Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot P39447 (ZO1_MOUSE)

Last modified November 25, 2008. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

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

Protein attributes

Sequence length1745 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Subunit structure

Homodimer, and heterodimer with TJP2/ZO-2 and TJP3/ZO-3. Interacts with CGN/cingulin, CXADR, GJD3 and HSPA4 By similarity. Interacts with occludin, claudins, GJA12 and KIRREL1.

Subcellular location

Cell membrane; Peripheral membrane protein; Cytoplasmic sideBy similarity. Cell junctiontight junctionBy similarity. Note= Movement of ZO-1 from the cytoplasm to membrane is an early event occurring concurrently with cell-cell contact By similarity.

Domain

The second PDZ domain mediates interaction with GJA12.

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Actn4P577803EBI-79508,EBI-445071
CGNQ9P2M71EBI-79508,EBI-79537From a different organism.
cgnQ9PTD71EBI-79508,EBI-79525From a different organism.

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 residue1311Phosphoserine By similarity
Modified residue1321Phosphotyrosine By similarity
Modified residue1661Phosphoserine By similarity
Modified residue1681Phosphoserine By similarity
Modified residue1751Phosphoserine
Modified residue2751Phosphoserine By similarity
Modified residue2771Phosphoserine By similarity
Modified residue2801Phosphoserine By similarity
Modified residue2841Phosphoserine
Modified residue2971Phosphoserine
Modified residue3001Phosphoserine
Modified residue3291Phosphoserine By similarity
Modified residue3371Phosphoserine By similarity
Modified residue4021Phosphoserine By similarity
Modified residue6171Phosphoserine
Modified residue8681Phosphothreonine By similarity
Modified residue9121Phosphoserine
Modified residue9271Phosphoserine By similarity
Modified residue11391Phosphotyrosine
Modified residue13531Phosphotyrosine
Modified residue13651Phosphoserine By similarity
Modified residue15421Phosphoserine By similarity
Modified residue16141Phosphoserine By similarity
Modified residue16161Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
P39447-1 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: C3DA2C0A9F411F66

FASTA1,745194,711
        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 RPASHIFVKE ISQDSLAARD GDIQEGDVVL 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 IAKSELRDAG 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 AAHVGLRGEG 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 QKPEVLRSAT 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 QPNFPSYSSK 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 PEFGSGVETF 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: 8486731] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: 129.
[2]"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: 12424224] [Abstract]
Cited for: INTERACTION WITH KIRREL1.
Strain: Swiss Webster.
Tissue: Brain.
[3]"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: 15183511] [Abstract]
Cited for: INTERACTION WITH GJA12, DOMAIN.
[4]"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: 17947660] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1139 AND TYR-1353, MASS SPECTROMETRY.
Tissue: Mast cell.
[5]"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: 17242355] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175; SER-284; SER-297; SER-300 AND SER-617, MASS SPECTROMETRY.
Tissue: Liver.
[6]"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: 18630941] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-912, MASS SPECTROMETRY.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

D14340 mRNA. Translation: BAA03274.1.
PIRA46431.
RefSeqNP_033412.1.
UniGeneMm.4342

3D structure databases

HSSPHSSP built from PDB template 1JXO based on UniProtKB P31016.
SMRP39447. Positions 18-110.
ModBaseSearch...

Protein-protein interaction databases

IntActP39447.

PTM databases

PhosphoSiteP39447.

Genome annotation databases

EnsemblENSMUSG00000030516. Mus musculus. [Contig view]
GeneID21872.
KEGGmmu:21872.

Organism-specific databases

MGIMGI:98759. Tjp1.

Phylogenomic databases

HOGENOMP39447.
HOVERGENP39447.

Gene expression databases

ArrayExpressP39447.
CleanExMM_TJP1.
GermOnlineENSMUSG00000030516. Mus musculus.

Family and domain databases

InterProIPR008144. Guanylate_kin.
IPR008145. Guanylt/Ca.
IPR001478. PDZ.
IPR001452. SH3.
IPR011511. SH3_2.
IPR005417. ZonOcculdens.
IPR005418. ZonOcculS1.
IPR000906. ZU5.
[Graphical view]
PANTHERPTHR13865:SF9. ZonOcculS1. 1 hit.
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]
PROSITEPS00856. GUANYLATE_KINASE_1. False negative.
PS50052. GUANYLATE_KINASE_2. 1 hit.
PS50106. PDZ. 3 hits.
PS50002. SH3. 1 hit.
PS51145. ZU5. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio301376.
SOURCESearch...

Entry information

Entry nameZO1_MOUSE
AccessionPrimary (citable) accession number: P39447
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 25, 2008
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents