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Protein

Tight junction protein ZO-2

Gene

TJP2

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

Functioni

Plays a role in tight junctions and adherens junctions.

GO - Molecular functioni

  • guanylate kinase activity Source: ProtInc
  • protein binding, bridging Source: UniProtKB
  • protein domain specific binding Source: UniProtKB

GO - Biological processi

  • apoptotic process Source: Reactome
  • cellular component disassembly involved in execution phase of apoptosis Source: Reactome
  • establishment of endothelial intestinal barrier Source: UniProtKB
  • hippo signaling Source: Reactome
  • intestinal absorption Source: UniProtKB
  • nucleotide phosphorylation Source: GOC
  • programmed cell death Source: Reactome
  • regulation of membrane permeability Source: UniProtKB
  • 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 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:11828. TJP2.

Subcellular locationi

GO - Cellular componenti

  • adherens junction Source: UniProtKB-SubCell
  • cell junction Source: HPA
  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • nucleoplasm Source: Reactome
  • plasma membrane Source: HPA
  • tight junction Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Involvement in diseasei

Familial hypercholanemia (FHCA)1 Publication

The disease may be caused by mutations affecting distinct genetic loci, including the gene represented in this entry.

Disease descriptionA disorder characterized by elevated serum bile acid concentrations, itching, and fat malabsorption.

See also OMIM:607748
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti48 – 481V → A in FHCA. 1 Publication
VAR_016004
Cholestasis, progressive familial intrahepatic, 4 (PFIC4)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA disorder characterized by early onset of cholestasis that progresses to hepatic fibrosis, cirrhosis, and end-stage liver disease before adulthood.

See also OMIM:615878

Keywords - Diseasei

Disease mutation, Intrahepatic cholestasis

Organism-specific databases

MIMi607748. phenotype.
615878. phenotype.
Orphaneti90635. Autosomal dominant non-syndromic sensorineural deafness type DFNA.
238475. Familial hypercholanemia.
79304. Progressive familial intrahepatic cholestasis type 2.
PharmGKBiPA36533.

Polymorphism and mutation databases

BioMutaiTJP2.
DMDMi317373313.

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 – 1301Phosphoserine4 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 residuei325 – 3251Phosphoserine1 Publication
Modified residuei400 – 4001Phosphoserine1 Publication
Modified residuei406 – 4061Phosphoserine1 Publication
Modified residuei430 – 4301Phosphoserine1 Publication
Modified residuei431 – 4311Phosphoserine1 Publication
Modified residuei455 – 4551Phosphothreonine1 Publication
Modified residuei574 – 5741PhosphotyrosineBy similarity
Modified residuei702 – 7021Phosphoserine2 Publications
Modified residuei920 – 9201Phosphoserine2 Publications
Modified residuei925 – 9251Phosphothreonine2 Publications
Modified residuei933 – 9331Phosphothreonine1 Publication
Modified residuei966 – 9661Phosphoserine2 Publications
Modified residuei978 – 9781Phosphoserine3 Publications
Modified residuei986 – 9861Phosphoserine5 Publications
Modified residuei1067 – 10671Phosphoserine2 Publications
Modified residuei1068 – 10681Phosphoserine2 Publications
Modified residuei1118 – 11181PhosphotyrosineBy similarity
Modified residuei1131 – 11311Phosphothreonine1 Publication
Modified residuei1147 – 11471Phosphoserine1 Publication
Modified residuei1159 – 11591Phosphoserine5 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

BgeeiQ9UDY2.
CleanExiHS_TJP2.
ExpressionAtlasiQ9UDY2. baseline and differential.
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. 45 interactions.
IntActiQ9UDY2. 21 interactions.
MINTiMINT-1207536.
STRINGi9606.ENSP00000366453.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OSGNMR-A/B306-385[»]
3E17X-ray1.75A/B306-384[»]
ProteinModelPortaliQ9UDY2.
SMRiQ9UDY2. Positions 21-129, 306-384, 511-887.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UDY2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 12088PDZ 1PROSITE-ProRule annotationAdd
BLAST
Domaini307 – 38579PDZ 2PROSITE-ProRule annotationAdd
BLAST
Domaini509 – 59082PDZ 3PROSITE-ProRule annotationAdd
BLAST
Domaini604 – 66966SH3PROSITE-ProRule annotationAdd
BLAST
Domaini678 – 876199Guanylate kinase-likePROSITE-ProRule annotationAdd
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.Curated
Contains 1 guanylate kinase-like domain.PROSITE-ProRule annotation
Contains 3 PDZ (DHR) domains.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiNOG239704.
GeneTreeiENSGT00640000091263.
HOGENOMiHOG000230923.
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. ZO.
IPR005419. ZO-2.
[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. AlignAdd to basket

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

        10         20         30         40         50
MPVRGDRGFP PRRELSGWLR APGMEELIWE QYTVTLQKDS KRGFGIAVSG
60 70 80 90 100
GRDNPHFENG ETSIVISDVL PGGPADGLLQ ENDRVVMVNG TPMEDVLHSF
110 120 130 140 150
AVQQLRKSGK VAAIVVKRPR KVQVAALQAS PPLDQDDRAF EVMDEFDGRS
160 170 180 190 200
FRSGYSERSR LNSHGGRSRS WEDSPERGRP HERARSRERD LSRDRSRGRS
210 220 230 240 250
LERGLDQDHA RTRDRSRGRS LERGLDHDFG PSRDRDRDRS RGRSIDQDYE
260 270 280 290 300
RAYHRAYDPD YERAYSPEYR RGARHDARSR GPRSRSREHP HSRSPSPEPR
310 320 330 340 350
GRPGPIGVLL MKSRANEEYG LRLGSQIFVK EMTRTGLATK DGNLHEGDII
360 370 380 390 400
LKINGTVTEN MSLTDARKLI EKSRGKLQLV VLRDSQQTLI NIPSLNDSDS
410 420 430 440 450
EIEDISEIES NRSFSPEERR HQYSDYDYHS SSEKLKERPS SREDTPSRLS
460 470 480 490 500
RMGATPTPFK STGDIAGTVV PETNKEPRYQ EDPPAPQPKA APRTFLRPSP
510 520 530 540 550
EDEAIYGPNT KMVRFKKGDS VGLRLAGGND VGIFVAGIQE GTSAEQEGLQ
560 570 580 590 600
EGDQILKVNT QDFRGLVRED AVLYLLEIPK GEMVTILAQS RADVYRDILA
610 620 630 640 650
CGRGDSFFIR SHFECEKETP QSLAFTRGEV FRVVDTLYDG KLGNWLAVRI
660 670 680 690 700
GNELEKGLIP NKSRAEQMAS VQNAQRDNAG DRADFWRMRG QRSGVKKNLR
710 720 730 740 750
KSREDLTAVV SVSTKFPAYE RVLLREAGFK RPVVLFGPIA DIAMEKLANE
760 770 780 790 800
LPDWFQTAKT EPKDAGSEKS TGVVRLNTVR QIIEQDKHAL LDVTPKAVDL
810 820 830 840 850
LNYTQWFPIV IFFNPDSRQG VKTMRQRLNP TSNKSSRKLF DQANKLKKTC
860 870 880 890 900
AHLFTATINL NSANDSWFGS LKDTIQHQQG EAVWVSEGKM EGMDDDPEDR
910 920 930 940 950
MSYLTAMGAD YLSCDSRLIS DFEDTDGEGG AYTDNELDEP AEEPLVSSIT
960 970 980 990 1000
RSSEPVQHEE SIRKPSPEPR AQMRRAASSD QLRDNSPPPA FKPEPPKAKT
1010 1020 1030 1040 1050
QNKEESYDFS KSYEYKSNPS AVAGNETPGA STKGYPPPVA AKPTFGRSIL
1060 1070 1080 1090 1100
KPSTPIPPQE GEEVGESSEE QDNAPKSVLG KVKIFEKMDH KARLQRMQEL
1110 1120 1130 1140 1150
QEAQNARIEI AQKHPDIYAV PIKTHKPDPG TPQHTSSRPP EPQKAPSRPY
1160 1170 1180 1190
QDTRGSYGSD AEEEEYRQQL SEHSKRGYYG QSARYRDTEL

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. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti411 – 4111N → T in AAA61300 (PubMed:7951235).Curated
Sequence conflicti411 – 4111N → T in AAM28524 (Ref. 3) Curated
Sequence conflicti718 – 7181A → V in BAH13722 (PubMed:14702039).Curated
Sequence conflicti782 – 7821I → V in AAA61300 (PubMed:7951235).Curated
Sequence conflicti782 – 7821I → V in AAM28524 (Ref. 3) Curated
Sequence conflicti808 – 8081P → S in AAA61300 (PubMed:7951235).Curated
Sequence conflicti812 – 8143FFN → SFT in AAA61300 (PubMed:7951235).Curated
Sequence conflicti834 – 8341K → N in AAA61300 (PubMed:7951235).Curated
Sequence conflicti842 – 8421Q → H in AAA61300 (PubMed:7951235).Curated
Sequence conflicti996 – 9961P → S in AAA61300 (PubMed:7951235).Curated
Sequence conflicti1093 – 10931R → G in AAA61300 (PubMed:7951235).Curated
Sequence conflicti1110 – 11101I → L in BAH13722 (PubMed:14702039).Curated
Sequence conflicti1136 – 11361S → N in AAB41794 (Ref. 9) Curated
Sequence conflicti1155 – 11584GSYG → RSFC in AAB41794 (Ref. 9) Curated
Sequence conflicti1165 – 11673EYR → IRS in AAB41794 (Ref. 9) Curated

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. CuratedVSP_006953Add
BLAST
Alternative sequencei1 – 2020MPVRG…SGWLR → MKTAQALHRMWIQAVKKLRR WKGRVSPSASSPLVFPNLSS WEGEGSKTILT in isoform 7. 1 PublicationVSP_046114Add
BLAST
Alternative sequencei1 – 1919MPVRG…LSGWL → MKTAQALHRMWIQAVKKLRR WKG in isoform 6. 1 PublicationVSP_046115Add
BLAST
Alternative sequencei961 – 1107147Missing in isoform A2 and isoform C2. CuratedVSP_003149Add
BLAST
Alternative sequencei961 – 99737Missing in isoform 6. 1 PublicationVSP_046116Add
BLAST
Alternative sequencei961 – 99333SIRKP…PAFKP → VRRGRPRAGTGEPGVFLALS WTAVCSGCCGRHS in isoform A3. 1 PublicationVSP_007835Add
BLAST
Alternative sequencei994 – 1190197Missing in isoform A3. 1 PublicationVSP_007836Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]

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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OSGNMR-A/B306-385[»]
3E17X-ray1.75A/B306-384[»]
ProteinModelPortaliQ9UDY2.
SMRiQ9UDY2. Positions 21-129, 306-384, 511-887.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114809. 45 interactions.
IntActiQ9UDY2. 21 interactions.
MINTiMINT-1207536.
STRINGi9606.ENSP00000366453.

PTM databases

PhosphoSiteiQ9UDY2.

Polymorphism and mutation databases

BioMutaiTJP2.
DMDMi317373313.

Proteomic databases

MaxQBiQ9UDY2.
PaxDbiQ9UDY2.
PRIDEiQ9UDY2.

Protocols and materials databases

DNASUi9414.
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi9414.
GeneCardsiGC09P071766.
HGNCiHGNC:11828. TJP2.
HPAiCAB009228.
HPA001813.
MIMi607709. gene.
607748. phenotype.
615878. phenotype.
neXtProtiNX_Q9UDY2.
Orphaneti90635. Autosomal dominant non-syndromic sensorineural deafness type DFNA.
238475. Familial hypercholanemia.
79304. Progressive familial intrahepatic cholestasis type 2.
PharmGKBiPA36533.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG239704.
GeneTreeiENSGT00640000091263.
HOGENOMiHOG000230923.
HOVERGENiHBG017627.
InParanoidiQ9UDY2.
KOiK06098.
OMAiPEPRAQM.
OrthoDBiEOG7T1RB4.
PhylomeDBiQ9UDY2.
TreeFamiTF315957.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiTJP2. human.
EvolutionaryTraceiQ9UDY2.
GeneWikiiTight_junction_protein_2.
GenomeRNAii9414.
NextBioi35268.
PROiQ9UDY2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UDY2.
CleanExiHS_TJP2.
ExpressionAtlasiQ9UDY2. baseline and differential.
GenevestigatoriQ9UDY2.

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. ZO.
IPR005419. ZO-2.
[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]
ProtoNetiSearch...

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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130; SER-325; SER-406; SER-431; SER-702; SER-966; SER-978; SER-986 AND SER-1159, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  21. Cited for: INVOLVEMENT IN PFIC4.
  22. "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.
  23. Cited for: VARIANT FHCA ALA-48.
  24. 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: May 27, 2015
This is version 165 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.