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Q9Z0U1

- ZO2_MOUSE

UniProt

Q9Z0U1 - ZO2_MOUSE

Protein

Tight junction protein ZO-2

Gene

Tjp2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 2 (02 May 2006)
      Previous versions | rss
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    Functioni

    Plays a role in tight junctions and adherens junctions.

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. response to organic substance Source: Ensembl

    Enzyme and pathway databases

    ReactomeiREACT_196537. Signaling by Hippo.

    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:Zo2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 19

    Organism-specific databases

    MGIiMGI:1341872. Tjp2.

    Subcellular locationi

    Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Nucleus By similarity. Cell junctiontight junction 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. cell junction Source: MGI
    2. cytoplasm Source: Ensembl
    3. nucleus Source: UniProtKB-SubCell
    4. plasma membrane Source: MGI
    5. tight junction Source: UniProtKB-SubCell

    Keywords - Cellular componenti

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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11671167Tight junction protein ZO-2PRO_0000094544Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei107 – 1071Phosphoserine3 Publications
    Modified residuei130 – 1301PhosphoserineBy similarity
    Modified residuei145 – 1451PhosphoserineBy similarity
    Modified residuei147 – 1471PhosphoserineBy similarity
    Modified residuei173 – 1731PhosphoserineBy similarity
    Modified residuei194 – 1941PhosphoserineBy similarity
    Modified residuei239 – 2391PhosphoserineBy similarity
    Modified residuei380 – 3801PhosphoserineBy similarity
    Modified residuei410 – 4101PhosphoserineBy similarity
    Modified residuei435 – 4351PhosphothreonineBy similarity
    Modified residuei554 – 5541Phosphotyrosine1 Publication
    Modified residuei684 – 6841PhosphoserineBy similarity
    Modified residuei902 – 9021PhosphoserineBy similarity
    Modified residuei907 – 9071PhosphothreonineBy similarity
    Modified residuei915 – 9151PhosphothreonineBy similarity
    Modified residuei948 – 9481PhosphoserineBy similarity
    Modified residuei960 – 9601PhosphoserineBy similarity
    Modified residuei968 – 9681Phosphoserine1 Publication
    Modified residuei1044 – 10441PhosphoserineBy similarity
    Modified residuei1095 – 10951Phosphotyrosine1 Publication
    Modified residuei1124 – 11241PhosphoserineBy similarity
    Modified residuei1136 – 11361Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9Z0U1.
    PaxDbiQ9Z0U1.
    PRIDEiQ9Z0U1.

    PTM databases

    PhosphoSiteiQ9Z0U1.

    Expressioni

    Gene expression databases

    BgeeiQ9Z0U1.
    CleanExiMM_TJP2.
    GenevestigatoriQ9Z0U1.

    Interactioni

    Subunit structurei

    Homodimer, and heterodimer with ZO1. Interacts with UBN1. Interacts with SCRIB By similarity. Interacts with occludin and SAFB. Interaction with SAFB occurs in the nucleus.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi204210. 3 interactions.
    IntActiQ9Z0U1. 3 interactions.
    MINTiMINT-113156.

    Structurei

    Secondary structure

    1
    1167
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 1411
    Beta strandi17 – 193
    Beta strandi23 – 264
    Beta strandi42 – 465
    Helixi52 – 554
    Beta strandi61 – 677
    Helixi75 – 8410
    Beta strandi87 – 9812

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CSJNMR-A1-104[»]
    ProteinModelPortaliQ9Z0U1.
    SMRiQ9Z0U1. Positions 1-106, 286-364, 488-869.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Z0U1.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini10 – 9788PDZ 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini287 – 36579PDZ 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini489 – 57082PDZ 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini584 – 64966SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini660 – 858199Guanylate kinase-likePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1165 – 11673Interaction with SCRIBBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1139 – 11424Poly-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.
    GeneTreeiENSGT00640000091263.
    HOGENOMiHOG000230923.
    HOVERGENiHBG017627.
    InParanoidiQ9Z0U1.
    KOiK06098.
    OMAiPEPRAQM.
    OrthoDBiEOG7T1RB4.
    PhylomeDBiQ9Z0U1.
    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]

    Sequencei

    Sequence statusi: Complete.

    Q9Z0U1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEEVIWEQYT VTLQKDSKRG FGIAVSGGRD NPHFENGETS IVISDVLPGG     50
    PADGLLQEND RVVMVNGTPM EDVLHSFAVQ QLRKSGKIAA IVVKRPRKVQ 100
    VAPLQGSPPL SHDDRGFEVI EEFDGRSFRS GYSERSRHSS HDMLSHSWEG 150
    NRERGRPHQR TQSRERERSR GRSLERGLDQ EDYGRSRERS RGRSLERGLD 200
    RDFVSRDHSR GRSIDRDYDR DYERSYHEAY EPDYGGGYSP SYDRRAHPET 250
    RYERSRSREH LRSRSPSPES RSRHEHKGQH DPDRPIGVLL TKSKANEEYG 300
    LRLGSQIFIK EMTRTGLATK DGNLHEGDII LKINGTVTEN MSLTDARKLI 350
    EKSRGKLQLV VLRDSKQTLI NIPALNDSDS EVEDISEIES NRSFSPEERR 400
    QQYSDQDYHS STEKLKERPS SREETSGRLS RMGATPTPFK STGDITAAGV 450
    TEASREPRYQ EEGPVPQPRT APRVFLRPSP EDEAIYGPNT KMVRFKKGDS 500
    VGLRLAGGND VGIFVAGIQE GTSAEQEGLQ EGDQILKVNT QDFRGLVRED 550
    AVLYLLEIPK GETVTILAQS RADVYRDILA CGRGDSFFIR SHFECEKETP 600
    QSLAFTRGEV FRVVDTLYDG KLGHWLAVRI GNELEKGLIP NKSRAEQMAS 650
    VQNAQRENAG DRADFWRMRG QRSSGGVKKN LRKSREDLAA AVSVSTKFPA 700
    YEKVLLREAG FKRPVVLFGP IADIAMERLA TELPDLFQTA KTEPKDAGSE 750
    KSSGVVRLNT VRQIIEQDKH ALLDVTPKAV DLLNYTQWFP IVIFFNPDSR 800
    QGVKTIRQRL SPTSNKSSRK LFDQANKLKK TCSHLFTATI NVNSANDGWF 850
    GSLKDSIQQQ QNEAVWVSEG KMEGMDDDAE DRMSYLTAMG ADYLSCDSRL 900
    ISDFEDTDGE GGAYTDNELE EPAEEPLVSS ITRSSEPVQH EENIRKSSPE 950
    PRAQMRRAAS RDQLRDASPP PAFKPEPPKA RSQNREDSFD YSKSNLPATA 1000
    GSEIPGGSTK GYPPPIAAKP AFGRPILKPS TPVPMPESEE VGESTEEQED 1050
    APRSVLGRVK IFEKMDHKAK LQRMQELQEA QNARIEIAQK HPDIYAVPIK 1100
    APKPDAGLPP HMSSRPPEPQ KAPSRLYQDT RGSYGSDPEE EEYRQQLAAH 1150
    SKRGYYSQPS RYRDTEL 1167
    Length:1,167
    Mass (Da):131,280
    Last modified:May 2, 2006 - v2
    Checksum:iC29AF94F423A3A70
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti100 – 1001Q → L in AAD19964. (PubMed:10026224)Curated
    Sequence conflicti105 – 1073QGS → LGC in AAD19964. (PubMed:10026224)Curated
    Sequence conflicti111 – 1122SH → CL in AAD19964. (PubMed:10026224)Curated
    Sequence conflicti156 – 1561R → G in AAD19964. (PubMed:10026224)Curated
    Sequence conflicti292 – 2921K → Q in AAD19964. (PubMed:10026224)Curated
    Sequence conflicti378 – 3781S → R in AAD19964. (PubMed:10026224)Curated
    Sequence conflicti447 – 4471A → P in AAD19964. (PubMed:10026224)Curated
    Sequence conflicti454 – 4541S → T in AAD19964. (PubMed:10026224)Curated
    Sequence conflicti470 – 4701T → A in AAD19964. (PubMed:10026224)Curated
    Sequence conflicti506 – 5061A → P in AAD19964. (PubMed:10026224)Curated
    Sequence conflicti633 – 6331E → D in AAD19964. (PubMed:10026224)Curated
    Sequence conflicti649 – 6491A → D in AAD19964. (PubMed:10026224)Curated
    Sequence conflicti664 – 6641D → V in AAD19964. (PubMed:10026224)Curated
    Sequence conflicti667 – 6671R → W in AAD19964. (PubMed:10026224)Curated
    Sequence conflicti670 – 6701G → R in AAD19964. (PubMed:10026224)Curated
    Sequence conflicti674 – 6741S → R in AAD19964. (PubMed:10026224)Curated
    Sequence conflicti677 – 6771V → D in AAD19964. (PubMed:10026224)Curated
    Sequence conflicti680 – 6801N → T in AAD19964. (PubMed:10026224)Curated
    Sequence conflicti690 – 6912AA → RS in AAD19964. (PubMed:10026224)Curated
    Sequence conflicti731 – 7311T → N in AAD19964. (PubMed:10026224)Curated
    Sequence conflicti1035 – 10351M → I in AAD19964. (PubMed:10026224)Curated
    Sequence conflicti1038 – 10381S → T in AAD19964. (PubMed:10026224)Curated
    Sequence conflicti1069 – 10691A → P in AAD19964. (PubMed:10026224)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF113005 mRNA. Translation: AAD19964.1.
    BC034677 mRNA. Translation: AAH34677.1.
    BC039924 mRNA. Translation: AAH39924.1.
    CCDSiCCDS37939.1.
    RefSeqiNP_035727.2. NM_011597.4.
    XP_006526971.1. XM_006526908.1.
    UniGeneiMm.104744.

    Genome annotation databases

    EnsembliENSMUST00000099558; ENSMUSP00000097154; ENSMUSG00000024812.
    GeneIDi21873.
    KEGGimmu:21873.
    UCSCiuc008ham.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF113005 mRNA. Translation: AAD19964.1 .
    BC034677 mRNA. Translation: AAH34677.1 .
    BC039924 mRNA. Translation: AAH39924.1 .
    CCDSi CCDS37939.1.
    RefSeqi NP_035727.2. NM_011597.4.
    XP_006526971.1. XM_006526908.1.
    UniGenei Mm.104744.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CSJ NMR - A 1-104 [» ]
    ProteinModelPortali Q9Z0U1.
    SMRi Q9Z0U1. Positions 1-106, 286-364, 488-869.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204210. 3 interactions.
    IntActi Q9Z0U1. 3 interactions.
    MINTi MINT-113156.

    PTM databases

    PhosphoSitei Q9Z0U1.

    Proteomic databases

    MaxQBi Q9Z0U1.
    PaxDbi Q9Z0U1.
    PRIDEi Q9Z0U1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000099558 ; ENSMUSP00000097154 ; ENSMUSG00000024812 .
    GeneIDi 21873.
    KEGGi mmu:21873.
    UCSCi uc008ham.2. mouse.

    Organism-specific databases

    CTDi 9414.
    MGIi MGI:1341872. Tjp2.

    Phylogenomic databases

    eggNOGi NOG239704.
    GeneTreei ENSGT00640000091263.
    HOGENOMi HOG000230923.
    HOVERGENi HBG017627.
    InParanoidi Q9Z0U1.
    KOi K06098.
    OMAi PEPRAQM.
    OrthoDBi EOG7T1RB4.
    PhylomeDBi Q9Z0U1.
    TreeFami TF315957.

    Enzyme and pathway databases

    Reactomei REACT_196537. Signaling by Hippo.

    Miscellaneous databases

    ChiTaRSi TJP2. mouse.
    EvolutionaryTracei Q9Z0U1.
    NextBioi 301380.
    PROi Q9Z0U1.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9Z0U1.
    CleanExi MM_TJP2.
    Genevestigatori Q9Z0U1.

    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. "Characterization of ZO-2 as a MAGUK family member associated with tight as well as adherens junctions with a binding affinity to occludin and alpha catenin."
      Itoh M., Morita K., Tsukita S.
      J. Biol. Chem. 274:5981-5986(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6 X CBA.
    2. "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].
      Strain: 129.
      Tissue: Mammary gland.
    3. "The tight junction protein ZO-2 localizes to the nucleus and interacts with the heterogeneous nuclear ribonucleoprotein scaffold attachment factor-B."
      Traweger A., Fuchs R., Krizbai I.A., Weiger T.M., Bauer H.-C., Bauer H.
      J. Biol. Chem. 278:2692-2700(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SAFB.
    4. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-554, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    5. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
      Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
      Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1136, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    7. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
      Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
      J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    8. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-968 AND TYR-1095, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    10. "Solution structure of N-terminal PDZ domain from mouse TJP2."
      RIKEN structural genomics initiative (RSGI)
      Submitted (MAY-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 1-106.

    Entry informationi

    Entry nameiZO2_MOUSE
    AccessioniPrimary (citable) accession number: Q9Z0U1
    Secondary accession number(s): Q8K210
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: May 2, 2006
    Last modified: October 1, 2014
    This is version 139 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3