Detail Information for IndEnz0002004867
IED ID IndEnz0002004867
Enzyme Type ID protease004867
Protein Name Myc box-dependent-interacting protein 1
Amphiphysin II
Amphiphysin-like protein
Bridging integrator 1
Gene Name Bin1 Amph2 Amphl
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 MAEMGSKGVTAGKIASNVQKKLTRAQEKVLQKLGKADETKDEQFEQCVQNFNKQLTEGTRLQKDLRTYLASVKAMHEASKKLSECLQEVYEPEWPGRDEANKIAENNDLLWMDYHQKLVDQALLTMDTYLGQFPDIKSRIAKRGRKLVDYDSARHHYESLQTAKKKDEAKIAKPVSLLEKAAPQWCQGKLQAHLVAQTNLLRNQAEEELIKAQKVFEEMNVDLQEELPSLWNSRVGFYVNTFQSIAGLEENFHKEMSKLNQNLNDVLVSLEKQHGSNTFTVKAQPSDSAPEKGNKSPSPPPDGSPAATPEIRVNHEPEPASGASPGATIPKSPSQLRKGPPVPPPPKHTPSKEMKQEQILSLFDDAFVPEISVTTPSQFEAPGPFSEQASLLDLDFEPLPPVASPVKAPTPSGQSIPWDLWEPTESQAGVLPSGEPSSAEGSFAVAWPSQTAEPGPAQPAEASEVVGGTQEPGETAASEATSSSLPAVVVETFSATVNGAVEGSTTTGRLDLPPGFMFKVQAQHDYTATDTDELQLKAGDVVLVIPFQNPEEQDEGWLMGVKESDWNQHKELEKCRGVFPENFTERVQ
Enzyme Length 588
Uniprot Accession Number O08839
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 (By similarity). Is a negative regulator of endocytosis (PubMed:9736607, PubMed:27760323). Is also involved in the regulation of intracellular vesicles sorting, modulation of BACE1 trafficking and the control of amyloid-beta production (By similarity). In neuronal circuits, endocytosis regulation may influence the internalization of PHF-tau aggregates (PubMed:27760323). May be involved in the regulation of MYC activity and the control cell proliferation (By similarity). {ECO:0000250|UniProtKB:O00499, ECO:0000250|UniProtKB:O08539, ECO:0000269|PubMed:27760323, ECO:0000269|PubMed:9736607}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Alternative sequence (5); Beta strand (5); Chain (1); Coiled coil (2); Compositional bias (1); Domain (2); Helix (4); Initiator methionine (1); Modified residue (7); Region (4)
Keywords 3D-structure;Acetylation;Alternative splicing;Cell membrane;Coiled coil;Cytoplasm;Developmental protein;Differentiation;Direct protein sequencing;Endocytosis;Endosome;Membrane;Nucleus;Phosphoprotein;Reference proteome;SH3 domain
Interact With O08838; P21575; Q9CR95
Induction
Subcellular Location SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O08539}. Cytoplasm {ECO:0000250|UniProtKB:O08539}. Endosome {ECO:0000250|UniProtKB:O08539}. Cell membrane, sarcolemma, T-tubule {ECO:0000269|PubMed:9182667}.
Modified Residue MOD_RES 2; /note=N-acetylalanine; /evidence=ECO:0000250|UniProtKB:O00499; MOD_RES 296; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:O00499; MOD_RES 298; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 304; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 308; /note=Phosphothreonine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 324; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 332; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:O00499
Post Translational Modification PTM: Phosphorylated by protein kinase C.
Signal Peptide
Structure 3D X-ray crystallography (1)
Cross Reference PDB 1BB9;
Mapped Pubmed ID 10692452; 16357825; 16396496; 17762867; 24130457;
Motif
Gene Encoded By
Mass 64,533
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda