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Q07157

- ZO1_HUMAN

UniProt

Q07157 - ZO1_HUMAN

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Protein

Tight junction protein ZO-1

Gene
TJP1, ZO1
Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. protein binding Source: UniProtKB

GO - Biological processi

  1. apoptotic process Source: Reactome
  2. blastocyst formation Source: Ensembl
  3. cell-cell junction assembly Source: ProtInc
  4. cell-cell signaling involved in cell-cell junction organization Source: UniProtKB
  5. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
  6. cellular response to glucose stimulus Source: Ensembl
  7. hippo signaling Source: Reactome
  8. membrane organization Source: Reactome
  9. negative regulation of vascular permeability Source: Ensembl
  10. response to drug Source: Ensembl
  11. response to ethanol Source: Ensembl
  12. response to lipopolysaccharide Source: Ensembl
  13. response to magnetism Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

Calmodulin-binding

Enzyme and pathway databases

ReactomeiREACT_11043. c-src mediated regulation of Cx43 function and closure of gap junctions.
REACT_118607. Signaling by Hippo.
REACT_13579. 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
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:11827. TJP1.

Subcellular locationi

Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junctiontight junction. Cell junction. Cell junctiongap junction
Note: Moves from the cytoplasm to the cell membrane concurrently with cell-cell contact. Detected at the leading edge of migrating and wounded cells.3 Publications

GO - Cellular componenti

  1. apical junction complex Source: MGI
  2. apical part of cell Source: MGI
  3. apical plasma membrane Source: Ensembl
  4. apicolateral plasma membrane Source: Ensembl
  5. basolateral plasma membrane Source: MGI
  6. cell-cell adherens junction Source: ProtInc
  7. cell junction Source: HPA
  8. cytoplasm Source: UniProtKB
  9. cytosol Source: Reactome
  10. gap junction Source: UniProtKB-SubCell
  11. intercalated disc Source: Ensembl
  12. intercellular canaliculus Source: Ensembl
  13. nucleus Source: Ensembl
  14. plasma membrane Source: HPA
  15. tight junction Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi201 – 2011R → A: Strongly reduced interaction with GJA1. 1 Publication
Mutagenesisi209 – 2091K → A: Abolishes interaction with GJA1. 1 Publication
Mutagenesisi1699 – 17002MC → AA: Abolishes interaction with CDC42BPB.
Mutagenesisi1748 – 17481Missing: Abolishes interaction with CDC42BPB and MYZAP. 1 Publication

Organism-specific databases

PharmGKBiPA36532.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 17481748Tight junction protein ZO-1PRO_0000094540Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei125 – 1251Phosphoserine3 Publications
Modified residuei175 – 1751Phosphoserine1 Publication
Modified residuei178 – 1781Phosphoserine1 Publication
Modified residuei179 – 1791Phosphoserine1 Publication
Modified residuei185 – 1851Phosphothreonine1 Publication
Modified residuei277 – 2771Phosphoserine1 Publication
Modified residuei297 – 2971Phosphoserine1 Publication
Modified residuei300 – 3001Phosphoserine1 Publication
Modified residuei329 – 3291Phosphoserine3 Publications
Modified residuei334 – 3341Phosphoserine1 Publication
Modified residuei337 – 3371Phosphoserine3 Publications
Modified residuei353 – 3531Phosphoserine1 Publication
Modified residuei617 – 6171Phosphoserine3 Publications
Modified residuei622 – 6221Phosphoserine1 Publication
Modified residuei912 – 9121Phosphoserine4 Publications
Modified residuei968 – 9681Phosphoserine2 Publications
Modified residuei1140 – 11401Phosphotyrosine By similarity
Modified residuei1165 – 11651Phosphotyrosine By similarity
Modified residuei1354 – 13541Phosphotyrosine By similarity
Modified residuei1366 – 13661Phosphoserine3 Publications
Modified residuei1545 – 15451Phosphoserine1 Publication
Modified residuei1617 – 16171Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated. Dephosphorylated by PTPRJ.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ07157.
PaxDbiQ07157.
PRIDEiQ07157.

PTM databases

PhosphoSiteiQ07157.

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

ArrayExpressiQ07157.
BgeeiQ07157.
CleanExiHS_TJP1.
GenevestigatoriQ07157.

Organism-specific databases

HPAiCAB010822.
HPA001636.
HPA001637.

Interactioni

Subunit structurei

Interacts with BVES (via the C-terminus cytoplasmic tail). Interacts with HSPA4 and KIRREL1 By similarity. Homodimer, and heterodimer with TJP2/ZO-2 and TJP3/ZO-3. Interacts with OCLN, CALM, claudins, CGN/cingulin, CXADR, GJA12, GJD3 and UBN1. Interacts (via ZU5 domain) with CDC42BPB and MYZAP. Interacts (via PDZ domain) with GJA1. Interacts (via PDZ domains) with ANKRD2.12 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi112937. 65 interactions.
IntActiQ07157. 40 interactions.
MINTiMINT-5006060.
STRINGi9606.ENSP00000281537.

Structurei

Secondary structure

1
1748
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi19 – 279
Turni30 – 323
Beta strandi36 – 405
Turni47 – 493
Beta strandi54 – 596
Turni64 – 685
Beta strandi74 – 785
Helixi88 – 969
Beta strandi100 – 11011
Beta strandi186 – 1905
Turni191 – 1933
Beta strandi194 – 1963
Beta strandi200 – 21112
Helixi216 – 2205
Beta strandi228 – 2325
Helixi242 – 2509
Turni251 – 2544
Beta strandi255 – 2617
Beta strandi423 – 4286
Beta strandi435 – 4395
Turni441 – 4433
Beta strandi445 – 4506
Beta strandi452 – 4543
Helixi455 – 4584
Beta strandi465 – 4706
Helixi480 – 48910
Beta strandi495 – 5028
Helixi504 – 5107
Beta strandi519 – 5235
Beta strandi542 – 5498
Helixi550 – 5523
Beta strandi553 – 56210
Helixi564 – 5663
Beta strandi568 – 5758
Helixi577 – 5848
Beta strandi632 – 6409
Beta strandi647 – 6515
Helixi654 – 66411
Turni666 – 6683
Beta strandi669 – 6713
Beta strandi679 – 6813
Helixi691 – 6988
Turni699 – 7013
Beta strandi703 – 7064
Helixi710 – 7189
Beta strandi724 – 7296
Helixi733 – 74311
Helixi751 – 76515
Helixi766 – 7683
Beta strandi770 – 7745
Helixi781 – 79515
Beta strandi796 – 8016
Beta strandi1633 – 16408
Beta strandi1645 – 16484
Turni1650 – 16523
Beta strandi1655 – 16584
Beta strandi1669 – 16779
Beta strandi1679 – 16813
Turni1687 – 16893
Beta strandi1701 – 17033
Beta strandi1706 – 171510
Helixi1720 – 17234
Helixi1732 – 17343
Turni1735 – 17373
Beta strandi1738 – 174710

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ07157.
SMRiQ07157. Positions 18-110, 185-264, 420-802, 1629-1748.

Miscellaneous databases

EvolutionaryTraceiQ07157.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 11088PDZ 1Add
BLAST
Domaini186 – 26479PDZ 2Add
BLAST
Domaini421 – 50282PDZ 3Add
BLAST
Domaini516 – 58469SH3Add
BLAST
Domaini598 – 779182Guanylate kinase-likeAdd
BLAST
Domaini1632 – 172493ZU5Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1243 – 12486Poly-Pro
Compositional biasi1426 – 14327Poly-Pro

Domaini

The second PDZ domain mediates interaction with GJA12 By similarity.

Sequence similaritiesi

Belongs to the MAGUK family.
Contains 3 PDZ (DHR) domains.
Contains 1 SH3 domain.
Contains 1 ZU5 domain.

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiNOG239704.
HOVERGENiHBG007849.
InParanoidiQ07157.
KOiK05701.
OrthoDBiEOG7T1RB4.
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.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
IPR011511. SH3_2.
IPR001452. SH3_domain.
IPR005417. ZonOcculdens.
IPR005418. ZonOcculS1.
IPR000906. ZU5.
[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.
SM00326. SH3. 1 hit.
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. Align

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

MSARAAAAKS TAMEETAIWE QHTVTLHRAP GFGFGIAISG GRDNPHFQSG     50
ETSIVISDVL KGGPAEGQLQ ENDRVAMVNG VSMDNVEHAF AVQQLRKSGK 100
NAKITIRRKK KVQIPVSRPD PEPVSDNEED SYDEEIHDPR SGRSGVVNRR 150
SEKIWPRDRS ASRERSLSPR SDRRSVASSQ PAKPTKVTLV KSRKNEEYGL 200
RLASHIFVKE ISQDSLAARD GNIQEGDVVL KINGTVTENM SLTDAKTLIE 250
RSKGKLKMVV QRDERATLLN VPDLSDSIHS ANASERDDIS EIQSLASDHS 300
GRSHDRPPRR SRSRSPDQRS EPSDHSRHSP QQPSNGSLRS RDEERISKPG 350
AVSTPVKHAD DHTPKTVEEV TVERNEKQTP SLPEPKPVYA QVGQPDVDLP 400
VSPSDGVLPN STHEDGILRP SMKLVKFRKG DSVGLRLAGG NDVGIFVAGV 450
LEDSPAAKEG LEEGDQILRV NNVDFTNIIR EEAVLFLLDL PKGEEVTILA 500
QKKKDVYRRI VESDVGDSFY IRTHFEYEKE SPYGLSFNKG EVFRVVDTLY 550
NGKLGSWLAI RIGKNHKEVE RGIIPNKNRA EQLASVQYTL PKTAGGDRAD 600
FWRFRGLRSS KRNLRKSRED LSAQPVQTKF PAYERVVLRE AGFLRPVTIF 650
GPIADVAREK LAREEPDIYQ IAKSEPRDAG TDQRSSGIIR LHTIKQIIDQ 700
DKHALLDVTP NAVDRLNYAQ WYPIVVFLNP DSKQGVKTMR MRLCPESRKS 750
ARKLYERSHK LRKNNHHLFT TTINLNSMND GWYGALKEAI QQQQNQLVWV 800
SEGKADGATS DDLDLHDDRL SYLSAPGSEY SMYSTDSRHT SDYEDTDTEG 850
GAYTDQELDE TLNDEVGTPP ESAITRSSEP VREDSSGMHH ENQTYPPYSP 900
QAQPQPIHRI DSPGFKPASQ QKAEASSPVP YLSPETNPAS STSAVNHNVN 950
LTNVRLEEPT PAPSTSYSPQ ADSLRTPSTE AAHIMLRDQE PSLSSHVDPT 1000
KVYRKDPYPE EMMRQNHVLK QPAVSHPGHR PDKEPNLTYE PQLPYVEKQA 1050
SRDLEQPTYR YESSSYTDQF SRNYEHRLRY EDRVPMYEEQ WSYYDDKQPY 1100
PSRPPFDNQH SQDLDSRQHP EESSERGYFP RFEEPAPLSY DSRPRYEQAP 1150
RASALRHEEQ PAPGYDTHGR LRPEAQPHPS AGPKPAESKQ YFEQYSRSYE 1200
QVPPQGFTSR AGHFEPLHGA AAVPPLIPSS QHKPEALPSN TKPLPPPPTQ 1250
TEEEEDPAMK PQSVLTRVKM FENKRSASLE TKKDVNDTGS FKPPEVASKP 1300
SGAPIIGPKP TSQNQFSEHD KTLYRIPEPQ KPQLKPPEDI VRSNHYDPEE 1350
DEEYYRKQLS YFDRRSFENK PPAHIAASHL SEPAKPAHSQ NQSNFSSYSS 1400
KGKPPEADGV DRSFGEKRYE PIQATPPPPP LPSQYAQPSQ PVTSASLHIH 1450
SKGAHGEGNS VSLDFQNSLV SKPDPPPSQN KPATFRPPNR EDTAQAAFYP 1500
QKSFPDKAPV NGTEQTQKTV TPAYNRFTPK PYTSSARPFE RKFESPKFNH 1550
NLLPSETAHK PDLSSKTPTS PKTLVKSHSL AQPPEFDSGV ETFSIHAEKP 1600
KYQINNISTV PKAIPVSPSA VEEDEDEDGH TVVATARGIF NSNGGVLSSI 1650
ETGVSIIIPQ GAIPEGVEQE IYFKVCRDNS ILPPLDKEKG ETLLSPLVMC 1700
GPHGLKFLKP VELRLPHCDP KTWQNKCLPG DPNYLVGANC VSVLIDHF 1748
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.

Note: Contains a phosphoserine at position 912.

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

Sequence cautioni

The sequence AAA02891.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti471 – 4711N → S.1 Publication
Corresponds to variant rs2229517 [ dbSNP | Ensembl ].
VAR_025153
Natural varianti790 – 7901I → V.3 Publications
Corresponds to variant rs7179270 [ dbSNP | Ensembl ].
VAR_025154
Natural varianti930 – 9301P → L.1 Publication
Corresponds to variant rs45529137 [ dbSNP | Ensembl ].
VAR_025155
Natural varianti1110 – 11101H → R.1 Publication
Corresponds to variant rs45567033 [ dbSNP | Ensembl ].
VAR_025156
Natural varianti1347 – 13471D → A.1 Publication
Corresponds to variant rs2291166 [ dbSNP | Ensembl ].
VAR_025157
Natural varianti1605 – 16051N → S.1 Publication
Corresponds to variant rs45578638 [ dbSNP | Ensembl ].
VAR_025158

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei922 – 100180Missing in isoform Short. VSP_003148Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti394 – 41724QPDVD…HEDGI → NQMWIYLSVHLMVSYLIQLM KMGF in AAA02891. 1 PublicationAdd
BLAST
Sequence conflicti545 – 5451V → A in AAA02891. 1 Publication
Sequence conflicti688 – 6881I → Y in AAA02891. 1 Publication
Sequence conflicti762 – 7621R → A in AAA02891. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_003257.3. [Q07157-1]
NP_783297.2. NM_175610.2. [Q07157-2]
UniGeneiHs.743990.

Genome annotation databases

EnsembliENST00000346128; ENSP00000281537; ENSG00000104067. [Q07157-1]
ENST00000545208; ENSP00000441202; ENSG00000104067. [Q07157-2]
GeneIDi7082.
KEGGihsa:7082.
UCSCiuc001zcr.3. human. [Q07157-1]
uc001zcs.3. human. [Q07157-2]

Polymorphism databases

DMDMi85700443.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS42007.1. [Q07157-1 ]
CCDS45199.1. [Q07157-2 ]
PIRi A47747.
RefSeqi NP_003248.3. NM_003257.3. [Q07157-1 ]
NP_783297.2. NM_175610.2. [Q07157-2 ]
UniGenei Hs.743990.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2H2B X-ray 1.60 A 18-110 [» ]
2H2C X-ray 2.00 A 18-110 [» ]
2H3M X-ray 2.90 A 18-110 [» ]
2JWE NMR - A/B 185-264 [» ]
2KXR NMR - A 1631-1748 [» ]
2KXS NMR - A 1631-1748 [» ]
2RCZ X-ray 1.70 A/B 186-264 [» ]
3CYY X-ray 2.40 A/B 182-273 [» ]
3LH5 X-ray 2.60 A 516-803 [» ]
3SHU X-ray 2.75 A/B 421-512 [» ]
3SHW X-ray 2.90 A 421-888 [» ]
3TSV X-ray 1.99 A 417-516 [» ]
3TSW X-ray 2.85 A/B/C/D 417-803 [» ]
3TSZ X-ray 2.50 A 417-803 [» ]
ProteinModelPortali Q07157.
SMRi Q07157. Positions 18-110, 185-264, 420-802, 1629-1748.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112937. 65 interactions.
IntActi Q07157. 40 interactions.
MINTi MINT-5006060.
STRINGi 9606.ENSP00000281537.

PTM databases

PhosphoSitei Q07157.

Polymorphism databases

DMDMi 85700443.

Proteomic databases

MaxQBi Q07157.
PaxDbi Q07157.
PRIDEi Q07157.

Protocols and materials databases

DNASUi 7082.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000346128 ; ENSP00000281537 ; ENSG00000104067 . [Q07157-1 ]
ENST00000545208 ; ENSP00000441202 ; ENSG00000104067 . [Q07157-2 ]
GeneIDi 7082.
KEGGi hsa:7082.
UCSCi uc001zcr.3. human. [Q07157-1 ]
uc001zcs.3. human. [Q07157-2 ]

Organism-specific databases

CTDi 7082.
GeneCardsi GC15M029991.
HGNCi HGNC:11827. TJP1.
HPAi CAB010822.
HPA001636.
HPA001637.
MIMi 601009. gene.
neXtProti NX_Q07157.
PharmGKBi PA36532.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG239704.
HOVERGENi HBG007849.
InParanoidi Q07157.
KOi K05701.
OrthoDBi EOG7T1RB4.
PhylomeDBi Q07157.
TreeFami TF315957.

Enzyme and pathway databases

Reactomei REACT_11043. c-src mediated regulation of Cx43 function and closure of gap junctions.
REACT_118607. Signaling by Hippo.
REACT_13579. Apoptotic cleavage of cell adhesion proteins.

Miscellaneous databases

EvolutionaryTracei Q07157.
GeneWikii Tight_junction_protein_1.
GenomeRNAii 7082.
NextBioi 27699.
PROi Q07157.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q07157.
Bgeei Q07157.
CleanExi HS_TJP1.
Genevestigatori Q07157.

Family and domain databases

Gene3Di 2.30.42.10. 3 hits.
3.40.50.300. 1 hit.
InterProi IPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
IPR011511. SH3_2.
IPR001452. SH3_domain.
IPR005417. ZonOcculdens.
IPR005418. ZonOcculS1.
IPR000906. ZU5.
[Graphical view ]
Pfami PF00625. Guanylate_kin. 1 hit.
PF00595. PDZ. 3 hits.
PF07653. SH3_2. 1 hit.
PF00791. ZU5. 1 hit.
[Graphical view ]
PRINTSi PR01597. ZONOCCLUDNS.
PR01598. ZONOCCLUDNS1.
SMARTi SM00072. GuKc. 1 hit.
SM00228. PDZ. 3 hits.
SM00326. SH3. 1 hit.
SM00218. ZU5. 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.
PS51145. ZU5. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The tight junction protein ZO-1 is homologous to the Drosophila discs-large tumor suppressor protein of septate junctions."
    Willott E., Balda M.S., Fanning A.S., Jameson B., van Itallie C., Anderson J.M.
    Proc. Natl. Acad. Sci. U.S.A. 90:7834-7838(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-790.
    Tissue: Liver.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG), VARIANT VAL-790.
    Tissue: Uterus.
  3. NIEHS SNPs program
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-471; VAL-790; LEU-930; ARG-1110; ALA-1347 AND SER-1605.
  4. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM LONG).
  6. "The coxsackievirus and adenovirus receptor is a transmembrane component of the tight junction."
    Cohen C.J., Shieh J.T.C., Pickles R.J., Okegawa T., Hsieh J.-T., Bergelson J.M.
    Proc. Natl. Acad. Sci. U.S.A. 98:15191-15196(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CXADR.
  7. "Evidence for a functional interaction between cingulin and ZO-1 in cultured cells."
    D'Atri F., Nadalutti F., Citi S.
    J. Biol. Chem. 277:27757-27764(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CGN.
  8. "Molecular cloning, functional expression, and tissue distribution of a novel human gap junction-forming protein, connexin-31.9. Interaction with zona occludens protein-1."
    Nielsen P.A., Beahm D.L., Giepmans B.N., Baruch A., Hall J.E., Kumar N.M.
    J. Biol. Chem. 277:38272-38283(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GJD3.
  9. "Connexin47, connexin29 and connexin32 co-expression in oligodendrocytes and Cx47 association with zonula occludens-1 (ZO-1) in mouse brain."
    Li X., Ionescu A.V., Lynn B.D., Lu S., Kamasawa N., Morita M., Davidson K.G.V., Yasumura T., Rash J.E., Nagy J.I.
    Neuroscience 126:611-630(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GJA12.
  10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337 AND SER-1366, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125 AND SER-912, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-277; SER-329; SER-617; SER-912; SER-968 AND SER-1545, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Characterization of the ubinuclein protein as a new member of the nuclear and adhesion complex components (NACos)."
    Aho S., Lupo J., Coly P.-A., Sabine A., Castellazzi M., Morand P., Sergeant A., Manet E., Boyer V., Gruffat H.
    Biol. Cell 101:319-334(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UBN1.
  15. "Density-enhanced phosphatase 1 regulates phosphorylation of tight junction proteins and enhances barrier function of epithelial cells."
    Sallee J.L., Burridge K.
    J. Biol. Chem. 284:14997-15006(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, DEPHOSPHORYLATION BY PTPRJ.
  16. "Myozap, a novel intercalated disc protein, activates serum response factor-dependent signaling and is required to maintain cardiac function in vivo."
    Seeger T.S., Frank D., Rohr C., Will R., Just S., Grund C., Lyon R., Luedde M., Koegl M., Sheikh F., Rottbauer W., Franke W.W., Katus H.A., Olson E.N., Frey N.
    Circ. Res. 106:880-890(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MYZAP.
  17. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329; SER-337; SER-353; SER-617; SER-968; SER-1366 AND SER-1617, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-912 (ISOFORM SHORT), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Multi-tasking role of the mechanosensing protein Ankrd2 in the signaling network of striated muscle."
    Belgrano A., Rakicevic L., Mittempergher L., Campanaro S., Martinelli V.C., Mouly V., Valle G., Kojic S., Faulkner G.
    PLoS ONE 6:E25519-E25519(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ANKRD2.
  20. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-175; SER-178; SER-179; THR-185; SER-297; SER-300; SER-329; SER-334; SER-337; SER-617; SER-622 AND SER-1366, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-912 (ISOFORM SHORT), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Comparative structural analysis of the erbin PDZ domain and the first PDZ domain of ZO-1. Insights into determinants of PDZ domain specificity."
    Appleton B.A., Zhang Y., Wu P., Yin J.P., Hunziker W., Skelton N.J., Sidhu S.S., Wiesmann C.
    J. Biol. Chem. 281:22312-22320(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 18-110, SUBUNIT.
  22. "Domain swapping within PDZ2 is responsible for dimerization of ZO proteins."
    Fanning A.S., Lye M.F., Anderson J.M., Lavie A.
    J. Biol. Chem. 282:37710-37716(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 185-264, SUBUNIT.
  23. "Domain-swapped dimerization of ZO-1 PDZ2 generates specific and regulatory connexin43-binding sites."
    Chen J., Pan L., Wei Z., Zhao Y., Zhang M.
    EMBO J. 27:2113-2123(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 182-273 IN COMPLEX WITH GJA1 PEPTIDE, SUBUNIT, MUTAGENESIS OF ARG-201 AND LYS-209, SUBCELLULAR LOCATION, INTERACTION WITH GJA1.
  24. "Insights into regulated ligand binding sites from the structure of ZO-1 Src homology 3-guanylate kinase module."
    Lye M.F., Fanning A.S., Su Y., Anderson J.M., Lavie A.
    J. Biol. Chem. 285:13907-13917(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 516-803, INTERACTION WITH CALM.
  25. "Cdc42-dependent formation of the ZO-1/MRCKbeta complex at the leading edge controls cell migration."
    Huo L., Wen W., Wang R., Kam C., Xia J., Feng W., Zhang M.
    EMBO J. 30:665-678(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1631-1748 OF MUTANT 1699-MET-CYS-1700 IN COMPLEX WITH MYZAP, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 1699-MET-CYS-1700 AND PHE-1748, INTERACTION WITH MYZAP AND CDC42BPB.
  26. "Solution structure of the second PDZ domain of Zonula Occludens 1."
    Ji P., Yang G., Zhang J., Wu J., Chen Z., Gong Q., Wu J., Shi Y.
    Proteins 79:1342-1346(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 185-264.

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: September 3, 2014
This is version 162 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

External Data

Dasty 3

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