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Q07157

- ZO1_HUMAN

UniProt

Q07157 - ZO1_HUMAN

Protein

Tight junction protein ZO-1

Gene

TJP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 163 (01 Oct 2014)
      Sequence version 3 (24 Jan 2006)
      Previous versions | rss
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    Functioni

    The N-terminal may be involved in transducing a signal required for tight junction assembly, while the C-terminal may have specific properties of tight junctions. The alpha domain might be involved in stabilizing junctions. Plays a role in the regulation of cell migration by targeting CDC42BPB to the leading edge of migrating cells.1 Publication

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: Reactome
    2. blastocyst formation Source: Ensembl
    3. cell-cell junction assembly Source: ProtInc
    4. cell-cell signaling involved in cell-cell junction organization Source: UniProtKB
    5. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
    6. cellular response to glucose stimulus Source: Ensembl
    7. hippo signaling Source: Reactome
    8. membrane organization Source: Reactome
    9. negative regulation of vascular permeability Source: Ensembl
    10. response to drug Source: Ensembl
    11. response to ethanol Source: Ensembl
    12. response to lipopolysaccharide Source: Ensembl
    13. response to magnetism Source: Ensembl

    Keywords - Ligandi

    Calmodulin-binding

    Enzyme and pathway databases

    ReactomeiREACT_11043. c-src mediated regulation of Cx43 function and closure of gap junctions.
    REACT_118607. Signaling by Hippo.
    REACT_13579. Apoptotic cleavage of cell adhesion proteins.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tight junction protein ZO-1
    Alternative name(s):
    Tight junction protein 1
    Zona occludens protein 1
    Zonula occludens protein 1
    Gene namesi
    Name:TJP1
    Synonyms:ZO1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:11827. TJP1.

    Subcellular locationi

    Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junctiontight junction. Cell junction. Cell junctiongap junction
    Note: Moves from the cytoplasm to the cell membrane concurrently with cell-cell contact. Detected at the leading edge of migrating and wounded cells.

    GO - Cellular componenti

    1. apical junction complex Source: MGI
    2. apical part of cell Source: MGI
    3. apical plasma membrane Source: Ensembl
    4. apicolateral plasma membrane Source: Ensembl
    5. basolateral plasma membrane Source: MGI
    6. cell-cell adherens junction Source: ProtInc
    7. cell junction Source: HPA
    8. cytoplasm Source: UniProtKB
    9. cytosol Source: Reactome
    10. gap junction Source: UniProtKB-SubCell
    11. intercalated disc Source: Ensembl
    12. intercellular canaliculus Source: Ensembl
    13. nucleus Source: Ensembl
    14. plasma membrane Source: HPA
    15. tight junction Source: UniProtKB

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Gap junction, Membrane, Tight junction

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi201 – 2011R → A: Strongly reduced interaction with GJA1. 1 Publication
    Mutagenesisi209 – 2091K → A: Abolishes interaction with GJA1. 1 Publication
    Mutagenesisi1699 – 17002MC → AA: Abolishes interaction with CDC42BPB.
    Mutagenesisi1748 – 17481Missing: Abolishes interaction with CDC42BPB and MYZAP. 1 Publication

    Organism-specific databases

    PharmGKBiPA36532.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 17481748Tight junction protein ZO-1PRO_0000094540Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei125 – 1251Phosphoserine4 Publications
    Modified residuei175 – 1751Phosphoserine2 Publications
    Modified residuei178 – 1781Phosphoserine2 Publications
    Modified residuei179 – 1791Phosphoserine2 Publications
    Modified residuei185 – 1851Phosphothreonine2 Publications
    Modified residuei277 – 2771Phosphoserine2 Publications
    Modified residuei297 – 2971Phosphoserine2 Publications
    Modified residuei300 – 3001Phosphoserine2 Publications
    Modified residuei329 – 3291Phosphoserine4 Publications
    Modified residuei334 – 3341Phosphoserine2 Publications
    Modified residuei337 – 3371Phosphoserine4 Publications
    Modified residuei353 – 3531Phosphoserine2 Publications
    Modified residuei617 – 6171Phosphoserine4 Publications
    Modified residuei622 – 6221Phosphoserine2 Publications
    Modified residuei912 – 9121Phosphoserine3 Publications
    Modified residuei968 – 9681Phosphoserine3 Publications
    Modified residuei1140 – 11401PhosphotyrosineBy similarity
    Modified residuei1165 – 11651PhosphotyrosineBy similarity
    Modified residuei1354 – 13541PhosphotyrosineBy similarity
    Modified residuei1366 – 13661Phosphoserine4 Publications
    Modified residuei1545 – 15451Phosphoserine2 Publications
    Modified residuei1617 – 16171Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated. Dephosphorylated by PTPRJ.6 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ07157.
    PaxDbiQ07157.
    PRIDEiQ07157.

    PTM databases

    PhosphoSiteiQ07157.

    Expressioni

    Tissue specificityi

    The alpha-containing isoform is found in most epithelial cell junctions. The short isoform is found both in endothelial cells and the highly specialized epithelial junctions of renal glomeruli and Sertoli cells of the seminiferous tubules.

    Gene expression databases

    ArrayExpressiQ07157.
    BgeeiQ07157.
    CleanExiHS_TJP1.
    GenevestigatoriQ07157.

    Organism-specific databases

    HPAiCAB010822.
    HPA001636.
    HPA001637.

    Interactioni

    Subunit structurei

    Interacts with BVES (via the C-terminus cytoplasmic tail). Interacts with HSPA4 and KIRREL1 By similarity. Homodimer, and heterodimer with TJP2/ZO-2 and TJP3/ZO-3. Interacts with OCLN, CALM, claudins, CGN/cingulin, CXADR, GJA12, GJD3 and UBN1. Interacts (via ZU5 domain) with CDC42BPB and MYZAP. Interacts (via PDZ domain) with GJA1. Interacts (via PDZ domains) with ANKRD2.By similarity12 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ACTN4O437074EBI-79553,EBI-351526
    GJA1P173023EBI-79553,EBI-1103439
    GJD3Q8N1442EBI-79553,EBI-2629520
    Wwtr1Q9EPK54EBI-79553,EBI-1211920From a different organism.

    Protein-protein interaction databases

    BioGridi112937. 65 interactions.
    IntActiQ07157. 40 interactions.
    MINTiMINT-5006060.
    STRINGi9606.ENSP00000281537.

    Structurei

    Secondary structure

    1
    1748
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi19 – 279
    Turni30 – 323
    Beta strandi36 – 405
    Turni47 – 493
    Beta strandi54 – 596
    Turni64 – 685
    Beta strandi74 – 785
    Helixi88 – 969
    Beta strandi100 – 11011
    Beta strandi186 – 1905
    Turni191 – 1933
    Beta strandi194 – 1963
    Beta strandi200 – 21112
    Helixi216 – 2205
    Beta strandi228 – 2325
    Helixi242 – 2509
    Turni251 – 2544
    Beta strandi255 – 2617
    Beta strandi423 – 4286
    Beta strandi435 – 4395
    Turni441 – 4433
    Beta strandi445 – 4506
    Beta strandi452 – 4543
    Helixi455 – 4584
    Beta strandi465 – 4706
    Helixi480 – 48910
    Beta strandi495 – 5028
    Helixi504 – 5107
    Beta strandi519 – 5235
    Beta strandi542 – 5498
    Helixi550 – 5523
    Beta strandi553 – 56210
    Helixi564 – 5663
    Beta strandi568 – 5758
    Helixi577 – 5848
    Beta strandi632 – 6409
    Beta strandi647 – 6515
    Helixi654 – 66411
    Turni666 – 6683
    Beta strandi669 – 6713
    Beta strandi679 – 6813
    Helixi691 – 6988
    Turni699 – 7013
    Beta strandi703 – 7064
    Helixi710 – 7189
    Beta strandi724 – 7296
    Helixi733 – 74311
    Helixi751 – 76515
    Helixi766 – 7683
    Beta strandi770 – 7745
    Helixi781 – 79515
    Beta strandi796 – 8016
    Beta strandi1633 – 16408
    Beta strandi1645 – 16484
    Turni1650 – 16523
    Beta strandi1655 – 16584
    Beta strandi1669 – 16779
    Beta strandi1679 – 16813
    Turni1687 – 16893
    Beta strandi1701 – 17033
    Beta strandi1706 – 171510
    Helixi1720 – 17234
    Helixi1732 – 17343
    Turni1735 – 17373
    Beta strandi1738 – 174710

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2H2BX-ray1.60A18-110[»]
    2H2CX-ray2.00A18-110[»]
    2H3MX-ray2.90A18-110[»]
    2JWENMR-A/B185-264[»]
    2KXRNMR-A1631-1748[»]
    2KXSNMR-A1631-1748[»]
    2RCZX-ray1.70A/B186-264[»]
    3CYYX-ray2.40A/B182-273[»]
    3LH5X-ray2.60A516-803[»]
    3SHUX-ray2.75A/B421-512[»]
    3SHWX-ray2.90A421-888[»]
    3TSVX-ray1.99A417-516[»]
    3TSWX-ray2.85A/B/C/D417-803[»]
    3TSZX-ray2.50A417-803[»]
    ProteinModelPortaliQ07157.
    SMRiQ07157. Positions 18-110, 185-264, 420-802, 1629-1748.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ07157.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini23 – 11088PDZ 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini186 – 26479PDZ 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini421 – 50282PDZ 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini516 – 58469SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini598 – 779182Guanylate kinase-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini1632 – 172493ZU5PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1243 – 12486Poly-Pro
    Compositional biasi1426 – 14327Poly-Pro

    Domaini

    The second PDZ domain mediates interaction with GJA12.By similarity

    Sequence similaritiesi

    Belongs to the MAGUK family.Curated
    Contains 1 guanylate kinase-like domain.PROSITE-ProRule annotation
    Contains 3 PDZ (DHR) domains.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation
    Contains 1 ZU5 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, SH3 domain

    Phylogenomic databases

    eggNOGiNOG239704.
    HOVERGENiHBG007849.
    InParanoidiQ07157.
    KOiK05701.
    OrthoDBiEOG7T1RB4.
    PhylomeDBiQ07157.
    TreeFamiTF315957.

    Family and domain databases

    Gene3Di2.30.42.10. 3 hits.
    3.40.50.300. 1 hit.
    InterProiIPR008145. GK/Ca_channel_bsu.
    IPR008144. Guanylate_kin-like.
    IPR027417. P-loop_NTPase.
    IPR001478. PDZ.
    IPR011511. SH3_2.
    IPR001452. SH3_domain.
    IPR005417. ZonOcculdens.
    IPR005418. ZonOcculS1.
    IPR000906. ZU5.
    [Graphical view]
    PfamiPF00625. Guanylate_kin. 1 hit.
    PF00595. PDZ. 3 hits.
    PF07653. SH3_2. 1 hit.
    PF00791. ZU5. 1 hit.
    [Graphical view]
    PRINTSiPR01597. ZONOCCLUDNS.
    PR01598. ZONOCCLUDNS1.
    SMARTiSM00072. GuKc. 1 hit.
    SM00228. PDZ. 3 hits.
    SM00326. SH3. 1 hit.
    SM00218. ZU5. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    SSF50156. SSF50156. 3 hits.
    SSF52540. SSF52540. 1 hit.
    PROSITEiPS50052. GUANYLATE_KINASE_2. 1 hit.
    PS50106. PDZ. 3 hits.
    PS50002. SH3. 1 hit.
    PS51145. ZU5. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Long (identifier: Q07157-1) [UniParc]FASTAAdd to Basket

    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

    MSARAAAAKS TAMEETAIWE QHTVTLHRAP GFGFGIAISG GRDNPHFQSG     50
    ETSIVISDVL KGGPAEGQLQ ENDRVAMVNG VSMDNVEHAF AVQQLRKSGK 100
    NAKITIRRKK KVQIPVSRPD PEPVSDNEED SYDEEIHDPR SGRSGVVNRR 150
    SEKIWPRDRS ASRERSLSPR SDRRSVASSQ PAKPTKVTLV KSRKNEEYGL 200
    RLASHIFVKE ISQDSLAARD GNIQEGDVVL KINGTVTENM SLTDAKTLIE 250
    RSKGKLKMVV QRDERATLLN VPDLSDSIHS ANASERDDIS EIQSLASDHS 300
    GRSHDRPPRR SRSRSPDQRS EPSDHSRHSP QQPSNGSLRS RDEERISKPG 350
    AVSTPVKHAD DHTPKTVEEV TVERNEKQTP SLPEPKPVYA QVGQPDVDLP 400
    VSPSDGVLPN STHEDGILRP SMKLVKFRKG DSVGLRLAGG NDVGIFVAGV 450
    LEDSPAAKEG LEEGDQILRV NNVDFTNIIR EEAVLFLLDL PKGEEVTILA 500
    QKKKDVYRRI VESDVGDSFY IRTHFEYEKE SPYGLSFNKG EVFRVVDTLY 550
    NGKLGSWLAI RIGKNHKEVE RGIIPNKNRA EQLASVQYTL PKTAGGDRAD 600
    FWRFRGLRSS KRNLRKSRED LSAQPVQTKF PAYERVVLRE AGFLRPVTIF 650
    GPIADVAREK LAREEPDIYQ IAKSEPRDAG TDQRSSGIIR LHTIKQIIDQ 700
    DKHALLDVTP NAVDRLNYAQ WYPIVVFLNP DSKQGVKTMR MRLCPESRKS 750
    ARKLYERSHK LRKNNHHLFT TTINLNSMND GWYGALKEAI QQQQNQLVWV 800
    SEGKADGATS DDLDLHDDRL SYLSAPGSEY SMYSTDSRHT SDYEDTDTEG 850
    GAYTDQELDE TLNDEVGTPP ESAITRSSEP VREDSSGMHH ENQTYPPYSP 900
    QAQPQPIHRI DSPGFKPASQ QKAEASSPVP YLSPETNPAS STSAVNHNVN 950
    LTNVRLEEPT PAPSTSYSPQ ADSLRTPSTE AAHIMLRDQE PSLSSHVDPT 1000
    KVYRKDPYPE EMMRQNHVLK QPAVSHPGHR PDKEPNLTYE PQLPYVEKQA 1050
    SRDLEQPTYR YESSSYTDQF SRNYEHRLRY EDRVPMYEEQ WSYYDDKQPY 1100
    PSRPPFDNQH SQDLDSRQHP EESSERGYFP RFEEPAPLSY DSRPRYEQAP 1150
    RASALRHEEQ PAPGYDTHGR LRPEAQPHPS AGPKPAESKQ YFEQYSRSYE 1200
    QVPPQGFTSR AGHFEPLHGA AAVPPLIPSS QHKPEALPSN TKPLPPPPTQ 1250
    TEEEEDPAMK PQSVLTRVKM FENKRSASLE TKKDVNDTGS FKPPEVASKP 1300
    SGAPIIGPKP TSQNQFSEHD KTLYRIPEPQ KPQLKPPEDI VRSNHYDPEE 1350
    DEEYYRKQLS YFDRRSFENK PPAHIAASHL SEPAKPAHSQ NQSNFSSYSS 1400
    KGKPPEADGV DRSFGEKRYE PIQATPPPPP LPSQYAQPSQ PVTSASLHIH 1450
    SKGAHGEGNS VSLDFQNSLV SKPDPPPSQN KPATFRPPNR EDTAQAAFYP 1500
    QKSFPDKAPV NGTEQTQKTV TPAYNRFTPK PYTSSARPFE RKFESPKFNH 1550
    NLLPSETAHK PDLSSKTPTS PKTLVKSHSL AQPPEFDSGV ETFSIHAEKP 1600
    KYQINNISTV PKAIPVSPSA VEEDEDEDGH TVVATARGIF NSNGGVLSSI 1650
    ETGVSIIIPQ GAIPEGVEQE IYFKVCRDNS ILPPLDKEKG ETLLSPLVMC 1700
    GPHGLKFLKP VELRLPHCDP KTWQNKCLPG DPNYLVGANC VSVLIDHF 1748
    Length:1,748
    Mass (Da):195,459
    Last modified:January 24, 2006 - v3
    Checksum:i189E31617084C0CC
    GO
    Isoform Short (identifier: Q07157-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         922-1001: Missing.

    Note: Contains a phosphoserine at position 912.

    Show »
    Length:1,668
    Mass (Da):186,966
    Checksum:i5AD0570EC32FD9C3
    GO

    Sequence cautioni

    The sequence AAA02891.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti394 – 41724QPDVD…HEDGI → NQMWIYLSVHLMVSYLIQLM KMGF in AAA02891. (PubMed:8395056)CuratedAdd
    BLAST
    Sequence conflicti545 – 5451V → A in AAA02891. (PubMed:8395056)Curated
    Sequence conflicti688 – 6881I → Y in AAA02891. (PubMed:8395056)Curated
    Sequence conflicti762 – 7621R → A in AAA02891. (PubMed:8395056)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti471 – 4711N → S.1 Publication
    Corresponds to variant rs2229517 [ dbSNP | Ensembl ].
    VAR_025153
    Natural varianti790 – 7901I → V.3 Publications
    Corresponds to variant rs7179270 [ dbSNP | Ensembl ].
    VAR_025154
    Natural varianti930 – 9301P → L.1 Publication
    Corresponds to variant rs45529137 [ dbSNP | Ensembl ].
    VAR_025155
    Natural varianti1110 – 11101H → R.1 Publication
    Corresponds to variant rs45567033 [ dbSNP | Ensembl ].
    VAR_025156
    Natural varianti1347 – 13471D → A.1 Publication
    Corresponds to variant rs2291166 [ dbSNP | Ensembl ].
    VAR_025157
    Natural varianti1605 – 16051N → S.1 Publication
    Corresponds to variant rs45578638 [ dbSNP | Ensembl ].
    VAR_025158

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei922 – 100180Missing in isoform Short. CuratedVSP_003148Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L14837 mRNA. Translation: AAA02891.1. Different initiation.
    AK304758 mRNA. Translation: BAG65513.1.
    DQ015919 Genomic DNA. Translation: AAY22179.1.
    AC022613 Genomic DNA. No translation available.
    BC111712 mRNA. Translation: AAI11713.1.
    CCDSiCCDS42007.1. [Q07157-1]
    CCDS45199.1. [Q07157-2]
    PIRiA47747.
    RefSeqiNP_003248.3. NM_003257.3. [Q07157-1]
    NP_783297.2. NM_175610.2. [Q07157-2]
    UniGeneiHs.743990.

    Genome annotation databases

    EnsembliENST00000346128; ENSP00000281537; ENSG00000104067. [Q07157-1]
    ENST00000545208; ENSP00000441202; ENSG00000104067. [Q07157-2]
    GeneIDi7082.
    KEGGihsa:7082.
    UCSCiuc001zcr.3. human. [Q07157-1]
    uc001zcs.3. human. [Q07157-2]

    Polymorphism databases

    DMDMi85700443.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L14837 mRNA. Translation: AAA02891.1 . Different initiation.
    AK304758 mRNA. Translation: BAG65513.1 .
    DQ015919 Genomic DNA. Translation: AAY22179.1 .
    AC022613 Genomic DNA. No translation available.
    BC111712 mRNA. Translation: AAI11713.1 .
    CCDSi CCDS42007.1. [Q07157-1 ]
    CCDS45199.1. [Q07157-2 ]
    PIRi A47747.
    RefSeqi NP_003248.3. NM_003257.3. [Q07157-1 ]
    NP_783297.2. NM_175610.2. [Q07157-2 ]
    UniGenei Hs.743990.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2H2B X-ray 1.60 A 18-110 [» ]
    2H2C X-ray 2.00 A 18-110 [» ]
    2H3M X-ray 2.90 A 18-110 [» ]
    2JWE NMR - A/B 185-264 [» ]
    2KXR NMR - A 1631-1748 [» ]
    2KXS NMR - A 1631-1748 [» ]
    2RCZ X-ray 1.70 A/B 186-264 [» ]
    3CYY X-ray 2.40 A/B 182-273 [» ]
    3LH5 X-ray 2.60 A 516-803 [» ]
    3SHU X-ray 2.75 A/B 421-512 [» ]
    3SHW X-ray 2.90 A 421-888 [» ]
    3TSV X-ray 1.99 A 417-516 [» ]
    3TSW X-ray 2.85 A/B/C/D 417-803 [» ]
    3TSZ X-ray 2.50 A 417-803 [» ]
    ProteinModelPortali Q07157.
    SMRi Q07157. Positions 18-110, 185-264, 420-802, 1629-1748.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112937. 65 interactions.
    IntActi Q07157. 40 interactions.
    MINTi MINT-5006060.
    STRINGi 9606.ENSP00000281537.

    PTM databases

    PhosphoSitei Q07157.

    Polymorphism databases

    DMDMi 85700443.

    Proteomic databases

    MaxQBi Q07157.
    PaxDbi Q07157.
    PRIDEi Q07157.

