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Protein

Tight junction protein ZO-1

Gene

TJP1

Organism
Homo sapiens (Human)
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.1 Publication

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Calmodulin-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000104067-MONOMER.
ReactomeiR-HSA-191647. c-src mediated regulation of Cx43 function and closure of gap junctions.
R-HSA-2028269. Signaling by Hippo.
R-HSA-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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:11827. TJP1.

Subcellular locationi

GO - Cellular componenti

  • apical junction complex Source: MGI
  • apical part of cell Source: MGI
  • apical plasma membrane Source: Ensembl
  • apicolateral plasma membrane Source: Ensembl
  • basolateral plasma membrane Source: MGI
  • bicellular tight junction Source: UniProtKB
  • cell-cell adherens junction Source: BHF-UCL
  • cell junction Source: HPA
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • gap junction Source: UniProtKB-SubCell
  • intercalated disc Source: Ensembl
  • intercellular canaliculus Source: Ensembl
  • nucleus Source: Ensembl
  • plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi201R → A: Strongly reduced interaction with GJA1. 1 Publication1
Mutagenesisi209K → A: Abolishes interaction with GJA1. 1 Publication1
Mutagenesisi1699 – 1700MC → AA: Abolishes interaction with CDC42BPB. 1 Publication2
Mutagenesisi1748Missing : Abolishes interaction with CDC42BPB and MYZAP. 1 Publication1

Organism-specific databases

DisGeNETi7082.
OpenTargetsiENSG00000104067.
PharmGKBiPA36532.

Polymorphism and mutation databases

BioMutaiTJP1.
DMDMi85700443.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000945401 – 1748Tight junction protein ZO-1Add BLAST1748

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei125PhosphoserineCombined sources1
Modified residuei175PhosphoserineCombined sources1
Modified residuei178PhosphoserineCombined sources1
Modified residuei179PhosphoserineCombined sources1
Modified residuei185PhosphothreonineCombined sources1
Modified residuei212PhosphoserineCombined sources1
Modified residuei241PhosphoserineBy similarity1
Modified residuei267PhosphothreonineCombined sources1
Modified residuei275PhosphoserineCombined sources1
Modified residuei277PhosphoserineCombined sources1
Modified residuei280PhosphoserineCombined sources1
Modified residuei284PhosphoserineCombined sources1
Modified residuei290PhosphoserineCombined sources1
Modified residuei294PhosphoserineCombined sources1
Modified residuei297PhosphoserineCombined sources1
Modified residuei300PhosphoserineCombined sources1
Modified residuei323PhosphoserineBy similarity1
Modified residuei329PhosphoserineCombined sources1
Modified residuei334PhosphoserineCombined sources1
Modified residuei337PhosphoserineCombined sources1
Modified residuei353PhosphoserineCombined sources1
Modified residuei354PhosphothreonineCombined sources1
Modified residuei617PhosphoserineCombined sources1
Modified residuei622PhosphoserineCombined sources1
Modified residuei809PhosphothreonineCombined sources1
Modified residuei810PhosphoserineBy similarity1
Modified residuei821PhosphoserineCombined sources1
Modified residuei822PhosphotyrosineBy similarity1
Modified residuei824PhosphoserineBy similarity1
Modified residuei837PhosphoserineCombined sources1
Modified residuei848PhosphothreonineBy similarity1
Modified residuei854PhosphothreonineCombined sources1
Modified residuei861PhosphothreonineCombined sources1
Modified residuei868PhosphothreonineCombined sources1
Modified residuei912PhosphoserineCombined sources1
Modified residuei968PhosphoserineCombined sources1
Modified residuei1071PhosphoserineBy similarity1
Modified residuei1111PhosphoserineCombined sources1
Modified residuei1139PhosphoserineBy similarity1
Modified residuei1140PhosphotyrosineBy similarity1
Modified residuei1165PhosphotyrosineBy similarity1
Modified residuei1354PhosphotyrosineBy similarity1
Modified residuei1366PhosphoserineCombined sources1
Modified residuei1413PhosphoserineCombined sources1
Modified residuei1545PhosphoserineCombined sources1
Modified residuei1617PhosphoserineCombined sources1
Isoform Short (identifier: Q07157-2)
Modified residuei912PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated. Dephosphorylated by PTPRJ.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ07157.
MaxQBiQ07157.
PaxDbiQ07157.
PeptideAtlasiQ07157.
PRIDEiQ07157.

PTM databases

iPTMnetiQ07157.
PhosphoSitePlusiQ07157.

Expressioni

Tissue specificityi

The alpha-containing isoform is found in most epithelial cell junctions. The short isoform is found both in endothelial cells and the highly specialized epithelial junctions of renal glomeruli and Sertoli cells of the seminiferous tubules.

Gene expression databases

BgeeiENSG00000104067.
CleanExiHS_TJP1.
ExpressionAtlasiQ07157. baseline and differential.
GenevisibleiQ07157. HS.

Organism-specific databases

HPAiCAB010822.
HPA001636.
HPA001637.

Interactioni

Subunit structurei

Homodimer, and heterodimer with TJP2/ZO-2 and TJP3/ZO-3 (PubMed:17928286, PubMed:16737969). Interacts with OCLN, CALM, claudins, CGN/cingulin, CXADR, GJA12, GJD3 and UBN1 (PubMed:11734628, PubMed:12023291, PubMed:12154091, PubMed:15183511, PubMed:18823282, PubMed:20200156). Interacts (via ZU5 domain) with CDC42BPB and MYZAP (PubMed:20093627, PubMed:21240187). Interacts (via PDZ domain) with GJA1 (PubMed:18636092). Interacts (via PDZ domains) with ANKRD2 (PubMed:22016770). Interacts with BVES (via the C-terminus cytoplasmic tail) (By similarity). Interacts with HSPA4 and KIRREL1 (By similarity). Interacts with DLL1 (By similarity). Interacts with USP53 (via the C-terminal region) (By similarity).By similarity12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ACTN4O437074EBI-79553,EBI-351526
GJA1P173023EBI-79553,EBI-1103439
GJD3Q8N1442EBI-79553,EBI-2629520
KIRRELQ96J847EBI-79553,EBI-3988456
Wwtr1Q9EPK54EBI-79553,EBI-1211920From a different organism.

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL

Protein-protein interaction databases

BioGridi112937. 104 interactors.
IntActiQ07157. 56 interactors.
MINTiMINT-5006060.
STRINGi9606.ENSP00000281537.

Structurei

Secondary structure

11748
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi19 – 27Combined sources9
Turni30 – 32Combined sources3
Beta strandi36 – 40Combined sources5
Turni47 – 49Combined sources3
Beta strandi54 – 59Combined sources6
Turni64 – 68Combined sources5
Beta strandi74 – 78Combined sources5
Helixi88 – 96Combined sources9
Beta strandi100 – 110Combined sources11
Beta strandi186 – 190Combined sources5
Turni191 – 193Combined sources3
Beta strandi194 – 196Combined sources3
Beta strandi200 – 211Combined sources12
Helixi216 – 220Combined sources5
Beta strandi228 – 232Combined sources5
Helixi242 – 250Combined sources9
Turni251 – 254Combined sources4
Beta strandi255 – 261Combined sources7
Beta strandi422 – 428Combined sources7
Beta strandi435 – 439Combined sources5
Beta strandi441 – 443Combined sources3
Beta strandi445 – 450Combined sources6
Beta strandi452 – 454Combined sources3
Helixi455 – 458Combined sources4
Beta strandi466 – 470Combined sources5
Helixi480 – 489Combined sources10
Beta strandi495 – 501Combined sources7
Helixi504 – 510Combined sources7
Beta strandi519 – 523Combined sources5
Beta strandi542 – 549Combined sources8
Helixi550 – 552Combined sources3
Beta strandi553 – 562Combined sources10
Helixi564 – 566Combined sources3
Beta strandi568 – 575Combined sources8
Helixi577 – 584Combined sources8
Beta strandi632 – 640Combined sources9
Beta strandi647 – 651Combined sources5
Helixi654 – 664Combined sources11
Turni666 – 668Combined sources3
Beta strandi669 – 671Combined sources3
Beta strandi679 – 681Combined sources3
Helixi691 – 698Combined sources8
Turni699 – 701Combined sources3
Beta strandi703 – 706Combined sources4
Helixi710 – 718Combined sources9
Beta strandi724 – 729Combined sources6
Helixi733 – 743Combined sources11
Helixi751 – 765Combined sources15
Helixi766 – 768Combined sources3
Beta strandi770 – 774Combined sources5
Helixi781 – 795Combined sources15
Beta strandi796 – 801Combined sources6
Beta strandi1633 – 1640Combined sources8
Beta strandi1645 – 1648Combined sources4
Turni1650 – 1652Combined sources3
Beta strandi1655 – 1658Combined sources4
Beta strandi1669 – 1677Combined sources9
Beta strandi1679 – 1681Combined sources3
Turni1687 – 1689Combined sources3
Beta strandi1701 – 1703Combined sources3
Beta strandi1706 – 1715Combined sources10
Helixi1720 – 1723Combined sources4
Helixi1732 – 1734Combined sources3
Turni1735 – 1737Combined sources3
Beta strandi1738 – 1747Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2H2BX-ray1.60A18-110[»]
2H2CX-ray2.00A18-110[»]
2H3MX-ray2.90A18-110[»]
2JWENMR-A/B185-264[»]
2KXRNMR-A1631-1748[»]
2KXSNMR-A1631-1748[»]
2RCZX-ray1.70A/B186-264[»]
3CYYX-ray2.40A/B182-273[»]
3LH5X-ray2.60A516-803[»]
3SHUX-ray2.75A/B421-512[»]
3SHWX-ray2.90A421-888[»]
3TSVX-ray1.99A417-516[»]
3TSWX-ray2.85A/B/C/D417-803[»]
3TSZX-ray2.50A417-803[»]
4OEOX-ray1.90A/B/C18-110[»]
4OEPX-ray2.35A/B18-110[»]
4Q2QX-ray1.45A419-504[»]
4YYXX-ray1.79A/B18-110[»]
ProteinModelPortaliQ07157.
SMRiQ07157.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ07157.

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
Domaini598 – 779Guanylate kinase-likePROSITE-ProRule annotationAdd BLAST182
Domaini1632 – 1724ZU5PROSITE-ProRule annotationAdd BLAST93

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1243 – 1248Poly-Pro6
Compositional biasi1426 – 1432Poly-Pro7

Domaini

The second PDZ domain mediates interaction with GJA12.By similarity

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.
HOVERGENiHBG007849.
InParanoidiQ07157.
KOiK05701.
OrthoDBiEOG091G0AJZ.
PhylomeDBiQ07157.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Long (identifier: Q07157-1) [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
MSARAAAAKS TAMEETAIWE QHTVTLHRAP GFGFGIAISG GRDNPHFQSG
60 70 80 90 100
ETSIVISDVL KGGPAEGQLQ ENDRVAMVNG VSMDNVEHAF AVQQLRKSGK
110 120 130 140 150
NAKITIRRKK KVQIPVSRPD PEPVSDNEED SYDEEIHDPR SGRSGVVNRR
160 170 180 190 200
SEKIWPRDRS 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 SRSRSPDQRS EPSDHSRHSP QQPSNGSLRS RDEERISKPG
360 370 380 390 400
AVSTPVKHAD DHTPKTVEEV TVERNEKQTP SLPEPKPVYA QVGQPDVDLP
410 420 430 440 450
VSPSDGVLPN STHEDGILRP 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 TDQRSSGIIR 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
QAQPQPIHRI DSPGFKPASQ QKAEASSPVP YLSPETNPAS STSAVNHNVN
960 970 980 990 1000
LTNVRLEEPT PAPSTSYSPQ ADSLRTPSTE AAHIMLRDQE PSLSSHVDPT
1010 1020 1030 1040 1050
KVYRKDPYPE EMMRQNHVLK QPAVSHPGHR PDKEPNLTYE PQLPYVEKQA
1060 1070 1080 1090 1100
SRDLEQPTYR YESSSYTDQF SRNYEHRLRY EDRVPMYEEQ WSYYDDKQPY
1110 1120 1130 1140 1150
PSRPPFDNQH SQDLDSRQHP EESSERGYFP RFEEPAPLSY DSRPRYEQAP
1160 1170 1180 1190 1200
RASALRHEEQ PAPGYDTHGR LRPEAQPHPS AGPKPAESKQ YFEQYSRSYE
1210 1220 1230 1240 1250
QVPPQGFTSR AGHFEPLHGA AAVPPLIPSS QHKPEALPSN TKPLPPPPTQ
1260 1270 1280 1290 1300
TEEEEDPAMK PQSVLTRVKM FENKRSASLE TKKDVNDTGS FKPPEVASKP
1310 1320 1330 1340 1350
SGAPIIGPKP TSQNQFSEHD KTLYRIPEPQ KPQLKPPEDI VRSNHYDPEE
1360 1370 1380 1390 1400
DEEYYRKQLS YFDRRSFENK PPAHIAASHL SEPAKPAHSQ NQSNFSSYSS
1410 1420 1430 1440 1450
KGKPPEADGV DRSFGEKRYE PIQATPPPPP LPSQYAQPSQ PVTSASLHIH
1460 1470 1480 1490 1500
SKGAHGEGNS VSLDFQNSLV SKPDPPPSQN KPATFRPPNR EDTAQAAFYP
1510 1520 1530 1540 1550
QKSFPDKAPV NGTEQTQKTV TPAYNRFTPK PYTSSARPFE RKFESPKFNH
1560 1570 1580 1590 1600
NLLPSETAHK PDLSSKTPTS PKTLVKSHSL AQPPEFDSGV ETFSIHAEKP
1610 1620 1630 1640 1650
KYQINNISTV PKAIPVSPSA VEEDEDEDGH TVVATARGIF NSNGGVLSSI
1660 1670 1680 1690 1700
ETGVSIIIPQ GAIPEGVEQE IYFKVCRDNS ILPPLDKEKG ETLLSPLVMC
1710 1720 1730 1740
GPHGLKFLKP VELRLPHCDP KTWQNKCLPG DPNYLVGANC VSVLIDHF
Length:1,748
Mass (Da):195,459
Last modified:January 24, 2006 - v3
Checksum:i189E31617084C0CC
GO
Isoform Short (identifier: Q07157-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     922-1001: Missing.

Show »
Length:1,668
Mass (Da):186,966
Checksum:i5AD0570EC32FD9C3
GO

Sequence cautioni

The sequence AAA02891 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti394 – 417QPDVD…HEDGI → NQMWIYLSVHLMVSYLIQLM KMGF in AAA02891 (PubMed:8395056).CuratedAdd BLAST24
Sequence conflicti545V → A in AAA02891 (PubMed:8395056).Curated1
Sequence conflicti688I → Y in AAA02891 (PubMed:8395056).Curated1
Sequence conflicti762R → A in AAA02891 (PubMed:8395056).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_025153471N → S.1 PublicationCorresponds to variant rs2229517dbSNPEnsembl.1
Natural variantiVAR_025154790I → V.3 PublicationsCorresponds to variant rs7179270dbSNPEnsembl.1
Natural variantiVAR_025155930P → L.1 PublicationCorresponds to variant rs45529137dbSNPEnsembl.1
Natural variantiVAR_0251561110H → R.1 PublicationCorresponds to variant rs45567033dbSNPEnsembl.1
Natural variantiVAR_0251571347D → A.1 PublicationCorresponds to variant rs2291166dbSNPEnsembl.1
Natural variantiVAR_0251581605N → S.1 PublicationCorresponds to variant rs45578638dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_003148922 – 1001Missing in isoform Short. CuratedAdd BLAST80

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L14837 mRNA. Translation: AAA02891.1. Different initiation.
AK304758 mRNA. Translation: BAG65513.1.
DQ015919 Genomic DNA. Translation: AAY22179.1.
AC022613 Genomic DNA. No translation available.
BC111712 mRNA. Translation: AAI11713.1.
CCDSiCCDS42007.1. [Q07157-1]
CCDS45199.1. [Q07157-2]
PIRiA47747.
RefSeqiNP_003248.3. NM_003257.4. [Q07157-1]
NP_783297.2. NM_175610.3. [Q07157-2]
UniGeneiHs.743990.

