Reviewed, UniProtKB/Swiss-Prot Q07157 (ZO1_HUMAN)

Names and origin

Protein names

Recommended name:
    Tight junction protein ZO-1
Alternative name(s):
    Zonula occludens protein 1
    Zona occludens protein 1
    Tight junction protein 1

Gene names

Name:	TJP1
Synonyms:	ZO1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1748 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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.
Subunit structure	Interacts with HSPA4 and KIRREL1 By similarity. Homodimer, and heterodimer with TJP2/ZO-2 and TJP3/ZO-3. Interacts with occludin, claudins, CGN/cingulin, CXADR, GJA12, GJD3 and UBN1.
Subcellular location	Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junction › tight junction. Note: Movement of ZO-1 from the cytoplasm to membrane is an early event occurring concurrently with cell-cell contact. Ref.5
Tissue specificity	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.
Domain	The second PDZ domain mediates interaction with GJA12 By similarity.
Post-translational modification	Phosphorylated. Ref.9 Ref.10 Ref.11 Ref.12
Sequence similarities	Belongs to the MAGUK family. Contains 1 guanylate kinase-like domain. Contains 3 PDZ (DHR) domains. Contains 1 SH3 domain. Contains 1 ZU5 domain.

Ontologies

Keywords
Cellular component	Cell junction Cell membrane Membrane Tight junction
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat SH3 domain
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	cell-cell junction assembly Traceable author statement. Source: ProtInc
Cellular component	basolateral plasma membrane Inferred from direct assay. Source: MGI cell-cell adherens junction Traceable author statement. Source: ProtInc cytoplasm Inferred from direct assay. Source: HPA tight junction Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ACTN4	O43707	2	EBI-79553,EBI-351526
CGN	Q9P2M7	1	EBI-79553,EBI-79537
cgn	Q9PTD7	1	EBI-79553,EBI-79525	From a different organism.
GJA1	P17302	1	EBI-79553,EBI-1103439

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Long (identifier: Q07157-1)

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.

Isoform Short (identifier: Q07157-2)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1748

1748

Tight junction protein ZO-1

PRO_0000094540

Regions

Domain

23 – 110

88

PDZ 1

Domain

186 – 264

79

PDZ 2

Domain

421 – 502

82

PDZ 3

Domain

516 – 584

69

SH3

Domain

598 – 779

182

Guanylate kinase-like

Domain

1632 – 1724

93

ZU5

Compositional bias

1243 – 1248

6

Poly-Pro

Compositional bias

1426 – 1432

7

Poly-Pro

Amino acid modifications

Modified residue

125

1

Phosphoserine Ref.11 Ref.12

Modified residue

131

1

Phosphoserine Ref.11

Modified residue

132

1

Phosphotyrosine Ref.11 Ref.12

Modified residue

166

1

Phosphoserine Ref.9

Modified residue

168

1

Phosphoserine Ref.9

Modified residue

175

1

Phosphoserine By similarity

Modified residue

275

1

Phosphoserine Ref.9

Modified residue

277

1

Phosphoserine Ref.9 Ref.12

Modified residue

280

1

Phosphoserine Ref.9 Ref.12

Modified residue

284

1

Phosphoserine By similarity

Modified residue

297

1

Phosphoserine By similarity

Modified residue

300

1

Phosphoserine By similarity

Modified residue

329

1

Phosphoserine Ref.12

Modified residue

337

1

Phosphoserine Ref.9

Modified residue

402

1

Phosphoserine Ref.9

Modified residue

617

1

Phosphoserine Ref.10 Ref.12

Modified residue

868

1

Phosphothreonine Ref.9

Modified residue

912

1

Phosphoserine Ref.11 Ref.12

Modified residue

927

1

Phosphoserine Ref.11

Modified residue

968

1

Phosphoserine Ref.11 Ref.12

Modified residue

1140

1

Phosphotyrosine By similarity

Modified residue

1165

1

Phosphotyrosine By similarity

Modified residue

1354

1

Phosphotyrosine By similarity

Modified residue

1366

1

Phosphoserine Ref.9

Modified residue

1545

1

Phosphoserine Ref.12

Modified residue

1617

1

Phosphoserine Ref.11

Modified residue

1619

1

Phosphoserine Ref.11

Natural variations

Alternative sequence

922 – 1001

80

Missing in isoform Short.

VSP_003148

Natural variant

471

1

N → S: dbSNP rs2229517. Ref.3

VAR_025153

Natural variant

790

1

I → V: dbSNP rs7179270. Ref.3 Ref.1 Ref.2

VAR_025154

Natural variant

930

1

P → L: dbSNP rs45529137. Ref.3

VAR_025155

Natural variant

1110

1

H → R: dbSNP rs45567033. Ref.3

VAR_025156

Natural variant

1347

1

D → A: dbSNP rs2291166. Ref.3

VAR_025157

Natural variant

1605

1

N → S: dbSNP rs45578638. Ref.3

VAR_025158

Experimental info

Sequence conflict

394 – 417

24

QPDVD…HEDGI → NQMWIYLSVHLMVSYLIQLM KMGF in AAA02891. Ref.1

Sequence conflict

545

1

V → A in AAA02891. Ref.1

Sequence conflict

688

1

I → Y in AAA02891. Ref.1

Sequence conflict

762

1

R → A in AAA02891. Ref.1

Secondary structure

1

.

.

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.

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.

.

.

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.

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.

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1748

Helix Strand Turn

Details...

Beta strand

19 – 27

9

Turn

30 – 32

3

Beta strand

36 – 40

5

Turn

47 – 49

3

Beta strand

54 – 59

6

Beta strand

74 – 78

5

Helix

88 – 96

9

Beta strand

100 – 110

11

Beta strand

186 – 190

5

Beta strand

200 – 211

12

Helix

216 – 220

5

Beta strand

228 – 232

5

Helix

242 – 250

9

Beta strand

255 – 261

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified January 24, 2006. Version 3. Checksum: 189E31617084C0CC	FASTA	1,748	195,459
	10 20 30 40 50 60 MSARAAAAKS TAMEETAIWE QHTVTLHRAP GFGFGIAISG GRDNPHFQSG ETSIVISDVL 70 80 90 100 110 120 KGGPAEGQLQ ENDRVAMVNG VSMDNVEHAF AVQQLRKSGK NAKITIRRKK KVQIPVSRPD 130 140 150 160 170 180 PEPVSDNEED SYDEEIHDPR SGRSGVVNRR SEKIWPRDRS ASRERSLSPR SDRRSVASSQ 190 200 210 220 230 240 PAKPTKVTLV KSRKNEEYGL RLASHIFVKE ISQDSLAARD GNIQEGDVVL KINGTVTENM 250 260 270 280 290 300 SLTDAKTLIE RSKGKLKMVV QRDERATLLN VPDLSDSIHS ANASERDDIS EIQSLASDHS 310 320 330 340 350 360 GRSHDRPPRR SRSRSPDQRS EPSDHSRHSP QQPSNGSLRS RDEERISKPG AVSTPVKHAD 370 380 390 400 410 420 DHTPKTVEEV TVERNEKQTP SLPEPKPVYA QVGQPDVDLP VSPSDGVLPN STHEDGILRP 430 440 450 460 470 480 SMKLVKFRKG DSVGLRLAGG NDVGIFVAGV LEDSPAAKEG LEEGDQILRV NNVDFTNIIR 490 500 510 520 530 540 EEAVLFLLDL PKGEEVTILA QKKKDVYRRI VESDVGDSFY IRTHFEYEKE SPYGLSFNKG 550 560 570 580 590 600 EVFRVVDTLY NGKLGSWLAI RIGKNHKEVE RGIIPNKNRA EQLASVQYTL PKTAGGDRAD 610 620 630 640 650 660 FWRFRGLRSS KRNLRKSRED LSAQPVQTKF PAYERVVLRE AGFLRPVTIF GPIADVAREK 670 680 690 700 710 720 LAREEPDIYQ IAKSEPRDAG TDQRSSGIIR LHTIKQIIDQ DKHALLDVTP NAVDRLNYAQ 730 740 750 760 770 780 WYPIVVFLNP DSKQGVKTMR MRLCPESRKS ARKLYERSHK LRKNNHHLFT TTINLNSMND 790 800 810 820 830 840 GWYGALKEAI QQQQNQLVWV SEGKADGATS DDLDLHDDRL SYLSAPGSEY SMYSTDSRHT 850 860 870 880 890 900 SDYEDTDTEG GAYTDQELDE TLNDEVGTPP ESAITRSSEP VREDSSGMHH ENQTYPPYSP 910 920 930 940 950 960 QAQPQPIHRI DSPGFKPASQ QKAEASSPVP YLSPETNPAS STSAVNHNVN LTNVRLEEPT 970 980 990 1000 1010 1020 PAPSTSYSPQ ADSLRTPSTE AAHIMLRDQE PSLSSHVDPT KVYRKDPYPE EMMRQNHVLK 1030 1040 1050 1060 1070 1080 QPAVSHPGHR PDKEPNLTYE PQLPYVEKQA SRDLEQPTYR YESSSYTDQF SRNYEHRLRY 1090 1100 1110 1120 1130 1140 EDRVPMYEEQ WSYYDDKQPY PSRPPFDNQH SQDLDSRQHP EESSERGYFP RFEEPAPLSY 1150 1160 1170 1180 1190 1200 DSRPRYEQAP RASALRHEEQ PAPGYDTHGR LRPEAQPHPS AGPKPAESKQ YFEQYSRSYE 1210 1220 1230 1240 1250 1260 QVPPQGFTSR AGHFEPLHGA AAVPPLIPSS QHKPEALPSN TKPLPPPPTQ TEEEEDPAMK 1270 1280 1290 1300 1310 1320 PQSVLTRVKM FENKRSASLE TKKDVNDTGS FKPPEVASKP SGAPIIGPKP TSQNQFSEHD 1330 1340 1350 1360 1370 1380 KTLYRIPEPQ KPQLKPPEDI VRSNHYDPEE DEEYYRKQLS YFDRRSFENK PPAHIAASHL 1390 1400 1410 1420 1430 1440 SEPAKPAHSQ NQSNFSSYSS KGKPPEADGV DRSFGEKRYE PIQATPPPPP LPSQYAQPSQ 1450 1460 1470 1480 1490 1500 PVTSASLHIH SKGAHGEGNS VSLDFQNSLV SKPDPPPSQN KPATFRPPNR EDTAQAAFYP 1510 1520 1530 1540 1550 1560 QKSFPDKAPV NGTEQTQKTV TPAYNRFTPK PYTSSARPFE RKFESPKFNH NLLPSETAHK 1570 1580 1590 1600 1610 1620 PDLSSKTPTS PKTLVKSHSL AQPPEFDSGV ETFSIHAEKP KYQINNISTV PKAIPVSPSA 1630 1640 1650 1660 1670 1680 VEEDEDEDGH TVVATARGIF NSNGGVLSSI ETGVSIIIPQ GAIPEGVEQE IYFKVCRDNS 1690 1700 1710 1720 1730 1740 ILPPLDKEKG ETLLSPLVMC GPHGLKFLKP VELRLPHCDP KTWQNKCLPG DPNYLVGANC VSVLIDHF
	Isoform Short. Checksum: 5AD0570EC32FD9C3	FASTA	1,668	186,966
	10 20 30 40 50 60 MSARAAAAKS TAMEETAIWE QHTVTLHRAP GFGFGIAISG GRDNPHFQSG ETSIVISDVL 70 80 90 100 110 120 KGGPAEGQLQ ENDRVAMVNG VSMDNVEHAF AVQQLRKSGK NAKITIRRKK KVQIPVSRPD 130 140 150 160 170 180 PEPVSDNEED SYDEEIHDPR SGRSGVVNRR SEKIWPRDRS ASRERSLSPR SDRRSVASSQ 190 200 210 220 230 240 PAKPTKVTLV KSRKNEEYGL RLASHIFVKE ISQDSLAARD GNIQEGDVVL KINGTVTENM 250 260 270 280 290 300 SLTDAKTLIE RSKGKLKMVV QRDERATLLN VPDLSDSIHS ANASERDDIS EIQSLASDHS 310 320 330 340 350 360 GRSHDRPPRR SRSRSPDQRS EPSDHSRHSP QQPSNGSLRS RDEERISKPG AVSTPVKHAD 370 380 390 400 410 420 DHTPKTVEEV TVERNEKQTP SLPEPKPVYA QVGQPDVDLP VSPSDGVLPN STHEDGILRP 430 440 450 460 470 480 SMKLVKFRKG DSVGLRLAGG NDVGIFVAGV LEDSPAAKEG LEEGDQILRV NNVDFTNIIR 490 500 510 520 530 540 EEAVLFLLDL PKGEEVTILA QKKKDVYRRI VESDVGDSFY IRTHFEYEKE SPYGLSFNKG 550 560 570 580 590 600 EVFRVVDTLY NGKLGSWLAI RIGKNHKEVE RGIIPNKNRA EQLASVQYTL PKTAGGDRAD 610 620 630 640 650 660 FWRFRGLRSS KRNLRKSRED LSAQPVQTKF PAYERVVLRE AGFLRPVTIF GPIADVAREK 670 680 690 700 710 720 LAREEPDIYQ IAKSEPRDAG TDQRSSGIIR LHTIKQIIDQ DKHALLDVTP NAVDRLNYAQ 730 740 750 760 770 780 WYPIVVFLNP DSKQGVKTMR MRLCPESRKS ARKLYERSHK LRKNNHHLFT TTINLNSMND 790 800 810 820 830 840 GWYGALKEAI QQQQNQLVWV SEGKADGATS DDLDLHDDRL SYLSAPGSEY SMYSTDSRHT 850 860 870 880 890 900 SDYEDTDTEG GAYTDQELDE TLNDEVGTPP ESAITRSSEP VREDSSGMHH ENQTYPPYSP 910 920 930 940 950 960 QAQPQPIHRI DSPGFKPASQ QVYRKDPYPE EMMRQNHVLK QPAVSHPGHR PDKEPNLTYE 970 980 990 1000 1010 1020 PQLPYVEKQA SRDLEQPTYR YESSSYTDQF SRNYEHRLRY