CLINT1
entrez
9685
canonical
uniprot
Q14677
canonical
ensembl
ENSG00000113282
resolver
ensp
ENSP00000388340
resolver
ensp
ENSP00000429345
resolver
ensp
ENSP00000429824
resolver
ensp
ENSP00000657802
resolver
ensp
ENSP00000701025
resolver
ensp
ENSP00000701026
resolver
genesymbol
CLINT1
resolver
genesymbol_syn
ENTH
resolver
genesymbol_syn
EPN4
resolver
genesymbol_syn
EPNR
resolver
genesymbol_syn
KIAA0171
resolver
hgnc
HGNC:23186
resolver
uniprot
A0A0S2Z4Y4
resolver
uniprot
A0A0S2Z5H3
resolver
uniprot
B7Z6F8
resolver
uniprot
D3DQJ6
resolver
uniprot
Q8NAF1
resolver
uniprot
Q96E05
resolver
uniprot_entry
A0A0S2Z4Y4_HUMAN
resolver
uniprot_entry
A0A0S2Z5H3_HUMAN
resolver
uniprot_entry
EPN4_HUMAN
resolver
uniprot_sec
B7Z6F8
resolver
uniprot_sec
D3DQJ6
resolver
uniprot_sec
Q8NAF1
resolver
uniprot_sec
Q96E05
resolver
amino_acid_sequence
MLNMWKVRELVDKATNVVMNYSEIESKVREATNDDPWGPSGQLMGEIAKATFMYEQFPELMNMLWSRMLKDNKKNWRRVYKSLLLLAYLIRNGSERVVTSAREHIYDLRSLENYHFVDEHGKDQGINIRQKVKELVEFAQDDDRLREERKKAKKNKDKYVGVSSDSVGGFRYSERYDPEPKSKWDEEWDKNKSAFPFSDKLGELSDKIGSTIDDTISKFRRKDREDSPERCSDSDEEKKARRGRSPKGEFKDEEETVTTKHIHITQATETTTTRHKRTANPSKTIDLGAAAHYTGDKASPDQNASTHTPQSSVKTSVPSSKSSGDLVDLFDGTSQSTGGSADLFGGFADFGSAAASGSFPSQVTATSGNGDFGDWSAFNQAPSGPVASSGEFFGSASQPAVELVSGSQSALGPPPAASNSSDLFDLMGSSQATMTSSQSMNFSMMSTNTVGLGLPMSRSQNTDMVQKSVSKTLPSTWSDPSVNISLDNLLPGMQPSKPQQPSLNTMIQQQNMQQPMNVMTQSFGAVNLSSPSNMLPVRPQTNALIGGPMPMSMPNVMTGTMGMAPLGNTPMMNQSMMGMNMNIGMSAAGMGLTGTMGMGMPNIAMTSGTVQPKQDAFANFANFSK
uniprot
proteins
function
FUNCTION: Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). May have a role in transport via clathrin-coated vesicles from the trans-Golgi network to endosomes. Stimulates clathrin assembly. {ECO:0000269|PubMed:12429846, ECO:0000269|PubMed:12538641}.
uniprot
proteins
mass_dalton
68259
uniprot
proteins
mutagenesis
MUTAGEN 29; /note="R->L: Reduces lipid binding. Abolishes lipid binding; when associated with G-34."; /evidence="ECO:0000269|PubMed:12538641"; MUTAGEN 34; /note="D->G: Abolishes lipid binding; when associated with L-29."; /evidence="ECO:0000269|PubMed:12538641"; MUTAGEN 41; /note="G->S: Normal binding to VTI1B."; /evidence="ECO:0000269|PubMed:18033301"; MUTAGEN 46; /note="E->W: Normal binding to VTI1B."; /evidence="ECO:0000269|PubMed:18033301"; MUTAGEN 52; /note="F->D: Abolished binding to VTI1B."; /evidence="ECO:0000269|PubMed:18033301"; MUTAGEN 53..54; /note="MY->DD: Abolished binding to VTI1B."; /evidence="ECO:0000269|PubMed:18033301"; MUTAGEN 95; /note="E->W: Normal binding to VTI1B."; /evidence="ECO:0000269|PubMed:18033301"; MUTAGEN 96; /note="R->S: Abolished binding to VTI1B."; /evidence="ECO:0000269|PubMed:18033301"; MUTAGEN 146; /note="R->E: Abolished binding to VTI1B. Rescued binding to VTI1BR-23 mutant."; /evidence="ECO:0000269|PubMed:18033301"; MUTAGEN 153; /note="K->D: Normal binding to VTI1B."; /evidence="ECO:0000269|PubMed:18033301"; MUTAGEN 159; /note="Y->S: Normal binding to VTI1B."; /evidence="ECO:0000269|PubMed:18033301"; MUTAGEN 349; /note="D->R: Decreases AP-1 and AP-2 binding."; /evidence="ECO:0000269|PubMed:12538641"; MUTAGEN 371; /note="D->R: Slightly decreases AP-1 binding."; /evidence="ECO:0000269|PubMed:12538641"; MUTAGEN 422; /note="D->R: Strongly decreases clathrin binding."; /evidence="ECO:0000269|PubMed:12538641"; MUTAGEN 423..426; /note="LFDL->AFAA: Strongly reduces clathrin binding."; /evidence="ECO:0000269|PubMed:12429846
uniprot
proteins
protein_family
Epsin family
uniprot
proteins
pubmed
12213833
uniprot
proteins
pubmed
12429846
uniprot
proteins
pubmed
12538641
uniprot
proteins
pubmed
14665628
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15372022
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15793701
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18033301
uniprot
proteins
pubmed
18318008
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19413330
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
8724849
uniprot
proteins
sequence_length
625
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region. Membrane; Peripheral membrane protein. Cytoplasmic vesicle, clathrin-coated vesicle. Note=Found throughout the cell, with the exception of the cell surface. Concentrated in the perinuclear region and associated with clathrin-coated vesicles close to the trans-Golgi network.
uniprot
proteins