| IED ID | IndEnz0002009544 |
| Enzyme Type ID | protease009544 |
| Protein Name |
AMSH-like protease AMSH-LP EC 3.4.19.- AMSH family protein AMSH-FP STAM-binding protein-like 1 |
| Gene Name | Stambpl1 Amshlp |
| 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 | MEQPFTVNSLKKLAAMPDHTDVSLSPEERVRALSKLGCNISINEDITPRRYFRSGVEMERMASVYLEEGNLENAFVLYNKFITLFVEKLPSHRDYQQCAVPEKQDIMKKLKEIAFPRTDELKTDLLRKYNIEYQEYLQSKNKYKAEILKKLEHQRLIEAERQRIAQMRQQQLESEQFLFFEDQLKKQELARGQIRGQDSPVLSEQTDGSALSCFSTHQSNSLRNAFADHPHKSDGSNFANYSPPVNRALKPAATLSAVQNLVVEGLRCVVLSRDLCHKFLLLADSNTVRGIETCGILCGKLTHNEFTITHVVVPKQSAGPDYCDVENVEELFNVQDQHGLLTLGWIHTHPTQTAFLSSVDLHTHCSYQLMLPEAIAIVCSPKHKDTGIFRLTNAGMLEVSTCKKKGFHPHTKDPKLFSICSHVLVKDIKTTVLDLR |
| Enzyme Length | 436 |
| Uniprot Accession Number | Q76N33 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| 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). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (1); Chain (1); Domain (1); Erroneous initiation (1); Metal binding (7); Modified residue (3); Motif (1); Sequence conflict (2); Site (1) |
| Keywords | Acetylation;Alternative splicing;Hydrolase;Metal-binding;Metalloprotease;Phosphoprotein;Protease;Reference proteome;Ubl conjugation pathway;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | MOD_RES 1; /note=N-acetylmethionine; /evidence=ECO:0000250|UniProtKB:Q96FJ0; MOD_RES 25; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q96FJ0; MOD_RES 242; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11217851; 12466851; 16141072; 18799693; 21267068; 21677750; 9705845; |
| Motif | MOTIF 347..360; /note=JAMM motif; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182 |
| Gene Encoded By | |
| Mass | 49,640 |
| Kinetics | |
| Metal Binding | METAL 347; /note=Zinc 1; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182; METAL 349; /note=Zinc 1; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182; METAL 360; /note=Zinc 1; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182; METAL 362; /note=Zinc 2; /evidence=ECO:0000250; METAL 402; /note=Zinc 2; /evidence=ECO:0000250; METAL 408; /note=Zinc 2; /evidence=ECO:0000250; METAL 410; /note=Zinc 2; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |