IED ID | IndEnz0002013601 |
Enzyme Type ID | protease013601 |
Protein Name |
Probable ubiquitin carboxyl-terminal hydrolase 4 EC 3.4.19.12 Deubiquitinating enzyme 4 Ubiquitin thioesterase 4 Ubiquitin-specific-processing protease 4 |
Gene Name | ubp4 SPBC18H10.08c |
Organism | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota Taphrinomycotina Schizosaccharomycetes Schizosaccharomycetales Schizosaccharomycetaceae Schizosaccharomyces Schizosaccharomyces pombe (Fission yeast) Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
Enzyme Sequence | MSDDYFDRLFELAFVYINEDETIQSCSFRGQRWLEEAQTLEQKNSLLKAYYYYLKALKLAYEIPCRFEISVKSTHYGEFKQFQKLAIQAVSKAFTIKSKLAVKHYLPVIQISDALSLSKKSSLKVLFLNFYSQESSKGYVFSKHTIAIPISCLQSMDSSKIYDFLKSAPFHPSMVICYSLERYFEDVSLAYKLYSMLRSLKLDPHFMELANPKKVDSSLSYENYQPIGLTNLGNTCYMNCVLQCLFACKDLTIPMLQGRGLLQNINTKNPLGTGGKITSAFFSLLQSVLLNHGQRSISPRNFLEIVQSLNRDFSIDGQCDAQEFLNFFLDKLHEDLNSNASRSPIAPLTEDQLSAREELPLSHFSHIEWNLHLRSNKSIVVNNFVGQLCSRTQCMTCGRTSTTFAPFTSLAIPIDDVSHVVSLQECLLKFSAPELLQGHDGWHCPVCKVQRSAKKVIMISKLPEYLIIQIQRFKISVMGRKKIDTPLGLSLQIPSKMLVPPSFQSGIGYIPSNYNLFAFICHYGQLENGHYISDVLFNNEWCHIDDSIVRTVGGITDLREDFSSSYILFYKRSSLLEEFEDKCPKMTLKRNVK |
Enzyme Length | 593 |
Uniprot Accession Number | O60139 |
Absorption | |
Active Site | ACT_SITE 236; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093"; ACT_SITE 530; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093" |
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; |
DNA Binding | |
EC Number | 3.4.19.12 |
Enzyme Function | FUNCTION: Has an ATP-independent isopeptidase activity, cleaving at the C-terminus of the ubiquitin moiety. Acts late in the proteolytic pathway in conjunction with the 26S proteasome. Plays a role in avoiding DNA overreplication (By similarity). {ECO:0000250}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (1); Domain (1); Modified residue (2) |
Keywords | Cytoplasm;Endosome;Hydrolase;Phosphoprotein;Protease;Reference proteome;Thiol protease;Ubl conjugation pathway |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. Endosome. |
Modified Residue | MOD_RES 338; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:18257517; MOD_RES 343; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:18257517 |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 19547744; 20473289; 21182284; 21247416; 23173672; 23697806; 25720772; 26412298; 29996109; 30726745; 32062975; |
Motif | |
Gene Encoded By | |
Mass | 67,747 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |