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D3ZHS6

- BAP1_RAT

UniProt

D3ZHS6 - BAP1_RAT

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Protein

Ubiquitin carboxyl-terminal hydrolase BAP1

Gene

Bap1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi

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 – 911NucleophileBy similarity
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. protein deubiquitination Source: UniProtKB
  4. protein K48-linked deubiquitination Source: UniProtKB
  5. regulation of cell cycle Source: UniProtKB
  6. regulation of cell growth Source: UniProtKB
  7. 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
Gene namesi
Name:Bap1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 16

Organism-specific databases

RGDi1311938. 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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 727727Ubiquitin carboxyl-terminal hydrolase BAP1PRO_0000395817Add
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

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

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni594 – 719126Interaction with BRCA1By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili628 – 65932Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi363 – 3664HBM-like motifBy similarity
Motifi715 – 7206Nuclear localization signalBy similarity

Sequence similaritiesi

Belongs to the peptidase C12 family. BAP1 subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

InParanoidiD3ZHS6.
KOiK08588.
OrthoDBiEOG7GN2M2.
PhylomeDBiD3ZHS6.
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.

D3ZHS6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNKGWLELES DPGLFTLLVE DFGVKGVQVE EIYDLQSKCQ GPVYGFIFLF
60 70 80 90 100
KWIEERRSRR KVSTLVDDTS VIDDDIVNSM 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 MAVVPDRRVK YEARLHVLKG
260 270 280 290 300
NRQTVLEALQ QLIRVTQPEL IQTHKSQESQ LPEESKPASS KSPFGLEAGR
310 320 330 340 350
TPAASECTHT DGAEEVAGSC PQTTTHSPPS KSKLVVKPSG SSLNGVPPTP
360 370 380 390 400
TPIVQRLPAF LDNHNYAKSP MQEEEDLAAG VGRSRVPVRP QQYSDDEEDY
410 420 430 440 450
EDEEEDVQNT SSAIRYKRKG TGKPGSLSNS SDGQLSVLQP NTINVLTEKL
460 470 480 490 500
QESQKDLSIP LSIKTSSGAG SPAVAVPTHS QPSPTPSNES TDTASEIGSA
510 520 530 540 550
FNSPLRSPIR SANPTRPSSP VTSHISKVLF GEDDSLLRVD CIRYNRAVRD
560 570 580 590 600
LGPVISTGLL HLAEDGVLSP LALTEGGKGS SPSTRSSQGS QGSSSLEEKE
610 620 630 640 650
VVEVTDSRDK SGLNRSSEPL SGEKYSPKEL LALLKCVEAE IANYEACLKE
660 670 680 690 700
EVEKRKKFKI DDQRRTHNYD EFICTFISML AQEGMLANLV EQNISVRRRQ
710 720
GVSIGRLHKQ RKPDRRKRSR PYKAKRQ
Length:727
Mass (Da):80,310
Last modified:July 13, 2010 - v2
Checksum:iCEC525B181CDC02A
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CH474046 Genomic DNA. Translation: EDL88955.1. Sequence problems.
RefSeqiNP_001100762.1. NM_001107292.1.
XP_006252668.1. XM_006252606.2.
UniGeneiRn.3382.

Genome annotation databases

GeneIDi306257.
KEGGirno:306257.
UCSCiRGD:1311938. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CH474046 Genomic DNA. Translation: EDL88955.1 . Sequence problems.
RefSeqi NP_001100762.1. NM_001107292.1.
XP_006252668.1. XM_006252606.2.
UniGenei Rn.3382.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi C12.004.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 306257.
KEGGi rno:306257.
UCSCi RGD:1311938. rat.

Organism-specific databases

CTDi 8314.
RGDi 1311938. Bap1.

Phylogenomic databases

InParanoidi D3ZHS6.
KOi K08588.
OrthoDBi EOG7GN2M2.
PhylomeDBi D3ZHS6.
TreeFami TF313976.

Miscellaneous databases

NextBioi 655725.
PROi D3ZHS6.

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. 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.

Entry informationi

Entry nameiBAP1_RAT
AccessioniPrimary (citable) accession number: D3ZHS6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: July 13, 2010
Last modified: October 29, 2014
This is version 28 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3