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Protein

Tight junction protein ZO-1

Gene

Tjp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The N-terminal may be involved in transducing a signal required for tight junction assembly, while the C-terminal may have specific properties of tight junctions. The alpha domain might be involved in stabilizing junctions. Plays a role in the regulation of cell migration by targeting CDC42BPB to the leading edge of migrating cells (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Calmodulin-binding

Enzyme and pathway databases

ReactomeiR-MMU-191647. c-src mediated regulation of Cx43 function and closure of gap junctions.
R-MMU-2028269. Signaling by Hippo.

Names & Taxonomyi

Protein namesi
Recommended name:
Tight junction protein ZO-1
Alternative name(s):
Tight junction protein 1
Zona occludens protein 1
Zonula occludens protein 1
Gene namesi
Name:Tjp1
Synonyms:Zo1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:98759. Tjp1.

Subcellular locationi

GO - Cellular componenti

  • adherens junction Source: MGI
  • apical junction complex Source: MGI
  • apical part of cell Source: MGI
  • apical plasma membrane Source: MGI
  • apicolateral plasma membrane Source: MGI
  • basolateral plasma membrane Source: MGI
  • bicellular tight junction Source: UniProtKB
  • cell-cell adherens junction Source: MGI
  • cell-cell junction Source: MGI
  • cell junction Source: MGI
  • cell surface Source: MGI
  • cytoplasm Source: MGI
  • gap junction Source: UniProtKB-SubCell
  • I band Source: UniProtKB-SubCell
  • intercalated disc Source: MGI
  • intercellular canaliculus Source: MGI
  • membrane Source: MGI
  • nucleus Source: MGI
  • plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Gap junction, Membrane, Tight junction

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000945411 – 1745Tight junction protein ZO-1Add BLAST1745

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei125PhosphoserineCombined sources1
Modified residuei175PhosphoserineBy similarity1
Modified residuei178PhosphoserineBy similarity1
Modified residuei179PhosphoserineBy similarity1
Modified residuei185PhosphothreonineBy similarity1
Modified residuei212PhosphoserineBy similarity1
Modified residuei241PhosphoserineCombined sources1
Modified residuei267PhosphothreonineBy similarity1
Modified residuei275PhosphoserineBy similarity1
Modified residuei277PhosphoserineCombined sources1
Modified residuei280PhosphoserineCombined sources1
Modified residuei284PhosphoserineCombined sources1
Modified residuei290PhosphoserineBy similarity1
Modified residuei294PhosphoserineCombined sources1
Modified residuei297PhosphoserineBy similarity1
Modified residuei300PhosphoserineBy similarity1
Modified residuei323PhosphoserineCombined sources1
Modified residuei329PhosphoserineBy similarity1
Modified residuei334PhosphoserineBy similarity1
Modified residuei337PhosphoserineBy similarity1
Modified residuei353PhosphoserineCombined sources1
Modified residuei354PhosphothreonineBy similarity1
Modified residuei617PhosphoserineCombined sources1
Modified residuei622PhosphoserineBy similarity1
Modified residuei809PhosphothreonineBy similarity1
Modified residuei810PhosphoserineCombined sources1
Modified residuei821PhosphoserineCombined sources1
Modified residuei822PhosphotyrosineCombined sources1
Modified residuei824PhosphoserineCombined sources1
Modified residuei837PhosphoserineBy similarity1
Modified residuei848PhosphothreonineCombined sources1
Modified residuei854PhosphothreonineBy similarity1
Modified residuei861PhosphothreonineBy similarity1
Modified residuei868PhosphothreonineCombined sources1
Modified residuei912PhosphoserineCombined sources1
Modified residuei1071PhosphoserineCombined sources1
Modified residuei1138PhosphoserineCombined sources1
Modified residuei1139PhosphotyrosineCombined sources1
Modified residuei1164PhosphotyrosineCombined sources1
Modified residuei1353PhosphotyrosineCombined sources1
Modified residuei1365PhosphoserineBy similarity1
Modified residuei1411PhosphoserineBy similarity1
Modified residuei1542PhosphoserineCombined sources1
Modified residuei1614PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylated. Dephosphorylated by PTPRJ (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP39447.
PaxDbiP39447.
PeptideAtlasiP39447.
PRIDEiP39447.

PTM databases

iPTMnetiP39447.
PhosphoSitePlusiP39447.

Expressioni

Gene expression databases

BgeeiENSMUSG00000030516.
CleanExiMM_TJP1.
ExpressionAtlasiP39447. baseline and differential.
GenevisibleiP39447. MM.