Genome annotation databases

EnsembliENST00000346128; ENSP00000281537; ENSG00000104067. [Q07157-1]
ENST00000545208; ENSP00000441202; ENSG00000104067. [Q07157-2]
ENST00000621049; ENSP00000484535; ENSG00000277401.
GeneIDi7082.
KEGGihsa:7082.
UCSCiuc001zcr.4. human. [Q07157-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L14837 mRNA. Translation: AAA02891.1. Different initiation.
AK304758 mRNA. Translation: BAG65513.1.
DQ015919 Genomic DNA. Translation: AAY22179.1.
AC022613 Genomic DNA. No translation available.
BC111712 mRNA. Translation: AAI11713.1.
CCDSiCCDS42007.1. [Q07157-1]
CCDS45199.1. [Q07157-2]
PIRiA47747.
RefSeqiNP_003248.3. NM_003257.4. [Q07157-1]
NP_783297.2. NM_175610.3. [Q07157-2]
UniGeneiHs.743990.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2H2BX-ray1.60A18-110[»]
2H2CX-ray2.00A18-110[»]
2H3MX-ray2.90A18-110[»]
2JWENMR-A/B185-264[»]
2KXRNMR-A1631-1748[»]
2KXSNMR-A1631-1748[»]
2RCZX-ray1.70A/B186-264[»]
3CYYX-ray2.40A/B182-273[»]
3LH5X-ray2.60A516-803[»]
3SHUX-ray2.75A/B421-512[»]
3SHWX-ray2.90A421-888[»]
3TSVX-ray1.99A417-516[»]
3TSWX-ray2.85A/B/C/D417-803[»]
3TSZX-ray2.50A417-803[»]
4OEOX-ray1.90A/B/C18-110[»]
4OEPX-ray2.35A/B18-110[»]
4Q2QX-ray1.45A419-504[»]
4YYXX-ray1.79A/B18-110[»]
ProteinModelPortaliQ07157.
SMRiQ07157.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112937. 104 interactors.
IntActiQ07157. 56 interactors.
MINTiMINT-5006060.
STRINGi9606.ENSP00000281537.

PTM databases

iPTMnetiQ07157.
PhosphoSitePlusiQ07157.

Polymorphism and mutation databases

BioMutaiTJP1.
DMDMi85700443.

Proteomic databases

EPDiQ07157.
MaxQBiQ07157.
PaxDbiQ07157.
PeptideAtlasiQ07157.
PRIDEiQ07157.

Protocols and materials databases

DNASUi7082.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000346128; ENSP00000281537; ENSG00000104067. [Q07157-1]
ENST00000545208; ENSP00000441202; ENSG00000104067. [Q07157-2]
ENST00000621049; ENSP00000484535; ENSG00000277401.
GeneIDi7082.
KEGGihsa:7082.
UCSCiuc001zcr.4. human. [Q07157-1]

Organism-specific databases

CTDi7082.
DisGeNETi7082.
GeneCardsiTJP1.
HGNCiHGNC:11827. TJP1.
HPAiCAB010822.
HPA001636.
HPA001637.
MIMi601009. gene.
neXtProtiNX_Q07157.
OpenTargetsiENSG00000104067.
PharmGKBiPA36532.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3580. Eukaryota.
ENOG410XQP3. LUCA.
GeneTreeiENSGT00840000129793.
HOVERGENiHBG007849.
InParanoidiQ07157.
KOiK05701.
OrthoDBiEOG091G0AJZ.
PhylomeDBiQ07157.
TreeFamiTF315957.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000104067-MONOMER.
ReactomeiR-HSA-191647. c-src mediated regulation of Cx43 function and closure of gap junctions.
R-HSA-2028269. Signaling by Hippo.
R-HSA-351906. Apoptotic cleavage of cell adhesion proteins.

Miscellaneous databases

ChiTaRSiTJP1. human.
EvolutionaryTraceiQ07157.
GeneWikiiTight_junction_protein_1.
GenomeRNAii7082.
PROiQ07157.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000104067.
CleanExiHS_TJP1.
ExpressionAtlasiQ07157. baseline and differential.
GenevisibleiQ07157. HS.

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_HUMAN
AccessioniPrimary (citable) accession number: Q07157
Secondary accession number(s): B4E3K1, Q2NKP3, Q4ZGJ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: January 24, 2006
Last modified: November 30, 2016
This is version 187 of the entry and version 3 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 15
    Human chromosome 15: 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

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.