EPN1
entrez
29924
canonical
uniprot
Q9Y6I3
canonical
ensembl
ENSG00000063245
resolver
ensp
ENSP00000085079
resolver
ensp
ENSP00000270460
resolver
ensp
ENSP00000406209
resolver
ensp
ENSP00000540122
resolver
genesymbol
EPN1
resolver
hgnc
HGNC:21604
resolver
uniprot
Q86ST3
resolver
uniprot
Q9HA18
resolver
uniprot_entry
EPN1_HUMAN
resolver
uniprot_sec
Q86ST3
resolver
uniprot_sec
Q9HA18
resolver
amino_acid_sequence
MSTSSLRRQMKNIVHNYSEAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKENMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLREERAHALKTKEKLAQTATASSAAVGSGPPPEAEQAWPQSSGEEELQLQLALAMSKEEADQPPSCGPEDDAQLQLALSLSREEHDKEERIRRGDDLRLQMAIEESKRETGGKEESSLMDLADVFTAPAPAPTTDPWGGPAPMAAAVPTAAPTSDPWGGPPVPPAADPWGGPAPTPASGDPWRPAAPAGPSVDPWGGTPAPAAGEGPTPDPWGSSDGGVPVSGPSASDPWTPAPAFSDPWGGSPAKPSTNGTTAAGGFDTEPDEFSDFDRLRTALPTSGSSAGELELLAGEVPARSPGAFDMSGVRGSLAEAVGSPPPAATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPGPTPPGAKASNPFLPGGGPATGPSVTNPFQPAPPATLTLNQLRLSPVPPVPGAPPTYISPLGGGPGLPPMMPPGPPAPNTNPFLL
uniprot
proteins
function
FUNCTION: Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations (By similarity). Regulates receptor-mediated endocytosis (PubMed:10393179, PubMed:10557078). {ECO:0000250|UniProtKB:O88339, ECO:0000269|PubMed:10393179, ECO:0000269|PubMed:10557078}.
uniprot
proteins
mass_dalton
60293
uniprot
proteins
mutagenesis
MUTAGEN 382; /note="S->A: Abolishes phosphorylation by CDK1."; /evidence="ECO:0000269|PubMed:10764745"; MUTAGEN 382; /note="S->D: Abolishes phosphorylation by CDK1 and reduces REPS2 binding."; /evidence="ECO:0000269|PubMed:10764745"; MUTAGEN 404; /note="F->A: Reduces interaction with AP2B1."; /evidence="ECO:0000269|PubMed:16516836
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on serine and/or threonine residues in mitotic cells. Phosphorylation reduces interaction with REPS2, AP-2 and the membrane fraction. Depolarization of synaptosomes results in dephosphorylation. {ECO:0000269|PubMed:10764745}.; PTM: Ubiquitinated. {ECO:0000250}.
uniprot
proteins
protein_family
Epsin family
uniprot
proteins
pubmed
10393179
uniprot
proteins
pubmed
10557078
uniprot
proteins
pubmed
10764745
uniprot
proteins
pubmed
12775724
uniprot
proteins
pubmed
12836669
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16516836
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18199683
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19367720
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
34927784
uniprot
proteins
sequence_length
576
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Nucleus {ECO:0000250}. Membrane, clathrin-coated pit {ECO:0000250}. Note=Associated with the cytoplasmic membrane at sites where clathrin-coated pits are forming. Colocalizes with clathrin and AP-2 in a punctate pattern on the plasma membrane. Detected in presynaptic nerve terminals and in Golgi stacks. May shuttle to the nucleus when associated with ZBTB16/ZNF145 (By similarity). {ECO:0000250}.
uniprot
proteins