Interactioni

Subunit structurei

Homodimer, and heterodimer with TJP2/ZO-2 and TJP3/ZO-3. Interacts with OCLN, CALM, claudins, CGN/cingulin, CXADR, GJD3 and UBN1. Interacts (via ZU5 domain) with CDC42BPB. Interacts (via PDZ domain) with GJA1. Interacts (via PDZ domains) with ANKRD2 (By similarity). Interacts with BVES (via the C-terminus cytoplasmic tail) (PubMed:16188940). Interacts with GJA12 and KIRREL1 (PubMed:12424224, PubMed:15183511). Interacts with HSPA4 (By similarity). Interacts (via ZU5 domain) with MYZAP (PubMed:20093627). Interacts with DLL1 (PubMed:24715457). Interacts with USP53 (via the C-terminal region) (PubMed:26609154).By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Actn4P577806EBI-79508,EBI-445071
Gja1P232423EBI-79508,EBI-298630
Gjb6P706893EBI-79508,EBI-2615416
VclQ647278EBI-79508,EBI-432047

GO - Molecular functioni

Protein-protein interaction databases

BioGridi204209. 7 interactors.
DIPiDIP-30946N.
IntActiP39447. 17 interactors.
MINTiMINT-113090.
STRINGi10090.ENSMUSP00000099652.

Structurei

Secondary structure

11745
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi20 – 26Combined sources7
Beta strandi36 – 39Combined sources4
Beta strandi44 – 46Combined sources3
Turni49 – 51Combined sources3
Beta strandi55 – 59Combined sources5
Beta strandi61 – 63Combined sources3
Turni64 – 68Combined sources5
Beta strandi73 – 78Combined sources6
Beta strandi84 – 86Combined sources3
Helixi88 – 96Combined sources9
Beta strandi102 – 108Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2RRMNMR-A18-110[»]
ProteinModelPortaliP39447.
SMRiP39447.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP39447.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini23 – 110PDZ 1PROSITE-ProRule annotationAdd BLAST88
Domaini186 – 264PDZ 2PROSITE-ProRule annotationAdd BLAST79
Domaini421 – 502PDZ 3PROSITE-ProRule annotationAdd BLAST82
Domaini516 – 584SH3PROSITE-ProRule annotationAdd BLAST69
Domaini610 – 791Guanylate kinase-likePROSITE-ProRule annotationAdd BLAST182
Domaini1629 – 1721ZU5PROSITE-ProRule annotationAdd BLAST93

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1242 – 1247Poly-Pro6
Compositional biasi1424 – 1430Poly-Pro7

Domaini

The second PDZ domain mediates interaction with GJA12.1 Publication

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
Contains 1 ZU5 domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiKOG3580. Eukaryota.
ENOG410XQP3. LUCA.
GeneTreeiENSGT00840000129793.
HOGENOMiHOG000230923.
HOVERGENiHBG007849.
InParanoidiP39447.
KOiK05701.
OMAiPMGYSPR.
OrthoDBiEOG091G0AJZ.
TreeFamiTF315957.

Family and domain databases

Gene3Di2.30.42.10. 3 hits.
3.40.50.300. 1 hit.
InterProiIPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like_dom.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
IPR011511. SH3_2.
IPR001452. SH3_domain.
IPR005417. ZO.
IPR005418. ZO-1.
IPR000906. ZU5_dom.
[Graphical view]
PfamiPF00625. Guanylate_kin. 1 hit.
PF00595. PDZ. 3 hits.
PF07653. SH3_2. 1 hit.
PF00791. ZU5. 1 hit.
[Graphical view]
PRINTSiPR01597. ZONOCCLUDNS.
PR01598. ZONOCCLUDNS1.
SMARTiSM00072. GuKc. 1 hit.
SM00228. PDZ. 3 hits.
SM00218. ZU5. 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.
PS51145. ZU5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P39447-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSARAAAAKS TAMEETAIWE QHTVTLHRAP GFGFGIAISG GRDNPHFQSG
60 70 80 90 100
ETSIVISDVL KGGPAEGQLQ ENDRVAMVNG VSMDNVEHAF AVQQLRKSGK
110 120 130 140 150
NAKITIRRKK KVQIPVSHPD PEPVSDNEDD SYDEEVHDPR AGRGALANRR
160 170 180 190 200
SEKSWARDRS ASRERSLSPR SDRRSVASSQ PAKPTKVTLV KSRKNEEYGL
210 220 230 240 250
RLASHIFVKE ISQDSLAARD GNIQEGDVVL KINGTVTENM SLTDAKTLIE
260 270 280 290 300
RSKGKLKMVV QRDERATLLN VPDLSDSIHS ANASERDDIS EIQSLASDHS
310 320 330 340 350
GRSHDRPPRR SQSRSPDQRS EPSDHSTQSP QQPSNGSLRS REEERMSKPG
360 370 380 390 400
AISTPVKHVD DHPPKAVEEV TVEKNEKQTP TLPEPKPVYA QVGQPDVDLP
410 420 430 440 450
VSPSDGALPN SAHEDGILRP SMKLVKFRKG DSVGLRLAGG NDVGIFVAGV
460 470 480 490 500
LEDSPAAKEG LEEGDQILRV NNVDFTNIIR EEAVLFLLDL PKGEEVTILA
510 520 530 540 550
QKKKDVYRRI VESDVGDSFY IRTHFEYEKE SPYGLSFNKG EVFRVVDTLY
560 570 580 590 600
NGKLGSWLAI RIGKNHKEVE RGIIPNKNRA EQLASVQYTL PKTAGGDRAD
610 620 630 640 650
FWRFRGLRSS KRNLRKSRED LSAQPVQTKF PAYERVVLRE AGFLRPVTIF
660 670 680 690 700
GPIADVAREK LAREEPDIYQ IAKSEPRDAG TDHRSSGIIR LHTIKQIIDQ
710 720 730 740 750
DKHALLDVTP NAVDRLNYAQ WYPIVVFLNP DSKQGVKTMR MRLCPESRKS
760 770 780 790 800
ARKLYERSHK LRKNNHHLFT TTINLNSMND GWYGALKEAI QQQQNQLVWV
810 820 830 840 850
SEGKADGATS DDLDLHDDRL SYLSAPGSEY SMYSTDSRHT SDYEDTDTEG
860 870 880 890 900
GAYTDQELDE TLNDEVGTPP ESAITRSSEP VREDSSGMHH ENQTYPPYSP
910 920 930 940 950
QAQPQAIHRI DSPGLKPASQ QKAEASSPVP YLSPETTPAS SASAVNHNVS
960 970 980 990 1000
VTNVSLEEPA PAPPTSHASQ PGCLGAPSAE AAHVVLRGEG PPLPPHADPA
1010 1020 1030 1040 1050
KVYRKEPYSE EMMRQNHILK QPALGHPGQR PDKEPNLAYE PQLPYIEKQA
1060 1070 1080 1090 1100
SRDLEQPSYR YEVSSYTDQF SRNYDHRLRF EDRIPTYEDQ WSYYDDKQPY
1110 1120 1130 1140 1150
QPRPFENQHP RDLDSRQHPE EASERGYFQR FEEPAPLSYD SRTRYEQLPR
1160 1170 1180 1190 1200
TSTLRHEEQP APAYEVHNRY RPEAQPYSST GPKSSEPKQY FDQYPRSYEQ
1210 1220 1230 1240 1250
VPPPGFTSKT GHYEPLHGAA VVPPLIPSSQ QKPEVLPSAT KPQPPPPTLT
1260 1270 1280 1290 1300
EEEEDPAMKP QSVLTRVKMF ENKRSASLEN KKDVNDTASF KPPEVASKPP
1310 1320 1330 1340 1350
GASLAGPKPV PQSQFSEHDK TLYRLPEPQK PQVKPPEDIV RSNHYDPEED
1360 1370 1380 1390 1400
EEYYRKQLSY FDRRSFESKP SAHLPAGHHS EPAKPVHSQS QPNFSSYSSK
1410 1420 1430 1440 1450
GKPETDAVDR SFSEKRYDPA QATPPPPPLP SQYSQPAPPL SSSSLHIHSK
1460 1470 1480 1490 1500
GAQGEGNSVS LDFQNSYMSK PDPPPSQSKP ATFRPPTRED PPQTFYPQKS
1510 1520 1530 1540 1550
FPDKAPVNGA EQTQKTITPV YNRFTPKPYT SSARPFERKF ESPKFNHNLL
1560 1570 1580 1590 1600
PSETVHKPEL SSKTPTSPKT LMKAHSSTQP PEFDSGVETF SVHTDKPKYQ
1610 1620 1630 1640 1650
MNNISTMPKA VPVSPSAVEE DEDEDGHTVV ATARGIFNSN GGVLSSIETG
1660 1670 1680 1690 1700
VSIIIPQGAI PEGIEQEIYF KVCRDNSILP PLDKEKGETL LSPLVMCGPH
1710 1720 1730 1740
GLKFLKPVEL RLPHCDPKTW QNKCLPGDPN YLVGANCVSV LIDHF
Length:1,745
Mass (Da):194,742
Last modified:July 27, 2011 - v2
Checksum:i002B96F5A998B5CD
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti202L → P in BAA03274 (PubMed:8486731).Curated1
Sequence conflicti222N → D in BAA03274 (PubMed:8486731).Curated1
Sequence conflicti676P → L in BAA03274 (PubMed:8486731).Curated1
Sequence conflicti985V → G in BAA03274 (PubMed:8486731).Curated1
Sequence conflicti1237P → R in BAA03274 (PubMed:8486731).Curated1
Sequence conflicti1395S → P in BAA03274 (PubMed:8486731).Curated1
Sequence conflicti1584D → G in BAA03274 (PubMed:8486731).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14340 mRNA. Translation: BAA03274.1.
AC122222 Genomic DNA. No translation available.
AC131741 Genomic DNA. No translation available.
CCDSiCCDS21338.1.
PIRiA46431.
RefSeqiNP_033412.2. NM_009386.2.
UniGeneiMm.4342.

Genome annotation databases

EnsembliENSMUST00000102592; ENSMUSP00000099652; ENSMUSG00000030516.
GeneIDi21872.
KEGGimmu:21872.
UCSCiuc009hgp.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14340 mRNA. Translation: BAA03274.1.
AC122222 Genomic DNA. No translation available.
AC131741 Genomic DNA. No translation available.
CCDSiCCDS21338.1.
PIRiA46431.
RefSeqiNP_033412.2. NM_009386.2.
UniGeneiMm.4342.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2RRMNMR-A18-110[»]
ProteinModelPortaliP39447.
SMRiP39447.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204209. 7 interactors.
DIPiDIP-30946N.
IntActiP39447. 17 interactors.
MINTiMINT-113090.
STRINGi10090.ENSMUSP00000099652.

PTM databases

iPTMnetiP39447.
PhosphoSitePlusiP39447.

Proteomic databases

MaxQBiP39447.
PaxDbiP39447.
PeptideAtlasiP39447.
PRIDEiP39447.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000102592; ENSMUSP00000099652; ENSMUSG00000030516.
GeneIDi21872.
KEGGimmu:21872.
UCSCiuc009hgp.2. mouse.

Organism-specific databases

CTDi7082.
MGIiMGI:98759. Tjp1.

Phylogenomic databases

eggNOGiKOG3580. Eukaryota.
ENOG410XQP3. LUCA.
GeneTreeiENSGT00840000129793.
HOGENOMiHOG000230923.
HOVERGENiHBG007849.
InParanoidiP39447.
KOiK05701.
OMAiPMGYSPR.
OrthoDBiEOG091G0AJZ.
TreeFamiTF315957.

Enzyme and pathway databases

ReactomeiR-MMU-191647. c-src mediated regulation of Cx43 function and closure of gap junctions.
R-MMU-2028269. Signaling by Hippo.

Miscellaneous databases

EvolutionaryTraceiP39447.
PROiP39447.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000030516.
CleanExiMM_TJP1.
ExpressionAtlasiP39447. baseline and differential.
GenevisibleiP39447. MM.

Family and domain databases

Gene3Di2.30.42.10. 3 hits.
3.40.50.300. 1 hit.
InterProiIPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like_dom.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
IPR011511. SH3_2.
IPR001452. SH3_domain.
IPR005417. ZO.
IPR005418. ZO-1.
IPR000906. ZU5_dom.
[Graphical view]
PfamiPF00625. Guanylate_kin. 1 hit.
PF00595. PDZ. 3 hits.
PF07653. SH3_2. 1 hit.
PF00791. ZU5. 1 hit.
[Graphical view]
PRINTSiPR01597. ZONOCCLUDNS.
PR01598. ZONOCCLUDNS1.
SMARTiSM00072. GuKc. 1 hit.
SM00228. PDZ. 3 hits.
SM00218. ZU5. 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.
PS51145. ZU5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiZO1_MOUSE
AccessioniPrimary (citable) accession number: P39447
Secondary accession number(s): E9QK00
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: July 27, 2011
Last modified: November 2, 2016
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

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

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 one 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.