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A2VDM8

- BAP1_BOVIN

UniProt

A2VDM8 - BAP1_BOVIN

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Protein

Ubiquitin carboxyl-terminal hydrolase BAP1

Gene

BAP1

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript 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 – 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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

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 – 711711Ubiquitin carboxyl-terminal hydrolase BAP1PRO_0000395816Add
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

Structurei

3D structure databases

ProteinModelPortaliA2VDM8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni578 – 703126Interaction with BRCA1By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili612 – 64332Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi345 – 3484HBM-like motifBy similarity
Motifi699 – 7046Nuclear localization signalBy similarity

Sequence similaritiesi

Belongs to the peptidase C12 family. BAP1 subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

HOVERGENiHBG054042.
InParanoidiA2VDM8.
KOiK08588.

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.

A2VDM8-1 [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 IKYEARLHVL KVNRQTVLEA LQQLIRVTQP
260 270 280 290 300
ELIQTHKSQE SQLPEESKPA SSKSPLALET SRAPVASEST HTDGVEEVAG
310 320 330 340 350
SCPQAPTHSP PSKPKLVVKP PGSNINGVPP NPTPIVQRLP AFLDNHNYAK
360 370 380 390 400
SPMQEEEDLA AGVGRSRVPV RPPQQYSDDE DDYEDEEEDD AQSTSSAIRY
410 420 430 440 450
KRKGPGKPGP LSSSGDGQLS VLQPNTINVL AEKLKESQKD LSIPLSIKTS
460 470 480 490 500
SGAGSPAVAV PTHSQPSPTP SNESTDTASE IGSAFNSPLR SPIRSANPTR
510 520 530 540 550
PSSPVTSHIS KVLFGEDDSL LRVDCIRYNR AVRDLGPVIS TGLLHLAEDG
560 570 580 590 600
VLSPLALTES GKGSSPSIRP SQGSQGSGSP EEKEVVEAVD SREKPGLVRP
610 620 630 640 650
SESLNGEKYS PKELLALLKC VEAEIANYEA CLKEEVEKRK KFKIDDQRRT
660 670 680 690 700
HNYDEFICTF ISMLAQEGML ANLVEQNISV RRRQGVSIGR LHKQRKPDRR
710
KRSRPYKAKR Q
Length:711
Mass (Da):78,333
Last modified:March 20, 2007 - v1
Checksum:i31D9E5B4AF11C286
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC133317 mRNA. Translation: AAI33318.1.
RefSeqiNP_001096019.1. NM_001102549.1.
UniGeneiBt.20209.

Genome annotation databases

GeneIDi100124510.
KEGGibta:100124510.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC133317 mRNA. Translation: AAI33318.1 .
RefSeqi NP_001096019.1. NM_001102549.1.
UniGenei Bt.20209.

3D structure databases

ProteinModelPortali A2VDM8.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi C12.004.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100124510.
KEGGi bta:100124510.

Organism-specific databases

CTDi 8314.

Phylogenomic databases

HOVERGENi HBG054042.
InParanoidi A2VDM8.
KOi K08588.

Miscellaneous databases

NextBioi 20788729.

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. NIH - Mammalian Gene Collection (MGC) project
    Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Basal ganglia.

Entry informationi

Entry nameiBAP1_BOVIN
AccessioniPrimary (citable) accession number: A2VDM8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: March 20, 2007
Last modified: October 29, 2014
This is version 35 of the entry and version 1 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