Detail Information for IndEnz0002002842
IED ID IndEnz0002002842
Enzyme Type ID protease002842
Protein Name Ubiquitin carboxyl-terminal hydrolase BAP1
EC 3.4.19.12
BRCA1-associated protein 1
Ubiquitin C-terminal hydrolase X4
UCH-X4
Gene Name Bap1 Kiaa0272
Organism Mus musculus (Mouse)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse)
Enzyme Sequence MNKGWLELESDPGLFTLLVEDFGVKGVQVEEIYDLQSKCQGPVYGFIFLFKWIEERRSRRKVSTLVDDTSVIDDDIVNNMFFAHQLIPNSCATHALLSVLLNCSNVDLGPTLSRMKDFTKGFSPESKGYAIGNAPELAKAHNSHARPEPRHLPEKQNGLSAVRTMEAFHFVSYVPITGRLFELDGLKVYPIDHGPWGEDEEWTDKARRVIMERIGLATAGEPYHDIRFNLMAVVPDRRIKYETRLHVLKVNRQTVLEALQQLIRVTQPELIQTHKSQESQLPEESKPASSKSPLGLEAGRTPVASECTQTDGAEEVAGSCPQTTTHSPPSKCKLVVKPPGSSLNGVPPNPAPIVQRLPAFLDNHNYAKSPMQEEEDLAAGVGRSRVPVRAPQQYSEDEDDYEDEDEDVQNTNPAIRYKRKGTGKPGSLSNSSDGQLSVLQPNTINVLTEKLQESQKDLSVPLSIKTSSGAGSPAVAVPTHSQPSPTPSNESTDTASEIGSAFNSPLRSPIRSANPTRPSSPVTSHISKVLFGEDDSLLRVDCIRYNRAVRDLGPVISTGLLHLAEDGVLSPLALTEGGKGSSPSTRSSQGSQGSSGLEEKEVVEVTESRDKPGLNRSSEPLSGEKYSPKELLALLKCVEAEIANYEACLKEEVEKRKKFKIDDQRRTHNYDEFICTFISMLAQEGMLANLVEQNISVRRRQGVSIGRLHKQRKPDRRKRSRPYKAKRQ
Enzyme Length 728
Uniprot Accession Number Q99PU7
Absorption
Active Site ACT_SITE 91; /note=Nucleophile; /evidence=ECO:0000269|PubMed:18757409; ACT_SITE 169; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P09936
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=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).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:Q92560};
DNA Binding
EC Number 3.4.19.12
Enzyme Function 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. {ECO:0000250|UniProtKB:Q92560}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Coiled coil (1); Compositional bias (5); Erroneous initiation (1); Modified residue (7); Motif (2); Mutagenesis (2); Region (6); Sequence conflict (1); Site (1)
Keywords Chromatin regulator;Coiled coil;Cytoplasm;Hydrolase;Nucleus;Phosphoprotein;Protease;Reference proteome;Thiol protease;Ubl conjugation;Ubl conjugation pathway
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q92560}. Nucleus {ECO:0000250|UniProtKB:Q92560}. Note=Mainly nuclear. Binds to chromatin. Localizes to the cytoplasm when monoubiquitinated by the E2/E3 hybrid ubiquitin-protein ligase UBE2O. {ECO:0000250|UniProtKB:Q92560}.
Modified Residue MOD_RES 292; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q92560; MOD_RES 369; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 395; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 492; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:Q92560; MOD_RES 520; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q92560; MOD_RES 536; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q92560; MOD_RES 584; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q92560
Post Translational Modification PTM: 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. {ECO:0000250|UniProtKB:Q92560}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 11217851; 12466851; 14610273; 18799693; 19188440; 20360068; 21267068; 21677750; 22878500; 24928783; 25283999; 25359211; 25575566; 26119930; 26437366; 26496610; 26896281; 27373151; 28275095; 28473526; 28765116; 29490280; 29539633; 29678836; 29743720; 30013160; 30156010; 31000662; 31151962; 31699823; 32271879; 32310225; 32541668; 33888563; 33912157; 34170818; 34815344;
Motif MOTIF 363..366; /note=HBM-like motif; /evidence=ECO:0000250|UniProtKB:Q92560; MOTIF 716..721; /note=Nuclear localization signal; /evidence=ECO:0000250|UniProtKB:Q92560
Gene Encoded By
Mass 80,492
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda