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Protein

Tight junction protein ZO-1

Gene

Tjp1

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

Functioni

Tjp1, TjpP2, and Tjp3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton (By similarity). The tight junction acts to limit movement of substances through the paracellular space and as a boundary between the compositionally distinct apical and basolateral plasma membrane domains of epithelial and endothelial cells. Necessary for lumenogenesis, and particularly efficient epithelial polarization and barrier formation (By similarity). Plays a role in the regulation of cell migration by targeting Cdc42bpb to the leading edge of migrating cells (By similarity). Plays an important role in podosome formation and associated function, thus regulating cell adhesion and matrix remodeling (By similarity). With Tjp2 and TJjp3, participates to the junctional retention and stability of the transcription factor Dbpa, but is not involved in its shuttling to the nucleus (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionCalmodulin-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
R-MMU-351906 Apoptotic cleavage of cell adhesion proteins

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:98759 Tjp1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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 residuei132PhosphotyrosineBy similarity1
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 residuei828PhosphoserineBy similarity1
Modified residuei837PhosphoserineBy similarity1
Modified residuei846PhosphothreonineBy 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 at tyrosine redidues in response to epidermal growth factor (EGF) (By similarity). This response is dependent on an intact actin microfilament system (By similarity). 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 Expressed in 306 organ(s), highest expression level in brain blood vessel
CleanExiMM_TJP1
ExpressionAtlasiP39447 baseline and differential
GenevisibleiP39447 MM

Interactioni

Subunit structurei

Homodimer, and heterodimer with TJP2 and TJP3. Interacts with OCLN, CALM, claudins, CGN/cingulin, CXADR, GJD3 and UBN1 (PubMed:10601346). Interacts (via ZU5 domain) with CDC42BPB (By similarity). Interacts (via PDZ domain) with GJA1 (By similarity). 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 similarity7 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi204209, 12 interactors
DIPiDIP-30946N
IntActiP39447, 24 interactors
MINTiP39447
STRINGi10090.ENSMUSP00000099652

Structurei

Secondary structure

11745
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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
Domaini1631 – 1745ZU5PROSITE-ProRule annotationAdd BLAST115

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni633 – 876Occludin (OCLN)-binding regionBy similarityAdd BLAST244
Regioni1150 – 1370Actin-binding region (ABR)By similarityAdd BLAST221

Compositional bias

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

Domaini

The 244-aa domain between residues 633 and 876 is the primary occludin (Ocln)-binding site and is required for stable association with the tight junction (By similarity).By similarity
The C-terminal region (residues 1151-1372) is an actin-binding region (ABR) that interacts directly with F-actin and plays an important role in the localization of Tjp1 at junctions (By similarity). The ABR is also required for the localization to puncta at the free edge of cells before initiation of cell-cell contact (By similarity). The ABR is also necessary for Tjp1 recruitment to podosomes (By similarity).By similarity
The second PDZ domain (PDZ2) mediates homodimerization and heterodimerization with Tjp2 and Tjp3 (By similarity). PDZ2 domain also mediates interaction with Gja12 (PubMed:15183511).By similarity1 Publication

Sequence similaritiesi

Belongs to the MAGUK family.Curated

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiKOG3580 Eukaryota
ENOG410XQP3 LUCA
GeneTreeiENSGT00760000118866
HOGENOMiHOG000230923
HOVERGENiHBG007849
InParanoidiP39447
KOiK05701
OrthoDBiEOG091G0AJZ
TreeFamiTF315957

Family and domain databases

CDDicd12026 SH3_ZO-1, 1 hit
InterProiView protein in InterPro
IPR008145 GK/Ca_channel_bsu
IPR008144 Guanylate_kin-like_dom
IPR027417 P-loop_NTPase
IPR001478 PDZ
IPR036034 PDZ_sf
IPR036028 SH3-like_dom_sf
IPR001452 SH3_domain
IPR005417 ZO
IPR005418 ZO-1
IPR035597 ZO-1_SH3
IPR000906 ZU5_dom
PANTHERiPTHR13865:SF25 PTHR13865:SF25, 1 hit
PfamiView protein in Pfam
PF00625 Guanylate_kin, 1 hit
PF00595 PDZ, 3 hits
PF07653 SH3_2, 1 hit
PF00791 ZU5, 1 hit
PRINTSiPR01597 ZONOCCLUDNS
PR01598 ZONOCCLUDNS1
SMARTiView protein in SMART
SM00072 GuKc, 1 hit
SM00228 PDZ, 3 hits
SM00218 ZU5, 1 hit
SUPFAMiSSF50044 SSF50044, 1 hit
SSF50156 SSF50156, 3 hits
SSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS50052 GUANYLATE_KINASE_2, 1 hit
PS50106 PDZ, 3 hits
PS50002 SH3, 1 hit
PS51145 ZU5, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B9EHJ3B9EHJ3_MOUSE
Tight junction protein ZO-1
Tjp1
1,685Annotation score:
A0A0U1RPW2A0A0U1RPW2_MOUSE
Tight junction protein ZO-1
Tjp1
1,128Annotation score:
A0A0U1RPB2A0A0U1RPB2_MOUSE
Tight junction protein ZO-1
Tjp1
171Annotation score:

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

Similar proteinsi

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, 12 interactors
DIPiDIP-30946N
IntActiP39447, 24 interactors
MINTiP39447
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
GeneTreeiENSGT00760000118866
HOGENOMiHOG000230923
HOVERGENiHBG007849
InParanoidiP39447
KOiK05701
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
R-MMU-351906 Apoptotic cleavage of cell adhesion proteins

Miscellaneous databases

EvolutionaryTraceiP39447
PROiPR:P39447
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000030516 Expressed in 306 organ(s), highest expression level in brain blood vessel
CleanExiMM_TJP1
ExpressionAtlasiP39447 baseline and differential
GenevisibleiP39447 MM

Family and domain databases

CDDicd12026 SH3_ZO-1, 1 hit
InterProiView protein in InterPro
IPR008145 GK/Ca_channel_bsu
IPR008144 Guanylate_kin-like_dom
IPR027417 P-loop_NTPase
IPR001478 PDZ
IPR036034 PDZ_sf
IPR036028 SH3-like_dom_sf
IPR001452 SH3_domain
IPR005417 ZO
IPR005418 ZO-1
IPR035597 ZO-1_SH3
IPR000906 ZU5_dom
PANTHERiPTHR13865:SF25 PTHR13865:SF25, 1 hit
PfamiView protein in Pfam
PF00625 Guanylate_kin, 1 hit
PF00595 PDZ, 3 hits
PF07653 SH3_2, 1 hit
PF00791 ZU5, 1 hit
PRINTSiPR01597 ZONOCCLUDNS
PR01598 ZONOCCLUDNS1
SMARTiView protein in SMART
SM00072 GuKc, 1 hit
SM00228 PDZ, 3 hits
SM00218 ZU5, 1 hit
SUPFAMiSSF50044 SSF50044, 1 hit
SSF50156 SSF50156, 3 hits
SSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS50052 GUANYLATE_KINASE_2, 1 hit
PS50106 PDZ, 3 hits
PS50002 SH3, 1 hit
PS51145 ZU5, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiZO1_MOUSE
AccessioniPrimary (citable) accession number: P39447
Secondary accession number(s): E9QK00
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: July 27, 2011
Last modified: November 7, 2018
This is version 185 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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