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Reviewed, UniProtKB/Swiss-Prot Q9UDY2 (ZO2_HUMAN)

Last modified September 2, 2008. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | 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

Names and origin

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

Protein attributes

Sequence length1190 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Plays a role in tight junctions and adherens junctions.

Subunit structure

Interacts with occludin and SAFB. Interaction with SAFB occurs in the nucleus.

Subcellular location

Cell junctionadherens junction. Cell membrane; Peripheral membrane protein; Cytoplasmic sideBy similarity. Cell junctiontight junctionBy similarity. NucleusBy 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 whereas isoform C1 is expressed at high level in the kidney, pancreas, heart and placenta. In brain and skeletal muscle, only isoform A1 is detectable. Isoform C1 is found in normal as well as in most neoplastic tissues while isoform A1 is present almost exclusively in normal tissue.

Involvement in disease

Defects in TJP2 are involved in familial hypercholanemia (FHCA) [MIM:607748]. FHCA is a disorder characterized by elevated serum bile acid concentrations, itching, and fat malabsorption.

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.

Ontologies

Alternative products

This entry describes 5 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.
Notes: Produced by alternative promoter usage.
Isoform A2 (identifier: Q9UDY2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     961-1108: Missing.
Notes: 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.
Notes: 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.
Notes: 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.
     961-1108: Missing.
Notes: Produced by alternative splicing of isoform C1.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Chain1 – 11901190Tight junction protein ZO-2

Regions

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

Amino acid modifications

Modified residue1301Phosphoserine
Modified residue1681Phosphoserine
Modified residue1701Phosphoserine
Modified residue1741Phosphoserine
Modified residue1921Phosphoserine
Modified residue2441Phosphoserine
Modified residue2611Phosphotyrosine
Modified residue2651Phosphotyrosine By similarity
Modified residue2661Phosphoserine
Modified residue2961Phosphoserine
Modified residue3941Phosphoserine
Modified residue3981Phosphoserine
Modified residue4001Phosphoserine
Modified residue4151Phosphoserine
Modified residue4401Phosphoserine
Modified residue4411Phosphoserine
Modified residue4451Phosphothreonine
Modified residue5741Phosphotyrosine
Modified residue7021Phosphoserine
Modified residue9661Phosphoserine
Modified residue9781Phosphoserine
Modified residue9861Phosphoserine
Modified residue11181Phosphotyrosine
Modified residue11311Phosphothreonine
Modified residue11591Phosphoserine

Natural variations

Alternative sequence1 – 2323Missing in isoform C1 and isoform C2.
Alternative sequence961 – 1108148Missing in isoform A2 and isoform C2.
Alternative sequence961 – 99333SIRKP…PAFKP → VRRGRPRAGTGEPGVFLALS WTAVCSGCCGRHS in isoform A3.
Alternative sequence994 – 1190197Missing in isoform A3.
Natural variant481V → A in FHCA.
Natural variant4821E → D: dbSNP rs2309428.

Experimental info

Sequence conflict4111N → T in AAA61300. Ref.1
Sequence conflict4111N → T in AAM28524. Ref.3
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 conflict8221K → N in AAA61300. Ref.1
Sequence conflict8291N → D 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 conflict11361S → N in AAB41794. Ref.8
Sequence conflict1155 – 11584GSYG → RSFC in AAB41794. Ref.8
Sequence conflict1165 – 11673EYR → IRS Ref.8

Sequences

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

Last modified May 1, 2000. Version 1.
Checksum: BE2BE6F181467058

FASTA1,190133,972
        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 
EEPPAPQPKA 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: ECBAD3D0FA2BF09C
Show »

1,042117,659
Isoform A3 [UniParc].

Checksum: 9A6279A73851A6D3
Show »

993111,677
Isoform C1 [UniParc].

Checksum: 08EC680BD978D8AA
Show »

1,167131,382
Isoform C2 [UniParc].

Checksum: DC790A47F4F210A3
Show »

1,019115,069

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: 7951235] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A1).
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: 11018256] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS A1; C1; A2 AND C2), ALTERNATIVE PROMOTER USAGE.
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).
[4]"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.,