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Q9UDY2

- ZO2_HUMAN

UniProt

Q9UDY2 - ZO2_HUMAN

Protein

Tight junction protein ZO-2

Gene

TJP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 158 (01 Oct 2014)
      Sequence version 2 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    Plays a role in tight junctions and adherens junctions.

    GO - Molecular functioni

    1. guanylate kinase activity Source: ProtInc
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: Reactome
    2. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
    3. hippo signaling Source: Reactome
    4. nucleotide phosphorylation Source: GOC
    5. response to organic substance Source: Ensembl

    Enzyme and pathway databases

    ReactomeiREACT_118607. Signaling by Hippo.
    REACT_13579. Apoptotic cleavage of cell adhesion proteins.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tight junction protein ZO-2
    Alternative name(s):
    Tight junction protein 2
    Zona occludens protein 2
    Zonula occludens protein 2
    Gene namesi
    Name:TJP2
    Synonyms:X104, ZO2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:11828. TJP2.

    Subcellular locationi

    Cell junctionadherens junction. Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cell junctiontight junction By similarity. Nucleus By similarity
    Note: Also nuclear under environmental stress conditions and in migratory endothelial cells and subconfluent epithelial cell cultures.By similarity

    GO - Cellular componenti

    1. adherens junction Source: UniProtKB-SubCell
    2. cell junction Source: HPA
    3. cytoplasm Source: HPA
    4. cytosol Source: Reactome
    5. nucleoplasm Source: Reactome
    6. plasma membrane Source: HPA
    7. tight junction Source: MGI

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Membrane, Nucleus, Tight junction

    Pathology & Biotechi

    Involvement in diseasei

    Familial hypercholanemia (FHCA) [MIM:607748]: A disorder characterized by elevated serum bile acid concentrations, itching, and fat malabsorption.1 Publication
    Note: The disease may be caused by mutations affecting distinct genetic loci, including the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti48 – 481V → A in FHCA. 1 Publication
    VAR_016004

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi607748. phenotype.
    Orphaneti90635. Autosomal dominant nonsyndromic sensorineural deafness type DFNA.
    238475. Familial hypercholanemia.
    PharmGKBiPA36533.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11901190Tight junction protein ZO-2PRO_0000094543Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei130 – 1301Phosphoserine3 Publications
    Modified residuei153 – 1531Phosphoserine1 Publication
    Modified residuei168 – 1681Phosphoserine1 Publication
    Modified residuei170 – 1701Phosphoserine2 Publications
    Modified residuei174 – 1741Phosphoserine4 Publications
    Modified residuei200 – 2001Phosphoserine1 Publication
    Modified residuei220 – 2201Phosphoserine1 Publication
    Modified residuei244 – 2441Phosphoserine5 Publications
    Modified residuei266 – 2661Phosphoserine1 Publication
    Modified residuei400 – 4001Phosphoserine1 Publication
    Modified residuei430 – 4301Phosphoserine1 Publication
    Modified residuei455 – 4551Phosphothreonine1 Publication
    Modified residuei574 – 5741PhosphotyrosineBy similarity
    Modified residuei702 – 7021Phosphoserine1 Publication
    Modified residuei920 – 9201Phosphoserine2 Publications
    Modified residuei925 – 9251Phosphothreonine2 Publications
    Modified residuei933 – 9331Phosphothreonine1 Publication
    Modified residuei966 – 9661Phosphoserine1 Publication
    Modified residuei978 – 9781Phosphoserine2 Publications
    Modified residuei986 – 9861Phosphoserine4 Publications
    Modified residuei1067 – 10671Phosphoserine2 Publications
    Modified residuei1068 – 10681Phosphoserine2 Publications
    Modified residuei1118 – 11181PhosphotyrosineBy similarity
    Modified residuei1131 – 11311Phosphothreonine1 Publication
    Modified residuei1147 – 11471Phosphoserine1 Publication
    Modified residuei1159 – 11591Phosphoserine4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9UDY2.
    PaxDbiQ9UDY2.
    PRIDEiQ9UDY2.

    PTM databases

    PhosphoSiteiQ9UDY2.

    Expressioni

    Tissue specificityi

    This protein is found in epithelial cell junctions. Isoform A1 is abundant in the heart and brain. Detected in brain and skeletal muscle. It is present almost exclusively in normal tissues. Isoform C1 is expressed at high level in the kidney, pancreas, heart and placenta. Not detected in brain and skeletal muscle. Found in normal as well as in most neoplastic tissues.1 Publication

    Gene expression databases

    ArrayExpressiQ9UDY2.
    BgeeiQ9UDY2.
    CleanExiHS_TJP2.
    GenevestigatoriQ9UDY2.

    Organism-specific databases

    HPAiCAB009228.
    HPA001813.

    Interactioni

    Subunit structurei

    Homodimer, and heterodimer with ZO1. Interacts with occludin, SAFB and UBN1. Interaction with SAFB occurs in the nucleus. Interacts with SCRIB.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LASP1Q148479EBI-1042602,EBI-742828

    Protein-protein interaction databases

    BioGridi114809. 36 interactions.
    IntActiQ9UDY2. 20 interactions.
    MINTiMINT-1207536.
    STRINGi9606.ENSP00000366453.

    Structurei

    Secondary structure

    1
    1190
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi306 – 3116
    Beta strandi315 – 3173
    Beta strandi321 – 33212
    Helixi337 – 3415
    Beta strandi349 – 3535
    Helixi363 – 37210
    Turni373 – 3753
    Beta strandi376 – 3816

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2OSGNMR-A/B306-385[»]
    3E17X-ray1.75A/B306-384[»]
    ProteinModelPortaliQ9UDY2.
    SMRiQ9UDY2. Positions 21-129, 306-384, 508-887.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UDY2.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini33 – 12088PDZ 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini307 – 38579PDZ 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini509 – 59082PDZ 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini604 – 66966SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini678 – 876199Guanylate kinase-likePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1188 – 11903Interaction with SCRIB

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1162 – 11654Poly-Glu

    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

    Keywords - Domaini

    Repeat, SH3 domain

    Phylogenomic databases

    eggNOGiNOG239704.
    HOVERGENiHBG017627.
    InParanoidiQ9UDY2.
    KOiK06098.
    OMAiPEPRAQM.
    OrthoDBiEOG7T1RB4.
    PhylomeDBiQ9UDY2.
    TreeFamiTF315957.

    Family and domain databases

    Gene3Di2.30.42.10. 3 hits.
    3.40.50.300. 2 hits.
    InterProiIPR008145. GK/Ca_channel_bsu.
    IPR008144. Guanylate_kin-like.
    IPR027417. P-loop_NTPase.
    IPR001478. PDZ.
    IPR011511. SH3_2.
    IPR001452. SH3_domain.
    IPR005417. ZonOcculdens.
    IPR005419. ZonOcculS2.
    [Graphical view]
    PfamiPF00625. Guanylate_kin. 1 hit.
    PF00595. PDZ. 3 hits.
    PF07653. SH3_2. 1 hit.
    [Graphical view]
    PRINTSiPR01597. ZONOCCLUDNS.
    PR01599. ZONOCCLUDNS2.
    SMARTiSM00072. GuKc. 1 hit.
    SM00228. PDZ. 3 hits.
    SM00326. SH3. 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.
    [Graphical view]

    Sequences (7)i

    Sequence statusi: Complete.

    This entry describes 7 isoformsi produced by alternative promoter usage and alternative splicing. Align

    Isoform A1 (identifier: Q9UDY2-1) [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

    MPVRGDRGFP PRRELSGWLR APGMEELIWE QYTVTLQKDS KRGFGIAVSG     50
    GRDNPHFENG ETSIVISDVL PGGPADGLLQ ENDRVVMVNG TPMEDVLHSF 100
    AVQQLRKSGK VAAIVVKRPR KVQVAALQAS PPLDQDDRAF EVMDEFDGRS 150
    FRSGYSERSR LNSHGGRSRS WEDSPERGRP HERARSRERD LSRDRSRGRS 200
    LERGLDQDHA RTRDRSRGRS LERGLDHDFG PSRDRDRDRS RGRSIDQDYE 250
    RAYHRAYDPD YERAYSPEYR RGARHDARSR GPRSRSREHP HSRSPSPEPR 300
    GRPGPIGVLL MKSRANEEYG LRLGSQIFVK EMTRTGLATK DGNLHEGDII 350
    LKINGTVTEN MSLTDARKLI EKSRGKLQLV VLRDSQQTLI NIPSLNDSDS 400
    EIEDISEIES NRSFSPEERR HQYSDYDYHS SSEKLKERPS SREDTPSRLS 450
    RMGATPTPFK STGDIAGTVV PETNKEPRYQ EDPPAPQPKA APRTFLRPSP 500
    EDEAIYGPNT KMVRFKKGDS VGLRLAGGND VGIFVAGIQE GTSAEQEGLQ 550
    EGDQILKVNT QDFRGLVRED AVLYLLEIPK GEMVTILAQS RADVYRDILA 600
    CGRGDSFFIR SHFECEKETP QSLAFTRGEV FRVVDTLYDG KLGNWLAVRI 650
    GNELEKGLIP NKSRAEQMAS VQNAQRDNAG DRADFWRMRG QRSGVKKNLR 700
    KSREDLTAVV SVSTKFPAYE RVLLREAGFK RPVVLFGPIA DIAMEKLANE 750
    LPDWFQTAKT EPKDAGSEKS TGVVRLNTVR QIIEQDKHAL LDVTPKAVDL 800
    LNYTQWFPIV IFFNPDSRQG VKTMRQRLNP TSNKSSRKLF DQANKLKKTC 850
    AHLFTATINL NSANDSWFGS LKDTIQHQQG EAVWVSEGKM EGMDDDPEDR 900
    MSYLTAMGAD YLSCDSRLIS DFEDTDGEGG AYTDNELDEP AEEPLVSSIT 950
    RSSEPVQHEE SIRKPSPEPR AQMRRAASSD QLRDNSPPPA FKPEPPKAKT 1000
    QNKEESYDFS KSYEYKSNPS AVAGNETPGA STKGYPPPVA AKPTFGRSIL 1050
    KPSTPIPPQE GEEVGESSEE QDNAPKSVLG KVKIFEKMDH KARLQRMQEL 1100
    QEAQNARIEI AQKHPDIYAV PIKTHKPDPG TPQHTSSRPP EPQKAPSRPY 1150
    QDTRGSYGSD AEEEEYRQQL SEHSKRGYYG QSARYRDTEL 1190

    Note: Produced by alternative promoter usage.

    Length:1,190
    Mass (Da):133,958
    Last modified:January 11, 2011 - v2
    Checksum:i27305B723043BF6C
    GO
    Isoform A2 (identifier: Q9UDY2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         961-1107: Missing.

    Note: Produced by alternative splicing of isoform A1.

    Show »
    Length:1,043
    Mass (Da):117,758
    Checksum:i6EE97CE690160E91
    GO
    Isoform A3 (identifier: Q9UDY2-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         961-993: SIRKPSPEPRAQMRRAASSDQLRDNSPPPAFKP → VRRGRPRAGTGEPGVFLALSWTAVCSGCCGRHS
         994-1190: Missing.

    Note: Produced by alternative splicing of isoform A1.

    Show »
    Length:993
    Mass (Da):111,663
    Checksum:iD469C9A73851A6D3
    GO
    Isoform C1 (identifier: Q9UDY2-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-23: Missing.

