| IED ID | IndEnz0002012733 |
| Enzyme Type ID | protease012733 |
| Protein Name |
STAM-binding protein EC 3.4.19.- Associated molecule with the SH3 domain of STAM Endosome-associated ubiquitin isopeptidase |
| Gene Name | STAMBP AMSH |
| Organism | Homo sapiens (Human) |
| 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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MSDHGDVSLPPEDRVRALSQLGSAVEVNEDIPPRRYFRSGVEIIRMASIYSEEGNIEHAFILYNKYITLFIEKLPKHRDYKSAVIPEKKDTVKKLKEIAFPKAEELKAELLKRYTKEYTEYNEEKKKEAEELARNMAIQQELEKEKQRVAQQKQQQLEQEQFHAFEEMIRNQELEKERLKIVQEFGKVDPGLGGPLVPDLEKPSLDVFPTLTVSSIQPSDCHTTVRPAKPPVVDRSLKPGALSNSESIPTIDGLRHVVVPGRLCPQFLQLASANTARGVETCGILCGKLMRNEFTITHVLIPKQSAGSDYCNTENEEELFLIQDQQGLITLGWIHTHPTQTAFLSSVDLHTHCSYQMMLPESVAIVCSPKFQETGFFKLTDHGLEEISSCRQKGFHPHSKDPPLFCSCSHVTVVDRAVTITDLR |
| Enzyme Length | 424 |
| Uniprot Accession Number | O95630 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by N-ethylmaleimide. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.19.- |
| Enzyme Function | FUNCTION: Zinc metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not cleave 'Lys-48'-linked polyubiquitin chains (By similarity). Plays a role in signal transduction for cell growth and MYC induction mediated by IL-2 and GM-CSF. Potentiates BMP (bone morphogenetic protein) signaling by antagonizing the inhibitory action of SMAD6 and SMAD7. Has a key role in regulation of cell surface receptor-mediated endocytosis and ubiquitin-dependent sorting of receptors to lysosomes. Endosomal localization of STAMBP is required for efficient EGFR degradation but not for its internalization (By similarity). Involved in the negative regulation of PI3K-AKT-mTOR and RAS-MAP signaling pathways. {ECO:0000250, ECO:0000269|PubMed:10383417, ECO:0000269|PubMed:11483516, ECO:0000269|PubMed:15314065, ECO:0000269|PubMed:17261583, ECO:0000269|PubMed:23542699}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (1); Beta strand (12); Chain (1); Domain (1); Helix (10); Metal binding (7); Modified residue (5); Motif (1); Mutagenesis (1); Natural variant (6); Region (2); Site (1); Turn (2) |
| Keywords | 3D-structure;Alternative splicing;Cytoplasm;Disease variant;Endosome;Hydrolase;Membrane;Metal-binding;Metalloprotease;Nucleus;Phosphoprotein;Protease;Reference proteome;Ubl conjugation;Ubl conjugation pathway;Zinc |
| Interact With | P31941; P54253; P48643; Q9HD42; Q7LBR1; Q9Y3E7; Q9Y3E7-1; Q9H444; Q9NZZ3; O75791; P62993; Q8WXH2; O60260-5; Q9Y3C5; O43541-2; Q92783; O75886; Q13148; Q15645; P0CG47 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus. Membrane; Peripheral membrane protein. Cytoplasm. Early endosome. |
| Modified Residue | MOD_RES 2; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:11483516, ECO:0007744|PubMed:23186163"; MOD_RES 48; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:11483516"; MOD_RES 243; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:11483516, ECO:0007744|PubMed:23186163"; MOD_RES 245; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:11483516"; MOD_RES 247; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:11483516, ECO:0007744|PubMed:23186163" |
| Post Translational Modification | PTM: Phosphorylated after BMP type I receptor activation. {ECO:0000269|PubMed:11483516}.; PTM: Ubiquitinated by SMURF2 in the presence of RNF11. {ECO:0000269|PubMed:14755250}. |
| Signal Peptide | |
| Structure 3D | NMR spectroscopy (1); X-ray crystallography (3) |
| Cross Reference PDB | 2XZE; 3RZU; 3RZV; 5IXF; |
| Mapped Pubmed ID | 10982817; 12773374; 16169070; 16189514; 16520378; 16716190; 16730941; 16760479; 16854379; 17078930; 17159328; 17711858; 18395747; 18758443; 19060904; 19373254; 19615732; 19684015; 20159979; 20936779; 21448666; 21706016; 21827950; 21888914; 21988832; 22800866; 24151880; 25070368; 25416956; 25692795; 26496610; 26601948; 27725184; 28492230; 29907875; 30454887; 31638258; 31671219; 34102455; 34425109; |
| Motif | MOTIF 335..348; /note=JAMM motif; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182 |
| Gene Encoded By | |
| Mass | 48,077 |
| Kinetics | |
| Metal Binding | METAL 335; /note=Zinc 1; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182; METAL 337; /note=Zinc 1; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182; METAL 348; /note=Zinc 1; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182; METAL 350; /note=Zinc 2; /evidence=ECO:0000250; METAL 390; /note=Zinc 2; /evidence=ECO:0000250; METAL 396; /note=Zinc 2; /evidence=ECO:0000250; METAL 398; /note=Zinc 2; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |