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Q9UDY2 (ZO2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 153. 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

Names and origin

Protein namesRecommended name:
Tight junction protein ZO-2
Alternative name(s):
Tight junction protein 2
Zona occludens protein 2
Zonula occludens protein 2
Gene names
Name:TJP2
Synonyms:X104, ZO2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1190 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in tight junctions and adherens junctions.

Subunit structure

Homodimer, and heterodimer with ZO1. Interacts with occludin, SAFB and UBN1. Interaction with SAFB occurs in the nucleus. Interacts with SCRIB. Ref.10 Ref.16 Ref.20

Subcellular location

Cell junctionadherens junction. Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cell junctiontight junction By similarity. Nucleus By similarity. Note: Also nuclear under environmental stress conditions and in migratory endothelial cells and subconfluent epithelial cell cultures By similarity.

Tissue specificity

This protein is found in epithelial cell junctions. Isoform A1 is abundant in the heart and brain. Detected in brain and skeletal muscle. It is present almost exclusively in normal tissues. Isoform C1 is expressed at high level in the kidney, pancreas, heart and placenta. Not detected in brain and skeletal muscle. Found in normal as well as in most neoplastic tissues. Ref.2

Involvement in disease

Familial hypercholanemia (FHCA) [MIM:607748]: A disorder characterized by elevated serum bile acid concentrations, itching, and fat malabsorption.
Note: The disease may be caused by mutations affecting distinct genetic loci, including the gene represented in this entry. Ref.21

Sequence similarities

Belongs to the MAGUK family.

Contains 1 guanylate kinase-like domain.

Contains 3 PDZ (DHR) domains.

Contains 1 SH3 domain.

Sequence caution

The sequence AAA61300.1 differs from that shown. Reason: Frameshift at positions 1086, 1092 and 1095.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

LASP1Q148479EBI-1042602,EBI-742828

Alternative products

This entry describes 7 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]
Isoform A1 (identifier: Q9UDY2-1)

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.
Note: Produced by alternative promoter usage.
Isoform A2 (identifier: Q9UDY2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     961-1107: Missing.
Note: Produced by alternative splicing of isoform A1.
Isoform A3 (identifier: Q9UDY2-5)

The sequence of this isoform differs from the canonical sequence as follows:
     961-993: SIRKPSPEPRAQMRRAASSDQLRDNSPPPAFKP → VRRGRPRAGTGEPGVFLALSWTAVCSGCCGRHS
     994-1190: Missing.
Note: Produced by alternative splicing of isoform A1.
Isoform C1 (identifier: Q9UDY2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: Missing.
Note: Produced by alternative promoter usage.
Isoform C2 (identifier: Q9UDY2-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: Missing.
     961-1107: Missing.
Note: Produced by alternative splicing of isoform C1.
Isoform 6 (identifier: Q9UDY2-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-19: MPVRGDRGFPPRRELSGWL → MKTAQALHRMWIQAVKKLRRWKG
     961-997: Missing.
Note: No experimental confirmation available.
Isoform 7 (identifier: Q9UDY2-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: MPVRGDRGFPPRRELSGWLR → MKTAQALHRMWIQAVKKLRRWKGRVSPSASSPLVFPNLSSWEGEGSKTILT
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11901190Tight junction protein ZO-2
PRO_0000094543

Regions

Domain33 – 12088PDZ 1
Domain307 – 38579PDZ 2
Domain509 – 59082PDZ 3
Domain604 – 66966SH3
Domain678 – 876199Guanylate kinase-like
Region1188 – 11903Interaction with SCRIB
Compositional bias1162 – 11654Poly-Glu

Amino acid modifications

Modified residue1301Phosphoserine Ref.11 Ref.18 Ref.19
Modified residue1531Phosphoserine Ref.19
Modified residue1681Phosphoserine Ref.19
Modified residue1701Phosphoserine Ref.13 Ref.18
Modified residue1741Phosphoserine Ref.12 Ref.13 Ref.18 Ref.19
Modified residue2001Phosphoserine Ref.19
Modified residue2201Phosphoserine Ref.19
Modified residue2441Phosphoserine Ref.12 Ref.13 Ref.17 Ref.18 Ref.19
Modified residue2661Phosphoserine Ref.13
Modified residue4001Phosphoserine Ref.13
Modified residue4301Phosphoserine Ref.19
Modified residue4551Phosphothreonine Ref.13
Modified residue5741Phosphotyrosine By similarity
Modified residue7021Phosphoserine Ref.12
Modified residue9201Phosphoserine Ref.13 Ref.18
Modified residue9251Phosphothreonine Ref.13 Ref.18
Modified residue9331Phosphothreonine Ref.13
Modified residue9661Phosphoserine Ref.12
Modified residue9781Phosphoserine Ref.13 Ref.19
Modified residue9861Phosphoserine Ref.12 Ref.13 Ref.18 Ref.19
Modified residue10671Phosphoserine Ref.13 Ref.19
Modified residue10681Phosphoserine Ref.13 Ref.19
Modified residue11181Phosphotyrosine By similarity
Modified residue11311Phosphothreonine Ref.13
Modified residue11471Phosphoserine Ref.19
Modified residue11591Phosphoserine Ref.13 Ref.17 Ref.18 Ref.19

Natural variations

Alternative sequence1 – 2323Missing in isoform C1 and isoform C2.
VSP_006953
Alternative sequence1 – 2020MPVRG…SGWLR → MKTAQALHRMWIQAVKKLRR WKGRVSPSASSPLVFPNLSS WEGEGSKTILT in isoform 7.
VSP_046114
Alternative sequence1 – 1919MPVRG…LSGWL → MKTAQALHRMWIQAVKKLRR WKG in isoform 6.
VSP_046115
Alternative sequence961 – 1107147Missing in isoform A2 and isoform C2.
VSP_003149
Alternative sequence961 – 99737Missing in isoform 6.
VSP_046116
Alternative sequence961 – 99333SIRKP…PAFKP → VRRGRPRAGTGEPGVFLALS WTAVCSGCCGRHS in isoform A3.
VSP_007835
Alternative sequence994 – 1190197Missing in isoform A3.
VSP_007836
Natural variant481V → A in FHCA. Ref.21
VAR_016004
Natural variant4821D → E. Ref.1 Ref.2 Ref.3 Ref.4 Ref.22
Corresponds to variant rs2309428 [ dbSNP | Ensembl ].
VAR_030798
Natural variant6681M → I. Ref.4
Corresponds to variant rs34774441 [ dbSNP | Ensembl ].
VAR_046675
Natural variant7111S → P.
Corresponds to variant rs35797487 [ dbSNP | Ensembl ].
VAR_046676
Natural variant8221K → N. Ref.1
Corresponds to variant rs1049624 [ dbSNP | Ensembl ].
VAR_046677
Natural variant8291N → D. Ref.1
Corresponds to variant rs1049625 [ dbSNP | Ensembl ].
VAR_046678

Experimental info

Sequence conflict4111N → T in AAA61300. Ref.1
Sequence conflict4111N → T in AAM28524. Ref.3
Sequence conflict7181A → V in BAH13722. Ref.4
Sequence conflict7821I → V in AAA61300. Ref.1
Sequence conflict7821I → V in AAM28524. Ref.3
Sequence conflict8081P → S in AAA61300. Ref.1
Sequence conflict812 – 8143FFN → SFT in AAA61300. Ref.1
Sequence conflict8341K → N in AAA61300. Ref.1
Sequence conflict8421Q → H in AAA61300. Ref.1
Sequence conflict9961P → S in AAA61300. Ref.1
Sequence conflict10931R → G in AAA61300. Ref.1
Sequence conflict11101I → L in BAH13722. Ref.4
Sequence conflict11361S → N in AAB41794. Ref.9
Sequence conflict1155 – 11584GSYG → RSFC in AAB41794. Ref.9
Sequence conflict1165 – 11673EYR → IRS in AAB41794. Ref.9

Secondary structure

............... 1190
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform A1 [UniParc].

Last modified January 11, 2011. Version 2.
Checksum: 27305B723043BF6C

FASTA1,190133,958
        10         20         30         40         50         60 
MPVRGDRGFP PRRELSGWLR APGMEELIWE QYTVTLQKDS KRGFGIAVSG GRDNPHFENG 

        70         80         90        100        110        120 
ETSIVISDVL PGGPADGLLQ ENDRVVMVNG TPMEDVLHSF AVQQLRKSGK VAAIVVKRPR 

       130        140        150        160        170        180 
KVQVAALQAS PPLDQDDRAF EVMDEFDGRS FRSGYSERSR LNSHGGRSRS WEDSPERGRP 

       190        200        210        220        230        240 
HERARSRERD LSRDRSRGRS LERGLDQDHA RTRDRSRGRS LERGLDHDFG PSRDRDRDRS 

       250        260        270        280        290        300 
RGRSIDQDYE RAYHRAYDPD YERAYSPEYR RGARHDARSR GPRSRSREHP HSRSPSPEPR 

       310        320        330        340        350        360 
GRPGPIGVLL MKSRANEEYG LRLGSQIFVK EMTRTGLATK DGNLHEGDII LKINGTVTEN 

       370        380        390        400        410        420 
MSLTDARKLI EKSRGKLQLV VLRDSQQTLI NIPSLNDSDS EIEDISEIES NRSFSPEERR 

       430        440        450        460        470        480 
HQYSDYDYHS SSEKLKERPS SREDTPSRLS RMGATPTPFK STGDIAGTVV PETNKEPRYQ 

       490        500        510        520        530        540 
EDPPAPQPKA APRTFLRPSP EDEAIYGPNT KMVRFKKGDS VGLRLAGGND VGIFVAGIQE 

       550        560        570        580        590        600 
GTSAEQEGLQ EGDQILKVNT QDFRGLVRED AVLYLLEIPK GEMVTILAQS RADVYRDILA 

       610        620        630        640        650        660 
CGRGDSFFIR SHFECEKETP QSLAFTRGEV FRVVDTLYDG KLGNWLAVRI GNELEKGLIP 

       670        680        690        700        710        720 
NKSRAEQMAS VQNAQRDNAG DRADFWRMRG QRSGVKKNLR KSREDLTAVV SVSTKFPAYE 

       730        740        750        760        770        780 
RVLLREAGFK RPVVLFGPIA DIAMEKLANE LPDWFQTAKT EPKDAGSEKS TGVVRLNTVR 

       790        800        810        820        830        840 
QIIEQDKHAL LDVTPKAVDL LNYTQWFPIV IFFNPDSRQG VKTMRQRLNP TSNKSSRKLF 

       850        860        870        880        890        900 
DQANKLKKTC AHLFTATINL NSANDSWFGS LKDTIQHQQG EAVWVSEGKM EGMDDDPEDR 

       910        920        930        940        950        960 
MSYLTAMGAD YLSCDSRLIS DFEDTDGEGG AYTDNELDEP AEEPLVSSIT RSSEPVQHEE 

       970        980        990       1000       1010       1020 
SIRKPSPEPR AQMRRAASSD QLRDNSPPPA FKPEPPKAKT QNKEESYDFS KSYEYKSNPS 

      1030       1040       1050       1060       1070       1080 
AVAGNETPGA STKGYPPPVA AKPTFGRSIL KPSTPIPPQE GEEVGESSEE QDNAPKSVLG 

      1090       1100       1110       1120       1130       1140 
KVKIFEKMDH KARLQRMQEL QEAQNARIEI AQKHPDIYAV PIKTHKPDPG TPQHTSSRPP 

      1150       1160       1170       1180       1190 
EPQKAPSRPY QDTRGSYGSD AEEEEYRQQL SEHSKRGYYG QSARYRDTEL 

« Hide

Isoform A2 [UniParc].

Checksum: 6EE97CE690160E91
Show »

FASTA1,043117,758
Isoform A3 [UniParc].

Checksum: D469C9A73851A6D3
Show »

FASTA993111,663
Isoform C1 [UniParc].

Checksum: 91F7D588687D179E
Show »

FASTA1,167131,368
Isoform C2 [UniParc].

Checksum: 4A49BF3F0718D771
Show »

FASTA1,020115,168
Isoform 6 [UniParc].

Checksum: 30C98BC65E29BC85
Show »

FASTA1,157130,446
Isoform 7 [UniParc].

Checksum: E185339B2A2F37B4
Show »

FASTA1,221137,342

References

« Hide 'large scale' references
[1]"The Friedreich ataxia region: characterization of two novel genes and reduction of the critical region to 300 kb."
Duclos F., Rodius F., Wrogemann K., Mandel J.-L., Koenig M.
Hum. Mol. Genet. 3:909-914(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A1), VARIANTS GLU-482; ASN-822 AND ASP-829.
Tissue: Brain.
[2]"Organization and expression of the human zo-2 gene (tjp-2) in normal and neoplastic tissues."
Chlenski A., Ketels K.V., Korovaitseva G.I., Talamonti M.S., Oyasu R., Scarpelli D.G.
Biochim. Biophys. Acta 1493:319-324(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS A1; C1; A2 AND C2), TISSUE SPECIFICITY, ALTERNATIVE PROMOTER USAGE, VARIANT GLU-482.
Tissue: Pancreas.
[3]"LIM protein KyoT2 interacts with human tight junction protein ZO-2-i3."
Yan H.H., Rong L., Qiang S., Jian W., Peng Z., Hua H., Hui Z.W.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A3), VARIANT GLU-482.
[4]"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] (ISOFORMS 6 AND 7), VARIANTS GLU-482 AND ILE-668.
Tissue: Brain and Testis.
[5]"DNA sequence and analysis of human chromosome 9."
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. expand/collapse author list , 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.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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 A1).
Tissue: Testis.
[7]"Tight junction protein ZO-2 is differentially expressed in normal pancreatic ducts compared to human pancreatic adenocarcinoma."
Chlenski A., Ketels K.V., Tsao M.-S., Talamonti M.S., Anderson M.R., Oyasu R., Scarpelli D.G.
Int. J. Cancer 82:137-144(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-166 (ISOFORMS A1/A2/A3), NUCLEOTIDE SEQUENCE [MRNA] OF 1-119 (ISOFORMS C1/C2).
Tissue: Pancreas.
[8]"Zo-2 gene alternative promoters in normal and neoplastic human pancreatic duct cells."
Chlenski A., Ketels K.V., Engeriser J.L., Talamonti M.S., Tsao M.-S., Koutnikova H., Oyasu R., Scarpelli D.G.
Int. J. Cancer 83:349-358(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE (ISOFORMS A1 AND C1), ALTERNATIVE PROMOTER USAGE.
Tissue: Pancreas.
[9]Adams L.D., Werny I., Schwartz S.M.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1047-1167.
Tissue: Aortic smooth muscle.
[10]"hScrib interacts with ZO-2 at the cell-cell junctions of epithelial cells."
Metais J.-Y., Navarro C., Santoni M.-J., Audebert S., Borg J.-P.
FEBS Lett. 579:3725-3730(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SCRIB.
[11]"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-130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174; SER-244; SER-702; SER-966 AND SER-986, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[13]"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-170; SER-174; SER-244; SER-266; SER-400; THR-455; SER-920; THR-925; THR-933; SER-978; SER-986; SER-1067; SER-1068; THR-1131 AND SER-1159, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[15]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"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.
[17]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244 AND SER-1159, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[18]"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-130; SER-170; SER-174; SER-244; SER-920; THR-925; SER-986 AND SER-1159, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"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-130; SER-153; SER-168; SER-174; SER-200; SER-220; SER-244; SER-430; SER-978; SER-986; SER-1067; SER-1068; SER-1147 AND SER-1159, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Domain-swapped dimerization of the second PDZ domain of ZO2 may provide a structural basis for the polymerization of claudins."
Wu J., Yang Y., Zhang J., Ji P., Du W., Jiang P., Xie D., Huang H., Wu M., Zhang G., Wu J., Shi Y.
J. Biol. Chem. 282:35988-35999(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 306-385, SUBUNIT.
[21]"Complex inheritance of familial hypercholanemia with associated mutations in TJP2 and BAAT."
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.
Nat. Genet. 34:91-96(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FHCA ALA-48.
[22]"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: VARIANT [LARGE SCALE ANALYSIS] GLU-482, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L27476 mRNA. Translation: AAA61300.1. Frameshift.
AF177533 expand/collapse EMBL AC list , AF043195, AF043196, AF043197, AF177518, AF177519, AF177520, AF177521, AF177522, AF177523, AF177524, AF177525, AF177526, AF177527, AF177528, AF177529, AF177530, AF177531, AF177532 Genomic DNA. Translation: AAD20387.2.
AF177533 expand/collapse EMBL AC list , AF043196, AF043197, AF177518, AF177519, AF177520, AF177521, AF177522, AF177523, AF177524, AF177525, AF177526, AF177527, AF177528, AF177529, AF177530, AF177531, AF177532 Genomic DNA. Translation: AAC02527.2.
AF177533 expand/collapse EMBL AC list , AF043195, AF043196, AF043197, AF177518, AF177519, AF177520, AF177521, AF177522, AF177523, AF177524, AF177525, AF177526, AF177527, AF177528, AF177529, AF177532 Genomic DNA. Translation: AAD56218.2.
AF177533 expand/collapse EMBL AC list , AF043196, AF043197, AF177518, AF177519, AF177520, AF177521, AF177522, AF177523, AF177524, AF177525, AF177526, AF177527, AF177528, AF177529, AF177532 Genomic DNA. Translation: AAD56219.2.
AF489824 mRNA. Translation: AAM28524.1.
AK295034 mRNA. Translation: BAH11954.1.
AK302483 mRNA. Translation: BAH13722.1.
AL162730 Genomic DNA. No translation available.
AL358113 Genomic DNA. Translation: CAH70867.1.
AL358113 Genomic DNA. Translation: CAH70868.1.
AL358113 Genomic DNA. Translation: CAM13389.1.
AL590238 Genomic DNA. No translation available.
BC027592 mRNA. Translation: AAH27592.1.
AF083892 mRNA. Translation: AAC33121.1.
AF083893 mRNA. Translation: AAC33122.1.
U84581 mRNA. Translation: AAB41794.1.
PIRI54378.
RefSeqNP_001163886.1. NM_001170415.1.
NP_001163887.1. NM_001170416.1.
NP_001164101.1. NM_001170630.1.
NP_004808.2. NM_004817.3.
UniGeneHs.50382.
Hs.736223.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2OSGNMR-A/B306-385[»]
3E17X-ray1.75A/B306-384[»]
ProteinModelPortalQ9UDY2.
SMRQ9UDY2. Positions 21-129, 306-384, 508-887.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114809. 36 interactions.
IntActQ9UDY2. 20 interactions.
MINTMINT-1207536.
STRING9606.ENSP00000366453.

PTM databases

PhosphoSiteQ9UDY2.

Polymorphism databases

DMDM317373313.

Proteomic databases

PaxDbQ9UDY2.
PRIDEQ9UDY2.

Protocols and materials databases

DNASU9414.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265384; ENSP00000265384; ENSG00000119139. [Q9UDY2-5]
ENST00000348208; ENSP00000345893; ENSG00000119139. [Q9UDY2-2]
ENST00000377245; ENSP00000366453; ENSG00000119139. [Q9UDY2-1]
ENST00000453658; ENSP00000392178; ENSG00000119139. [Q9UDY2-4]
ENST00000535702; ENSP00000442090; ENSG00000119139. [Q9UDY2-6]
ENST00000539225; ENSP00000438262; ENSG00000119139. [Q9UDY2-7]
GeneID9414.
KEGGhsa:9414.
UCSCuc004ahd.3. human. [Q9UDY2-5]
uc004ahe.3. human. [Q9UDY2-1]
uc004ahf.3. human. [Q9UDY2-2]
uc011lrs.2. human. [Q9UDY2-4]

Organism-specific databases

CTD9414.
GeneCardsGC09P071766.
HGNCHGNC:11828. TJP2.
HPACAB009228.
HPA001813.
MIM607709. gene.
607748. phenotype.
neXtProtNX_Q9UDY2.
Orphanet90635. Autosomal dominant nonsyndromic sensorineural deafness type DFNA.
238475. Familial hypercholanemia.
PharmGKBPA36533.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG239704.
HOVERGENHBG017627.
InParanoidQ9UDY2.
KOK06098.
OMAPEPRAQM.
OrthoDBEOG7T1RB4.
PhylomeDBQ9UDY2.
TreeFamTF315957.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_578. Apoptosis.

Gene expression databases

ArrayExpressQ9UDY2.
BgeeQ9UDY2.
CleanExHS_TJP2.
GenevestigatorQ9UDY2.

Family and domain databases

Gene3D2.30.42.10. 3 hits.
3.40.50.300. 2 hits.
InterProIPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
IPR011511. SH3_2.
IPR001452. SH3_domain.
IPR005417. ZonOcculdens.
IPR005419. ZonOcculS2.
[Graphical view]
PfamPF00625. Guanylate_kin. 1 hit.
PF00595. PDZ. 3 hits.
PF07653. SH3_2. 1 hit.
[Graphical view]
PRINTSPR01597. ZONOCCLUDNS.
PR01599. ZONOCCLUDNS2.
SMARTSM00072. GuKc. 1 hit.
SM00228. PDZ. 3 hits.
SM00326. SH3. 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.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9UDY2.
GeneWikiTight_junction_protein_2.
GenomeRNAi9414.
NextBio35268.
PROQ9UDY2.
SOURCESearch...

Entry information

Entry nameZO2_HUMAN
AccessionPrimary (citable) accession number: Q9UDY2
Secondary accession number(s): A2A3H9 expand/collapse secondary AC list , B7Z2R8, B7Z7T6, F5H301, F5H886, Q15883, Q5VXL0, Q5VXL1, Q8N756, Q8NI14, Q99839, Q9UDY0, Q9UDY1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: January 11, 2011
Last modified: April 16, 2014
This is version 153 of the entry and version 2 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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM