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Q07157 (ZO1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length1748 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. Ref.23

Subunit structure

Interacts with BVES (via the C-terminus cytoplasmic tail). Interacts with HSPA4 and KIRREL1 By similarity. Homodimer, and heterodimer with TJP2/ZO-2 and TJP3/ZO-3. Interacts with OCLN, CALM, claudins, CGN/cingulin, CXADR, GJA12, GJD3 and UBN1. Interacts (via ZU5 domain) with CDC42BPB and MYZAP. Interacts (via PDZ domain) with GJA1. Ref.6 Ref.7 Ref.8 Ref.9 Ref.13 Ref.15 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23

Subcellular location

Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junction › tight junction. Cell junction. Cell junction › gap junction. Note: Moves from the cytoplasm to the cell membrane concurrently with cell-cell contact. Detected at the leading edge of migrating and wounded cells. Ref.6 Ref.21 Ref.23

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. Dephosphorylated by PTPRJ. Ref.14

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.

Sequence caution

The sequence AAA02891.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

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

Inferred from electronic annotation. Source: Compara

cell-cell junction assembly

Traceable author statement PubMed 8486731. Source: ProtInc

cell-cell signaling involved in cell-cell junction organization

Non-traceable author statement Ref.1. Source: UniProtKB

cellular component disassembly involved in execution phase of apoptosis

Traceable author statement. Source: Reactome

cellular response to glucose stimulus

Inferred from electronic annotation. Source: Compara

hippo signaling cascade

Traceable author statement. Source: Reactome

negative regulation of vascular permeability

Inferred from electronic annotation. Source: Compara

response to drug

Inferred from electronic annotation. Source: Compara

response to ethanol

Inferred from electronic annotation. Source: Compara

response to lipopolysaccharide

Inferred from electronic annotation. Source: Compara

response to magnetism

Inferred from electronic annotation. Source: Compara

   Cellular_componentapical part of cell

Inferred from direct assay PubMed 22006950. Source: MGI

apicolateral plasma membrane

Inferred from electronic annotation. Source: Compara

basolateral plasma membrane

Inferred from direct assay PubMed 16427635. Source: MGI

cell-cell adherens junction

Traceable author statement PubMed 8486731. Source: ProtInc

cytosol

Traceable author statement. Source: Reactome

gap junction

Inferred from electronic annotation. Source: UniProtKB-SubCell

intercalated disc

Inferred from electronic annotation. Source: Compara

intercellular canaliculus

Inferred from electronic annotation. Source: Compara

nucleus

Inferred from electronic annotation. Source: Compara

tight junction

Inferred from direct assay Ref.6Ref.13. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ACTN4O437074EBI-79553,EBI-351526
GJD3Q8N1442EBI-79553,EBI-2629520

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.
Note: Contains a phosphoserine at position 912.

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 Ref.11 Ref.12 Ref.18
Modified residue1751Phosphoserine Ref.18
Modified residue1781Phosphoserine Ref.18
Modified residue1791Phosphoserine Ref.18
Modified residue1851Phosphothreonine Ref.18
Modified residue2771Phosphoserine Ref.12
Modified residue2841Phosphoserine By similarity
Modified residue2971Phosphoserine Ref.18
Modified residue3001Phosphoserine Ref.18
Modified residue3291Phosphoserine Ref.12 Ref.16 Ref.18
Modified residue3341Phosphoserine Ref.18
Modified residue3371Phosphoserine Ref.10 Ref.16 Ref.18
Modified residue3531Phosphoserine Ref.16
Modified residue6171Phosphoserine Ref.12 Ref.16 Ref.18
Modified residue6221Phosphoserine Ref.18
Modified residue9121Phosphoserine Ref.11 Ref.12 Ref.16 Ref.18
Modified residue9681Phosphoserine Ref.12 Ref.16
Modified residue11401Phosphotyrosine By similarity
Modified residue11651Phosphotyrosine By similarity
Modified residue13541Phosphotyrosine By similarity
Modified residue13661Phosphoserine Ref.10 Ref.16 Ref.18
Modified residue15451Phosphoserine Ref.12
Modified residue16171Phosphoserine Ref.16

Natural variations

Alternative sequence922 – 100180Missing in isoform Short.
VSP_003148
Natural variant4711N → S. Ref.3
Corresponds to variant rs2229517 [ dbSNP | Ensembl ].
VAR_025153
Natural variant7901I → V. Ref.1 Ref.2 Ref.3
Corresponds to variant rs7179270 [ dbSNP | Ensembl ].
VAR_025154
Natural variant9301P → L. Ref.3
Corresponds to variant rs45529137 [ dbSNP | Ensembl ].
VAR_025155
Natural variant11101H → R. Ref.3
Corresponds to variant rs45567033 [ dbSNP | Ensembl ].
VAR_025156
Natural variant13471D → A. Ref.3
Corresponds to variant rs2291166 [ dbSNP | Ensembl ].
VAR_025157
Natural variant16051N → S. Ref.3
Corresponds to variant rs45578638 [ dbSNP | Ensembl ].
VAR_025158

Experimental info

Mutagenesis2011R → A: Strongly reduced interaction with GJA1. Ref.21
Mutagenesis2091K → A: Abolishes interaction with GJA1. Ref.21
Mutagenesis1699 – 17002MC → AA: Abolishes interaction with CDC42BPB.
Mutagenesis17481Missing: Abolishes interaction with CDC42BPB and MYZAP. Ref.23
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...

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 »

FASTA1,668186,966

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-790.
Tissue: Liver.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG), VARIANT VAL-790.
Tissue: Uterus.
[3]NIEHS SNPs program
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.
[4]"Analysis of the DNA sequence and duplication history of human chromosome 15."
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. expand/collapse author list , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORM LONG).
[6]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CXADR.
[7]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CGN.
[8]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GJD3.
[9]"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.
[10]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337 AND SER-1366, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[11]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125 AND SER-912, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-277; SER-329; SER-617; SER-912; SER-968 AND SER-1545, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[13]"Characterization of the ubinuclein protein as a new member of the nuclear and adhesion complex components (NACos)."
Aho S., Lupo J., Coly P.-A., Sabine A., Castellazzi M., Morand P., Sergeant A., Manet E., Boyer V., Gruffat H.
Biol. Cell 101:319-334(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UBN1.
[14]"Density-enhanced phosphatase 1 regulates phosphorylation of tight junction proteins and enhances barrier function of epithelial cells."
Sallee J.L., Burridge K.
J. Biol. Chem. 284:14997-15006(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, DEPHOSPHORYLATION BY PTPRJ.
[15]"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.
[16]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329; SER-337; SER-353; SER-617; SER-968; SER-1366 AND SER-1617, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-912 (ISOFORM SHORT), MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-175; SER-178; SER-179; THR-185; SER-297; SER-300; SER-329; SER-334; SER-337; SER-617; SER-622 AND SER-1366, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-912 (ISOFORM SHORT), MASS SPECTROMETRY.
[19]"Comparative structural analysis of the erbin PDZ domain and the first PDZ domain of ZO-1. Insights into determinants of PDZ domain specificity."
Appleton B.A., Zhang Y., Wu P., Yin J.P., Hunziker W., Skelton N.J., Sidhu S.S., Wiesmann C.
J. Biol. Chem. 281:22312-22320(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 18-110, SUBUNIT.
[20]"Domain swapping within PDZ2 is responsible for dimerization of ZO proteins."
Fanning A.S., Lye M.F., Anderson J.M., Lavie A.
J. Biol. Chem. 282:37710-37716(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 185-264, SUBUNIT.
[21]"Domain-swapped dimerization of ZO-1 PDZ2 generates specific and regulatory connexin43-binding sites."
Chen J., Pan L., Wei Z., Zhao Y., Zhang M.
EMBO J. 27:2113-2123(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 182-273 IN COMPLEX WITH GJA1 PEPTIDE, SUBUNIT, MUTAGENESIS OF ARG-201 AND LYS-209, SUBCELLULAR LOCATION, INTERACTION WITH GJA1.
[22]"Insights into regulated ligand binding sites from the structure of ZO-1 Src homology 3-guanylate kinase module."
Lye M.F., Fanning A.S., Su Y., Anderson J.M., Lavie A.
J. Biol. Chem. 285:13907-13917(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 516-803, INTERACTION WITH CALM.
[23]"Cdc42-dependent formation of the ZO-1/MRCKbeta complex at the leading edge controls cell migration."
Huo L., Wen W., Wang R., Kam C., Xia J., Feng W., Zhang M.
EMBO J. 30:665-678(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1631-1748 OF MUTANT 1699-MET-CYS-1700 IN COMPLEX WITH MYZAP, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 1699-MET-CYS-1700 AND PHE-1748, INTERACTION WITH MYZAP AND CDC42BPB.
[24]"Solution structure of the second PDZ domain of Zonula Occludens 1."
Ji P., Yang G., Zhang J., Wu J., Chen Z., Gong Q., Wu J., Shi Y.
Proteins 79:1342-1346(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 185-264.
+Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L14837 mRNA. Translation: AAA02891.1. Different initiation.
AK304758 mRNA. Translation: BAG65513.1.
DQ015919 Genomic DNA. Translation: AAY22179.1.
AC022613 Genomic DNA. No translation available.
BC111712 mRNA. Translation: AAI11713.1.
IPIIPI00216219.
IPI00335824.
PIRA47747.
RefSeqNP_003248.3. NM_003257.3.
NP_783297.2. NM_175610.2.
UniGeneHs.510833.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2H2BX-ray1.60A18-110[»]
2H2CX-ray2.00A18-110[»]
2H3MX-ray2.90A18-110[»]
2JWENMR-A/B185-264[»]
2KXRNMR-A1631-1748[»]
2KXSNMR-A1631-1748[»]
2RCZX-ray1.70A/B186-264[»]
3CYYX-ray2.40A/B182-273[»]
3LH5X-ray2.60A516-803[»]
3SHUX-ray2.75A/B421-512[»]
3SHWX-ray2.90A421-888[»]
3TSVX-ray1.99A417-516[»]
3TSWX-ray2.85A/B/C/D417-803[»]
3TSZX-ray2.50A417-803[»]
ProteinModelPortalQ07157.
ModBaseSearch...

