OCLN
entrez
100506658
canonical
uniprot
Q16625
canonical
ensembl
ENSG00000197822
resolver
ensp
ENSP00000347379
resolver
ensp
ENSP00000379719
resolver
ensp
ENSP00000445940
resolver
ensp
ENSP00000506305
resolver
ensp
ENSP00000571885
resolver
ensp
ENSP00000571887
resolver
ensp
ENSP00000625826
resolver
genesymbol
OCLN
resolver
hgnc
HGNC:8104
resolver
uniprot
A8K3T2
resolver
uniprot
B5BU70
resolver
uniprot
D2DU64
resolver
uniprot
D2DU65
resolver
uniprot
D2IGC0
resolver
uniprot
D2IGC1
resolver
uniprot
E2CYV9
resolver
uniprot
Q5U1V4
resolver
uniprot
Q8N6K1
resolver
uniprot_entry
A8K3T2_HUMAN
resolver
uniprot_entry
OCLN_HUMAN
resolver
uniprot_sec
B5BU70
resolver
uniprot_sec
D2DU64
resolver
uniprot_sec
D2DU65
resolver
uniprot_sec
D2IGC0
resolver
uniprot_sec
D2IGC1
resolver
uniprot_sec
E2CYV9
resolver
uniprot_sec
Q5U1V4
resolver
uniprot_sec
Q8N6K1
resolver
amino_acid_sequence
MSSRPLESPPPYRPDEFKPNHYAPSNDIYGGEMHVRPMLSQPAYSFYPEDEILHFYKWTSPPGVIRILSMLIIVMCIAIFACVASTLAWDRGYGTSLLGGSVGYPYGGSGFGSYGSGYGYGYGYGYGYGGYTDPRAAKGFMLAMAAFCFIAALVIFVTSVIRSEMSRTRRYYLSVIIVSAILGIMVFIATIVYIMGVNPTAQSSGSLYGSQIYALCNQFYTPAATGLYVDQYLYHYCVVDPQEAIAIVLGFMIIVAFALIIFFAVKTRRKMDRYDKSNILWDKEHIYDEQPPNVEEWVKNVSAGTQDVPSPPSDYVERVDSPMAYSSNGKVNDKRFYPESSYKSTPVPEVVQELPLTSPVDDFRQPRYSSGGNFETPSKRAPAKGRAGRSKRTEQDHYETDYTTGGESCDELEEDWIREYPPITSDQQRQLYKRNFDTGLQEYKSLQSELDEINKELSRLDKELDDYREESEEYMAAADEYNRLKQVKGSADYKSKKNHCKQLKSKLSHIKKMVGDYDRQKT
uniprot
proteins
disease_involvement
DISEASE: Pseudo-TORCH syndrome 1 (PTORCH1) [MIM:251290]: An autosomal recessive neurologic disorder with characteristic clinical and neuroradiologic features that mimic intrauterine TORCH infection in the absence of evidence of infection. Affected individuals have congenital microcephaly, intracranial calcifications, and severe developmental delay. {ECO:0000269|PubMed:20727516}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: May play a role in the formation and regulation of the tight junction (TJ) paracellular permeability barrier. It is able to induce adhesion when expressed in cells lacking tight junctions. {ECO:0000269|PubMed:19114660}.; FUNCTION: (Microbial infection) Acts as a coreceptor for hepatitis C virus (HCV) in hepatocytes. {ECO:0000269|PubMed:19182773, ECO:0000269|PubMed:20375010}.
uniprot
proteins
mass_dalton
59144
uniprot
proteins
mutagenesis
MUTAGEN 398; /note="Y->A: Loss of phosphorylation and loss of regulation of TJP1 binding; when associated with A-402."; /evidence="ECO:0000269|PubMed:19017651"; MUTAGEN 398; /note="Y->D: Loss of phosphorylation, almost complete loss of binding to TJP1, loss of regulation of TJP1 binding and loss of localization to plasma membrane and sites of cell-cell contact; when associated with D-402."; /evidence="ECO:0000269|PubMed:19017651"; MUTAGEN 398; /note="Y->F: Loss of phosphorylation, decrease in binding to TJP1 and significant loss of regulation of TJP1 binding; when associated with F-402."; /evidence="ECO:0000269|PubMed:19017651"; MUTAGEN 402; /note="Y->A: Loss of phosphorylation and loss of regulation of TJP1 binding; when associated with A-398."; /evidence="ECO:0000269|PubMed:19017651"; MUTAGEN 402; /note="Y->D: Loss of phosphorylation, almost complete loss of binding to TJP1, loss of regulation of TJP1 binding and loss of localization to plasma membrane and sites of cell-cell contact; when associated with D-398."; /evidence="ECO:0000269|PubMed:19017651"; MUTAGEN 402; /note="Y->F: Loss of phosphorylation, decrease in binding to TJP1 and significant loss of regulation of TJP1 binding; when associated with F-398."; /evidence="ECO:0000269|PubMed:19017651"; MUTAGEN 404; /note="T->A: Loss of localization to the tight junctions."; /evidence="ECO:0000269|PubMed:19114660
uniprot
proteins
post_translational_modification
PTM: Dephosphorylated by PTPRJ. The tyrosine phosphorylation on Tyr-398 and Tyr-402 reduces its ability to interact with TJP1. Phosphorylation at Ser-490 also attenuates the interaction with TJP1. {ECO:0000269|PubMed:19017651, ECO:0000269|PubMed:19114660, ECO:0000269|PubMed:19125584, ECO:0000269|PubMed:19332538}.; PTM: (Microbial infection) Cleaved by S.pyogenes SpeB protease; leading to its degradation (PubMed:23532847). Degradation by SpeB promotes bacterial translocation across the host epithelial barrier (PubMed:23532847). {ECO:0000269|PubMed:23532847}.
uniprot
proteins
protein_family
ELL/occludin family
uniprot
proteins
pubmed
10523508
uniprot
proteins
pubmed
12118072
uniprot
proteins
pubmed
15372022
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17525332
uniprot
proteins
pubmed
18318008
uniprot
proteins
pubmed
19017651
uniprot
proteins
pubmed
19054851
uniprot
proteins
pubmed
19114660
uniprot
proteins
pubmed
19125584
uniprot
proteins
pubmed
19182773
uniprot
proteins
pubmed
19332538
uniprot
proteins
pubmed
20375010
uniprot
proteins
pubmed
20463075
uniprot
proteins
pubmed
20727516
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21806988
uniprot
proteins
pubmed
23239027
uniprot
proteins
pubmed
23532847
uniprot
proteins
pubmed
23923978
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
30734065
uniprot
proteins
pubmed
8601611
uniprot
proteins
pubmed
9175707
uniprot
proteins
sequence_length
522
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19017651, ECO:0000269|PubMed:19114660, ECO:0000269|PubMed:9175707}; Multi-pass membrane protein {ECO:0000255}. Cell junction, tight junction {ECO:0000269|PubMed:10523508, ECO:0000269|PubMed:19017651, ECO:0000269|PubMed:19114660, ECO:0000269|PubMed:19332538, ECO:0000269|PubMed:23239027, ECO:0000269|PubMed:30734065, ECO:0000269|PubMed:9175707}.
uniprot
proteins
transmembrane_region
TRANSMEM 67..89; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 136..160; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 171..195; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 244..265; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins