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Q16625

- OCLN_HUMAN

UniProt

Q16625 - OCLN_HUMAN

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Protein

Occludin

Gene

OCLN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  1. protein domain specific binding Source: UniProt
  2. structural molecule activity Source: InterPro
  3. thiopurine S-methyltransferase activity Source: Ensembl

GO - Biological processi

  1. apoptotic process Source: Reactome
  2. cell-cell junction organization Source: MGI
  3. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
  4. protein complex assembly Source: ProtInc
  5. S-adenosylhomocysteine metabolic process Source: Ensembl
  6. S-adenosylmethionine metabolic process Source: Ensembl
  7. tight junction assembly Source: UniProt
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_13579. Apoptotic cleavage of cell adhesion proteins.

Protein family/group databases

TCDBi9.B.41.1.1. the occludin (occludin) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Occludin
Gene namesi
Name:OCLN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:8104. OCLN.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 6666CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei67 – 8923HelicalSequence AnalysisAdd
BLAST
Topological domaini90 – 13546Extracellular1 PublicationAdd
BLAST
Transmembranei136 – 16025HelicalSequence AnalysisAdd
BLAST
Topological domaini161 – 17010CytoplasmicSequence Analysis
Transmembranei171 – 19525HelicalSequence AnalysisAdd
BLAST
Topological domaini196 – 24348ExtracellularSequence AnalysisAdd
BLAST
Transmembranei244 – 26522HelicalSequence AnalysisAdd
BLAST
Topological domaini266 – 522257CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. apical plasma membrane Source: Ensembl
  2. apicolateral plasma membrane Source: Ensembl
  3. cell-cell junction Source: UniProtKB
  4. cell junction Source: HPA
  5. cytoplasmic vesicle Source: UniProt
  6. cytosol Source: Ensembl
  7. endocytic vesicle Source: Ensembl
  8. integral component of membrane Source: UniProtKB-KW
  9. plasma membrane Source: HPA
  10. tight junction Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Membrane, Tight junction

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti219 – 2191F → S in BLCPMG. 1 Publication
VAR_064910

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi398 – 3981Y → A: Loss of phosphorylation and loss of regulation of TJP1 binding; when associated with A-402. 1 Publication
Mutagenesisi398 – 3981Y → 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. 1 Publication
Mutagenesisi398 – 3981Y → F: Loss of phosphorylation, decrease in binding to TJP1 and significant loss of regulation of TJP1 binding; when associated with F-402. 1 Publication
Mutagenesisi402 – 4021Y → A: Loss of phosphorylation and loss of regulation of TJP1 binding; when associated with A-398. 1 Publication
Mutagenesisi402 – 4021Y → 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. 1 Publication
Mutagenesisi402 – 4021Y → F: Loss of phosphorylation, decrease in binding to TJP1 and significant loss of regulation of TJP1 binding; when associated with F-398. 1 Publication
Mutagenesisi404 – 4041T → A: Loss of localization to the tight junctions. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi251290. phenotype.
Orphaneti1229. Congenital intrauterine infection-like syndrome.
PharmGKBiPA31893.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 522522OccludinPRO_0000146739Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei321 – 3211Phosphoserine1 Publication
Modified residuei340 – 3401PhosphoserineBy similarity
Modified residuei369 – 3691Phosphoserine1 Publication
Modified residuei370 – 3701Phosphoserine1 Publication
Modified residuei398 – 3981Phosphotyrosine1 Publication
Modified residuei402 – 4021Phosphotyrosine1 Publication
Modified residuei403 – 4031Phosphothreonine; by PKC/PRKCH1 Publication
Modified residuei404 – 4041Phosphothreonine; by PKC/PRKCH1 Publication
Modified residuei408 – 4081Phosphoserine1 Publication
Modified residuei490 – 4901Phosphoserine1 Publication

Post-translational modificationi

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 TJP1.6 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ16625.
PaxDbiQ16625.
PRIDEiQ16625.

PTM databases

PhosphoSiteiQ16625.

Miscellaneous databases

PMAP-CutDBQ16625.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ16625.
CleanExiHS_OCLN.
GenevestigatoriQ16625.

Organism-specific databases

HPAiCAB013075.
HPA005933.

Interactioni

Subunit structurei

Interacts with TJP1/ZO1 and with VAPA.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CSNK1EP496747EBI-2903088,EBI-749343
PLSCR1O151622EBI-2903088,EBI-740019

Protein-protein interaction databases

BioGridi111004. 25 interactions.
DIPiDIP-42791N.
IntActiQ16625. 6 interactions.
MINTiMINT-5006137.
STRINGi9606.ENSP00000347379.

Structurei

Secondary structure

1
522
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni417 – 4193Combined sources
Helixi426 – 46641Combined sources
Helixi472 – 48817Combined sources
Helixi491 – 52030Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WPAX-ray1.50A413-522[»]
1XAWX-ray1.45A383-522[»]
3G7CX-ray2.00A416-522[»]
ProteinModelPortaliQ16625.
SMRiQ16625. Positions 416-522.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16625.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini60 – 269210MARVELPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili426 – 48964Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi92 – 13140Gly/Tyr-richAdd
BLAST

Domaini

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.By similarity1 Publication

Sequence similaritiesi

Belongs to the ELL/occludin family.Curated
Contains 1 MARVEL domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG71745.
GeneTreeiENSGT00730000110989.
HOGENOMiHOG000233490.
HOVERGENiHBG004523.
InParanoidiQ16625.
KOiK06088.
OMAiYAPSNDV.
OrthoDBiEOG7PS1F4.
PhylomeDBiQ16625.
TreeFamiTF326161.

Family and domain databases

InterProiIPR008253. Marvel.
IPR016196. MFS_dom_general_subst_transpt.
IPR002958. Occludin.
IPR010844. Occludin_RNApol2_elong_fac_ELL.
[Graphical view]
PANTHERiPTHR23288:SF4. PTHR23288:SF4. 1 hit.
PfamiPF01284. MARVEL. 1 hit.
PF07303. Occludin_ELL. 1 hit.
[Graphical view]
PIRSFiPIRSF005993. Occludin. 1 hit.
PRINTSiPR01258. OCCLUDIN.
SUPFAMiSSF103473. SSF103473. 1 hit.
PROSITEiPS51225. MARVEL. 1 hit.
[Graphical view]

Sequences (7)i

Sequence statusi: Complete.

This entry describes 7 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q16625-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MSSRPLESPP PYRPDEFKPN HYAPSNDIYG GEMHVRPMLS QPAYSFYPED
60 70 80 90 100
EILHFYKWTS PPGVIRILSM LIIVMCIAIF ACVASTLAWD RGYGTSLLGG
110 120 130 140 150
SVGYPYGGSG FGSYGSGYGY GYGYGYGYGG YTDPRAAKGF MLAMAAFCFI
160 170 180 190 200
AALVIFVTSV IRSEMSRTRR YYLSVIIVSA ILGIMVFIAT IVYIMGVNPT
210 220 230 240 250
AQSSGSLYGS QIYALCNQFY TPAATGLYVD QYLYHYCVVD PQEAIAIVLG
260 270 280 290 300
FMIIVAFALI IFFAVKTRRK MDRYDKSNIL WDKEHIYDEQ PPNVEEWVKN
310 320 330 340 350
VSAGTQDVPS PPSDYVERVD SPMAYSSNGK VNDKRFYPES SYKSTPVPEV
360 370 380 390 400
VQELPLTSPV DDFRQPRYSS GGNFETPSKR APAKGRAGRS KRTEQDHYET
410 420 430 440 450
DYTTGGESCD ELEEDWIREY PPITSDQQRQ LYKRNFDTGL QEYKSLQSEL
460 470 480 490 500
DEINKELSRL DKELDDYREE SEEYMAAADE YNRLKQVKGS ADYKSKKNHC
510 520
KQLKSKLSHI KKMVGDYDRQ KT
Length:522
Mass (Da):59,144
Last modified:November 1, 1996 - v1
Checksum:iA0CF9574BCF6E974
GO
Isoform 2 (identifier: Q16625-2) [UniParc]FASTAAdd to Basket

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

The sequence of this isoform differs from the canonical sequence as follows:
     244-297: Missing.

Show »
Length:468
Mass (Da):52,706
Checksum:i570C03F39D5B9F09
GO
Isoform 3 (identifier: Q16625-3) [UniParc]FASTAAdd to Basket

Also known as: OCLN-ex7ext

The sequence of this isoform differs from the canonical sequence as follows:
     476-522: AAADEYNRLKQVKGSADYKSKKNHCKQLKSKLSHIKKMVGDYDRQKT → VNST

Show »
Length:479
Mass (Da):54,124
Checksum:iBAC5CDCFD4AB3FE9
GO
Isoform 4 (identifier: Q16625-4) [UniParc]FASTAAdd to Basket

Also known as: OCLN-ex3del, OCLN-ex3pdel

The sequence of this isoform differs from the canonical sequence as follows:
     1-251: Missing.

Show »
Length:271
Mass (Da):31,602
Checksum:i17110B0747658560
GO
Isoform 5 (identifier: Q16625-5) [UniParc]FASTAAdd to Basket

Also known as: OCLN-ex3-4del

The sequence of this isoform differs from the canonical sequence as follows:
     1-251: Missing.
     252-322: Missing.

Show »
Length:200
Mass (Da):23,324
Checksum:iCA521768CF62815F
GO
Isoform 6 (identifier: Q16625-6) [UniParc]FASTAAdd to Basket

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.

Show »
Length:69
Mass (Da):8,033
Checksum:i44E322DFFA119B8E
GO
Isoform 7 (identifier: Q16625-7) [UniParc]FASTAAdd to Basket

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.

Show »
Length:70
Mass (Da):8,175
Checksum:iFF4DA5B4703A5BAD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti233 – 2331L → S in AAH29886. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti219 – 2191F → S in BLCPMG. 1 Publication
VAR_064910

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 251251Missing in isoform 4 and isoform 5. 1 PublicationVSP_043872Add
BLAST
Alternative sequencei50 – 6920DEILH…IRILS → ESLQAVKEQIVTHQEDGWRL in isoform 6. 1 PublicationVSP_043873Add
BLAST
Alternative sequencei52 – 7019ILHFY…RILSM → MTIEKKVKSTWLLLMNTID in isoform 7. 1 PublicationVSP_043874Add
BLAST
Alternative sequencei70 – 701Missing in isoform 6. 1 PublicationVSP_043875
Alternative sequencei71 – 522452Missing in isoform 6 and isoform 7. 1 PublicationVSP_043876Add
BLAST
Alternative sequencei244 – 29754Missing in isoform 2. CuratedVSP_043877Add
BLAST
Alternative sequencei252 – 32271Missing in isoform 5. 1 PublicationVSP_043878Add
BLAST
Alternative sequencei476 – 52247AAADE…DRQKT → VNST in isoform 3. 1 PublicationVSP_043879Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49184 mRNA. Translation: AAC50451.1.
U53823 mRNA. Translation: AAB00195.1.
FJ786083 mRNA. Translation: ACT53743.1.
FJ786084 mRNA. Translation: ACT53744.1.
AF400630
, 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.
CCDSiCCDS4006.1. [Q16625-1]
CCDS54864.1. [Q16625-4]
PIRiG02533.
RefSeqiNP_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]
UniGeneiHs.592605.

Genome annotation databases

EnsembliENST00000355237; ENSP00000347379; ENSG00000197822. [Q16625-1]
ENST00000396442; ENSP00000379719; ENSG00000197822. [Q16625-1]
ENST00000538151; ENSP00000445940; ENSG00000197822. [Q16625-4]
GeneIDi100506658.
KEGGihsa:100506658.
UCSCiuc003jwu.3. human. [Q16625-1]
uc021xzt.1. human. [Q16625-5]

Polymorphism databases

DMDMi3914196.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Wikipedia

Occludin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49184 mRNA. Translation: AAC50451.1 .
U53823 mRNA. Translation: AAB00195.1 .
FJ786083 mRNA. Translation: ACT53743.1 .
FJ786084 mRNA. Translation: ACT53744.1 .
AF400630
, 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 .
CCDSi CCDS4006.1. [Q16625-1 ]
CCDS54864.1. [Q16625-4 ]
PIRi G02533.
RefSeqi NP_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 ]
UniGenei Hs.592605.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1WPA X-ray 1.50 A 413-522 [» ]
1XAW X-ray 1.45 A 383-522 [» ]
3G7C X-ray 2.00 A 416-522 [» ]
ProteinModelPortali Q16625.
SMRi Q16625. Positions 416-522.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111004. 25 interactions.
DIPi DIP-42791N.
IntActi Q16625. 6 interactions.
MINTi MINT-5006137.
STRINGi 9606.ENSP00000347379.

Protein family/group databases

TCDBi 9.B.41.1.1. the occludin (occludin) family.

PTM databases

PhosphoSitei Q16625.

Polymorphism databases

DMDMi 3914196.

Proteomic databases

MaxQBi Q16625.
PaxDbi Q16625.
PRIDEi Q16625.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000355237 ; ENSP00000347379 ; ENSG00000197822 . [Q16625-1 ]
ENST00000396442 ; ENSP00000379719 ; ENSG00000197822 . [Q16625-1 ]
ENST00000538151 ; ENSP00000445940 ; ENSG00000197822 . [Q16625-4 ]
GeneIDi 100506658.
KEGGi hsa:100506658.
UCSCi uc003jwu.3. human. [Q16625-1 ]
uc021xzt.1. human. [Q16625-5 ]

Organism-specific databases

CTDi 100506658.
GeneCardsi GC05P068788.
HGNCi HGNC:8104. OCLN.
HPAi CAB013075.
HPA005933.
MIMi 251290. phenotype.
602876. gene.
neXtProti NX_Q16625.
Orphaneti 1229. Congenital intrauterine infection-like syndrome.
PharmGKBi PA31893.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG71745.
GeneTreei ENSGT00730000110989.
HOGENOMi HOG000233490.
HOVERGENi HBG004523.
InParanoidi Q16625.
KOi K06088.
OMAi YAPSNDV.
OrthoDBi EOG7PS1F4.
PhylomeDBi Q16625.
TreeFami TF326161.

Enzyme and pathway databases

Reactomei REACT_13579. Apoptotic cleavage of cell adhesion proteins.

Miscellaneous databases

EvolutionaryTracei Q16625.
GeneWikii Occludin.
GenomeRNAii 100506658.
NextBioi 34054345.
PMAP-CutDB Q16625.
PROi Q16625.
SOURCEi Search...

Gene expression databases

Bgeei Q16625.
CleanExi HS_OCLN.
Genevestigatori Q16625.

Family and domain databases

InterProi IPR008253. Marvel.
IPR016196. MFS_dom_general_subst_transpt.
IPR002958. Occludin.
IPR010844. Occludin_RNApol2_elong_fac_ELL.
[Graphical view ]
PANTHERi PTHR23288:SF4. PTHR23288:SF4. 1 hit.
Pfami PF01284. MARVEL. 1 hit.
PF07303. Occludin_ELL. 1 hit.
[Graphical view ]
PIRSFi PIRSF005993. Occludin. 1 hit.
PRINTSi PR01258. OCCLUDIN.
SUPFAMi SSF103473. SSF103473. 1 hit.
PROSITEi PS51225. MARVEL. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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.

Entry informationi

Entry nameiOCLN_HUMAN
AccessioniPrimary (citable) accession number: Q16625
Secondary accession number(s): B5BU70
, D2DU64, D2DU65, D2IGC0, D2IGC1, E2CYV9, Q5U1V4, Q8N6K1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: November 26, 2014
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3