Protein-protein interaction databases

IntActQ07157. 27 interactions.
MINTMINT-5006060.
STRING9606.ENSP00000281537.

PTM databases

PhosphoSiteQ07157.

Polymorphism databases

DMDM85700443.

Proteomic databases

PaxDbQ07157.
PRIDEQ07157.

Protocols and materials databases

DNASU7082.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000346128; ENSP00000281537; ENSG00000104067.
ENST00000545208; ENSP00000441202; ENSG00000104067.
GeneID7082.
KEGGhsa:7082.
UCSCuc001zcr.3. human.
uc001zcs.3. human.

Organism-specific databases

CTD7082.
GeneCardsGC15M029991.
HGNCHGNC:11827. TJP1.
HPACAB010822.
HPA001636.
HPA001637.
MIM601009. gene.
neXtProtNX_Q07157.
PharmGKBPA36532.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG239704.
HOVERGENHBG007849.
InParanoidQ07157.
KOK05701.
OrthoDBEOG4WSW8R.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_11123. Membrane Trafficking.
REACT_578. Apoptosis.

Gene expression databases

ArrayExpressQ07157.
BgeeQ07157.
CleanExHS_TJP1.
GenevestigatorQ07157.
GermOnlineENSG00000104067. Homo sapiens.

Family and domain databases

InterProIPR008144. Guanylate_kin.
IPR008145. Guanylate_kin/L-typ_Ca_channel.
IPR001478. PDZ.
IPR011511. SH3_2.
IPR001452. SH3_domain.
IPR005417. ZonOcculdens.
IPR005418. ZonOcculS1.
IPR000906. ZU5.
[Graphical view]
PANTHERPTHR13865:SF9. PTHR13865:SF9. 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]
SUPFAMSSF50156. PDZ. 3 hits.
SSF50044. SH3. 1 hit.
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

EvolutionaryTraceQ07157.
GenomeRNAi7082.
NextBio27699.
SOURCESearch...

Entry information

Entry nameZO1_HUMAN
AccessionPrimary (citable) accession number: Q07157
Secondary accession number(s): B4E3K1, Q2NKP3, Q4ZGJ6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: January 24, 2006
Last modified: May 1, 2013
This is version 148 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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