EDRVPMYEEQ WSYYDDKQPY 1030 1040 1050 1060 1070 1080 PSRPPFDNQH SQDLDSRQHP EESSERGYFP RFEEPAPLSY DSRPRYEQAP RASALRHEEQ 1090 1100 1110 1120 1130 1140 PAPGYDTHGR LRPEAQPHPS AGPKPAESKQ YFEQYSRSYE QVPPQGFTSR AGHFEPLHGA 1150 1160 1170 1180 1190 1200 AAVPPLIPSS QHKPEALPSN TKPLPPPPTQ TEEEEDPAMK PQSVLTRVKM FENKRSASLE 1210 1220 1230 1240 1250 1260 TKKDVNDTGS FKPPEVASKP SGAPIIGPKP TSQNQFSEHD KTLYRIPEPQ KPQLKPPEDI 1270 1280 1290 1300 1310 1320 VRSNHYDPEE DEEYYRKQLS YFDRRSFENK PPAHIAASHL SEPAKPAHSQ NQSNFSSYSS 1330 1340 1350 1360 1370 1380 KGKPPEADGV DRSFGEKRYE PIQATPPPPP LPSQYAQPSQ PVTSASLHIH SKGAHGEGNS 1390 1400 1410 1420 1430 1440 VSLDFQNSLV SKPDPPPSQN KPATFRPPNR EDTAQAAFYP QKSFPDKAPV NGTEQTQKTV 1450 1460 1470 1480 1490 1500 TPAYNRFTPK PYTSSARPFE RKFESPKFNH NLLPSETAHK PDLSSKTPTS PKTLVKSHSL 1510 1520 1530 1540 1550 1560 AQPPEFDSGV ETFSIHAEKP KYQINNISTV PKAIPVSPSA VEEDEDEDGH TVVATARGIF 1570 1580 1590 1600 1610 1620 NSNGGVLSSI ETGVSIIIPQ GAIPEGVEQE IYFKVCRDNS ILPPLDKEKG ETLLSPLVMC 1630 1640 1650 1660 GPHGLKFLKP VELRLPHCDP KTWQNKCLPG DPNYLVGANC VSVLIDHF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 8395056] [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: 14702039] [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]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]	"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: 11734628] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CXADR.
[6]	"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: 12023291] [Abstract] Cited for: INTERACTION WITH CGN.
[7]	"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: 12154091] [Abstract] Cited for: INTERACTION WITH GJD3.
[8]	"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: 15183511] [Abstract] Cited for: INTERACTION WITH GJA12.
[9]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166; SER-168; SER-275; SER-277; SER-280; SER-337; SER-402; THR-868 AND SER-1366, MASS SPECTROMETRY. Tissue: Epithelium.
[10]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617, MASS SPECTROMETRY.
[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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-131; TYR-132; SER-912; SER-927; SER-968; SER-1617 AND SER-1619, MASS SPECTROMETRY.
[12]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; TYR-132; SER-277; SER-280; SER-329; SER-617; SER-912; SER-968 AND SER-1545, MASS SPECTROMETRY.
[13]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[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: 18823282] [Abstract] Cited for: INTERACTION WITH UBN1.
[15]	"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: 16737969] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 18-110, SUBUNIT.
[16]	"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: 17928286] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 185-264, SUBUNIT.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBLGenBankDDBJ

L14837 mRNA. Translation: AAA02891.1. Different initiation.
AK304758 mRNA. Translation: BAG65513.1.
DQ015919 Genomic DNA. Translation: AAY22179.1.
BC111712 mRNA. Translation: AAI11713.1.

IPI

IPI00216219.
IPI00335824.

PIR

A47747.

RefSeq

NP_003248.3.
NP_783297.2.

UniGene

Hs.510833

3D structure databases

PDBPDBe

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	[»]
2RCZ	X-ray	1.70	A/B	186-264	[»]
3CYY	X-ray	2.40	A/B	182-273	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q07157. 21 interactions.

PTM databases

PhosphoSite

Q07157.

Proteomic databases

PRIDE

Q07157.

Genome annotation databases

Ensembl

ENSG00000104067. Homo sapiens. [Contig view]

GeneID

7082.

KEGG

hsa:7082.

Organism-specific databases

GeneCards

GC15M027779.

H-InvDB

HIX0026773.

HGNC

HGNC:11827. TJP1.

HPA

CAB010822.
HPA001636.
HPA001637.

MIM

601009. gene.

PharmGKB

PA36532.

GenAtlas

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Phylogenomic databases

HOGENOM

Q07157.

HOVERGEN

Q07157.

OMA

Q07157. DFQNSLV.

Enzyme and pathway databases

Reactome

REACT_578. Apoptosis.
REACT_9480. Gap junction trafficking and regulation.

Gene expression databases

ArrayExpress

Q07157.

Bgee

Q07157.

CleanEx

HS_TJP1.

GermOnline

ENSG00000104067. Homo sapiens.

Family and domain databases

InterPro

IPR019586. Gua_kin_assoc_C.
IPR008144. Guanylate_kin.
IPR008145. Guanylt/Ca.
IPR001478. PDZ/DHR/GLGF.
IPR011511. SH3_2.
IPR001452. SH3_domain.
IPR005417. ZonOcculdens.
IPR005418. ZonOcculS1.
IPR000906. ZU5.
[Graphical view]

PANTHER

PTHR13865:SF9. ZonOcculS1. 1 hit.

Pfam

PF10603. Gua_kin_assoc_C. 1 hit.
PF00625. Guanylate_kin. 1 hit.
PF00595. PDZ. 3 hits.
PF07653. SH3_2. 1 hit.
PF00791. ZU5. 1 hit.
[Graphical view]

PRINTS

PR01597. ZONOCCLUDNS.
PR01598. ZONOCCLUDNS1.

SMART

SM00072. GuKc. 1 hit.
SM00228. PDZ. 3 hits.
SM00326. SH3. 1 hit.
SM00218. ZU5. 1 hit.
[Graphical view]

PROSITE

PS00856. GUANYLATE_KINASE_1. False negative.
PS50052. GUANYLATE_KINASE_2. 1 hit.
PS50106. PDZ. 3 hits.
PS50002. SH3. 1 hit.
PS51145. ZU5. 1 hit.
[Graphical view]

ProtoNet

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Other Resources

NextBio

27699.

SOURCE

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Entry information

Entry name

ZO1_HUMAN

Accession

Primary (citable) accession number: Q07157
Secondary accession number(s): B4E3K1, Q2NKP3, Q4ZGJ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	January 24, 2006
Last modified:	June 16, 2009
This is version 104 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)