbl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmonoubiquitinated histone H2A deubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell proliferation

Inferred from sequence alignment Ref.5. Source: MGI

protein K48-linked deubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

protein deubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell cycle

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell growth

Inferred from sequence or structural similarity. Source: UniProtKB

ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentPR-DUB complex

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

nucleolus

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionchromatin binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.5. Source: MGI

ubiquitin thiolesterase activity

Inferred from sequence or structural similarity. Source: UniProtKB

ubiquitin-specific protease activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 728728Ubiquitin carboxyl-terminal hydrolase BAP1
PRO_0000211070

Regions

Region595 – 720126Interaction with BRCA1 By similarity
Coiled coil629 – 66032 Potential
Motif363 – 3664HBM-like motif By similarity
Motif716 – 7216Nuclear localization signal By similarity

Sites

Active site911Nucleophile Probable
Active site1691Proton donor By similarity
Site1841Important for enzyme activity By similarity

Experimental info

Mutagenesis911C → A: Abolishes ability to suppress tumorigenicity when expressed in NCI-H226 cells. Ref.6
Mutagenesis716 – 7216RRKRSR → AAAAAA: Abolishes ability to suppress tumorigenicity when expressed in NCI-H226 cells. Ref.6
Sequence conflict7251A → V in BAC97918. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q99PU7 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 2BDEAFB09CD276DB

FASTA72880,492
        10         20         30         40         50         60 
MNKGWLELES DPGLFTLLVE DFGVKGVQVE EIYDLQSKCQ GPVYGFIFLF KWIEERRSRR 

        70         80         90        100        110        120 
KVSTLVDDTS VIDDDIVNNM FFAHQLIPNS CATHALLSVL LNCSNVDLGP TLSRMKDFTK 

       130        140        150        160        170        180 
GFSPESKGYA IGNAPELAKA HNSHARPEPR HLPEKQNGLS AVRTMEAFHF VSYVPITGRL 

       190        200        210        220        230        240 
FELDGLKVYP IDHGPWGEDE EWTDKARRVI MERIGLATAG EPYHDIRFNL MAVVPDRRIK 

       250        260        270        280        290        300 
YETRLHVLKV NRQTVLEALQ QLIRVTQPEL IQTHKSQESQ LPEESKPASS KSPLGLEAGR 

       310        320        330        340        350        360 
TPVASECTQT DGAEEVAGSC PQTTTHSPPS KCKLVVKPPG SSLNGVPPNP APIVQRLPAF 

       370        380        390        400        410        420 
LDNHNYAKSP MQEEEDLAAG VGRSRVPVRA PQQYSEDEDD YEDEDEDVQN TNPAIRYKRK 

       430        440        450        460        470        480 
GTGKPGSLSN SSDGQLSVLQ PNTINVLTEK LQESQKDLSV PLSIKTSSGA GSPAVAVPTH 

       490        500        510        520        530        540 
SQPSPTPSNE STDTASEIGS AFNSPLRSPI RSANPTRPSS PVTSHISKVL FGEDDSLLRV 

       550        560        570        580        590        600 
DCIRYNRAVR DLGPVISTGL LHLAEDGVLS PLALTEGGKG SSPSTRSSQG SQGSSGLEEK 

       610        620        630        640        650        660 
EVVEVTESRD KPGLNRSSEP LSGEKYSPKE LLALLKCVEA EIANYEACLK EEVEKRKKFK 

       670        680        690        700        710        720 
IDDQRRTHNY DEFICTFISM LAQEGMLANL VEQNISVRRR QGVSIGRLHK QRKPDRRKRS 


RPYKAKRQ 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"BAP1: a novel ubiquitin hydrolase which binds to the BRCA1 RING finger and enhances BRCA1-mediated cell growth suppression."
Jensen D.E., Proctor M., Marquis S.T., Gardner H.P., Ha S.I., Chodosh L.A., Ishov A.M., Tommerup N., Vissing H., Sekido Y., Minna J., Borodovsky A., Schultz D.C., Wilkinson K.D., Maul G.G., Barlev N., Berger S., Prendergast G.C., Rauscher F.J. III
Oncogene 16:1097-1112(1998) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB047820 mRNA. Translation: BAB32976.1.
AK129108 mRNA. Translation: BAC97918.1. Different initiation.
AK170576 mRNA. Translation: BAE41889.1.
BC050901 mRNA. Translation: AAH50901.1.
CCDSCCDS26910.1.
RefSeqNP_081364.1. NM_027088.2.
UniGeneMm.3779.

3D structure databases

ProteinModelPortalQ99PU7.
SMRQ99PU7. Positions 5-284, 629-690.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid222625. 10 interactions.
IntActQ99PU7. 5 interactions.

Protein family/group databases

MEROPSC12.004.

PTM databases

PhosphoSiteQ99PU7.

Proteomic databases

PRIDEQ99PU7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022458; ENSMUSP00000022458; ENSMUSG00000021901.
GeneID104416.
KEGGmmu:104416.
UCSCuc007sxh.1. mouse.

Organism-specific databases

CTD8314.
MGIMGI:1206586. Bap1.
RougeSearch...

Phylogenomic databases

eggNOGNOG249036.
GeneTreeENSGT00510000046560.
HOGENOMHOG000013189.
HOVERGENHBG054042.
InParanoidQ3TCR6.
KOK08588.
OMAPQQYSDD.
OrthoDBEOG7GN2M2.
PhylomeDBQ99PU7.
TreeFamTF313976.

Gene expression databases

BgeeQ99PU7.
CleanExMM_BAP1.
GenevestigatorQ99PU7.

Family and domain databases

Gene3D3.40.532.10. 1 hit.
InterProIPR001578. Peptidase_C12_UCH.
[Graphical view]
PANTHERPTHR10589. PTHR10589. 1 hit.
PfamPF01088. Peptidase_C12. 1 hit.
[Graphical view]
PRINTSPR00707. UBCTHYDRLASE.
ProtoNetSearch...

Other

ChiTaRSBAP1. mouse.
NextBio357097.
PROQ99PU7.
SOURCESearch...

Entry information

Entry nameBAP1_MOUSE
AccessionPrimary (citable) accession number: Q99PU7
Secondary accession number(s): Q3TCR6, Q6ZQE6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot