Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot Q07157 (ZO1_HUMAN)

Last modified November 25, 2008. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

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
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Hide | Top

Protein attributes

Sequence length1748 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

Hide | Top

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

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

Subcellular location

Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junction › tight junction. Note= Movement of ZO-1 from the cytoplasm to membrane is an early event occurring concurrently with cell-cell contact.

Tissue specificity

The alpha-containing isoform is found in most epithelial cell junctions. The short isoform is found both in endothelial cells and the highly specialized epithelial junctions of renal glomeruli and Sertoli cells of the seminiferous tubules.

Domain

The second PDZ domain mediates interaction with GJA12 By similarity.

Post-translational modification

Phosphorylated.

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.

Hide | Top

Ontologies

Keywords

   Cellular componentCell junction
Cell membrane
Membrane
Tight junction
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
SH3 domain
   PTMPhosphoprotein
   Technical term3D-structure

Gene Ontology (GO)

   Biological processcell-cell junction assembly

Traceable author statement. Source: ProtInc

   Cellular componentbasolateral plasma membrane

Inferred from direct assay. Source: MGI

cell-cell adherens junction

Traceable author statement. Source: ProtInc

cytoplasm

Inferred from direct assay. Source: HPA

tight junction

Traceable author statement. Source: ProtInc

   Molecular functionprotein binding Ref.5 Ref.6

Inferred from physical interaction. Source: UniProtKB

Complete GO annotation...

Hide | Top

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ACTN4O437072EBI-79553,EBI-351526
CGNQ9P2M71EBI-79553,EBI-79537
cgnQ9PTD71EBI-79553,EBI-79525From a different organism.
GJA1P173021EBI-79553,EBI-1103439

Hide | Top

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: Q07157-1)

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.
Isoform Short (identifier: Q07157-2)

The sequence of this isoform differs from the canonical sequence as follows:
     922-1001: Missing.

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 17481748Tight junction protein ZO-1
PRO_0000094540

Regions

Domain23 – 11088PDZ 1
Domain186 – 26479PDZ 2
Domain421 – 50282PDZ 3
Domain516 – 58469SH3
Domain598 – 779182Guanylate kinase-like
Domain1632 – 172493ZU5
Compositional bias1243 – 12486Poly-Pro
Compositional bias1426 – 14327Poly-Pro

Amino acid modifications

Modified residue1251Phosphoserine
Modified residue1311Phosphoserine
Modified residue1321Phosphotyrosine
Modified residue1661Phosphoserine
Modified residue1681Phosphoserine
Modified residue1751Phosphoserine By similarity
Modified residue2751Phosphoserine
Modified residue2771Phosphoserine
Modified residue2801Phosphoserine
Modified residue2841Phosphoserine By similarity
Modified residue2971Phosphoserine By similarity
Modified residue3001Phosphoserine By similarity
Modified residue3291Phosphoserine
Modified residue3371Phosphoserine
Modified residue4021Phosphoserine
Modified residue6171Phosphoserine
Modified residue8681Phosphothreonine
Modified residue9121Phosphoserine
Modified residue9271Phosphoserine
Modified residue9681Phosphoserine
Modified residue11401Phosphotyrosine By similarity
Modified residue13541Phosphotyrosine By similarity
Modified residue13661Phosphoserine
Modified residue15451Phosphoserine
Modified residue16171Phosphoserine
Modified residue16191Phosphoserine

Natural variations

Alternative sequence922 – 100180Missing in isoform Short.
VSP_003148
Natural variant4711N → S: dbSNP rs2229517.
VAR_025153
Natural variant7901I → V: dbSNP rs7179270.
VAR_025154
Natural variant9301P → L: dbSNP rs45529137.
VAR_025155
Natural variant11101H → R: dbSNP rs45567033.
VAR_025156
Natural variant13471D → A: dbSNP rs2291166.
VAR_025157
Natural variant16051N → S: dbSNP rs45578638.
VAR_025158

Experimental info

Sequence conflict394 – 41724QPDVD…HEDGI → NQMWIYLSVHLMVSYLIQLM KMGF in AAA02891. Ref.1
Sequence conflict5451V → A in AAA02891. Ref.1
Sequence conflict6881I → Y in AAA02891. Ref.1
Sequence conflict7621R → A in AAA02891. Ref.1

Secondary structure

1 ............................. 1748
Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified January 24, 2006. Version 3.
Checksum: 189E31617084C0CC

FASTA1,748195,459
        10         20         30         40         50         60 
MSARAAAAKS TAMEETAIWE QHTVTLHRAP GFGFGIAISG GRDNPHFQSG ETSIVISDVL 

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

       130        140        150        160        170        180 
PEPVSDNEED SYDEEIHDPR SGRSGVVNRR SEKIWPRDRS 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 SRSRSPDQRS EPSDHSRHSP QQPSNGSLRS RDEERISKPG AVSTPVKHAD 

       370        380        390        400        410        420 
DHTPKTVEEV TVERNEKQTP SLPEPKPVYA QVGQPDVDLP VSPSDGVLPN STHEDGILRP 

       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 TDQRSSGIIR 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 
QAQPQPIHRI DSPGFKPASQ QKAEASSPVP YLSPETNPAS STSAVNHNVN LTNVRLEEPT 

       970        980        990       1000       1010       1020 
PAPSTSYSPQ ADSLRTPSTE AAHIMLRDQE PSLSSHVDPT KVYRKDPYPE EMMRQNHVLK 

      1030       1040       1050       1060       1070       1080 
QPAVSHPGHR PDKEPNLTYE PQLPYVEKQA SRDLEQPTYR YESSSYTDQF SRNYEHRLRY 

      1090       1100       1110       1120       1130       1140 
EDRVPMYEEQ WSYYDDKQPY PSRPPFDNQH SQDLDSRQHP EESSERGYFP RFEEPAPLSY 

      1150       1160       1170       1180       1190       1200 
DSRPRYEQAP RASALRHEEQ PAPGYDTHGR LRPEAQPHPS AGPKPAESKQ YFEQYSRSYE 

      1210       1220       1230       1240       1250       1260 
QVPPQGFTSR AGHFEPLHGA AAVPPLIPSS QHKPEALPSN TKPLPPPPTQ TEEEEDPAMK 

      1270       1280       1290       1300       1310       1320 
PQSVLTRVKM FENKRSASLE TKKDVNDTGS FKPPEVASKP SGAPIIGPKP TSQNQFSEHD 

      1330       1340       1350       1360       1370       1380 
KTLYRIPEPQ KPQLKPPEDI VRSNHYDPEE DEEYYRKQLS YFDRRSFENK PPAHIAASHL 

      1390       1400       1410       1420       1430       1440 
SEPAKPAHSQ NQSNFSSYSS KGKPPEADGV DRSFGEKRYE PIQATPPPPP LPSQYAQPSQ 

      1450       1460       1470       1480       1490       1500 
PVTSASLHIH SKGAHGEGNS VSLDFQNSLV SKPDPPPSQN KPATFRPPNR EDTAQAAFYP 

      1510       1520       1530       1540       1550       1560 
QKSFPDKAPV NGTEQTQKTV TPAYNRFTPK PYTSSARPFE RKFESPKFNH NLLPSETAHK 

      1570       1580       1590       1600       1610       1620 
PDLSSKTPTS PKTLVKSHSL AQPPEFDSGV ETFSIHAEKP KYQINNISTV PKAIPVSPSA 

      1630       1640       1650       1660       1670       1680 
VEEDEDEDGH TVVATARGIF NSNGGVLSSI ETGVSIIIPQ GAIPEGVEQE IYFKVCRDNS 

      1690       1700       1710       1720       1730       1740 
ILPPLDKEKG ETLLSPLVMC GPHGLKFLKP VELRLPHCDP KTWQNKCLPG DPNYLVGANC 


VSVLIDHF

« Hide

Isoform Short [UniParc].

Checksum: 5AD0570EC32FD9C3
Show »

1,668186,966

Hide | Top

References

« Hide 'large scale' references
[1]"The tight junction protein ZO-1 is homologous to the Drosophila discs-large tumor suppressor protein of septate junctions."
Willott E., Balda M.S., Fanning A.S., Jameson B., van Itallie C., Anderson J.M.
Proc. Natl. Acad. Sci. U.S.A. 90:7834-7838(1993) [PubMed: 8395056] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-790.
Tissue: Liver.
[2]"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu)."
Livingston R.J., Rieder M.J., Shaffer T., Bertucci C., Baier C.N., Rajkumar N., Willa H.T., Daniels M., Downing T.K., Stanaway I.B., Nguyen C.P., Gildersleeve H., Cassidy C.M., Johnson E.J., Swanson J.E., McFarland I., Yool B., Park C., Nickerson D.A.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-471; VAL-790; LEU-930; ARG-1110; ALA-1347 AND SER-1605.
[3]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]"The coxsackievirus and adenovirus receptor is a transmembrane component of the tight junction."
Cohen C.J., Shieh J.T.C., Pickles R.J., Okegawa T., Hsieh J.-T., Bergelson J.M.
Proc. Natl. Acad. Sci. U.S.A. 98:15191-15196(2001) [PubMed: 11734628] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CXADR.
[5]"Evidence for a functional interaction between cingulin and ZO-1 in cultured cells."
D'Atri F., Nadalutti F., Citi S.
J. Biol. Chem. 277:27757-27764(2002) [PubMed: 12023291] [Abstract]
Cited for: INTERACTION WITH CGN.
[6]"Molecular cloning, functional expression, and tissue distribution of a novel human gap junction-forming protein, connexin-31.9. Interaction with zona occludens protein-1."
Nielsen P.A., Beahm D.L., Giepmans B.N., Baruch A., Hall J.E., Kumar N.M.
J. Biol. Chem. 277:38272-38283(2002) [PubMed: 12154091] [Abstract]
Cited for: INTERACTION WITH GJD3.
[7]"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.
[8]"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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166; SER-168; SER-275; SER-277; SER-280; SER-337; SER-402; THR-868 AND SER-1366, MASS SPECTROMETRY.
Tissue: Epithelium.
[9]"Global proteomic profiling of phosphopeptides