ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q9UDY2


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name ZO2_HUMAN
Primary accession number Q9UDY2
Secondary accession numbers Q15883 Q5VXL0 Q8N756 Q8NI14 Q99839 Q9UDY0 Q9UDY1
Integrated into Swiss-Prot on April 27, 2001
Sequence was last modified on May 1, 2000 (Sequence version 1)
Annotations were last modified on    July 1, 2008 (Entry version 87)
Name and origin of the protein
Protein name Tight junction protein ZO-2
Synonyms Zonula occludens protein 2
Zona occludens protein 2
Tight junction protein 2
Gene name
Name: TJP2
Synonyms: X104, ZO2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A1).
TISSUE=Brain;
DOI=10.1093/hmg/3.6.909; PubMed=7951235 [NCBI, ExPASy, EBI, Israel, Japan]
Duclos F., Rodius F., Wrogemann K., Mandel J.-L., Koenig M.;
"The Friedreich ataxia region: characterization of two novel genes and reduction of the critical region to 300 kb.";
Hum. Mol. Genet. 3:909-914(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS A1; C1; A2 AND C2), AND ALTERNATIVE PROMOTER USAGE.
TISSUE=Pancreas;
DOI=10.1016/S0167-4781(00)00185-8; PubMed=11018256 [NCBI, ExPASy, EBI, Israel, Japan]
Chlenski A., Ketels K.V., Korovaitseva G.I., Talamonti M.S., Oyasu R., Scarpelli D.G.;
"Organization and expression of the human zo-2 gene (tjp-2) in normal and neoplastic tissues.";
Biochim. Biophys. Acta 1493:319-324(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A3).
Yan H.H., Rong L., Qiang S., Jian W., Peng Z., Hua H., Hui Z.W.;
"LIM protein KyoT2 interacts with human tight junction protein ZO-2-i3.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASP-482.
DOI=10.1038/nature02465; PubMed=15164053 [NCBI, ExPASy, EBI, Israel, Japan]
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A1), AND VARIANT ASP-482.
TISSUE=Testis;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE OF 1-104 (ISOFORMS A1 AND C1).
TISSUE=Pancreas;
DOI=10.1002/(SICI)1097-0215(19990702)82:1<137::AID-IJC23>3.0.CO;2-F; PubMed=10360833 [NCBI, ExPASy, EBI, Israel, Japan]
Chlenski A., Ketels K.V., Tsao M.-S., Talamonti M.S., Anderson M.R., Oyasu R., Scarpelli D.G.;
"Tight junction protein ZO-2 is differentially expressed in normal pancreatic ducts compared to human pancreatic adenocarcinoma.";
Int. J. Cancer 82:137-144(1999).
[7]
PARTIAL NUCLEOTIDE SEQUENCE (ISOFORMS A1 AND C1), AND ALTERNATIVE PROMOTER USAGE.
TISSUE=Pancreas;
DOI=10.1002/(SICI)1097-0215(19991029)83:3<349::AID-IJC10>3.0.CO;2-C; PubMed=10495427 [NCBI, ExPASy, EBI, Israel, Japan]
Chlenski A., Ketels K.V., Engeriser J.L., Talamonti M.S., Tsao M.-S., Koutnikova H., Oyasu R., Scarpelli D.G.;
"Zo-2 gene alternative promoters in normal and neoplastic human pancreatic duct cells.";
Int. J. Cancer 83:349-358(1999).
[8]
NUCLEOTIDE SEQUENCE OF 1047-1167.
TISSUE=Aortic smooth muscle;
Adams L.D., Werny I., Schwartz S.M.;
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266; SER-296 AND SER-1159, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170; SER-174; SER-244 AND SER-415, AND MASS SPECTROMETRY.
DOI=10.1021/pr050048h; PubMed=16083285 [NCBI, ExPASy, EBI, Israel, Japan]
Kim J.-E., Tannenbaum S.R., White F.M.;
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
J. Proteome Res. 4:1339-1346(2005).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-574, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130; SER-170; SER-192; SER-244; SER-394; SER-398; SER-400; SER-440; SER-441; THR-445 AND SER-986, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1131, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan]
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168; SER-170; SER-174; SER-244; SER-266; SER-415; SER-702; SER-966; SER-978; SER-986 AND SER-1159, AND MASS SPECTROMETRY.
TISSUE=Platelet;
DOI=10.1021/pr0704130; PubMed=18088087 [NCBI, ExPASy, EBI, Israel, Japan]
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1159, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1002/pmic.200700884; PubMed=18318008 [NCBI, ExPASy, EBI, Israel, Japan]
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography.";
Proteomics 8:1346-1361(2008).
[17]
VARIANT FHCA ALA-48.
DOI=10.1038/ng1147; PubMed=12704386 [NCBI, ExPASy, EBI, Israel, Japan]
Carlton V.E.H., Harris B.Z., Puffenberger E.G., Batta A.K., Knisely A.S., Robinson D.L., Strauss K.A., Shneider B.L., Lim W.A., Salen G., Morton D.H., Bull L.N.;
"Complex inheritance of familial hypercholanemia with associated mutations in TJP2 and BAAT.";
Nat. Genet. 34:91-96(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L27476; AAA61300.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177533; AAD20387.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF043195; AAD20387.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF043196; AAD20387.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF043197; AAD20387.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177518; AAD20387.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177519; AAD20387.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177520; AAD20387.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177521; AAD20387.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177522; AAD20387.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177523; AAD20387.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177524; AAD20387.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177525; AAD20387.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177526; AAD20387.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177527; AAD20387.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177528; AAD20387.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177529; AAD20387.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177530; AAD20387.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177531; AAD20387.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177532; AAD20387.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177533; AAC02527.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF043196; AAC02527.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF043197; AAC02527.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177518; AAC02527.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177519; AAC02527.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177520; AAC02527.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177521; AAC02527.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177522; AAC02527.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177523; AAC02527.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177524; AAC02527.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177525; AAC02527.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177526; AAC02527.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177527; AAC02527.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177528; AAC02527.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177529; AAC02527.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177530; AAC02527.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177531; AAC02527.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177532; AAC02527.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177533; AAD56218.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF043195; AAD56218.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF043196; AAD56218.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF043197; AAD56218.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177518; AAD56218.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177519; AAD56218.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177520; AAD56218.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177521; AAD56218.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177522; AAD56218.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177523; AAD56218.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177524; AAD56218.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177525; AAD56218.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177526; AAD56218.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177527; AAD56218.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177528; AAD56218.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177529; AAD56218.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177532; AAD56218.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177533; AAD56219.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF043196; AAD56219.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF043197; AAD56219.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177518; AAD56219.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177519; AAD56219.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177520; AAD56219.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177521; AAD56219.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177522; AAD56219.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177523; AAD56219.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177524; AAD56219.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177525; AAD56219.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177526; AAD56219.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177527; AAD56219.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177528; AAD56219.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177529; AAD56219.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177532; AAD56219.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF489824; AAM28524.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL358113; CAH70868.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC027592; AAH27592.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF083892; AAC33121.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF083893; AAC33122.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U84581; AAB41794.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR I54378; I54378.
RefSeq NP_004808.2; -.
NP_963923.1; -.
UniGene Hs.50382
3D structure databases
PDB
2OSG; NMR; -; A/B=306-385.[ExPASy / RCSB / EBI]
PDBsum 2OSG; -.
SMR Q9UDY2; 21-129.
ModBase Q9UDY2.
Protein-protein interaction databases
IntAct Q9UDY2; -.
PTM databases
PhosphoSite Q9UDY2; -.
Organism-specific databases
H-InvDB HIX0079048; -.
HGNC HGNC:11828; TJP2.
GeneLynx TJP2; Homo sapiens.
GenAtlas TJP2.
HPA CAB009228; -.
HPA001813; -.
MIM 607709; gene. [NCBI / EBI]
607748; phenotype. [NCBI / EBI]
PharmGKB PA36533; -.
GeneCards Q9UDY2.
Gene expression databases
ArrayExpress Q9UDY2; -.
CleanEx HS_TJP2; -.
GermOnline ENSG00000119139; Homo sapiens.
Ontologies
GO
GO:0004385; Molecular function: guanylate kinase activity (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
InterPro IPR008144; Guanylate_kin.
IPR008145; Guanylt/Ca.
IPR001478; PDZ.
IPR001452; SH3.
IPR011511; SH3_2.
IPR005417; ZonOcculdens.
IPR005419; ZonOcculS2.
Graphical view of domain structure.
Pfam PF00625; Guanylate_kin; 1.
PF00595; PDZ; 3.
PF07653; SH3_2; 1.
Pfam graphical view of domain structure.
PRINTS PR01597; ZONOCCLUDNS.
PR01599; ZONOCCLUDNS2.
SMART SM00072; GuKc; 1.
SM00228; PDZ; 3.
SM00326; SH3; 1.
SMART graphical view of domain structure.
PROSITE PS00856; GUANYLATE_KINASE_1; FALSE_NEG.
PS50052; GUANYLATE_KINASE_2; 1.
PS50106; PDZ; 3.
PS50002; SH3; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q9UDY2.
Genome annotation databases
Ensembl ENSG00000119139; Homo sapiens. [Contig view]
GeneID 9414; -.
KEGG hsa:9414; -.
Phylogenomic databases
HOVERGEN Q9UDY2; -.
Other
SOURCE TJP2; Homo sapiens.
ProtoNet Q9UDY2.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative promoter usage; Alternative splicing; Cell junction; Disease mutation; Membrane; Nucleus; Phosphoprotein; Polymorphism; Repeat; SH3 domain; Tight junction.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   1190  1190     Tight junction protein ZO-2. PRO_0000094543
DOMAIN   33    120  88     PDZ 1. 
DOMAIN   307    385  79     PDZ 2. 
DOMAIN   509    590  82     PDZ 3. 
DOMAIN   604    669  66     SH3. 
DOMAIN   678    876  199     Guanylate kinase-like. 
COMPBIAS   1162   1165  4     Poly-Glu. 
MOD_RES   130    130        Phosphoserine. 
MOD_RES   168    168        Phosphoserine. 
MOD_RES   170    170        Phosphoserine. 
MOD_RES   174    174        Phosphoserine. 
MOD_RES   192    192        Phosphoserine. 
MOD_RES   244    244        Phosphoserine. 
MOD_RES   265    265        Phosphotyrosine (By similarity). 
MOD_RES   266    266        Phosphoserine. 
MOD_RES   296    296        Phosphoserine. 
MOD_RES   394    394        Phosphoserine. 
MOD_RES   398    398        Phosphoserine. 
MOD_RES   400    400        Phosphoserine. 
MOD_RES   415    415        Phosphoserine. 
MOD_RES   440    440        Phosphoserine. 
MOD_RES   441    441        Phosphoserine. 
MOD_RES   445    445        Phosphothreonine. 
MOD_RES   574    574        Phosphotyrosine. 
MOD_RES   702    702