Epn1
entrez
117277
canonical
uniprot
O88339
canonical
ensembl
ENSRNOG00000015753
resolver
ensp
ENSRNOP00000021286
resolver
genesymbol
Epn1
resolver
uniprot_entry
EPN1_RAT
resolver
amino_acid_sequence
MSTSSLRRQMKNIVHNYSEAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKENMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLREERAHALKTKEKLAQTATASSAAVGSGPPPEAEQAWPQSSGEEELQLQLALAMSKEEADQPPSCGPEDDVQLQLALSLSREEHDKEERIRRGDDLRLQMAIEESKRETGGKEESSLMDLADVFTTPAPPQASDPWGGPASVPTAVPVAAAASDPWGAPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTSDPWGSADGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAVGGFDTEPDEFSDFDRLRTALPTSGSSTGELELLAGEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPGPTPPGAKASNPFLPSGAPATGPSVTNPFQPAPPATLTLNQLRLSPVPPVPGAPPTYISPLGGGPGLPPMMPPGPPAPNTNPFLL
uniprot
proteins
function
FUNCTION: Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) (PubMed:11161217). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations (PubMed:12353027, PubMed:9723620). Regulates receptor-mediated endocytosis (By similarity). {ECO:0000250|UniProtKB:Q9Y6I3, ECO:0000269|PubMed:11161217, ECO:0000269|PubMed:12353027, ECO:0000269|PubMed:9723620}.
uniprot
proteins
mass_dalton
60158
uniprot
proteins
mutagenesis
MUTAGEN 6; /note="L->E,H,Q: Reduces lipid binding."; /evidence="ECO:0000269|PubMed:12353027"; MUTAGEN 8; /note="R->A: Strongly reduces lipid binding."; /evidence="ECO:0000269|PubMed:11161217"; MUTAGEN 63; /note="R->L: Strongly reduces lipid binding. Abolishes lipid binding; when associated with L-73."; /evidence="ECO:0000269|PubMed:11161217, ECO:0000269|PubMed:12353027"; MUTAGEN 72; /note="R->A: Abolishes ZNF145 binding."; /evidence="ECO:0000269|PubMed:11161217"; MUTAGEN 73; /note="H->L: Abolishes lipid binding; when associated with L-63."; /evidence="ECO:0000269|PubMed:12353027"; MUTAGEN 76; /note="K->A: Strongly reduces lipid binding."; /evidence="ECO:0000269|PubMed:11161217"; MUTAGEN 190; /note="L->A: Abolishes mono-ubiquitination."; /evidence="ECO:0000269|PubMed:11919637"; MUTAGEN 257..259; /note="LMD->AAA: Strongly reduces clathrin binding."; /evidence="ECO:0000269|PubMed:10692452"; MUTAGEN 260..263; /note="LADV->AAAA: Strongly reduces clathrin binding."; /evidence="ECO:0000269|PubMed:10692452
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated. {ECO:0000269|PubMed:11919637}.; 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:9920862}.
uniprot
proteins
protein_family
Epsin family
uniprot
proteins
pubmed
10380931
uniprot
proteins
pubmed
10393179
uniprot
proteins
pubmed
10430869
uniprot
proteins
pubmed
10692452
uniprot
proteins
pubmed
10791968
uniprot
proteins
pubmed
10944104
uniprot
proteins
pubmed
11161217
uniprot
proteins
pubmed
11919637
uniprot
proteins
pubmed
12057195
uniprot
proteins
pubmed
12353027
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
9723620
uniprot
proteins
pubmed
9920862
uniprot
proteins
sequence_length
575
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral membrane protein. Nucleus. Membrane, clathrin-coated pit. 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. Colocalizes with clathrin at the Golgi complex. Detected in presynaptic nerve terminals and in synaptosomes. May shuttle to the nucleus when associated with ZBTB16/ZNF145.
uniprot
proteins