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Q16625 (OCLN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Occludin
Gene names
Name:OCLN
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length522 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.13

Subunit structure

Interacts with TJP1/ZO1 and with VAPA. Ref.11

Subcellular location

Membrane; Multi-pass membrane protein. Cell junctiontight junction Ref.11 Ref.12 Ref.13.

Tissue specificity

Localized at tight junctions of both epithelial and endothelial cells. Highly expressed in kidney. Not detected in testis.

Domain

The C-terminal is cytoplasmic and is important for interaction with ZO-1. Sufficient for the tight junction localization. Involved in the regulation of the permeability barrier function of the tight junction By similarity. The first extracellular loop participates in an adhesive interaction. Ref.2

Post-translational modification

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. Ref.11 Ref.12 Ref.13 Ref.15

Involvement in disease

Band-like calcification with simplified gyration and polymicrogyria (BLCPMG) [MIM:251290]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16

Sequence similarities

Belongs to the ELL/occludin family.

Contains 1 MARVEL domain.

Ontologies

Keywords
   Cellular componentCell junction
Membrane
Tight junction
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
   DomainCoiled coil
Transmembrane
Transmembrane helix
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processS-adenosylhomocysteine metabolic process

Inferred from electronic annotation. Source: Ensembl

S-adenosylmethionine metabolic process

Inferred from electronic annotation. Source: Ensembl

apoptotic process

Traceable author statement. Source: Reactome

cell-cell junction organization

Inferred from mutant phenotype PubMed 20164257. Source: MGI

cellular component disassembly involved in execution phase of apoptosis

Traceable author statement. Source: Reactome

protein complex assembly

Traceable author statement PubMed 10749869. Source: ProtInc

tight junction assembly

Inferred from mutant phenotype PubMed 20164257. Source: UniProt

   Cellular_componentapical plasma membrane

Inferred from electronic annotation. Source: Ensembl

apicolateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

cell junction

Inferred from direct assay. Source: HPA

cell-cell junction

Inferred from direct assay Ref.12. Source: UniProtKB

cytoplasmic vesicle

Inferred from direct assay PubMed 20164257. Source: UniProt

cytosol

Inferred from electronic annotation. Source: Ensembl

endocytic vesicle

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from direct assay. Source: HPA

tight junction

Inferred from direct assay PubMed 20028514. Source: BHF-UCL

   Molecular_functionprotein binding

Inferred from physical interaction Ref.12. Source: UniProtKB

protein domain specific binding

Inferred from physical interaction PubMed 20164257. Source: UniProt

structural molecule activity

Inferred from electronic annotation. Source: InterPro

thiopurine S-methyltransferase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CSNK1EP496746EBI-2903088,EBI-749343
PLSCR1O151622EBI-2903088,EBI-740019

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q16625-1)

Also known as: WT-OCLN; TM4(+);

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q16625-2)

Also known as: OCLN-ex4del; TM4(-);

The sequence of this isoform differs from the canonical sequence as follows:
     244-297: Missing.
Isoform 3 (identifier: Q16625-3)

Also known as: OCLN-ex7ext;

The sequence of this isoform differs from the canonical sequence as follows:
     476-522: AAADEYNRLKQVKGSADYKSKKNHCKQLKSKLSHIKKMVGDYDRQKT → VNST
Isoform 4 (identifier: Q16625-4)

Also known as: OCLN-ex3del; OCLN-ex3pdel;

The sequence of this isoform differs from the canonical sequence as follows:
     1-251: Missing.
Isoform 5 (identifier: Q16625-5)

Also known as: OCLN-ex3-4del;

The sequence of this isoform differs from the canonical sequence as follows:
     1-251: Missing.
     252-322: Missing.
Isoform 6 (identifier: Q16625-6)

Also known as: OCLN-ex3p-9pdel;

The sequence of this isoform differs from the canonical sequence as follows:
     50-69: DEILHFYKWTSPPGVIRILS → ESLQAVKEQIVTHQEDGWRL
     70-70: Missing.
     71-522: Missing.
Isoform 7 (identifier: Q16625-7)

Also known as: OCLN-ex3p-7pdel;

The sequence of this isoform differs from the canonical sequence as follows:
     52-70: ILHFYKWTSPPGVIRILSM → MTIEKKVKSTWLLLMNTID
     71-522: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 522522Occludin
PRO_0000146739

Regions

Topological domain1 – 6666Cytoplasmic Potential
Transmembrane67 – 8923Helical; Potential
Topological domain90 – 13546Extracellular Ref.2
Transmembrane136 – 16025Helical; Potential
Topological domain161 – 17010Cytoplasmic Potential
Transmembrane171 – 19525Helical; Potential
Topological domain196 – 24348Extracellular Potential
Transmembrane244 – 26522Helical; Potential
Topological domain266 – 522257Cytoplasmic Potential
Domain60 – 269210MARVEL
Coiled coil426 – 48964 Potential
Compositional bias92 – 13140Gly/Tyr-rich

Amino acid modifications

Modified residue3211Phosphoserine Ref.14
Modified residue3401Phosphoserine By similarity
Modified residue3691Phosphoserine Ref.14
Modified residue3701Phosphoserine Ref.14
Modified residue3981Phosphotyrosine Ref.11
Modified residue4021Phosphotyrosine Ref.11
Modified residue4031Phosphothreonine; by PKC/PRKCH Ref.13
Modified residue4041Phosphothreonine; by PKC/PRKCH Ref.13
Modified residue4081Phosphoserine Ref.10
Modified residue4901Phosphoserine Ref.15

Natural variations

Alternative sequence1 – 251251Missing in isoform 4 and isoform 5.
VSP_043872
Alternative sequence50 – 6920DEILH…IRILS → ESLQAVKEQIVTHQEDGWRL in isoform 6.
VSP_043873
Alternative sequence52 – 7019ILHFY…RILSM → MTIEKKVKSTWLLLMNTID in isoform 7.
VSP_043874
Alternative sequence701Missing in isoform 6.
VSP_043875
Alternative sequence71 – 522452Missing in isoform 6 and isoform 7.
VSP_043876
Alternative sequence244 – 29754Missing in isoform 2.
VSP_043877
Alternative sequence252 – 32271Missing in isoform 5.
VSP_043878
Alternative sequence476 – 52247AAADE…DRQKT → VNST in isoform 3.
VSP_043879
Natural variant2191F → S in BLCPMG. Ref.16
VAR_064910

Experimental info

Mutagenesis3981Y → A: Loss of phosphorylation and loss of regulation of TJP1 binding; when associated with A-402. Ref.11
Mutagenesis3981Y → 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. Ref.11
Mutagenesis3981Y → F: Loss of phosphorylation, decrease in binding to TJP1 and significant loss of regulation of TJP1 binding; when associated with F-402. Ref.11
Mutagenesis4021Y → A: Loss of phosphorylation and loss of regulation of TJP1 binding; when associated with A-398. Ref.11
Mutagenesis4021Y → 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. Ref.11
Mutagenesis4021Y → F: Loss of phosphorylation, decrease in binding to TJP1 and significant loss of regulation of TJP1 binding; when associated with F-398. Ref.11
Mutagenesis4041T → A: Loss of localization to the tight junctions. Ref.13
Sequence conflict2331L → S in AAH29886. Ref.7

Secondary structure

......... 522
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (WT-OCLN) (TM4(+)) [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: A0CF9574BCF6E974

FASTA52259,144
        10         20         30         40         50         60 
MSSRPLESPP PYRPDEFKPN HYAPSNDIYG GEMHVRPMLS QPAYSFYPED EILHFYKWTS 

        70         80         90        100        110        120 
PPGVIRILSM LIIVMCIAIF ACVASTLAWD RGYGTSLLGG SVGYPYGGSG FGSYGSGYGY 

       130        140        150        160        170        180 
GYGYGYGYGG YTDPRAAKGF MLAMAAFCFI AALVIFVTSV IRSEMSRTRR YYLSVIIVSA 

       190        200        210        220        230        240 
ILGIMVFIAT IVYIMGVNPT AQSSGSLYGS QIYALCNQFY TPAATGLYVD QYLYHYCVVD 

       250        260        270        280        290        300 
PQEAIAIVLG FMIIVAFALI IFFAVKTRRK MDRYDKSNIL WDKEHIYDEQ PPNVEEWVKN 

       310        320        330        340        350        360 
VSAGTQDVPS PPSDYVERVD SPMAYSSNGK VNDKRFYPES SYKSTPVPEV VQELPLTSPV 

       370        380        390        400        410        420 
DDFRQPRYSS GGNFETPSKR APAKGRAGRS KRTEQDHYET DYTTGGESCD ELEEDWIREY 

       430        440        450        460        470        480 
PPITSDQQRQ LYKRNFDTGL QEYKSLQSEL DEINKELSRL DKELDDYREE SEEYMAAADE 

       490        500        510        520 
YNRLKQVKGS ADYKSKKNHC KQLKSKLSHI KKMVGDYDRQ KT 

« Hide

Isoform 2 (OCLN-ex4del) (TM4(-)) [UniParc].

