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Q9Z0U1 (ZO2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tight junction protein ZO-2
Alternative name(s):
Tight junction protein 2
Zona occludens protein 2
Zonula occludens protein 2
Gene names
Name:Tjp2
Synonyms:Zo2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1167 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in tight junctions and adherens junctions.

Subunit structure

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

Subcellular location

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. Ref.3

Sequence similarities

Belongs to the MAGUK family.

Contains 1 guanylate kinase-like domain.

Contains 3 PDZ (DHR) domains.

Contains 1 SH3 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11671167Tight junction protein ZO-2
PRO_0000094544

Regions

Domain10 – 9788PDZ 1
Domain287 – 36579PDZ 2
Domain489 – 57082PDZ 3
Domain584 – 64966SH3
Domain660 – 858199Guanylate kinase-like
Region1165 – 11673Interaction with SCRIB By similarity
Compositional bias1139 – 11424Poly-Glu

Amino acid modifications

Modified residue1071Phosphoserine Ref.5 Ref.7 Ref.8
Modified residue1301Phosphoserine By similarity
Modified residue1451Phosphoserine By similarity
Modified residue1471Phosphoserine By similarity
Modified residue1731Phosphoserine By similarity
Modified residue1941Phosphoserine By similarity
Modified residue2391Phosphoserine By similarity
Modified residue3801Phosphoserine By similarity
Modified residue4101Phosphoserine By similarity
Modified residue4351Phosphothreonine By similarity
Modified residue5541Phosphotyrosine Ref.4
Modified residue6841Phosphoserine By similarity
Modified residue9021Phosphoserine By similarity
Modified residue9071Phosphothreonine By similarity
Modified residue9151Phosphothreonine By similarity
Modified residue9481Phosphoserine By similarity
Modified residue9601Phosphoserine By similarity
Modified residue9681Phosphoserine Ref.9
Modified residue10441Phosphoserine By similarity
Modified residue10951Phosphotyrosine Ref.9
Modified residue11241Phosphoserine By similarity
Modified residue11361Phosphoserine Ref.6

Experimental info

Sequence conflict1001Q → L in AAD19964. Ref.1
Sequence conflict105 – 1073QGS → LGC in AAD19964. Ref.1
Sequence conflict111 – 1122SH → CL in AAD19964. Ref.1
Sequence conflict1561R → G in AAD19964. Ref.1
Sequence conflict2921K → Q in AAD19964. Ref.1
Sequence conflict3781S → R in AAD19964. Ref.1
Sequence conflict4471A → P in AAD19964. Ref.1
Sequence conflict4541S → T in AAD19964. Ref.1
Sequence conflict4701T → A in AAD19964. Ref.1
Sequence conflict5061A → P in AAD19964. Ref.1
Sequence conflict6331E → D in AAD19964. Ref.1
Sequence conflict6491A → D in AAD19964. Ref.1
Sequence conflict6641D → V in AAD19964. Ref.1
Sequence conflict6671R → W in AAD19964. Ref.1
Sequence conflict6701G → R in AAD19964. Ref.1
Sequence conflict6741S → R in AAD19964. Ref.1
Sequence conflict6771V → D in AAD19964. Ref.1
Sequence conflict6801N → T in AAD19964. Ref.1
Sequence conflict690 – 6912AA → RS in AAD19964. Ref.1
Sequence conflict7311T → N in AAD19964. Ref.1
Sequence conflict10351M → I in AAD19964. Ref.1
Sequence conflict10381S → T in AAD19964. Ref.1
Sequence conflict10691A → P in AAD19964. Ref.1

Secondary structure

................. 1167
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9Z0U1 [UniParc].

Last modified May 2, 2006. Version 2.
Checksum: C29AF94F423A3A70

FASTA1,167131,280
        10         20         30         40         50         60 
MEEVIWEQYT VTLQKDSKRG FGIAVSGGRD NPHFENGETS IVISDVLPGG PADGLLQEND 

        70         80         90        100        110        120 
RVVMVNGTPM EDVLHSFAVQ QLRKSGKIAA IVVKRPRKVQ VAPLQGSPPL SHDDRGFEVI 

       130        140        150        160        170        180 
EEFDGRSFRS GYSERSRHSS HDMLSHSWEG NRERGRPHQR TQSRERERSR GRSLERGLDQ 

       190        200        210        220        230        240 
EDYGRSRERS RGRSLERGLD RDFVSRDHSR GRSIDRDYDR DYERSYHEAY EPDYGGGYSP 

       250        260        270        280        290        300 
SYDRRAHPET RYERSRSREH LRSRSPSPES RSRHEHKGQH DPDRPIGVLL TKSKANEEYG 

       310        320        330        340        350        360 
LRLGSQIFIK EMTRTGLATK DGNLHEGDII LKINGTVTEN MSLTDARKLI EKSRGKLQLV 

       370        380        390        400        410        420 
VLRDSKQTLI NIPALNDSDS EVEDISEIES NRSFSPEERR QQYSDQDYHS STEKLKERPS 

       430        440        450        460        470        480 
SREETSGRLS RMGATPTPFK STGDITAAGV TEASREPRYQ EEGPVPQPRT APRVFLRPSP 

       490        500        510        520        530        540 
EDEAIYGPNT KMVRFKKGDS VGLRLAGGND VGIFVAGIQE GTSAEQEGLQ EGDQILKVNT 

       550        560        570        580        590        600 
QDFRGLVRED AVLYLLEIPK GETVTILAQS RADVYRDILA CGRGDSFFIR SHFECEKETP 

       610        620        630        640        650        660 
QSLAFTRGEV FRVVDTLYDG KLGHWLAVRI GNELEKGLIP NKSRAEQMAS VQNAQRENAG 

       670        680        690        700        710        720 
DRADFWRMRG QRSSGGVKKN LRKSREDLAA AVSVSTKFPA YEKVLLREAG FKRPVVLFGP 

       730        740        750        760        770        780 
IADIAMERLA TELPDLFQTA KTEPKDAGSE KSSGVVRLNT VRQIIEQDKH ALLDVTPKAV 

       790        800        810        820        830        840 
DLLNYTQWFP IVIFFNPDSR QGVKTIRQRL SPTSNKSSRK LFDQANKLKK TCSHLFTATI 

       850        860        870        880        890        900 
NVNSANDGWF GSLKDSIQQQ QNEAVWVSEG KMEGMDDDAE DRMSYLTAMG ADYLSCDSRL 

       910        920        930        940        950        960 
ISDFEDTDGE GGAYTDNELE EPAEEPLVSS ITRSSEPVQH EENIRKSSPE PRAQMRRAAS 

       970        980        990       1000       1010       1020 
RDQLRDASPP PAFKPEPPKA RSQNREDSFD YSKSNLPATA GSEIPGGSTK GYPPPIAAKP 

      1030       1040       1050       1060       1070       1080 
AFGRPILKPS TPVPMPESEE VGESTEEQED APRSVLGRVK IFEKMDHKAK LQRMQELQEA 

      1090       1100       1110       1120       1130       1140 
QNARIEIAQK HPDIYAVPIK APKPDAGLPP HMSSRPPEPQ KAPSRLYQDT RGSYGSDPEE 

      1150       1160 
EEYRQQLAAH SKRGYYSQPS RYRDTEL 

« Hide

References

« Hide 'large scale' references
[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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF113005 mRNA. Translation: AAD19964.1.
BC034677 mRNA. Translation: AAH34677.1.
BC039924 mRNA. Translation: AAH39924.1.
CCDSCCDS37939.1.
RefSeqNP_035727.2. NM_011597.4.
XP_006526971.1. XM_006526908.1.
UniGeneMm.104744.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CSJNMR-A1-104[»]
ProteinModelPortalQ9Z0U1.
SMRQ9Z0U1. Positions 1-106, 286-364, 488-869.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204210. 3 interactions.
IntActQ9Z0U1. 3 interactions.
MINTMINT-113156.

PTM databases

PhosphoSiteQ9Z0U1.

Proteomic databases

MaxQBQ9Z0U1.
PaxDbQ9Z0U1.
PRIDEQ9Z0U1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000099558; ENSMUSP00000097154; ENSMUSG00000024812.
GeneID21873.
KEGGmmu:21873.
UCSCuc008ham.2. mouse.

Organism-specific databases

CTD9414.
MGIMGI:1341872. Tjp2.

Phylogenomic databases

eggNOGNOG239704.
GeneTreeENSGT00640000091263.
HOGENOMHOG000230923.
HOVERGENHBG017627.
InParanoidQ9Z0U1.
KOK06098.
OMAPEPRAQM.
OrthoDBEOG7T1RB4.
PhylomeDBQ9Z0U1.
TreeFamTF315957.

Gene expression databases

BgeeQ9Z0U1.
CleanExMM_TJP2.
GenevestigatorQ9Z0U1.

Family and domain databases

Gene3D2.30.42.10. 3 hits.
3.40.50.300. 2 hits.
InterProIPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
IPR011511. SH3_2.
IPR001452. SH3_domain.
IPR005417. ZonOcculdens.
IPR005419. ZonOcculS2.
[Graphical view]
PfamPF00625. Guanylate_kin. 1 hit.
PF00595. PDZ. 3 hits.
PF07653. SH3_2. 1 hit.
[Graphical view]
PRINTSPR01597. ZONOCCLUDNS.
PR01599. ZONOCCLUDNS2.
SMARTSM00072. GuKc. 1 hit.
SM00228. PDZ. 3 hits.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
SSF50156. SSF50156. 3 hits.
SSF52540. SSF52540. 1 hit.
PROSITEPS50052. GUANYLATE_KINASE_2. 1 hit.
PS50106. PDZ. 3 hits.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTJP2. mouse.
EvolutionaryTraceQ9Z0U1.
NextBio301380.
PROQ9Z0U1.
SOURCESearch...

Entry information

Entry nameZO2_MOUSE
AccessionPrimary (citable) accession number: Q9Z0U1
Secondary accession number(s): Q8K210
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 2, 2006
Last modified: July 9, 2014
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot