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Q9UDY2

- ZO2_HUMAN

UniProt

Q9UDY2 - ZO2_HUMAN

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Protein

Tight junction protein ZO-2

Gene
TJP2, X104, ZO2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Plays a role in tight junctions and adherens junctions.

GO - Molecular functioni

  1. guanylate kinase activity Source: ProtInc
  2. protein binding Source: UniProtKB

GO - Biological processi

  1. apoptotic process Source: Reactome
  2. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
  3. hippo signaling Source: Reactome
  4. nucleotide phosphorylation Source: GOC
  5. response to organic substance Source: Ensembl
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_118607. Signaling by Hippo.
REACT_13579. Apoptotic cleavage of cell adhesion proteins.

Names & Taxonomyi

Protein namesi
Recommended name:
Tight junction protein ZO-2
Alternative name(s):
Tight junction protein 2
Zona occludens protein 2
Zonula occludens protein 2
Gene namesi
Name:TJP2
Synonyms:X104, ZO2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:11828. TJP2.

Subcellular locationi

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.

GO - Cellular componenti

  1. adherens junction Source: UniProtKB-SubCell
  2. cell junction Source: HPA
  3. cytoplasm Source: HPA
  4. cytosol Source: Reactome
  5. nucleoplasm Source: Reactome
  6. plasma membrane Source: HPA
  7. tight junction Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Nucleus, Tight junction

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti48 – 481V → A in FHCA. 1 Publication
VAR_016004

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi607748. phenotype.
Orphaneti90635. Autosomal dominant nonsyndromic sensorineural deafness type DFNA.
238475. Familial hypercholanemia.
PharmGKBiPA36533.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11901190Tight junction protein ZO-2PRO_0000094543Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei130 – 1301Phosphoserine3 Publications
Modified residuei153 – 1531Phosphoserine1 Publication
Modified residuei168 – 1681Phosphoserine1 Publication
Modified residuei170 – 1701Phosphoserine2 Publications
Modified residuei174 – 1741Phosphoserine4 Publications
Modified residuei200 – 2001Phosphoserine1 Publication
Modified residuei220 – 2201Phosphoserine1 Publication
Modified residuei244 – 2441Phosphoserine5 Publications
Modified residuei266 – 2661Phosphoserine1 Publication
Modified residuei400 – 4001Phosphoserine1 Publication
Modified residuei430 – 4301Phosphoserine1 Publication
Modified residuei455 – 4551Phosphothreonine1 Publication
Modified residuei574 – 5741Phosphotyrosine By similarity
Modified residuei702 – 7021Phosphoserine1 Publication
Modified residuei920 – 9201Phosphoserine2 Publications
Modified residuei925 – 9251Phosphothreonine2 Publications
Modified residuei933 – 9331Phosphothreonine1 Publication
Modified residuei966 – 9661Phosphoserine1 Publication
Modified residuei978 – 9781Phosphoserine2 Publications
Modified residuei986 – 9861Phosphoserine4 Publications
Modified residuei1067 – 10671Phosphoserine2 Publications
Modified residuei1068 – 10681Phosphoserine2 Publications
Modified residuei1118 – 11181Phosphotyrosine By similarity
Modified residuei1131 – 11311Phosphothreonine1 Publication
Modified residuei1147 – 11471Phosphoserine1 Publication
Modified residuei1159 – 11591Phosphoserine4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UDY2.
PaxDbiQ9UDY2.
PRIDEiQ9UDY2.

PTM databases

PhosphoSiteiQ9UDY2.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

ArrayExpressiQ9UDY2.
BgeeiQ9UDY2.
CleanExiHS_TJP2.
GenevestigatoriQ9UDY2.

Organism-specific databases

HPAiCAB009228.
HPA001813.

Interactioni

Subunit structurei

Homodimer, and heterodimer with ZO1. Interacts with occludin, SAFB and UBN1. Interaction with SAFB occurs in the nucleus. Interacts with SCRIB.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
LASP1Q148479EBI-1042602,EBI-742828

Protein-protein interaction databases

BioGridi114809. 36 interactions.
IntActiQ9UDY2. 20 interactions.
MINTiMINT-1207536.
STRINGi9606.ENSP00000366453.

Structurei

Secondary structure

1
1190
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi306 – 3116
Beta strandi315 – 3173
Beta strandi321 – 33212
Helixi337 – 3415
Beta strandi349 – 3535
Helixi363 – 37210
Turni373 – 3753
Beta strandi376 – 3816

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OSGNMR-A/B306-385[»]
3E17X-ray1.75A/B306-384[»]
ProteinModelPortaliQ9UDY2.
SMRiQ9UDY2. Positions 21-129, 306-384, 508-887.

Miscellaneous databases

EvolutionaryTraceiQ9UDY2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 12088PDZ 1Add
BLAST
Domaini307 – 38579PDZ 2Add
BLAST
Domaini509 – 59082PDZ 3Add
BLAST
Domaini604 – 66966SH3Add
BLAST
Domaini678 – 876199Guanylate kinase-likeAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1188 – 11903Interaction with SCRIB

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1162 – 11654Poly-Glu

Sequence similaritiesi

Belongs to the MAGUK family.
Contains 3 PDZ (DHR) domains.
Contains 1 SH3 domain.

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiNOG239704.
HOVERGENiHBG017627.
InParanoidiQ9UDY2.
KOiK06098.
OMAiPEPRAQM.
OrthoDBiEOG7T1RB4.
PhylomeDBiQ9UDY2.
TreeFamiTF315957.

Family and domain databases

Gene3Di2.30.42.10. 3 hits.
3.40.50.300. 2 hits.
InterProiIPR008145. 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]
PfamiPF00625. Guanylate_kin. 1 hit.
PF00595. PDZ. 3 hits.
PF07653. SH3_2. 1 hit.
[Graphical view]
PRINTSiPR01597. ZONOCCLUDNS.
PR01599. ZONOCCLUDNS2.
SMARTiSM00072. GuKc. 1 hit.
SM00228. PDZ. 3 hits.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF50156. SSF50156. 3 hits.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50052. GUANYLATE_KINASE_2. 1 hit.
PS50106. PDZ. 3 hits.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (7)i

Sequence statusi: Complete.

This entry describes 7 isoformsi produced by alternative promoter usage and alternative splicing. Align

Isoform A1 (identifier: Q9UDY2-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MPVRGDRGFP PRRELSGWLR APGMEELIWE QYTVTLQKDS KRGFGIAVSG     50
GRDNPHFENG ETSIVISDVL PGGPADGLLQ ENDRVVMVNG TPMEDVLHSF 100
AVQQLRKSGK VAAIVVKRPR KVQVAALQAS PPLDQDDRAF EVMDEFDGRS 150
FRSGYSERSR LNSHGGRSRS WEDSPERGRP HERARSRERD LSRDRSRGRS 200
LERGLDQDHA RTRDRSRGRS LERGLDHDFG PSRDRDRDRS RGRSIDQDYE 250
RAYHRAYDPD YERAYSPEYR RGARHDARSR GPRSRSREHP HSRSPSPEPR 300
GRPGPIGVLL MKSRANEEYG LRLGSQIFVK EMTRTGLATK DGNLHEGDII 350
LKINGTVTEN MSLTDARKLI EKSRGKLQLV VLRDSQQTLI NIPSLNDSDS 400
EIEDISEIES NRSFSPEERR HQYSDYDYHS SSEKLKERPS SREDTPSRLS 450
RMGATPTPFK STGDIAGTVV PETNKEPRYQ EDPPAPQPKA APRTFLRPSP 500
EDEAIYGPNT KMVRFKKGDS VGLRLAGGND VGIFVAGIQE GTSAEQEGLQ 550
EGDQILKVNT QDFRGLVRED AVLYLLEIPK GEMVTILAQS RADVYRDILA 600
CGRGDSFFIR SHFECEKETP QSLAFTRGEV FRVVDTLYDG KLGNWLAVRI 650
GNELEKGLIP NKSRAEQMAS VQNAQRDNAG DRADFWRMRG QRSGVKKNLR 700
KSREDLTAVV SVSTKFPAYE RVLLREAGFK RPVVLFGPIA DIAMEKLANE 750
LPDWFQTAKT EPKDAGSEKS TGVVRLNTVR QIIEQDKHAL LDVTPKAVDL 800
LNYTQWFPIV IFFNPDSRQG VKTMRQRLNP TSNKSSRKLF DQANKLKKTC 850
AHLFTATINL NSANDSWFGS LKDTIQHQQG EAVWVSEGKM EGMDDDPEDR 900
MSYLTAMGAD YLSCDSRLIS DFEDTDGEGG AYTDNELDEP AEEPLVSSIT 950
RSSEPVQHEE SIRKPSPEPR AQMRRAASSD QLRDNSPPPA FKPEPPKAKT 1000
QNKEESYDFS KSYEYKSNPS AVAGNETPGA STKGYPPPVA AKPTFGRSIL 1050
KPSTPIPPQE GEEVGESSEE QDNAPKSVLG KVKIFEKMDH KARLQRMQEL 1100
QEAQNARIEI AQKHPDIYAV PIKTHKPDPG TPQHTSSRPP EPQKAPSRPY 1150
QDTRGSYGSD AEEEEYRQQL SEHSKRGYYG QSARYRDTEL 1190

Note: Produced by alternative promoter usage.

Length:1,190
Mass (Da):133,958
Last modified:January 11, 2011 - v2
Checksum:i27305B723043BF6C
GO
Isoform A2 (identifier: Q9UDY2-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     961-1107: Missing.

Note: Produced by alternative splicing of isoform A1.

Show »
Length:1,043
Mass (Da):117,758
Checksum:i6EE97CE690160E91
GO
Isoform A3 (identifier: Q9UDY2-5) [UniParc]FASTAAdd to Basket

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.

Show »
Length:993
Mass (Da):111,663
Checksum:iD469C9A73851A6D3
GO
Isoform C1 (identifier: Q9UDY2-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: Missing.

Note: Produced by alternative promoter usage.

Show »
Length:1,167
Mass (Da):131,368
Checksum:i91F7D588687D179E
GO
Isoform C2 (identifier: Q9UDY2-4) [UniParc]FASTAAdd to Basket

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.

Show »
Length:1,020
Mass (Da):115,168
Checksum:i4A49BF3F0718D771
GO
Isoform 6 (identifier: Q9UDY2-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-19: MPVRGDRGFPPRRELSGWL → MKTAQALHRMWIQAVKKLRRWKG
     961-997: Missing.

Note: No experimental confirmation available.

Show »
Length:1,157
Mass (Da):130,446
Checksum:i30C98BC65E29BC85
GO
Isoform 7 (identifier: Q9UDY2-7) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: MPVRGDRGFPPRRELSGWLR → MKTAQALHRMWIQAVKKLRRWKGRVSPSASSPLVFPNLSSWEGEGSKTILT

Note: No experimental confirmation available.

Show »
Length:1,221
Mass (Da):137,342
Checksum:iE185339B2A2F37B4
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti48 – 481V → A in FHCA. 1 Publication
VAR_016004
Natural varianti482 – 4821D → E.5 Publications
Corresponds to variant rs2309428 [ dbSNP | Ensembl ].
VAR_030798
Natural varianti668 – 6681M → I.1 Publication
Corresponds to variant rs34774441 [ dbSNP | Ensembl ].
VAR_046675
Natural varianti711 – 7111S → P.
Corresponds to variant rs35797487 [ dbSNP | Ensembl ].
VAR_046676
Natural varianti822 – 8221K → N.1 Publication
Corresponds to variant rs1049624 [ dbSNP | Ensembl ].
VAR_046677
Natural varianti829 – 8291N → D.1 Publication
Corresponds to variant rs1049625 [ dbSNP | Ensembl ].
VAR_046678

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2323Missing in isoform C1 and isoform C2. VSP_006953Add
BLAST
Alternative sequencei1 – 2020MPVRG…SGWLR → MKTAQALHRMWIQAVKKLRR WKGRVSPSASSPLVFPNLSS WEGEGSKTILT in isoform 7. VSP_046114Add
BLAST
Alternative sequencei1 – 1919MPVRG…LSGWL → MKTAQALHRMWIQAVKKLRR WKG in isoform 6. VSP_046115Add
BLAST
Alternative sequencei961 – 1107147Missing in isoform A2 and isoform C2. VSP_003149Add
BLAST
Alternative sequencei961 – 99737Missing in isoform 6. VSP_046116Add
BLAST
Alternative sequencei961 – 99333SIRKP…PAFKP → VRRGRPRAGTGEPGVFLALS WTAVCSGCCGRHS in isoform A3. VSP_007835Add
BLAST
Alternative sequencei994 – 1190197Missing in isoform A3. VSP_007836Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti411 – 4111N → T in AAA61300. 1 Publication
Sequence conflicti411 – 4111N → T in AAM28524. 1 Publication
Sequence conflicti718 – 7181A → V in BAH13722. 1 Publication
Sequence conflicti782 – 7821I → V in AAA61300. 1 Publication
Sequence conflicti782 – 7821I → V in AAM28524. 1 Publication
Sequence conflicti808 – 8081P → S in AAA61300. 1 Publication
Sequence conflicti812 – 8143FFN → SFT in AAA61300. 1 Publication
Sequence conflicti834 – 8341K → N in AAA61300. 1 Publication
Sequence conflicti842 – 8421Q → H in AAA61300. 1 Publication
Sequence conflicti996 – 9961P → S in AAA61300. 1 Publication
Sequence conflicti1093 – 10931R → G in AAA61300. 1 Publication
Sequence conflicti1110 – 11101I → L in BAH13722. 1 Publication
Sequence conflicti1136 – 11361S → N in AAB41794. 1 Publication
Sequence conflicti1155 – 11584GSYG → RSFC in AAB41794. 1 Publication
Sequence conflicti1165 – 11673EYR → IRS in AAB41794. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L27476 mRNA. Translation: AAA61300.1. Frameshift.
AF177533
, AF043195, AF043196, AF043197, AF177518, AF177519, AF177520, AF177521, AF177522, AF177523, AF177524, AF177525, AF177526, AF177527, AF177528, AF177529, AF177530, AF177531, AF177532 Genomic DNA. Translation: AAD20387.2.
AF177533
, AF043196, AF043197, AF177518, AF177519, AF177520, AF177521, AF177522, AF177523, AF177524, AF177525, AF177526, AF177527, AF177528, AF177529, AF177530, AF177531, AF177532 Genomic DNA. Translation: AAC02527.2.
AF177533
, AF043195, AF043196, AF043197, AF177518, AF177519, AF177520, AF177521, AF177522, AF177523, AF177524, AF177525, AF177526, AF177527, AF177528, AF177529, AF177532 Genomic DNA. Translation: AAD56218.2.
AF177533
, 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.
CCDSiCCDS55314.1. [Q9UDY2-5]
CCDS55315.1. [Q9UDY2-6]
CCDS55316.1. [Q9UDY2-7]
CCDS55317.1. [Q9UDY2-4]
CCDS6627.1. [Q9UDY2-1]
CCDS6628.1. [Q9UDY2-2]
PIRiI54378.
RefSeqiNP_001163886.1. NM_001170415.1. [Q9UDY2-6]
NP_001163887.1. NM_001170416.1. [Q9UDY2-7]
NP_001164101.1. NM_001170630.1. [Q9UDY2-5]
NP_004808.2. NM_004817.3. [Q9UDY2-1]
UniGeneiHs.50382.
Hs.736223.

Genome annotation databases

EnsembliENST00000265384; 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]
GeneIDi9414.
KEGGihsa:9414.
UCSCiuc004ahd.3. human. [Q9UDY2-5]
uc004ahe.3. human. [Q9UDY2-1]
uc004ahf.3. human. [Q9UDY2-2]
uc011lrs.2. human. [Q9UDY2-4]

Polymorphism databases

DMDMi317373313.

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L27476 mRNA. Translation: AAA61300.1 . Frameshift.
AF177533
, AF043195 , AF043196 , AF043197 , AF177518 , AF177519 , AF177520 , AF177521 , AF177522 , AF177523 , AF177524 , AF177525 , AF177526 , AF177527 , AF177528 , AF177529 , AF177530 , AF177531 , AF177532 Genomic DNA. Translation: AAD20387.2 .
AF177533
, AF043196 , AF043197 , AF177518 , AF177519 , AF177520 , AF177521 , AF177522 , AF177523 , AF177524 , AF177525 , AF177526 , AF177527 , AF177528 , AF177529 , AF177530 , AF177531 , AF177532 Genomic DNA. Translation: AAC02527.2 .
AF177533
, AF043195 , AF043196 , AF043197 , AF177518 , AF177519 , AF177520 , AF177521 , AF177522 , AF177523 , AF177524 , AF177525 , AF177526 , AF177527 , AF177528 , AF177529 , AF177532 Genomic DNA. Translation: AAD56218.2 .
AF177533
, 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 .
CCDSi CCDS55314.1. [Q9UDY2-5 ]
CCDS55315.1. [Q9UDY2-6 ]
CCDS55316.1. [Q9UDY2-7 ]
CCDS55317.1. [Q9UDY2-4 ]
CCDS6627.1. [Q9UDY2-1 ]
CCDS6628.1. [Q9UDY2-2 ]
PIRi I54378.
RefSeqi NP_001163886.1. NM_001170415.1. [Q9UDY2-6 ]
NP_001163887.1. NM_001170416.1. [Q9UDY2-7 ]
NP_001164101.1. NM_001170630.1. [Q9UDY2-5 ]
NP_004808.2. NM_004817.3. [Q9UDY2-1 ]
UniGenei Hs.50382.
Hs.736223.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2OSG NMR - A/B 306-385 [» ]
3E17 X-ray 1.75 A/B 306-384 [» ]
ProteinModelPortali Q9UDY2.
SMRi Q9UDY2. Positions 21-129, 306-384, 508-887.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114809. 36 interactions.
IntActi Q9UDY2. 20 interactions.
MINTi MINT-1207536.
STRINGi 9606.ENSP00000366453.

PTM databases

PhosphoSitei Q9UDY2.

Polymorphism databases

DMDMi 317373313.

Proteomic databases

MaxQBi Q9UDY2.
PaxDbi Q9UDY2.
PRIDEi Q9UDY2.

Protocols and materials databases

DNASUi 9414.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000265384 ; 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 ]
GeneIDi 9414.
KEGGi hsa:9414.
UCSCi uc004ahd.3. human. [Q9UDY2-5 ]
uc004ahe.3. human. [Q9UDY2-1 ]
uc004ahf.3. human. [Q9UDY2-2 ]
uc011lrs.2. human. [Q9UDY2-4 ]

Organism-specific databases

CTDi 9414.
GeneCardsi GC09P071766.
HGNCi HGNC:11828. TJP2.
HPAi CAB009228.
HPA001813.
MIMi 607709. gene.
607748. phenotype.
neXtProti NX_Q9UDY2.
Orphaneti 90635. Autosomal dominant nonsyndromic sensorineural deafness type DFNA.
238475. Familial hypercholanemia.
PharmGKBi PA36533.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG239704.
HOVERGENi HBG017627.
InParanoidi Q9UDY2.
KOi K06098.
OMAi PEPRAQM.
OrthoDBi EOG7T1RB4.
PhylomeDBi Q9UDY2.
TreeFami TF315957.

Enzyme and pathway databases

Reactomei REACT_118607. Signaling by Hippo.
REACT_13579. Apoptotic cleavage of cell adhesion proteins.

Miscellaneous databases

EvolutionaryTracei Q9UDY2.
GeneWikii Tight_junction_protein_2.
GenomeRNAii 9414.
NextBioi 35268.
PROi Q9UDY2.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9UDY2.
Bgeei Q9UDY2.
CleanExi HS_TJP2.
Genevestigatori Q9UDY2.

Family and domain databases

Gene3Di 2.30.42.10. 3 hits.
3.40.50.300. 2 hits.
InterProi IPR008145. 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 ]
Pfami PF00625. Guanylate_kin. 1 hit.
PF00595. PDZ. 3 hits.
PF07653. SH3_2. 1 hit.
[Graphical view ]
PRINTSi PR01597. ZONOCCLUDNS.
PR01599. ZONOCCLUDNS2.
SMARTi SM00072. GuKc. 1 hit.
SM00228. PDZ. 3 hits.
SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
SSF50156. SSF50156. 3 hits.
SSF52540. SSF52540. 1 hit.
PROSITEi PS50052. GUANYLATE_KINASE_2. 1 hit.
PS50106. PDZ. 3 hits.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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. Cited for: VARIANT FHCA ALA-48.
  22. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLU-482, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiZO2_HUMAN
AccessioniPrimary (citable) accession number: Q9UDY2
Secondary accession number(s): A2A3H9
, B7Z2R8, B7Z7T6, F5H301, F5H886, Q15883, Q5VXL0, Q5VXL1, Q8N756, Q8NI14, Q99839, Q9UDY0, Q9UDY1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: January 11, 2011
Last modified: September 3, 2014
This is version 157 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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