| IED ID | IndEnz0002009935 |
| Enzyme Type ID | protease009935 |
| Protein Name |
STAM-binding protein EC 3.4.19.- Associated molecule with the SH3 domain of STAM |
| Gene Name | Stambp Amsh |
| Organism | Rattus norvegicus (Rat) |
| 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 Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MSDHADVSLPPQDRVRILSQLGSAVELNEDIPPRRYFRSGVEIIRMASIYSEEGNIEHAFILYNKYITLFIEKLPKHRDYKSAIIPEKKDAVKKLKNVAFPKAEELKTELLKRYTKEYEQYKERKKKEEEELARNIAIQQELEKEKQRVAQQKQKQLEQEQFHAFEKMIQKQELEKERLKIVQEFGKVDPGPCGPLLPDLEKPCVDVAPSSPFSPTQTSDCNTTLRPAKPPVVDRSLKPGALSVIENVPTIEGLRHIVVPRNLCSEFLQLASANTAKGIETCGVLCGKLMRNEFTITHVLIPRQNGGPDYCHTENEEEIFFMQDDLGLLTLGWIHTHPTQTAFLSSVDLHTHCSYQMMLPESIAIVCSPKFQETGFFKLTDYGLQEISTCRQKGFHPHGRDPPLFCDCSHVTVKDRIVTITDLR |
| Enzyme Length | 424 |
| Uniprot Accession Number | Q8R424 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by N-ethylmaleimide. {ECO:0000250}. |
| 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 (By similarity). Involved in the ubiquitin-dependent sorting and trafficking of receptors from endosomes to lysosome. Endosomal localization of STAMBP is required for efficient EGFR degradation but not for its internalization. Involved in the negative regulation of PI3K-AKT-mTOR and RAS-MAP signaling pathways (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Domain (1); Metal binding (7); Modified residue (3); Motif (1); Region (2); Site (1) |
| Keywords | Cytoplasm;Endosome;Hydrolase;Membrane;Metal-binding;Metalloprotease;Nucleus;Phosphoprotein;Protease;Reference proteome;Ubl conjugation;Ubl conjugation pathway;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Endosome {ECO:0000250}. |
| Modified Residue | MOD_RES 2; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:O95630; MOD_RES 48; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:O95630; MOD_RES 243; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:O95630 |
| Post Translational Modification | PTM: Phosphorylated after BMP type I receptor activation. {ECO:0000250}.; PTM: Ubiquitinated by SMURF2 in the presence of RNF11. {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 335..348; /note=JAMM motif; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182 |
| Gene Encoded By | |
| Mass | 48,512 |
| 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 |