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D3ZHS6 (BAP1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 24. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
Gene names
Name:Bap1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length727 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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. 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 By similarity.

Sequence similarities

Belongs to the peptidase C12 family. BAP1 subfamily.

Sequence caution

The sequence EDL88955.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

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

Inferred from sequence or structural similarity. Source: UniProtKB

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

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 – 727727Ubiquitin carboxyl-terminal hydrolase BAP1
PRO_0000395817

Regions

Region594 – 719126Interaction with BRCA1 By similarity
Coiled coil628 – 65932 Potential
Motif363 – 3664HBM-like motif By similarity
Motif715 – 7206Nuclear localization signal By similarity

Sites

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

Sequences

Sequence LengthMass (Da)Tools
D3ZHS6 [UniParc].

Last modified July 13, 2010. Version 2.
Checksum: CEC525B181CDC02A

FASTA72780,310
        10         20         30         40         50         60 
MNKGWLELES DPGLFTLLVE DFGVKGVQVE EIYDLQSKCQ GPVYGFIFLF KWIEERRSRR 

        70         80         90        100        110        120 
KVSTLVDDTS VIDDDIVNSM 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 MAVVPDRRVK 

       250        260        270        280        290        300 
YEARLHVLKG NRQTVLEALQ QLIRVTQPEL IQTHKSQESQ LPEESKPASS KSPFGLEAGR 

       310        320        330        340        350        360 
TPAASECTHT DGAEEVAGSC PQTTTHSPPS KSKLVVKPSG SSLNGVPPTP TPIVQRLPAF 

       370        380        390        400        410        420 
LDNHNYAKSP MQEEEDLAAG VGRSRVPVRP QQYSDDEEDY EDEEEDVQNT SSAIRYKRKG 

       430        440        450        460        470        480 
TGKPGSLSNS SDGQLSVLQP NTINVLTEKL QESQKDLSIP LSIKTSSGAG SPAVAVPTHS 

       490        500        510        520        530        540 
QPSPTPSNES TDTASEIGSA FNSPLRSPIR SANPTRPSSP VTSHISKVLF GEDDSLLRVD 

       550        560        570        580        590        600 
CIRYNRAVRD LGPVISTGLL HLAEDGVLSP LALTEGGKGS SPSTRSSQGS QGSSSLEEKE 

       610        620        630        640        650        660 
VVEVTDSRDK SGLNRSSEPL SGEKYSPKEL LALLKCVEAE IANYEACLKE EVEKRKKFKI 

       670        680        690        700        710        720 
DDQRRTHNYD EFICTFISML AQEGMLANLV EQNISVRRRQ GVSIGRLHKQ RKPDRRKRSR 


PYKAKRQ 

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References

[1]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH474046 Genomic DNA. Translation: EDL88955.1. Sequence problems.
RefSeqNP_001100762.1. NM_001107292.1.
XP_006252668.1. XM_006252606.1.
UniGeneRn.3382.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSC12.004.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID306257.
KEGGrno:306257.
UCSCRGD:1311938. rat.

Organism-specific databases

CTD8314.
RGD1311938. Bap1.

Phylogenomic databases

KOK08588.
OrthoDBEOG7GN2M2.
PhylomeDBD3ZHS6.
TreeFamTF313976.

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

NextBio655725.
PROD3ZHS6.

Entry information

Entry nameBAP1_RAT
AccessionPrimary (citable) accession number: D3ZHS6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: July 13, 2010
Last modified: April 16, 2014
This is version 24 of the entry and version 2 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