Checksum: 570C03F39D5B9F09
Show »

FASTA46852,706
Isoform 3 (OCLN-ex7ext) [UniParc].

Checksum: BAC5CDCFD4AB3FE9
Show »

FASTA47954,124
Isoform 4 (OCLN-ex3del) (OCLN-ex3pdel) [UniParc].

Checksum: 17110B0747658560
Show »

FASTA27131,602
Isoform 5 (OCLN-ex3-4del) [UniParc].

Checksum: CA521768CF62815F
Show »

FASTA20023,324
Isoform 6 (OCLN-ex3p-9pdel) [UniParc].

Checksum: 44E322DFFA119B8E
Show »

FASTA698,033
Isoform 7 (OCLN-ex3p-7pdel) [UniParc].

Checksum: FF4DA5B4703A5BAD
Show »

FASTA708,175

References

« Hide 'large scale' references
[1]"Interspecies diversity of the occludin sequence: cDNA cloning of human, mouse, dog, and rat-kangaroo homologues."
Ando-Akatsuka Y., Saitou M., Hirase T., Kishi M., Sakakibara A., Itoh M., Yonemura S., Furuse M., Tsukita S.
J. Cell Biol. 133:43-47(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Colon carcinoma.
[2]"Occludin confers adhesiveness when expressed in fibroblasts."
Van Itallie C.M., Anderson J.M.
J. Cell Sci. 110:1113-1121(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DOMAIN, TOPOLOGY.
Tissue: Liver.
[3]"Splicing diversity of the human OCLN gene and its biological significance for hepatitis C virus entry."
Kohaar I., Ploss A., Korol E., Mu K., Schoggins J.W., O'Brien T.R., Rice C.M., Prokunina-Olsson L.
J. Virol. 84:6987-6994(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4; 5; 6 AND 7), ALTERNATIVE SPLICING.
Tissue: Liver.
[4]"Genomic structure of occludin gene."
Fukasawa M., Toyota T., Yoshitsugu K., Yoshikawa T.
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B. expand/collapse author list , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain and Lung.
[8]"Occludin TM4(-): an isoform of the tight junction protein present in primates lacking the fourth transmembrane domain."
Ghassemifar M.R., Sheth B., Papenbrock T., Leese H.J., Houghton F.D., Fleming T.P.
J. Cell Sci. 115:3171-3180(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORM 2).
[9]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[10]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[11]"Phosphorylation of Tyr-398 and Tyr-402 in occludin prevents its interaction with ZO-1 and destabilizes its assembly at the tight junctions."
Elias B.C., Suzuki T., Seth A., Giorgianni F., Kale G., Shen L., Turner J.R., Naren A., Desiderio D.M., Rao R.
J. Biol. Chem. 284:1559-1569(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TJP1, PHOSPHORYLATION AT TYR-398 AND TYR-402, MUTAGENESIS OF TYR-398 AND TYR-402, SUBCELLULAR LOCATION.
[12]"Density-enhanced phosphatase 1 regulates phosphorylation of tight junction proteins and enhances barrier function of epithelial cells."
Sallee J.L., Burridge K.
J. Biol. Chem. 284:14997-15006(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, DEPHOSPHORYLATION BY PTPRJ, SUBCELLULAR LOCATION.
[13]"PKC eta regulates occludin phosphorylation and epithelial tight junction integrity."
Suzuki T., Elias B.C., Seth A., Shen L., Turner J.R., Giorgianni F., Desiderio D., Guntaka R., Rao R.
Proc. Natl. Acad. Sci. U.S.A. 106:61-66(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-403 AND THR-404, MUTAGENESIS OF THR-404.
[14]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321; SER-369 AND SER-370, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Identification and analysis of occludin phosphosites: a combined mass spectrometry and bioinformatics approach."
Sundstrom J.M., Tash B.R., Murakami T., Flanagan J.M., Bewley M.C., Stanley B.A., Gonsar K.B., Antonetti D.A.
J. Proteome Res. 8:808-817(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 416-522, PHOSPHORYLATION AT SER-490.
[16]"Recessive mutations in the gene encoding the tight junction protein occludin cause band-like calcification with simplified gyration and polymicrogyria."
O'Driscoll M.C., Daly S.B., Urquhart J.E., Black G.C., Pilz D.T., Brockmann K., McEntagart M., Abdel-Salam G., Zaki M., Wolf N.I., Ladda R.L., Sell S., D'Arrigo S., Squier W., Dobyns W.B., Livingston J.H., Crow Y.J.
Am. J. Hum. Genet. 87:354-364(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BLCPMG SER-219.
+Additional computationally mapped references.

Web resources

Wikipedia

Occludin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U49184 mRNA. Translation: AAC50451.1.
U53823 mRNA. Translation: AAB00195.1.
FJ786083 mRNA. Translation: ACT53743.1.
FJ786084 mRNA. Translation: ACT53744.1.
AF400630 expand/collapse EMBL AC list , AF400623, AF400624, AF400625, AF400626, AF400627, AF400628, AF400629 Genomic DNA. Translation: AAL47094.1.
GQ225096 mRNA. Translation: ACT83431.1.
GQ225097 mRNA. Translation: ACT83432.1.
GQ225098 mRNA. Translation: ACT83433.1.
GQ402517 mRNA. Translation: ACZ80515.1.
AB451306 mRNA. Translation: BAG70120.1.
AB451437 mRNA. Translation: BAG70251.1.
AC145146 Genomic DNA. No translation available.
AC147575 Genomic DNA. No translation available.
BC029886 mRNA. Translation: AAH29886.1.
BK001650 mRNA. Translation: DAA01837.1.
CCDSCCDS4006.1. [Q16625-1]
CCDS54864.1. [Q16625-4]
PIRG02533.
RefSeqNP_001192183.1. NM_001205254.1. [Q16625-1]
NP_001192184.1. NM_001205255.1. [Q16625-4]
NP_002529.1. NM_002538.3. [Q16625-1]
XP_006714575.1. XM_006714512.1. [Q16625-2]
UniGeneHs.592605.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WPAX-ray1.50A413-522[»]
1XAWX-ray1.45A383-522[»]
3G7CX-ray2.00A416-522[»]
ProteinModelPortalQ16625.
SMRQ16625. Positions 416-522.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111004. 17 interactions.
DIPDIP-42791N.
IntActQ16625. 6 interactions.
MINTMINT-5006137.
STRING9606.ENSP00000347379.

Protein family/group databases

TCDB9.B.41.1.1. the occludin (occludin) family.

PTM databases

PhosphoSiteQ16625.

Polymorphism databases

DMDM3914196.

Proteomic databases

MaxQBQ16625.
PaxDbQ16625.
PRIDEQ16625.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000355237; ENSP00000347379; ENSG00000197822. [Q16625-1]
ENST00000380766; ENSP00000370143; ENSG00000197822. [Q16625-2]
ENST00000396442; ENSP00000379719; ENSG00000197822. [Q16625-1]
ENST00000538151; ENSP00000445940; ENSG00000197822. [Q16625-4]
ENST00000542132; ENSP00000440000; ENSG00000197822. [Q16625-5]
GeneID100506658.
KEGGhsa:100506658.
UCSCuc003jwu.3. human. [Q16625-1]
uc021xzt.1. human. [Q16625-5]

Organism-specific databases

CTD100506658.
GeneCardsGC05P068788.
HGNCHGNC:8104. OCLN.
HPACAB013075.
HPA005933.
MIM251290. phenotype.
602876. gene.
neXtProtNX_Q16625.
Orphanet1229. Congenital intrauterine infection-like syndrome.
PharmGKBPA31893.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG71745.
HOGENOMHOG000233490.
HOVERGENHBG004523.
InParanoidQ16625.
KOK06088.
OMAYAPSNDV.
OrthoDBEOG7PS1F4.
PhylomeDBQ16625.
TreeFamTF326161.

Enzyme and pathway databases

ReactomeREACT_578. Apoptosis.

Gene expression databases

BgeeQ16625.
CleanExHS_OCLN.
GenevestigatorQ16625.

Family and domain databases

InterProIPR008253. Marvel.
IPR016196. MFS_dom_general_subst_transpt.
IPR002958. Occludin.
IPR010844. Occludin_RNApol2_elong_fac_ELL.
[Graphical view]
PANTHERPTHR23288:SF4. PTHR23288:SF4. 1 hit.
PfamPF01284. MARVEL. 1 hit.
PF07303. Occludin_ELL. 1 hit.
[Graphical view]
PIRSFPIRSF005993. Occludin. 1 hit.
PRINTSPR01258. OCCLUDIN.
SUPFAMSSF103473. SSF103473. 1 hit.
PROSITEPS51225. MARVEL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ16625.
GeneWikiOccludin.
GenomeRNAi100506658.
NextBio34054345.
PMAP-CutDBQ16625.
PROQ16625.
SOURCESearch...

Entry information

Entry nameOCLN_HUMAN
AccessionPrimary (citable) accession number: Q16625
Secondary accession number(s): B5BU70 expand/collapse secondary AC list , D2DU64, D2DU65, D2IGC0, D2IGC1, E2CYV9, Q5U1V4, Q8N6K1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM