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Q16625

- OCLN_HUMAN

UniProt

Q16625 - OCLN_HUMAN

Protein

Occludin

Gene

OCLN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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 binding Source: UniProtKB
    2. protein domain specific binding Source: UniProt
    3. structural molecule activity Source: InterPro
    4. 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

    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

    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

    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 – 3211Phosphoserine2 Publications
    Modified residuei340 – 3401PhosphoserineBy similarity
    Modified residuei369 – 3691Phosphoserine2 Publications
    Modified residuei370 – 3701Phosphoserine2 Publications
    Modified residuei398 – 3981Phosphotyrosine2 Publications
    Modified residuei402 – 4021Phosphotyrosine2 Publications
    Modified residuei403 – 4031Phosphothreonine; by PKC/PRKCH2 Publications
    Modified residuei404 – 4041Phosphothreonine; by PKC/PRKCH2 Publications
    Modified residuei408 – 4081Phosphoserine2 Publications
    Modified residuei490 – 4901Phosphoserine2 Publications

    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. 17 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 – 4193
    Helixi426 – 46641
    Helixi472 – 48817
    Helixi491 – 52030

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 6666CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini90 – 13546Extracellular1 PublicationAdd
    BLAST
    Topological domaini161 – 17010CytoplasmicSequence Analysis
    Topological domaini196 – 24348ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini266 – 522257CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei67 – 8923HelicalSequence AnalysisAdd
    BLAST
    Transmembranei136 – 16025HelicalSequence AnalysisAdd
    BLAST
    Transmembranei171 – 19525HelicalSequence AnalysisAdd
    BLAST
    Transmembranei244 – 26522HelicalSequence AnalysisAdd
    BLAST

    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.
    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

    MSSRPLESPP PYRPDEFKPN HYAPSNDIYG GEMHVRPMLS QPAYSFYPED    50
    EILHFYKWTS PPGVIRILSM LIIVMCIAIF ACVASTLAWD RGYGTSLLGG 100
    SVGYPYGGSG FGSYGSGYGY GYGYGYGYGG YTDPRAAKGF MLAMAAFCFI 150
    AALVIFVTSV IRSEMSRTRR YYLSVIIVSA ILGIMVFIAT IVYIMGVNPT 200
    AQSSGSLYGS QIYALCNQFY TPAATGLYVD QYLYHYCVVD PQEAIAIVLG 250
    FMIIVAFALI IFFAVKTRRK MDRYDKSNIL WDKEHIYDEQ PPNVEEWVKN 300
    VSAGTQDVPS PPSDYVERVD SPMAYSSNGK VNDKRFYPES SYKSTPVPEV 350
    VQELPLTSPV DDFRQPRYSS GGNFETPSKR APAKGRAGRS KRTEQDHYET 400
    DYTTGGESCD ELEEDWIREY PPITSDQQRQ LYKRNFDTGL QEYKSLQSEL 450
    DEINKELSRL DKELDDYREE SEEYMAAADE YNRLKQVKGS ADYKSKKNHC 500
    KQLKSKLSHI KKMVGDYDRQ KT 522
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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. 17 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.
    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

    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: October 1, 2014
    This is version 136 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