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Q07157

- ZO1_HUMAN

UniProt

Q07157 - ZO1_HUMAN

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Protein

Tight junction protein ZO-1

Gene

TJP1

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 - 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
  14. sensory perception of sound 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.

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-KW
  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. 1 Publication
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 – 9121Phosphoserine2 Publications
Modified residuei968 – 9681Phosphoserine2 Publications
Modified residuei1140 – 11401PhosphotyrosineBy similarity
Modified residuei1165 – 11651PhosphotyrosineBy similarity
Modified residuei1354 – 13541PhosphotyrosineBy similarity
Modified residuei1366 – 13661Phosphoserine3 Publications
Modified residuei1545 – 15451Phosphoserine1 Publication
Modified residuei1617 – 16171Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated. Dephosphorylated by PTPRJ.6 Publications

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

BgeeiQ07157.
CleanExiHS_TJP1.
ExpressionAtlasiQ07157. baseline and differential.
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.By similarity12 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. 68 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 – 279Combined sources
Turni30 – 323Combined sources
Beta strandi36 – 405Combined sources
Turni47 – 493Combined sources
Beta strandi54 – 596Combined sources
Turni64 – 685Combined sources
Beta strandi74 – 785Combined sources
Helixi88 – 969Combined sources
Beta strandi100 – 11011Combined sources
Beta strandi186 – 1905Combined sources
Turni191 – 1933Combined sources
Beta strandi194 – 1963Combined sources
Beta strandi200 – 21112Combined sources
Helixi216 – 2205Combined sources
Beta strandi228 – 2325Combined sources
Helixi242 – 2509Combined sources
Turni251 – 2544Combined sources
Beta strandi255 – 2617Combined sources
Beta strandi422 – 4287Combined sources
Beta strandi435 – 4395Combined sources
Beta strandi441 – 4433Combined sources
Beta strandi445 – 4506Combined sources
Beta strandi452 – 4543Combined sources
Helixi455 – 4584Combined sources
Beta strandi466 – 4705Combined sources
Helixi480 – 48910Combined sources
Beta strandi495 – 5017Combined sources
Helixi504 – 5107Combined sources
Beta strandi519 – 5235Combined sources
Beta strandi542 – 5498Combined sources
Helixi550 – 5523Combined sources
Beta strandi553 – 56210Combined sources
Helixi564 – 5663Combined sources
Beta strandi568 – 5758Combined sources
Helixi577 – 5848Combined sources
Beta strandi632 – 6409Combined sources
Beta strandi647 – 6515Combined sources
Helixi654 – 66411Combined sources
Turni666 – 6683Combined sources
Beta strandi669 – 6713Combined sources
Beta strandi679 – 6813Combined sources
Helixi691 – 6988Combined sources
Turni699 – 7013Combined sources
Beta strandi703 – 7064Combined sources
Helixi710 – 7189Combined sources
Beta strandi724 – 7296Combined sources
Helixi733 – 74311Combined sources
Helixi751 – 76515Combined sources
Helixi766 – 7683Combined sources
Beta strandi770 – 7745Combined sources
Helixi781 – 79515Combined sources
Beta strandi796 – 8016Combined sources
Beta strandi1633 – 16408Combined sources
Beta strandi1645 – 16484Combined sources
Turni1650 – 16523Combined sources
Beta strandi1655 – 16584Combined sources
Beta strandi1669 – 16779Combined sources
Beta strandi1679 – 16813Combined sources
Turni1687 – 16893Combined sources
Beta strandi1701 – 17033Combined sources
Beta strandi1706 – 171510Combined sources
Helixi1720 – 17234Combined sources
Helixi1732 – 17343Combined sources
Turni1735 – 17373Combined sources
Beta strandi1738 – 174710Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4Q2QX-ray1.45A419-504[»]
ProteinModelPortaliQ07157.
SMRiQ07157. Positions 18-110, 185-264, 420-802, 1629-1748.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ07157.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 11088PDZ 1PROSITE-ProRule annotationAdd
BLAST
Domaini186 – 26479PDZ 2PROSITE-ProRule annotationAdd
BLAST
Domaini421 – 50282PDZ 3PROSITE-ProRule annotationAdd
BLAST
Domaini516 – 58469SH3PROSITE-ProRule annotationAdd
BLAST
Domaini598 – 779182Guanylate kinase-likePROSITE-ProRule annotationAdd
BLAST
Domaini1632 – 172493ZU5PROSITE-ProRule annotationAdd
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.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

eggNOGiNOG239704.
GeneTreeiENSGT00640000091263.
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_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.
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

        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.

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.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti394 – 41724QPDVD…HEDGI → NQMWIYLSVHLMVSYLIQLM KMGF in AAA02891. (PubMed:8395056)CuratedAdd
BLAST
Sequence conflicti545 – 5451V → A in AAA02891. (PubMed:8395056)Curated
Sequence conflicti688 – 6881I → Y in AAA02891. (PubMed:8395056)Curated
Sequence conflicti762 – 7621R → A in AAA02891. (PubMed:8395056)Curated

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. CuratedVSP_003148Add
BLAST

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. [Q07157-1]
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:
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 .
CCDSi CCDS42007.1. [Q07157-1 ]
CCDS45199.1. [Q07157-2 ]
PIRi A47747.
RefSeqi NP_003248.3. NM_003257.4. [Q07157-1 ]
NP_783297.2. NM_175610.3. [Q07157-2 ]
UniGenei Hs.743990.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 [» ]
4Q2Q X-ray 1.45 A 419-504 [» ]
ProteinModelPortali Q07157.
SMRi Q07157. Positions 18-110, 185-264, 420-802, 1629-1748.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112937. 68 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 ]
ENST00000621049 ; ENSP00000484535 ; ENSG00000277401 . [Q07157-1 ]
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.
GeneTreei ENSGT00640000091263.
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

ChiTaRSi TJP1. human.
EvolutionaryTracei Q07157.
GeneWikii Tight_junction_protein_1.
GenomeRNAii 7082.
NextBioi 27699.
PROi Q07157.
SOURCEi Search...

Gene expression databases

Bgeei Q07157.
CleanExi HS_TJP1.
ExpressionAtlasi Q07157. baseline and differential.
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_dom.
[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: November 26, 2014
This is version 165 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