    Protocols and materials databases

    DNASUi 7082.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000346128 ; ENSP00000281537 ; ENSG00000104067 . [Q07157-1 ]
    ENST00000545208 ; ENSP00000441202 ; ENSG00000104067 . [Q07157-2 ]
    GeneIDi 7082.
    KEGGi hsa:7082.
    UCSCi uc001zcr.3. human. [Q07157-1 ]
    uc001zcs.3. human. [Q07157-2 ]

    Organism-specific databases

    CTDi 7082.
    GeneCardsi GC15M029991.
    HGNCi HGNC:11827. TJP1.
    HPAi CAB010822.
    HPA001636.
    HPA001637.
    MIMi 601009. gene.
    neXtProti NX_Q07157.
    PharmGKBi PA36532.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG239704.
    HOVERGENi HBG007849.
    InParanoidi Q07157.
    KOi K05701.
    OrthoDBi EOG7T1RB4.
    PhylomeDBi Q07157.
    TreeFami TF315957.

    Enzyme and pathway databases

    Reactomei REACT_11043. c-src mediated regulation of Cx43 function and closure of gap junctions.
    REACT_118607. Signaling by Hippo.
    REACT_13579. Apoptotic cleavage of cell adhesion proteins.

    Miscellaneous databases

    EvolutionaryTracei Q07157.
    GeneWikii Tight_junction_protein_1.
    GenomeRNAii 7082.
    NextBioi 27699.
    PROi Q07157.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q07157.
    Bgeei Q07157.
    CleanExi HS_TJP1.
    Genevestigatori Q07157.

    Family and domain databases

    Gene3Di 2.30.42.10. 3 hits.
    3.40.50.300. 1 hit.
    InterProi IPR008145. GK/Ca_channel_bsu.
    IPR008144. Guanylate_kin-like.
    IPR027417. P-loop_NTPase.
    IPR001478. PDZ.
    IPR011511. SH3_2.
    IPR001452. SH3_domain.
    IPR005417. ZonOcculdens.
    IPR005418. ZonOcculS1.
    IPR000906. ZU5.
    [Graphical view ]
    Pfami PF00625. Guanylate_kin. 1 hit.
    PF00595. PDZ. 3 hits.
    PF07653. SH3_2. 1 hit.
    PF00791. ZU5. 1 hit.
    [Graphical view ]
    PRINTSi PR01597. ZONOCCLUDNS.
    PR01598. ZONOCCLUDNS1.
    SMARTi SM00072. GuKc. 1 hit.
    SM00228. PDZ. 3 hits.
    SM00326. SH3. 1 hit.
    SM00218. ZU5. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    SSF50156. SSF50156. 3 hits.
    SSF52540. SSF52540. 1 hit.
    PROSITEi PS50052. GUANYLATE_KINASE_2. 1 hit.
    PS50106. PDZ. 3 hits.
    PS50002. SH3. 1 hit.
    PS51145. ZU5. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The tight junction protein ZO-1 is homologous to the Drosophila discs-large tumor suppressor protein of septate junctions."
      Willott E., Balda M.S., Fanning A.S., Jameson B., van Itallie C., Anderson J.M.
      Proc. Natl. Acad. Sci. U.S.A. 90:7834-7838(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-790.
      Tissue: Liver.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG), VARIANT VAL-790.
      Tissue: Uterus.
    3. NIEHS SNPs program
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-471; VAL-790; LEU-930; ARG-1110; ALA-1347 AND SER-1605.
    4. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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 LONG).
    6. "The coxsackievirus and adenovirus receptor is a transmembrane component of the tight junction."
      Cohen C.J., Shieh J.T.C., Pickles R.J., Okegawa T., Hsieh J.-T., Bergelson J.M.
      Proc. Natl. Acad. Sci. U.S.A. 98:15191-15196(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CXADR.
    7. "Evidence for a functional interaction between cingulin and ZO-1 in cultured cells."
      D'Atri F., Nadalutti F., Citi S.
      J. Biol. Chem. 277:27757-27764(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CGN.
    8. "Molecular cloning, functional expression, and tissue distribution of a novel human gap junction-forming protein, connexin-31.9. Interaction with zona occludens protein-1."
      Nielsen P.A., Beahm D.L., Giepmans B.N., Baruch A., Hall J.E., Kumar N.M.
      J. Biol. Chem. 277:38272-38283(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GJD3.
    9. "Connexin47, connexin29 and connexin32 co-expression in oligodendrocytes and Cx47 association with zonula occludens-1 (ZO-1) in mouse brain."
      Li X., Ionescu A.V., Lynn B.D., Lu S., Kamasawa N., Morita M., Davidson K.G.V., Yasumura T., Rash J.E., Nagy J.I.
      Neuroscience 126:611-630(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GJA12.
    10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337 AND SER-1366, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125 AND SER-912, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-277; SER-329; SER-617; SER-912; SER-968 AND SER-1545, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Characterization of the ubinuclein protein as a new member of the nuclear and adhesion complex components (NACos)."
      Aho S., Lupo J., Coly P.-A., Sabine A., Castellazzi M., Morand P., Sergeant A., Manet E., Boyer V., Gruffat H.
      Biol. Cell 101:319-334(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UBN1.
    15. "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.
    16. "Myozap, a novel intercalated disc protein, activates serum response factor-dependent signaling and is required to maintain cardiac function in vivo."
      Seeger T.S., Frank D., Rohr C., Will R., Just S., Grund C., Lyon R., Luedde M., Koegl M., Sheikh F., Rottbauer W., Franke W.W., Katus H.A., Olson E.N., Frey N.
      Circ. Res. 106:880-890(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MYZAP.
    17. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329; SER-337; SER-353; SER-617; SER-968; SER-1366 AND SER-1617, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-912 (ISOFORM SHORT), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Multi-tasking role of the mechanosensing protein Ankrd2 in the signaling network of striated muscle."
      Belgrano A., Rakicevic L., Mittempergher L., Campanaro S., Martinelli V.C., Mouly V., Valle G., Kojic S., Faulkner G.
      PLoS ONE 6:E25519-E25519(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ANKRD2.
    20. "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-125; SER-175; SER-178; SER-179; THR-185; SER-297; SER-300; SER-329; SER-334; SER-337; SER-617; SER-622 AND SER-1366, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-912 (ISOFORM SHORT), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Comparative structural analysis of the erbin PDZ domain and the first PDZ domain of ZO-1. Insights into determinants of PDZ domain specificity."
      Appleton B.A., Zhang Y., Wu P., Yin J.P., Hunziker W., Skelton N.J., Sidhu S.S., Wiesmann C.
      J. Biol. Chem. 281:22312-22320(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 18-110, SUBUNIT.
    22. "Domain swapping within PDZ2 is responsible for dimerization of ZO proteins."
      Fanning A.S., Lye M.F., Anderson J.M., Lavie A.
      J. Biol. Chem. 282:37710-37716(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 185-264, SUBUNIT.
    23. "Domain-swapped dimerization of ZO-1 PDZ2 generates specific and regulatory connexin43-binding sites."
      Chen J., Pan L., Wei Z., Zhao Y., Zhang M.
      EMBO J. 27:2113-2123(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 182-273 IN COMPLEX WITH GJA1 PEPTIDE, SUBUNIT, MUTAGENESIS OF ARG-201 AND LYS-209, SUBCELLULAR LOCATION, INTERACTION WITH GJA1.
    24. "Insights into regulated ligand binding sites from the structure of ZO-1 Src homology 3-guanylate kinase module."
      Lye M.F., Fanning A.S., Su Y., Anderson J.M., Lavie A.
      J. Biol. Chem. 285:13907-13917(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 516-803, INTERACTION WITH CALM.
    25. "Cdc42-dependent formation of the ZO-1/MRCKbeta complex at the leading edge controls cell migration."
      Huo L., Wen W., Wang R., Kam C., Xia J., Feng W., Zhang M.
      EMBO J. 30:665-678(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1631-1748 OF MUTANT 1699-MET-CYS-1700 IN COMPLEX WITH MYZAP, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 1699-MET-CYS-1700 AND PHE-1748, INTERACTION WITH MYZAP AND CDC42BPB.
    26. "Solution structure of the second PDZ domain of Zonula Occludens 1."
      Ji P., Yang G., Zhang J., Wu J., Chen Z., Gong Q., Wu J., Shi Y.
      Proteins 79:1342-1346(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 185-264.

    Entry informationi

    Entry nameiZO1_HUMAN
    AccessioniPrimary (citable) accession number: Q07157
    Secondary accession number(s): B4E3K1, Q2NKP3, Q4ZGJ6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: January 24, 2006
    Last modified: October 1, 2014
    This is version 163 of the entry and version 3 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 15
      Human chromosome 15: 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