| IED ID | IndEnz0002004863 |
| Enzyme Type ID | protease004863 |
| Protein Name |
Myc box-dependent-interacting protein 1 Amphiphysin II Amphiphysin-like protein Bridging integrator 1 SH3 domain-containing protein 9 |
| Gene Name | Bin1 Amphl Sh3p9 |
| 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 | MAEMGSKGVTAGKIASNVQKKLTRAQEKVLQKLGKADETKDEQFEQCVQNFNKQLTEGTRLQKDLRTYLASVKAMHEASKKLSECLQEVYEPEWPGRDEANKIAENNDLLWMDYHQKLVDQALLTMDTYLGQFPDIKSRIAKRGRKLVDYDSARHHYESLQTAKKKDEAKIAKPVSLLEKAAPQWCQGKLQAHLVAQTNLLRNQAEEELIKAQKVFEEMNVDLQEELPSLWNSRVGFYVNTFQSIAGLEENFHKEMSKLNQNLNDVLVSLEKQHGSNTFTVKAQPSDNAPEKGNKSPSPPPDGSPAATPEIRVNHEPEPASGASPGATIPKSPSQLRKGPPVPPPPKHTPSKEMKQEQILSLFDDAFVPEISVTTPSQFEAPGPFSEQASLLDLDFEPLPPVASPVKAPTPSGQSIPWDLWEPTESQAGILPSGEPSSAEGSFAVAWPSQTAEPGPAQPAEASEVVGGAQEPGETAASEATSSSLPAVVVETFSATVNGAVEGSAGTGRLDLPPGFMFKVQAQHDYTATDTDELQLKAGDVVLVIPFQNPEEQDEGWLMGVKESDWNQHKELEKCRGVFPENFTERVQ |
| Enzyme Length | 588 |
| Uniprot Accession Number | O08539 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Is a key player in the control of plasma membrane curvature, and membrane shaping and remodeling. Required in muscle cells for the formation of T-tubules, tubular invaginations of the plasma membrane that function in depolarization-contraction coupling. Required in muscle cells for the formation of T-tubules, tubular invaginations of the plasma membrane that function in depolarization-contraction coupling (PubMed:12183633). Is a negative regulator of endocytosis (By similarity). Is also involved in the regulation of intracellular vesicles sorting, modulation of BACE1 trafficking and the control of amyloid-beta production (PubMed:12668730, PubMed:27179792). In neuronal circuits, endocytosis regulation may influence the internalization of PHF-tau aggregates (By similarity). May be involved in the regulation of MYC activity and the control cell proliferation (By similarity). {ECO:0000250|UniProtKB:O00499, ECO:0000250|UniProtKB:O08839, ECO:0000269|PubMed:12183633, ECO:0000269|PubMed:12668730, ECO:0000269|PubMed:27179792}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (2); Chain (1); Coiled coil (2); Compositional bias (1); Domain (2); Initiator methionine (1); Modified residue (7); Region (4) |
| Keywords | Acetylation;Alternative splicing;Cell membrane;Coiled coil;Cytoplasm;Developmental protein;Differentiation;Endocytosis;Endosome;Membrane;Nucleus;Phosphoprotein;Reference proteome;SH3 domain |
| Interact With | P10637; Q9Z2C5 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O00499}. Cytoplasm {ECO:0000269|PubMed:12668730}. Endosome {ECO:0000269|PubMed:12668730}. Cell membrane, sarcolemma, T-tubule {ECO:0000250|UniProtKB:O08839}. |
| Modified Residue | MOD_RES 2; /note="N-acetylalanine"; /evidence="ECO:0000250|UniProtKB:O00499"; MOD_RES 296; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"; MOD_RES 298; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"; MOD_RES 304; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:15345747, ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"; MOD_RES 308; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"; MOD_RES 324; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 332; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:19131326" |
| Post Translational Modification | PTM: Phosphorylated by protein kinase C. {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10036185; 10087302; 11044609; 11879655; 12466851; 12773571; 12789266; 14660576; 15226823; 15711557; 16602821; 16615898; 16635246; 17210688; 17699764; 19629135; 19633357; 20169111; 21267068; 22421546; 22526583; 22707207; 23399914; 23640057; 23715556; 23917616; 24534009; 24836577; 25257171; 25939245; 26195312; 26506308; 26733606; 26833786; 27895104; 28806752; 29130937; 30692199; 30894500; 31065832; 31263146; 31291551; 31408457; 32160554; 32552912; 32994313; 33682352; 34633413; 9356459; |
| Motif | |
| Gene Encoded By | |
| Mass | 64,470 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |