Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P39447

- ZO1_MOUSE

UniProt

P39447 - ZO1_MOUSE

Protein

Tight junction protein ZO-1

Gene

Tjp1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 By similarity.By similarity

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. protein domain specific binding Source: MGI

    GO - Biological processi

    1. blastocyst formation Source: MGI
    2. cellular response to glucose stimulus Source: Ensembl
    3. negative regulation of vascular permeability Source: Ensembl
    4. response to drug Source: Ensembl
    5. response to ethanol Source: Ensembl
    6. response to lipopolysaccharide Source: Ensembl
    7. response to magnetism Source: Ensembl
    8. sensory perception of sound Source: MGI

    Keywords - Ligandi

    Calmodulin-binding

    Enzyme and pathway databases

    ReactomeiREACT_196537. Signaling by Hippo.
    REACT_224600. c-src mediated regulation of Cx43 function and closure of gap junctions.

    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:98759. Tjp1.

    Subcellular locationi

    Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cell junctiontight junction By similarity. Cell junctiongap junction 1 Publication. CytoplasmmyofibrilsarcomereI band 1 Publication
    Note: Moves from the cytoplasm to the cell membrane concurrently with cell-cell contact. Detected at the leading edge of migrating and wounded cells By similarity.By similarity

    GO - Cellular componenti

    1. adherens junction Source: MGI
    2. apical junction complex Source: MGI
    3. apical part of cell Source: MGI
    4. apical plasma membrane Source: MGI
    5. apicolateral plasma membrane Source: MGI
    6. basolateral plasma membrane Source: MGI
    7. cell-cell adherens junction Source: MGI
    8. cell-cell junction Source: MGI
    9. cell junction Source: MGI
    10. cell surface Source: MGI
    11. cytoplasm Source: MGI
    12. gap junction Source: UniProtKB-SubCell
    13. I band Source: UniProtKB-SubCell
    14. intercalated disc Source: MGI
    15. intercellular canaliculus Source: MGI
    16. membrane Source: MGI
    17. nucleus Source: MGI
    18. plasma membrane Source: MGI
    19. tight junction Source: UniProtKB

    Keywords - Cellular componenti

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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 17451745Tight junction protein ZO-1PRO_0000094541Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei125 – 1251PhosphoserineBy similarity
    Modified residuei175 – 1751PhosphoserineBy similarity
    Modified residuei178 – 1781PhosphoserineBy similarity
    Modified residuei179 – 1791PhosphoserineBy similarity
    Modified residuei185 – 1851PhosphothreonineBy similarity
    Modified residuei277 – 2771PhosphoserineBy similarity
    Modified residuei297 – 2971PhosphoserineBy similarity
    Modified residuei300 – 3001PhosphoserineBy similarity
    Modified residuei329 – 3291PhosphoserineBy similarity
    Modified residuei334 – 3341PhosphoserineBy similarity
    Modified residuei337 – 3371PhosphoserineBy similarity
    Modified residuei353 – 3531PhosphoserineBy similarity
    Modified residuei617 – 6171PhosphoserineBy similarity
    Modified residuei622 – 6221PhosphoserineBy similarity
    Modified residuei912 – 9121Phosphoserine2 Publications
    Modified residuei1139 – 11391Phosphotyrosine1 Publication
    Modified residuei1164 – 11641Phosphotyrosine1 Publication
    Modified residuei1353 – 13531Phosphotyrosine1 Publication
    Modified residuei1365 – 13651PhosphoserineBy similarity
    Modified residuei1542 – 15421PhosphoserineBy similarity
    Modified residuei1614 – 16141PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated. Dephosphorylated by PTPRJ By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP39447.
    PaxDbiP39447.
    PRIDEiP39447.

    PTM databases

    PhosphoSiteiP39447.

    Expressioni

    Gene expression databases

    ArrayExpressiP39447.
    BgeeiP39447.
    CleanExiMM_TJP1.
    GenevestigatoriP39447.

    Interactioni

    Subunit structurei

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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Actn4P577806EBI-79508,EBI-445071
    Gjb6P706893EBI-79508,EBI-2615416

    Protein-protein interaction databases

    BioGridi204209. 7 interactions.
    DIPiDIP-30946N.
    IntActiP39447. 15 interactions.
    MINTiMINT-113090.
    STRINGi10090.ENSMUSP00000032729.

    Structurei

    Secondary structure

    1
    1745
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi20 – 267
    Beta strandi36 – 394
    Beta strandi44 – 463
    Turni49 – 513
    Beta strandi55 – 595
    Beta strandi61 – 633
    Turni64 – 685
    Beta strandi73 – 786
    Beta strandi84 – 863
    Helixi88 – 969
    Beta strandi102 – 1087

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2RRMNMR-A18-110[»]
    ProteinModelPortaliP39447.
    SMRiP39447. Positions 18-110, 185-264, 420-802, 1626-1745.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP39447.

    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
    Domaini610 – 791182Guanylate kinase-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini1629 – 172193ZU5PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1242 – 12476Poly-Pro
    Compositional biasi1424 – 14307Poly-Pro

    Domaini

    The second PDZ domain mediates interaction with GJA12.1 Publication

    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.
    GeneTreeiENSGT00640000091263.
    HOGENOMiHOG000230923.
    HOVERGENiHBG007849.
    KOiK05701.
    OMAiQANSIER.
    OrthoDBiEOG7T1RB4.
    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]

    Sequencei

    Sequence statusi: Complete.

    P39447-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSARAAAAKS TAMEETAIWE QHTVTLHRAP GFGFGIAISG GRDNPHFQSG     50
    ETSIVISDVL KGGPAEGQLQ ENDRVAMVNG VSMDNVEHAF AVQQLRKSGK 100
    NAKITIRRKK KVQIPVSHPD PEPVSDNEDD SYDEEVHDPR AGRGALANRR 150
    SEKSWARDRS ASRERSLSPR SDRRSVASSQ PAKPTKVTLV KSRKNEEYGL 200
    RLASHIFVKE ISQDSLAARD GNIQEGDVVL KINGTVTENM SLTDAKTLIE 250
    RSKGKLKMVV QRDERATLLN VPDLSDSIHS ANASERDDIS EIQSLASDHS 300
    GRSHDRPPRR SQSRSPDQRS EPSDHSTQSP QQPSNGSLRS REEERMSKPG 350
    AISTPVKHVD DHPPKAVEEV TVEKNEKQTP TLPEPKPVYA QVGQPDVDLP 400
    VSPSDGALPN SAHEDGILRP 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 TDHRSSGIIR 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
    QAQPQAIHRI DSPGLKPASQ QKAEASSPVP YLSPETTPAS SASAVNHNVS 950
    VTNVSLEEPA PAPPTSHASQ PGCLGAPSAE AAHVVLRGEG PPLPPHADPA 1000
    KVYRKEPYSE EMMRQNHILK QPALGHPGQR PDKEPNLAYE PQLPYIEKQA 1050
    SRDLEQPSYR YEVSSYTDQF SRNYDHRLRF EDRIPTYEDQ WSYYDDKQPY 1100
    QPRPFENQHP RDLDSRQHPE EASERGYFQR FEEPAPLSYD SRTRYEQLPR 1150
    TSTLRHEEQP APAYEVHNRY RPEAQPYSST GPKSSEPKQY FDQYPRSYEQ 1200
    VPPPGFTSKT GHYEPLHGAA VVPPLIPSSQ QKPEVLPSAT KPQPPPPTLT 1250
    EEEEDPAMKP QSVLTRVKMF ENKRSASLEN KKDVNDTASF KPPEVASKPP 1300
    GASLAGPKPV PQSQFSEHDK TLYRLPEPQK PQVKPPEDIV RSNHYDPEED 1350
    EEYYRKQLSY FDRRSFESKP SAHLPAGHHS EPAKPVHSQS QPNFSSYSSK 1400
    GKPETDAVDR SFSEKRYDPA QATPPPPPLP SQYSQPAPPL SSSSLHIHSK 1450
    GAQGEGNSVS LDFQNSYMSK PDPPPSQSKP ATFRPPTRED PPQTFYPQKS 1500
    FPDKAPVNGA EQTQKTITPV YNRFTPKPYT SSARPFERKF ESPKFNHNLL 1550
    PSETVHKPEL SSKTPTSPKT LMKAHSSTQP PEFDSGVETF SVHTDKPKYQ 1600
    MNNISTMPKA VPVSPSAVEE DEDEDGHTVV ATARGIFNSN GGVLSSIETG 1650
    VSIIIPQGAI PEGIEQEIYF KVCRDNSILP PLDKEKGETL LSPLVMCGPH 1700
    GLKFLKPVEL RLPHCDPKTW QNKCLPGDPN YLVGANCVSV LIDHF 1745
    Length:1,745
    Mass (Da):194,742
    Last modified:July 27, 2011 - v2
    Checksum:i002B96F5A998B5CD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti202 – 2021L → P in BAA03274. (PubMed:8486731)Curated
    Sequence conflicti222 – 2221N → D in BAA03274. (PubMed:8486731)Curated
    Sequence conflicti676 – 6761P → L in BAA03274. (PubMed:8486731)Curated
    Sequence conflicti985 – 9851V → G in BAA03274. (PubMed:8486731)Curated
    Sequence conflicti1237 – 12371P → R in BAA03274. (PubMed:8486731)Curated
    Sequence conflicti1395 – 13951S → P in BAA03274. (PubMed:8486731)Curated
    Sequence conflicti1584 – 15841D → G in BAA03274. (PubMed:8486731)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D14340 mRNA. Translation: BAA03274.1.
    AC122222 Genomic DNA. No translation available.
    AC131741 Genomic DNA. No translation available.
    CCDSiCCDS21338.1.
    PIRiA46431.
    RefSeqiNP_033412.2. NM_009386.2.
    UniGeneiMm.4342.

    Genome annotation databases

    EnsembliENSMUST00000102592; ENSMUSP00000099652; ENSMUSG00000030516.
    GeneIDi21872.
    KEGGimmu:21872.
    UCSCiuc009hgp.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D14340 mRNA. Translation: BAA03274.1 .
    AC122222 Genomic DNA. No translation available.
    AC131741 Genomic DNA. No translation available.
    CCDSi CCDS21338.1.
    PIRi A46431.
    RefSeqi NP_033412.2. NM_009386.2.
    UniGenei Mm.4342.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2RRM NMR - A 18-110 [» ]
    ProteinModelPortali P39447.
    SMRi P39447. Positions 18-110, 185-264, 420-802, 1626-1745.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204209. 7 interactions.
    DIPi DIP-30946N.
    IntActi P39447. 15 interactions.
    MINTi MINT-113090.
    STRINGi 10090.ENSMUSP00000032729.

    PTM databases

    PhosphoSitei P39447.

    Proteomic databases

    MaxQBi P39447.
    PaxDbi P39447.
    PRIDEi P39447.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000102592 ; ENSMUSP00000099652 ; ENSMUSG00000030516 .
    GeneIDi 21872.
    KEGGi mmu:21872.
    UCSCi uc009hgp.2. mouse.

    Organism-specific databases

    CTDi 7082.
    MGIi MGI:98759. Tjp1.

    Phylogenomic databases

    eggNOGi NOG239704.
    GeneTreei ENSGT00640000091263.
    HOGENOMi HOG000230923.
    HOVERGENi HBG007849.
    KOi K05701.
    OMAi QANSIER.
    OrthoDBi EOG7T1RB4.
    TreeFami TF315957.

    Enzyme and pathway databases

    Reactomei REACT_196537. Signaling by Hippo.
    REACT_224600. c-src mediated regulation of Cx43 function and closure of gap junctions.

    Miscellaneous databases

    EvolutionaryTracei P39447.
    NextBioi 301376.
    PROi P39447.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P39447.
    Bgeei P39447.
    CleanExi MM_TJP1.
    Genevestigatori P39447.

    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 220-kD protein colocalizing with cadherins in non-epithelial cells is identical to ZO-1, a tight junction-associated protein in epithelial cells: cDNA cloning and immunoelectron microscopy."
      Itoh M., Nagafuchi A., Yonemura S., Yasuda-Kitani T., Tsukita S., Tsukita S.
      J. Cell Biol. 121:491-502(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: 129.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "NEPH1 defines a novel family of podocin interacting proteins."
      Sellin L., Huber T.B., Gerke P., Quack I., Pavenstaedt H., Walz G.
      FASEB J. 17:115-117(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KIRREL1.
      Strain: Swiss Webster.
      Tissue: Brain.
    4. "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, DOMAIN.
    5. "Bves modulates epithelial integrity through an interaction at the tight junction."
      Osler M.E., Chang M.S., Bader D.M.
      J. Cell Sci. 118:4667-4678(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BVES.
    6. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    8. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
      Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
      J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1139 AND TYR-1353, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Mast cell.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-912, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    10. "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-912, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    11. "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 TYR-1164, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    12. "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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    13. "(1)H, (13)C, and (15)N resonance assignment of the first PDZ domain of mouse ZO-1."
      Umetsu Y., Goda N., Taniguchi R., Satomura K., Ikegami T., Furuse M., Hiroaki H.
      Biomol. NMR. Assign. 5:207-210(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 18-110.

    Entry informationi

    Entry nameiZO1_MOUSE
    AccessioniPrimary (citable) accession number: P39447
    Secondary accession number(s): E9QK00
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 146 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