    Note: Produced by alternative promoter usage.

    Show »
    Length:1,167
    Mass (Da):131,368
    Checksum:i91F7D588687D179E
    GO
    Isoform C2 (identifier: Q9UDY2-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-23: Missing.
         961-1107: Missing.

    Note: Produced by alternative splicing of isoform C1.

    Show »
    Length:1,020
    Mass (Da):115,168
    Checksum:i4A49BF3F0718D771
    GO
    Isoform 6 (identifier: Q9UDY2-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-19: MPVRGDRGFPPRRELSGWL → MKTAQALHRMWIQAVKKLRRWKG
         961-997: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,157
    Mass (Da):130,446
    Checksum:i30C98BC65E29BC85
    GO
    Isoform 7 (identifier: Q9UDY2-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-20: MPVRGDRGFPPRRELSGWLR → MKTAQALHRMWIQAVKKLRRWKGRVSPSASSPLVFPNLSSWEGEGSKTILT

    Note: No experimental confirmation available.

    Show »
    Length:1,221
    Mass (Da):137,342
    Checksum:iE185339B2A2F37B4
    GO

    Sequence cautioni

    The sequence AAA61300.1 differs from that shown. Reason: Frameshift at positions 1086, 1092 and 1095.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti411 – 4111N → T in AAA61300. (PubMed:7951235)Curated
    Sequence conflicti411 – 4111N → T in AAM28524. 1 PublicationCurated
    Sequence conflicti718 – 7181A → V in BAH13722. (PubMed:14702039)Curated
    Sequence conflicti782 – 7821I → V in AAA61300. (PubMed:7951235)Curated
    Sequence conflicti782 – 7821I → V in AAM28524. 1 PublicationCurated
    Sequence conflicti808 – 8081P → S in AAA61300. (PubMed:7951235)Curated
    Sequence conflicti812 – 8143FFN → SFT in AAA61300. (PubMed:7951235)Curated
    Sequence conflicti834 – 8341K → N in AAA61300. (PubMed:7951235)Curated
    Sequence conflicti842 – 8421Q → H in AAA61300. (PubMed:7951235)Curated
    Sequence conflicti996 – 9961P → S in AAA61300. (PubMed:7951235)Curated
    Sequence conflicti1093 – 10931R → G in AAA61300. (PubMed:7951235)Curated
    Sequence conflicti1110 – 11101I → L in BAH13722. (PubMed:14702039)Curated
    Sequence conflicti1136 – 11361S → N in AAB41794. 1 PublicationCurated
    Sequence conflicti1155 – 11584GSYG → RSFC in AAB41794. 1 PublicationCurated
    Sequence conflicti1165 – 11673EYR → IRS in AAB41794. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti48 – 481V → A in FHCA. 1 Publication
    VAR_016004
    Natural varianti482 – 4821D → E.5 Publications
    Corresponds to variant rs2309428 [ dbSNP | Ensembl ].
    VAR_030798
    Natural varianti668 – 6681M → I.1 Publication
    Corresponds to variant rs34774441 [ dbSNP | Ensembl ].
    VAR_046675
    Natural varianti711 – 7111S → P.
    Corresponds to variant rs35797487 [ dbSNP | Ensembl ].
    VAR_046676
    Natural varianti822 – 8221K → N.1 Publication
    Corresponds to variant rs1049624 [ dbSNP | Ensembl ].
    VAR_046677
    Natural varianti829 – 8291N → D.1 Publication
    Corresponds to variant rs1049625 [ dbSNP | Ensembl ].
    VAR_046678

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2323Missing in isoform C1 and isoform C2. CuratedVSP_006953Add
    BLAST
    Alternative sequencei1 – 2020MPVRG…SGWLR → MKTAQALHRMWIQAVKKLRR WKGRVSPSASSPLVFPNLSS WEGEGSKTILT in isoform 7. 1 PublicationVSP_046114Add
    BLAST
    Alternative sequencei1 – 1919MPVRG…LSGWL → MKTAQALHRMWIQAVKKLRR WKG in isoform 6. 1 PublicationVSP_046115Add
    BLAST
    Alternative sequencei961 – 1107147Missing in isoform A2 and isoform C2. CuratedVSP_003149Add
    BLAST
    Alternative sequencei961 – 99737Missing in isoform 6. 1 PublicationVSP_046116Add
    BLAST
    Alternative sequencei961 – 99333SIRKP…PAFKP → VRRGRPRAGTGEPGVFLALS WTAVCSGCCGRHS in isoform A3. 1 PublicationVSP_007835Add
    BLAST
    Alternative sequencei994 – 1190197Missing in isoform A3. 1 PublicationVSP_007836Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L27476 mRNA. Translation: AAA61300.1. Frameshift.
    AF177533
    , AF043195, AF043196, AF043197, AF177518, AF177519, AF177520, AF177521, AF177522, AF177523, AF177524, AF177525, AF177526, AF177527, AF177528, AF177529, AF177530, AF177531, AF177532 Genomic DNA. Translation: AAD20387.2.
    AF177533
    , AF043196, AF043197, AF177518, AF177519, AF177520, AF177521, AF177522, AF177523, AF177524, AF177525, AF177526, AF177527, AF177528, AF177529, AF177530, AF177531, AF177532 Genomic DNA. Translation: AAC02527.2.
    AF177533
    , AF043195, AF043196, AF043197, AF177518, AF177519, AF177520, AF177521, AF177522, AF177523, AF177524, AF177525, AF177526, AF177527, AF177528, AF177529, AF177532 Genomic DNA. Translation: AAD56218.2.
    AF177533
    , AF043196, AF043197, AF177518, AF177519, AF177520, AF177521, AF177522, AF177523, AF177524, AF177525, AF177526, AF177527, AF177528, AF177529, AF177532 Genomic DNA. Translation: AAD56219.2.
    AF489824 mRNA. Translation: AAM28524.1.
    AK295034 mRNA. Translation: BAH11954.1.
    AK302483 mRNA. Translation: BAH13722.1.
    AL162730 Genomic DNA. No translation available.
    AL358113 Genomic DNA. Translation: CAH70867.1.
    AL358113 Genomic DNA. Translation: CAH70868.1.
    AL358113 Genomic DNA. Translation: CAM13389.1.
    AL590238 Genomic DNA. No translation available.
    BC027592 mRNA. Translation: AAH27592.1.
    AF083892 mRNA. Translation: AAC33121.1.
    AF083893 mRNA. Translation: AAC33122.1.
    U84581 mRNA. Translation: AAB41794.1.
    CCDSiCCDS55314.1. [Q9UDY2-5]
    CCDS55315.1. [Q9UDY2-6]
    CCDS55316.1. [Q9UDY2-7]
    CCDS55317.1. [Q9UDY2-4]
    CCDS6627.1. [Q9UDY2-1]
    CCDS6628.1. [Q9UDY2-2]
    PIRiI54378.
    RefSeqiNP_001163886.1. NM_001170415.1. [Q9UDY2-6]
    NP_001163887.1. NM_001170416.1. [Q9UDY2-7]
    NP_001164101.1. NM_001170630.1. [Q9UDY2-5]
    NP_004808.2. NM_004817.3. [Q9UDY2-1]
    UniGeneiHs.50382.
    Hs.736223.

    Genome annotation databases

    EnsembliENST00000265384; ENSP00000265384; ENSG00000119139. [Q9UDY2-5]
    ENST00000348208; ENSP00000345893; ENSG00000119139. [Q9UDY2-2]
    ENST00000377245; ENSP00000366453; ENSG00000119139. [Q9UDY2-1]
    ENST00000453658; ENSP00000392178; ENSG00000119139. [Q9UDY2-4]
    ENST00000535702; ENSP00000442090; ENSG00000119139. [Q9UDY2-6]
    ENST00000539225; ENSP00000438262; ENSG00000119139. [Q9UDY2-7]
    GeneIDi9414.
    KEGGihsa:9414.
    UCSCiuc004ahd.3. human. [Q9UDY2-5]
    uc004ahe.3. human. [Q9UDY2-1]
    uc004ahf.3. human. [Q9UDY2-2]
    uc011lrs.2. human. [Q9UDY2-4]

    Polymorphism databases

    DMDMi317373313.

    Keywords - Coding sequence diversityi

    Alternative promoter usage, Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L27476 mRNA. Translation: AAA61300.1 . Frameshift.
    AF177533
    , AF043195 , AF043196 , AF043197 , AF177518 , AF177519 , AF177520 , AF177521 , AF177522 , AF177523 , AF177524 , AF177525 , AF177526 , AF177527 , AF177528 , AF177529 , AF177530 , AF177531 , AF177532 Genomic DNA. Translation: AAD20387.2 .
    AF177533
    , AF043196 , AF043197 , AF177518 , AF177519 , AF177520 , AF177521 , AF177522 , AF177523 , AF177524 , AF177525 , AF177526 , AF177527 , AF177528 , AF177529 , AF177530 , AF177531 , AF177532 Genomic DNA. Translation: AAC02527.2 .
    AF177533
    , AF043195 , AF043196 , AF043197 , AF177518 , AF177519 , AF177520 , AF177521 , AF177522 , AF177523 , AF177524 , AF177525 , AF177526 , AF177527 , AF177528 , AF177529 , AF177532 Genomic DNA. Translation: AAD56218.2 .
    AF177533
    , AF043196 , AF043197 , AF177518 , AF177519 , AF177520 , AF177521 , AF177522 , AF177523 , AF177524 , AF177525 , AF177526 , AF177527 , AF177528 , AF177529 , AF177532 Genomic DNA. Translation: AAD56219.2 .
    AF489824 mRNA. Translation: AAM28524.1 .
    AK295034 mRNA. Translation: BAH11954.1 .
    AK302483 mRNA. Translation: BAH13722.1 .
    AL162730 Genomic DNA. No translation available.
    AL358113 Genomic DNA. Translation: CAH70867.1 .
    AL358113 Genomic DNA. Translation: CAH70868.1 .
    AL358113 Genomic DNA. Translation: CAM13389.1 .
    AL590238 Genomic DNA. No translation available.
    BC027592 mRNA. Translation: AAH27592.1 .
    AF083892 mRNA. Translation: AAC33121.1 .
    AF083893 mRNA. Translation: AAC33122.1 .
    U84581 mRNA. Translation: AAB41794.1 .
    CCDSi CCDS55314.1. [Q9UDY2-5 ]
    CCDS55315.1. [Q9UDY2-6 ]
    CCDS55316.1. [Q9UDY2-7 ]
    CCDS55317.1. [Q9UDY2-4 ]
    CCDS6627.1. [Q9UDY2-1 ]
    CCDS6628.1. [Q9UDY2-2 ]
    PIRi I54378.
    RefSeqi NP_001163886.1. NM_001170415.1. [Q9UDY2-6 ]
    NP_001163887.1. NM_001170416.1. [Q9UDY2-7 ]
    NP_001164101.1. NM_001170630.1. [Q9UDY2-5 ]
    NP_004808.2. NM_004817.3. [Q9UDY2-1 ]
    UniGenei Hs.50382.
    Hs.736223.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2OSG NMR - A/B 306-385 [» ]
    3E17 X-ray 1.75 A/B 306-384 [» ]
    ProteinModelPortali Q9UDY2.
    SMRi Q9UDY2. Positions 21-129, 306-384, 508-887.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114809. 36 interactions.
    IntActi Q9UDY2. 20 interactions.
    MINTi MINT-1207536.
    STRINGi 9606.ENSP00000366453.

    PTM databases

    PhosphoSitei Q9UDY2.

    Polymorphism databases

    DMDMi 317373313.

    Proteomic databases

    MaxQBi Q9UDY2.
    PaxDbi Q9UDY2.
    PRIDEi Q9UDY2.

    Protocols and materials databases

    DNASUi 9414.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265384 ; ENSP00000265384 ; ENSG00000119139 . [Q9UDY2-5 ]
    ENST00000348208 ; ENSP00000345893 ; ENSG00000119139 . [Q9UDY2-2 ]
    ENST00000377245 ; ENSP00000366453 ; ENSG00000119139 . [Q9UDY2-1 ]
    ENST00000453658 ; ENSP00000392178 ; ENSG00000119139 . [Q9UDY2-4 ]
    ENST00000535702 ; ENSP00000442090 ; ENSG00000119139 . [Q9UDY2-6 ]
    ENST00000539225 ; ENSP00000438262 ; ENSG00000119139 . [Q9UDY2-7 ]
    GeneIDi 9414.
    KEGGi hsa:9414.
    UCSCi uc004ahd.3. human. [Q9UDY2-5 ]
    uc004ahe.3. human. [Q9UDY2-1 ]
    uc004ahf.3. human. [Q9UDY2-2 ]
    uc011lrs.2. human. [Q9UDY2-4 ]

    Organism-specific databases

    CTDi 9414.
    GeneCardsi GC09P071766.
    HGNCi HGNC:11828. TJP2.
    HPAi CAB009228.
    HPA001813.
    MIMi 607709. gene.
    607748. phenotype.
    neXtProti NX_Q9UDY2.
    Orphaneti 90635. Autosomal dominant nonsyndromic sensorineural deafness type DFNA.
    238475. Familial hypercholanemia.
    PharmGKBi PA36533.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG239704.
    HOVERGENi HBG017627.
    InParanoidi Q9UDY2.
    KOi K06098.
    OMAi PEPRAQM.
    OrthoDBi EOG7T1RB4.
    PhylomeDBi Q9UDY2.
    TreeFami TF315957.

    Enzyme and pathway databases

    Reactomei REACT_118607. Signaling by Hippo.
    REACT_13579. Apoptotic cleavage of cell adhesion proteins.

    Miscellaneous databases

    EvolutionaryTracei Q9UDY2.
    GeneWikii Tight_junction_protein_2.
    GenomeRNAii 9414.
    NextBioi 35268.
    PROi Q9UDY2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UDY2.
    Bgeei Q9UDY2.
    CleanExi HS_TJP2.
    Genevestigatori Q9UDY2.

    Family and domain databases

    Gene3Di 2.30.42.10. 3 hits.
    3.40.50.300. 2 hits.
    InterProi IPR008145. GK/Ca_channel_bsu.
    IPR008144. Guanylate_kin-like.
    IPR027417. P-loop_NTPase.
    IPR001478. PDZ.
    IPR011511. SH3_2.
    IPR001452. SH3_domain.
    IPR005417. ZonOcculdens.
    IPR005419. ZonOcculS2.
    [Graphical view ]
    Pfami PF00625. Guanylate_kin. 1 hit.
    PF00595. PDZ. 3 hits.
    PF07653. SH3_2. 1 hit.
    [Graphical view ]
    PRINTSi PR01597. ZONOCCLUDNS.
    PR01599. ZONOCCLUDNS2.
    SMARTi SM00072. GuKc. 1 hit.
    SM00228. PDZ. 3 hits.
    SM00326. SH3. 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.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The Friedreich ataxia region: characterization of two novel genes and reduction of the critical region to 300 kb."
      Duclos F., Rodius F., Wrogemann K., Mandel J.-L., Koenig M.
      Hum. Mol. Genet. 3:909-914(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A1), VARIANTS GLU-482; ASN-822 AND ASP-829.
      Tissue: Brain.
    2. "Organization and expression of the human zo-2 gene (tjp-2) in normal and neoplastic tissues."
      Chlenski A., Ketels K.V., Korovaitseva G.I., Talamonti M.S., Oyasu R., Scarpelli D.G.
      Biochim. Biophys. Acta 1493:319-324(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS A1; C1; A2 AND C2), TISSUE SPECIFICITY, ALTERNATIVE PROMOTER USAGE, VARIANT GLU-482.
      Tissue: Pancreas.
    3. "LIM protein KyoT2 interacts with human tight junction protein ZO-2-i3."
      Yan H.H., Rong L., Qiang S., Jian W., Peng Z., Hua H., Hui Z.W.
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A3), VARIANT GLU-482.
    4. "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] (ISOFORMS 6 AND 7), VARIANTS GLU-482 AND ILE-668.
      Tissue: Brain and Testis.
    5. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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 A1).
      Tissue: Testis.
    7. "Tight junction protein ZO-2 is differentially expressed in normal pancreatic ducts compared to human pancreatic adenocarcinoma."
      Chlenski A., Ketels K.V., Tsao M.-S., Talamonti M.S., Anderson M.R., Oyasu R., Scarpelli D.G.
      Int. J. Cancer 82:137-144(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-166 (ISOFORMS A1/A2/A3), NUCLEOTIDE SEQUENCE [MRNA] OF 1-119 (ISOFORMS C1/C2).
      Tissue: Pancreas.
    8. "Zo-2 gene alternative promoters in normal and neoplastic human pancreatic duct cells."
      Chlenski A., Ketels K.V., Engeriser J.L., Talamonti M.S., Tsao M.-S., Koutnikova H., Oyasu R., Scarpelli D.G.
      Int. J. Cancer 83:349-358(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE (ISOFORMS A1 AND C1), ALTERNATIVE PROMOTER USAGE.
      Tissue: Pancreas.
    9. Adams L.D., Werny I., Schwartz S.M.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1047-1167.
      Tissue: Aortic smooth muscle.
    10. "hScrib interacts with ZO-2 at the cell-cell junctions of epithelial cells."
      Metais J.-Y., Navarro C., Santoni M.-J., Audebert S., Borg J.-P.
      FEBS Lett. 579:3725-3730(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SCRIB.
    11. "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-130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174; SER-244; SER-702; SER-966 AND SER-986, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170; SER-174; SER-244; SER-266; SER-400; THR-455; SER-920; THR-925; THR-933; SER-978; SER-986; SER-1067; SER-1068; THR-1131 AND SER-1159, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    15. "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].
    16. "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.
    17. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244 AND SER-1159, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    18. "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-130; SER-170; SER-174; SER-244; SER-920; THR-925; SER-986 AND SER-1159, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "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-130; SER-153; SER-168; SER-174; SER-200; SER-220; SER-244; SER-430; SER-978; SER-986; SER-1067; SER-1068; SER-1147 AND SER-1159, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Domain-swapped dimerization of the second PDZ domain of ZO2 may provide a structural basis for the polymerization of claudins."
      Wu J., Yang Y., Zhang J., Ji P., Du W., Jiang P., Xie D., Huang H., Wu M., Zhang G., Wu J., Shi Y.
      J. Biol. Chem. 282:35988-35999(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 306-385, SUBUNIT.
    21. Cited for: VARIANT FHCA ALA-48.
    22. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLU-482, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiZO2_HUMAN
    AccessioniPrimary (citable) accession number: Q9UDY2
    Secondary accession number(s): A2A3H9
    , B7Z2R8, B7Z7T6, F5H301, F5H886, Q15883, Q5VXL0, Q5VXL1, Q8N756, Q8NI14, Q99839, Q9UDY0, Q9UDY1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 158 of the entry and version 2 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 9
      Human chromosome 9: 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