| IED ID | IndEnz0002004862 |
| Enzyme Type ID | protease004862 |
| Protein Name |
Myc box-dependent-interacting protein 1 Amphiphysin II Amphiphysin-like protein Box-dependent myc-interacting protein 1 Bridging integrator 1 |
| Gene Name | BIN1 AMPHL |
| 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 | MAEMGSKGVTAGKIASNVQKKLTRAQEKVLQKLGKADETKDEQFEQCVQNFNKQLTEGTRLQKDLRTYLASVKAMHEASKKLNECLQEVYEPDWPGRDEANKIAENNDLLWMDYHQKLVDQALLTMDTYLGQFPDIKSRIAKRGRKLVDYDSARHHYESLQTAKKKDEAKIAKPVSLLEKAAPQWCQGKLQAHLVAQTNLLRNQAEEELIKAQKVFEEMNVDLQEELPSLWNSRVGFYVNTFQSIAGLEENFHKEMSKLNQNLNDVLVGLEKQHGSNTFTVKAQPSDNAPAKGNKSPSPPDGSPAATPEIRVNHEPEPAGGATPGATLPKSPSQLRKGPPVPPPPKHTPSKEVKQEQILSLFEDTFVPEISVTTPSQFEAPGPFSEQASLLDLDFDPLPPVTSPVKAPTPSGQSIPWDLWEPTESPAGSLPSGEPSAAEGTFAVSWPSQTAEPGPAQPAEASEVAGGTQPAAGAQEPGETAASEAASSSLPAVVVETFPATVNGTVEGGSGAGRLDLPPGFMFKVQAQHDYTATDTDELQLKAGDVVLVIPFQNPEEQDEGWLMGVKESDWNQHKELEKCRGVFPENFTERVP |
| Enzyme Length | 593 |
| Uniprot Accession Number | O00499 |
| 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, membrane shaping and membrane remodeling. Required in muscle cells for the formation of T-tubules, tubular invaginations of the plasma membrane that function in depolarization-contraction coupling (PubMed:24755653). 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: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 (PubMed:8782822). Has actin bundling activity and stabilizes actin filaments against depolymerization in vitro (PubMed:28893863). {ECO:0000250|UniProtKB:O08839, ECO:0000269|PubMed:24755653, ECO:0000269|PubMed:27179792, ECO:0000269|PubMed:28893863, ECO:0000269|PubMed:8782822}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (8); Beta strand (7); Chain (1); Coiled coil (2); Domain (2); Erroneous initiation (1); Helix (10); Initiator methionine (1); Modified residue (7); Natural variant (8); Region (4); Sequence conflict (10) |
| Keywords | 3D-structure;Acetylation;Alternative splicing;Cell membrane;Coiled coil;Cytoplasm;Developmental protein;Differentiation;Disease variant;Endocytosis;Endosome;Host-virus interaction;Membrane;Nucleus;Phosphoprotein;Reference proteome;SH3 domain |
| Interact With | Itself; Q9UBW5; Q9Y2H0; P09467; Q13496; Q8NFH8; Q8TB24; O95219; Q13426; P27958; Q9WMX2; P10636-7; P10636-8; P27958; P01106; P01106 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Isoform BIN1]: Nucleus {ECO:0000269|PubMed:8782822}. Cytoplasm {ECO:0000269|PubMed:9182667}. Endosome {ECO:0000250|UniProtKB:O08539}. Cell membrane, sarcolemma, T-tubule {ECO:0000250|UniProtKB:O08839}.; SUBCELLULAR LOCATION: [Isoform IIA]: Cytoplasm {ECO:0000269|PubMed:9182667}. |
| Modified Residue | MOD_RES 2; /note="N-acetylalanine"; /evidence="ECO:0007744|PubMed:22814378"; MOD_RES 296; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"; MOD_RES 298; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"; MOD_RES 303; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"; MOD_RES 307; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19367720"; MOD_RES 323; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231"; MOD_RES 331; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231" |
| Post Translational Modification | PTM: Phosphorylated by protein kinase C. {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | NMR spectroscopy (6); X-ray crystallography (1) |
| Cross Reference PDB | 1MUZ; 1MV0; 1MV3; 2FIC; 2RMY; 2RND; 5I22; |
| Mapped Pubmed ID | 10449755; 10535736; 10542231; 10559861; 10559924; 10625686; 10652430; 10738240; 11082044; 11231140; 11470803; 11517213; 11532990; 11577110; 11889126; 12057195; 12183633; 12532338; 12604805; 12773571; 12952949; 12972505; 14622578; 14622579; 14704274; 15252009; 15260957; 15318165; 15483625; 15502812; 15502813; 15649145; 15703209; 15895077; 15992821; 16103228; 16169070; 16275660; 16326391; 16410077; 16516635; 16798879; 16903783; 17059209; 17158794; 17210688; 17218774; 17474147; 17512409; 17540576; 17609109; 17611416; 17671430; 17681954; 17699764; 17765681; 17978091; 18093523; 18348166; 18388313; 18647389; 18658220; 18790740; 18817572; 18981233; 18985028; 19004523; 19092055; 19418541; 19536138; 19575674; 19603039; 19629135; 19851296; 19915558; 20033059; 20059951; 20140253; 20169111; 20198315; 20428113; 20448150; 20460622; 20558387; 20826345; 20927630; 20946875; 21059989; 21129173; 2115402; 21220176; 21278753; 21316588; 21321396; 21347408; 21379329; 21445324; 21447796; 21482805; 21613550; 21623381; 21678469; 21779028; 21841790; 21927000; 21927001; 21962517; 22099461; 22233676; 22281836; 22505844; 22539578; 22544318; 22810585; 22960267; 22976291; 23202439; 23297414; 23399914; 23414517; 23416715; 23570733; 23754947; 23803295; 23823722; 23861397; 23871436; 23891661; 23917616; 24205320; 24581490; 24582639; 24590001; 24606918; 24616074; 24660791; 24966051; 25022885; 25024306; 25036637; 25051234; 25107275; 25129075; 25257171; 25262827; 25341920; 25365775; 25461955; 25487648; 25578476; 25630570; 25683635; 25957634; 26042225; 26101835; 26194865; 26195312; 26233692; 26733302; 26738348; 26833786; 26846281; 26947052; 27003210; 27268056; 27346750; 27538496; 27773727; 27854204; 28152502; 28714960; 28755476; 28806752; 29504051; 29764032; 30253944; 30260023; 30353632; 30733337; 30885349; 30967682; 30992433; 31263146; 31335457; 31478261; 31815296; 31874619; 32568785; 32719966; 32727516; 32842621; 33326746; 33531457; 34072165; 34375641; 6146630; 7877694; 8524399; 8552632; 9092476; 9100026; 9427626; 9428629; 9635431; 9736607; |
| Motif | |
| Gene Encoded By | |
| Mass | 64,699 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |