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Q9Z0U1

- ZO2_MOUSE

UniProt

Q9Z0U1 - ZO2_MOUSE

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Protein
Tight junction protein ZO-2
Gene
Tjp2, Zo2
Organism
Mus musculus (Mouse)
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. protein binding Source: UniProtKB

GO - Biological processi

  1. response to organic substance Source: Ensembl
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_196537. Signaling by Hippo.

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:Zo2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 19

Organism-specific databases

MGIiMGI:1341872. Tjp2.

Subcellular locationi

Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Nucleus By similarity. Cell junctiontight junction By similarity
Note: Also nuclear under environmental stress conditions and in migratory endothelial cells and subconfluent epithelial cell cultures By similarity.1 Publication

GO - Cellular componenti

  1. cell junction Source: MGI
  2. cytoplasm Source: Ensembl
  3. nucleus Source: UniProtKB-SubCell
  4. plasma membrane Source: MGI
  5. tight junction Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11671167Tight junction protein ZO-2
PRO_0000094544Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei107 – 1071Phosphoserine3 Publications
Modified residuei130 – 1301Phosphoserine By similarity
Modified residuei145 – 1451Phosphoserine By similarity
Modified residuei147 – 1471Phosphoserine By similarity
Modified residuei173 – 1731Phosphoserine By similarity
Modified residuei194 – 1941Phosphoserine By similarity
Modified residuei239 – 2391Phosphoserine By similarity
Modified residuei380 – 3801Phosphoserine By similarity
Modified residuei410 – 4101Phosphoserine By similarity
Modified residuei435 – 4351Phosphothreonine By similarity
Modified residuei554 – 5541Phosphotyrosine1 Publication
Modified residuei684 – 6841Phosphoserine By similarity
Modified residuei902 – 9021Phosphoserine By similarity
Modified residuei907 – 9071Phosphothreonine By similarity
Modified residuei915 – 9151Phosphothreonine By similarity
Modified residuei948 – 9481Phosphoserine By similarity
Modified residuei960 – 9601Phosphoserine By similarity
Modified residuei968 – 9681Phosphoserine1 Publication
Modified residuei1044 – 10441Phosphoserine By similarity
Modified residuei1095 – 10951Phosphotyrosine1 Publication
Modified residuei1124 – 11241Phosphoserine By similarity
Modified residuei1136 – 11361Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9Z0U1.
PaxDbiQ9Z0U1.
PRIDEiQ9Z0U1.

PTM databases

PhosphoSiteiQ9Z0U1.

Expressioni

Gene expression databases

BgeeiQ9Z0U1.
CleanExiMM_TJP2.
GenevestigatoriQ9Z0U1.

Interactioni

Subunit structurei

Homodimer, and heterodimer with ZO1. Interacts with UBN1. Interacts with SCRIB By similarity. Interacts with occludin and SAFB. Interaction with SAFB occurs in the nucleus.1 Publication

Protein-protein interaction databases

BioGridi204210. 3 interactions.
IntActiQ9Z0U1. 3 interactions.
MINTiMINT-113156.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 1411
Beta strandi17 – 193
Beta strandi23 – 264
Beta strandi42 – 465
Helixi52 – 554
Beta strandi61 – 677
Helixi75 – 8410
Beta strandi87 – 9812

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CSJNMR-A1-104[»]
ProteinModelPortaliQ9Z0U1.
SMRiQ9Z0U1. Positions 1-106, 286-364, 488-869.

Miscellaneous databases

EvolutionaryTraceiQ9Z0U1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 9788PDZ 1
Add
BLAST
Domaini287 – 36579PDZ 2
Add
BLAST
Domaini489 – 57082PDZ 3
Add
BLAST
Domaini584 – 64966SH3
Add
BLAST
Domaini660 – 858199Guanylate kinase-like
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1165 – 11673Interaction with SCRIB By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1139 – 11424Poly-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.
GeneTreeiENSGT00640000091263.
HOGENOMiHOG000230923.
HOVERGENiHBG017627.
InParanoidiQ9Z0U1.
KOiK06098.
OMAiPEPRAQM.
OrthoDBiEOG7T1RB4.
PhylomeDBiQ9Z0U1.
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]

Sequencei

Sequence statusi: Complete.

Q9Z0U1-1 [UniParc]FASTAAdd to Basket

« Hide

MEEVIWEQYT VTLQKDSKRG FGIAVSGGRD NPHFENGETS IVISDVLPGG     50
PADGLLQEND RVVMVNGTPM EDVLHSFAVQ QLRKSGKIAA IVVKRPRKVQ 100
VAPLQGSPPL SHDDRGFEVI EEFDGRSFRS GYSERSRHSS HDMLSHSWEG 150
NRERGRPHQR TQSRERERSR GRSLERGLDQ EDYGRSRERS RGRSLERGLD 200
RDFVSRDHSR GRSIDRDYDR DYERSYHEAY EPDYGGGYSP SYDRRAHPET 250
RYERSRSREH LRSRSPSPES RSRHEHKGQH DPDRPIGVLL TKSKANEEYG 300
LRLGSQIFIK EMTRTGLATK DGNLHEGDII LKINGTVTEN MSLTDARKLI 350
EKSRGKLQLV VLRDSKQTLI NIPALNDSDS EVEDISEIES NRSFSPEERR 400
QQYSDQDYHS STEKLKERPS SREETSGRLS RMGATPTPFK STGDITAAGV 450
TEASREPRYQ EEGPVPQPRT APRVFLRPSP EDEAIYGPNT KMVRFKKGDS 500
VGLRLAGGND VGIFVAGIQE GTSAEQEGLQ EGDQILKVNT QDFRGLVRED 550
AVLYLLEIPK GETVTILAQS RADVYRDILA CGRGDSFFIR SHFECEKETP 600
QSLAFTRGEV FRVVDTLYDG KLGHWLAVRI GNELEKGLIP NKSRAEQMAS 650
VQNAQRENAG DRADFWRMRG QRSSGGVKKN LRKSREDLAA AVSVSTKFPA 700
YEKVLLREAG FKRPVVLFGP IADIAMERLA TELPDLFQTA KTEPKDAGSE 750
KSSGVVRLNT VRQIIEQDKH ALLDVTPKAV DLLNYTQWFP IVIFFNPDSR 800
QGVKTIRQRL SPTSNKSSRK LFDQANKLKK TCSHLFTATI NVNSANDGWF 850
GSLKDSIQQQ QNEAVWVSEG KMEGMDDDAE DRMSYLTAMG ADYLSCDSRL 900
ISDFEDTDGE GGAYTDNELE EPAEEPLVSS ITRSSEPVQH EENIRKSSPE 950
PRAQMRRAAS RDQLRDASPP PAFKPEPPKA RSQNREDSFD YSKSNLPATA 1000
GSEIPGGSTK GYPPPIAAKP AFGRPILKPS TPVPMPESEE VGESTEEQED 1050
APRSVLGRVK IFEKMDHKAK LQRMQELQEA QNARIEIAQK HPDIYAVPIK 1100
APKPDAGLPP HMSSRPPEPQ KAPSRLYQDT RGSYGSDPEE EEYRQQLAAH 1150
SKRGYYSQPS RYRDTEL 1167
Length:1,167
Mass (Da):131,280
Last modified:May 2, 2006 - v2
Checksum:iC29AF94F423A3A70
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti100 – 1001Q → L in AAD19964. 1 Publication
Sequence conflicti105 – 1073QGS → LGC in AAD19964. 1 Publication
Sequence conflicti111 – 1122SH → CL in AAD19964. 1 Publication
Sequence conflicti156 – 1561R → G in AAD19964. 1 Publication
Sequence conflicti292 – 2921K → Q in AAD19964. 1 Publication
Sequence conflicti378 – 3781S → R in AAD19964. 1 Publication
Sequence conflicti447 – 4471A → P in AAD19964. 1 Publication
Sequence conflicti454 – 4541S → T in AAD19964. 1 Publication
Sequence conflicti470 – 4701T → A in AAD19964. 1 Publication
Sequence conflicti506 – 5061A → P in AAD19964. 1 Publication
Sequence conflicti633 – 6331E → D in AAD19964. 1 Publication
Sequence conflicti649 – 6491A → D in AAD19964. 1 Publication
Sequence conflicti664 – 6641D → V in AAD19964. 1 Publication
Sequence conflicti667 – 6671R → W in AAD19964. 1 Publication
Sequence conflicti670 – 6701G → R in AAD19964. 1 Publication
Sequence conflicti674 – 6741S → R in AAD19964. 1 Publication
Sequence conflicti677 – 6771V → D in AAD19964. 1 Publication
Sequence conflicti680 – 6801N → T in AAD19964. 1 Publication
Sequence conflicti690 – 6912AA → RS in AAD19964. 1 Publication
Sequence conflicti731 – 7311T → N in AAD19964. 1 Publication
Sequence conflicti1035 – 10351M → I in AAD19964. 1 Publication
Sequence conflicti1038 – 10381S → T in AAD19964. 1 Publication
Sequence conflicti1069 – 10691A → P in AAD19964. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF113005 mRNA. Translation: AAD19964.1.
BC034677 mRNA. Translation: AAH34677.1.
BC039924 mRNA. Translation: AAH39924.1.
CCDSiCCDS37939.1.
RefSeqiNP_035727.2. NM_011597.4.
XP_006526971.1. XM_006526908.1.
UniGeneiMm.104744.

Genome annotation databases

EnsembliENSMUST00000099558; ENSMUSP00000097154; ENSMUSG00000024812.
GeneIDi21873.
KEGGimmu:21873.
UCSCiuc008ham.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF113005 mRNA. Translation: AAD19964.1 .
BC034677 mRNA. Translation: AAH34677.1 .
BC039924 mRNA. Translation: AAH39924.1 .
CCDSi CCDS37939.1.
RefSeqi NP_035727.2. NM_011597.4.
XP_006526971.1. XM_006526908.1.
UniGenei Mm.104744.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2CSJ NMR - A 1-104 [» ]
ProteinModelPortali Q9Z0U1.
SMRi Q9Z0U1. Positions 1-106, 286-364, 488-869.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204210. 3 interactions.
IntActi Q9Z0U1. 3 interactions.
MINTi MINT-113156.

PTM databases

PhosphoSitei Q9Z0U1.

Proteomic databases

MaxQBi Q9Z0U1.
PaxDbi Q9Z0U1.
PRIDEi Q9Z0U1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000099558 ; ENSMUSP00000097154 ; ENSMUSG00000024812 .
GeneIDi 21873.
KEGGi mmu:21873.
UCSCi uc008ham.2. mouse.

Organism-specific databases

CTDi 9414.
MGIi MGI:1341872. Tjp2.

Phylogenomic databases

eggNOGi NOG239704.
GeneTreei ENSGT00640000091263.
HOGENOMi HOG000230923.
HOVERGENi HBG017627.
InParanoidi Q9Z0U1.
KOi K06098.
OMAi PEPRAQM.
OrthoDBi EOG7T1RB4.
PhylomeDBi Q9Z0U1.
TreeFami TF315957.

Enzyme and pathway databases

Reactomei REACT_196537. Signaling by Hippo.

Miscellaneous databases

ChiTaRSi TJP2. mouse.
EvolutionaryTracei Q9Z0U1.
NextBioi 301380.
PROi Q9Z0U1.
SOURCEi Search...

Gene expression databases

Bgeei Q9Z0U1.
CleanExi MM_TJP2.
Genevestigatori Q9Z0U1.

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. "Characterization of ZO-2 as a MAGUK family member associated with tight as well as adherens junctions with a binding affinity to occludin and alpha catenin."
    Itoh M., Morita K., Tsukita S.
    J. Biol. Chem. 274:5981-5986(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6 X CBA.
  2. "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].
    Strain: 129.
    Tissue: Mammary gland.
  3. "The tight junction protein ZO-2 localizes to the nucleus and interacts with the heterogeneous nuclear ribonucleoprotein scaffold attachment factor-B."
    Traweger A., Fuchs R., Krizbai I.A., Weiger T.M., Bauer H.-C., Bauer H.
    J. Biol. Chem. 278:2692-2700(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SAFB.
  4. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-554, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1136, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-968 AND TYR-1095, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  10. "Solution structure of N-terminal PDZ domain from mouse TJP2."
    RIKEN structural genomics initiative (RSGI)
    Submitted (MAY-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 1-106.

Entry informationi

Entry nameiZO2_MOUSE
AccessioniPrimary (citable) accession number: Q9Z0U1
Secondary accession number(s): Q8K210
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 2, 2006
Last modified: September 3, 2014
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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