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P39447 (ZO1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tight junction protein ZO-1
Alternative name(s):
Tight junction protein 1
Zona occludens protein 1
Zonula occludens protein 1
Gene names
Name:Tjp1
Synonyms:Zo1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1745 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.3 Ref.4 Ref.5 Ref.12

Subcellular location

Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cell junctiontight junction By similarity. Cell junctiongap junction. CytoplasmmyofibrilsarcomereI band. 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. Ref.12

Domain

The second PDZ domain mediates interaction with GJA12. Ref.4

Post-translational modification

Phosphorylated. Dephosphorylated by PTPRJ By similarity.

Sequence similarities

Belongs to the MAGUK family.

Contains 1 guanylate kinase-like domain.

Contains 3 PDZ (DHR) domains.

Contains 1 SH3 domain.

Contains 1 ZU5 domain.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Cytoplasm
Gap junction
Membrane
Tight junction
   DomainRepeat
SH3 domain
   LigandCalmodulin-binding
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processblastocyst formation

Inferred from mutant phenotype PubMed 18423437. Source: MGI

cellular response to glucose stimulus

Inferred from electronic annotation. Source: Ensembl

negative regulation of vascular permeability

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

response to magnetism

Inferred from electronic annotation. Source: Ensembl

sensory perception of sound

Inferred from mutant phenotype PubMed 23979167. Source: MGI

   Cellular_componentI band

Inferred from electronic annotation. Source: UniProtKB-SubCell

adherens junction

Inferred from direct assay PubMed 12203721. Source: MGI

apical junction complex

Inferred from sequence orthology PubMed 16427635. Source: MGI

apical part of cell

Inferred from direct assay PubMed 23434913PubMed 23610556PubMed 23863479PubMed 24191021. Source: MGI

apical plasma membrane

Inferred from direct assay PubMed 21947081. Source: MGI

apicolateral plasma membrane

Inferred from direct assay PubMed 16520537. Source: MGI

basolateral plasma membrane

Inferred from sequence orthology PubMed 16427635. Source: MGI

cell junction

Inferred from direct assay PubMed 16427635PubMed 21411630PubMed 21884682. Source: MGI

cell surface

Inferred from sequence orthology PubMed 12507281. Source: MGI

cell-cell adherens junction

Inferred from direct assay PubMed 11731229PubMed 15728677PubMed 17666436. Source: MGI

cell-cell junction

Inferred from direct assay PubMed 18423437PubMed 20089884PubMed 20473291. Source: MGI

cytoplasm

Inferred from direct assay PubMed 16427635. Source: MGI

gap junction

Inferred from electronic annotation. Source: UniProtKB-SubCell

intercalated disc

Inferred from direct assay PubMed 18603586. Source: MGI

intercellular canaliculus

Inferred from direct assay PubMed 12068294. Source: MGI

membrane

Inferred from direct assay PubMed 15788452. Source: MGI

nucleus

Inferred from direct assay PubMed 14685273PubMed 16427635. Source: MGI

plasma membrane

Inferred from direct assay PubMed 12060405PubMed 12507281PubMed 15084279PubMed 15775979PubMed 17122142PubMed 18337546. Source: MGI

tight junction

Inferred from direct assay PubMed 16275913. Source: UniProtKB

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 10601346Ref.5. Source: UniProtKB

protein domain specific binding

Inferred from physical interaction PubMed 17666436. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Actn4P577806EBI-79508,EBI-445071
Gjb6P706893EBI-79508,EBI-2615416

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 17451745Tight junction protein ZO-1
PRO_0000094541

Regions

Domain23 – 11088PDZ 1
Domain186 – 26479PDZ 2
Domain421 – 50282PDZ 3
Domain516 – 58469SH3
Domain610 – 791182Guanylate kinase-like
Domain1629 – 172193ZU5
Compositional bias1242 – 12476Poly-Pro
Compositional bias1424 – 14307Poly-Pro

Amino acid modifications

Modified residue1251Phosphoserine By similarity
Modified residue1751Phosphoserine By similarity
Modified residue1781Phosphoserine By similarity
Modified residue1791Phosphoserine By similarity
Modified residue1851Phosphothreonine By similarity
Modified residue2771Phosphoserine By similarity
Modified residue2971Phosphoserine By similarity
Modified residue3001Phosphoserine By similarity
Modified residue3291Phosphoserine By similarity
Modified residue3341Phosphoserine By similarity
Modified residue3371Phosphoserine By similarity
Modified residue3531Phosphoserine By similarity
Modified residue6171Phosphoserine By similarity
Modified residue6221Phosphoserine By similarity
Modified residue9121Phosphoserine Ref.9 Ref.10
Modified residue11391Phosphotyrosine Ref.8
Modified residue11641Phosphotyrosine Ref.11
Modified residue13531Phosphotyrosine Ref.8
Modified residue13651Phosphoserine By similarity
Modified residue15421Phosphoserine By similarity
Modified residue16141Phosphoserine By similarity

Experimental info

Sequence conflict2021L → P in BAA03274. Ref.1
Sequence conflict2221N → D in BAA03274. Ref.1
Sequence conflict6761P → L in BAA03274. Ref.1
Sequence conflict9851V → G in BAA03274. Ref.1
Sequence conflict12371P → R in BAA03274. Ref.1
Sequence conflict13951S → P in BAA03274. Ref.1
Sequence conflict15841D → G in BAA03274. Ref.1

Secondary structure

...................... 1745
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P39447 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 002B96F5A998B5CD

FASTA1,745194,742
        10         20         30         40         50         60 
MSARAAAAKS TAMEETAIWE QHTVTLHRAP GFGFGIAISG GRDNPHFQSG ETSIVISDVL 

        70         80         90        100        110        120 
KGGPAEGQLQ ENDRVAMVNG VSMDNVEHAF AVQQLRKSGK NAKITIRRKK KVQIPVSHPD 

       130        140        150        160        170        180 
PEPVSDNEDD SYDEEVHDPR AGRGALANRR SEKSWARDRS ASRERSLSPR SDRRSVASSQ 

       190        200        210        220        230        240 
PAKPTKVTLV KSRKNEEYGL RLASHIFVKE ISQDSLAARD GNIQEGDVVL KINGTVTENM 

       250        260        270        280        290        300 
SLTDAKTLIE RSKGKLKMVV QRDERATLLN VPDLSDSIHS ANASERDDIS EIQSLASDHS 

       310        320        330        340        350        360 
GRSHDRPPRR SQSRSPDQRS EPSDHSTQSP QQPSNGSLRS REEERMSKPG AISTPVKHVD 

       370        380        390        400        410        420 
DHPPKAVEEV TVEKNEKQTP TLPEPKPVYA QVGQPDVDLP VSPSDGALPN SAHEDGILRP 

       430        440        450        460        470        480 
SMKLVKFRKG DSVGLRLAGG NDVGIFVAGV LEDSPAAKEG LEEGDQILRV NNVDFTNIIR 

       490        500        510        520        530        540 
EEAVLFLLDL PKGEEVTILA QKKKDVYRRI VESDVGDSFY IRTHFEYEKE SPYGLSFNKG 

       550        560        570        580        590        600 
EVFRVVDTLY NGKLGSWLAI RIGKNHKEVE RGIIPNKNRA EQLASVQYTL PKTAGGDRAD 

       610        620        630        640        650        660 
FWRFRGLRSS KRNLRKSRED LSAQPVQTKF PAYERVVLRE AGFLRPVTIF GPIADVAREK 

       670        680        690        700        710        720 
LAREEPDIYQ IAKSEPRDAG TDHRSSGIIR LHTIKQIIDQ DKHALLDVTP NAVDRLNYAQ 

       730        740        750        760        770        780 
WYPIVVFLNP DSKQGVKTMR MRLCPESRKS ARKLYERSHK LRKNNHHLFT TTINLNSMND 

       790        800        810        820        830        840 
GWYGALKEAI QQQQNQLVWV SEGKADGATS DDLDLHDDRL SYLSAPGSEY SMYSTDSRHT 

       850        860        870        880        890        900 
SDYEDTDTEG GAYTDQELDE TLNDEVGTPP ESAITRSSEP VREDSSGMHH ENQTYPPYSP 

       910        920        930        940        950        960 
QAQPQAIHRI DSPGLKPASQ QKAEASSPVP YLSPETTPAS SASAVNHNVS VTNVSLEEPA 

       970        980        990       1000       1010       1020 
PAPPTSHASQ PGCLGAPSAE AAHVVLRGEG PPLPPHADPA KVYRKEPYSE EMMRQNHILK 

      1030       1040       1050       1060       1070       1080 
QPALGHPGQR PDKEPNLAYE PQLPYIEKQA SRDLEQPSYR YEVSSYTDQF SRNYDHRLRF 

      1090       1100       1110       1120       1130       1140 
EDRIPTYEDQ WSYYDDKQPY QPRPFENQHP RDLDSRQHPE EASERGYFQR FEEPAPLSYD 

      1150       1160       1170       1180       1190       1200 
SRTRYEQLPR TSTLRHEEQP APAYEVHNRY RPEAQPYSST GPKSSEPKQY FDQYPRSYEQ 

      1210       1220       1230       1240       1250       1260 
VPPPGFTSKT GHYEPLHGAA VVPPLIPSSQ QKPEVLPSAT KPQPPPPTLT EEEEDPAMKP 

      1270       1280       1290       1300       1310       1320 
QSVLTRVKMF ENKRSASLEN KKDVNDTASF KPPEVASKPP GASLAGPKPV PQSQFSEHDK 

      1330       1340       1350       1360       1370       1380 
TLYRLPEPQK PQVKPPEDIV RSNHYDPEED EEYYRKQLSY FDRRSFESKP SAHLPAGHHS 

      1390       1400       1410       1420       1430       1440 
EPAKPVHSQS QPNFSSYSSK GKPETDAVDR SFSEKRYDPA QATPPPPPLP SQYSQPAPPL 

      1450       1460       1470       1480       1490       1500 
SSSSLHIHSK GAQGEGNSVS LDFQNSYMSK PDPPPSQSKP ATFRPPTRED PPQTFYPQKS 

      1510       1520       1530       1540       1550       1560 
FPDKAPVNGA EQTQKTITPV YNRFTPKPYT SSARPFERKF ESPKFNHNLL PSETVHKPEL 

      1570       1580       1590       1600       1610       1620 
SSKTPTSPKT LMKAHSSTQP PEFDSGVETF SVHTDKPKYQ MNNISTMPKA VPVSPSAVEE 

      1630       1640       1650       1660       1670       1680 
DEDEDGHTVV ATARGIFNSN GGVLSSIETG VSIIIPQGAI PEGIEQEIYF KVCRDNSILP 

      1690       1700       1710       1720       1730       1740 
PLDKEKGETL LSPLVMCGPH GLKFLKPVEL RLPHCDPKTW QNKCLPGDPN YLVGANCVSV 


LIDHF 

« Hide

References

« Hide 'large scale' references
[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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D14340 mRNA. Translation: BAA03274.1.
AC122222 Genomic DNA. No translation available.
AC131741 Genomic DNA. No translation available.
CCDSCCDS21338.1.
PIRA46431.
RefSeqNP_033412.2. NM_009386.2.
UniGeneMm.4342.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2RRMNMR-A18-110[»]
ProteinModelPortalP39447.
SMRP39447. Positions 18-110, 185-264, 420-802, 1626-1745.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204209. 7 interactions.
DIPDIP-30946N.
IntActP39447. 15 interactions.
MINTMINT-113090.
STRING10090.ENSMUSP00000032729.

PTM databases

PhosphoSiteP39447.

Proteomic databases

MaxQBP39447.
PaxDbP39447.
PRIDEP39447.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000102592; ENSMUSP00000099652; ENSMUSG00000030516.
GeneID21872.
KEGGmmu:21872.
UCSCuc009hgp.2. mouse.

Organism-specific databases

CTD7082.
MGIMGI:98759. Tjp1.

Phylogenomic databases

eggNOGNOG239704.
GeneTreeENSGT00640000091263.
HOGENOMHOG000230923.
HOVERGENHBG007849.
KOK05701.
OMAQANSIER.
OrthoDBEOG7T1RB4.
TreeFamTF315957.

Gene expression databases

ArrayExpressP39447.
BgeeP39447.
CleanExMM_TJP1.
GenevestigatorP39447.

Family and domain databases

Gene3D2.30.42.10. 3 hits.
3.40.50.300. 1 hit.
InterProIPR008145. 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]
PfamPF00625. Guanylate_kin. 1 hit.
PF00595. PDZ. 3 hits.
PF07653. SH3_2. 1 hit.
PF00791. ZU5. 1 hit.
[Graphical view]
PRINTSPR01597. ZONOCCLUDNS.
PR01598. ZONOCCLUDNS1.
SMARTSM00072. GuKc. 1 hit.
SM00228. PDZ. 3 hits.
SM00326. SH3. 1 hit.
SM00218. ZU5. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
SSF50156. SSF50156. 3 hits.
SSF52540. SSF52540. 1 hit.
PROSITEPS50052. GUANYLATE_KINASE_2. 1 hit.
PS50106. PDZ. 3 hits.
PS50002. SH3. 1 hit.
PS51145. ZU5. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP39447.
NextBio301376.
PROP39447.
SOURCESearch...

Entry information

Entry nameZO1_MOUSE
AccessionPrimary (citable) accession number: P39447
Secondary accession number(s): E9QK00
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot