Reviewed, UniProtKB/Swiss-Prot Q9UDY2 (ZO2_HUMAN)

Names and origin

Protein names

Recommended name:
    Tight junction protein ZO-2
Alternative name(s):
    Zonula occludens protein 2
    Zona occludens protein 2
    Tight junction protein 2

Gene names

Name:	TJP2
Synonyms:	X104, ZO2

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	1190 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Plays a role in tight junctions and adherens junctions.
Subunit structure	Homodimer, and heterodimer with ZO1. Interacts with occludin, SAFB and UBN1. Interaction with SAFB occurs in the nucleus. Ref.20 Ref.21
Subcellular location	Cell junction › adherens junction. Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cell junction › tight junction By similarity. Nucleus By similarity. Note: Also nuclear under environmental stress conditions and in migratory endothelial cells and subconfluent epithelial cell cultures By similarity.
Tissue specificity	This protein is found in epithelial cell junctions. Isoform A1 is abundant in the heart and brain whereas isoform C1 is expressed at high level in the kidney, pancreas, heart and placenta. In brain and skeletal muscle, only isoform A1 is detectable. Isoform C1 is found in normal as well as in most neoplastic tissues while isoform A1 is present almost exclusively in normal tissue.
Involvement in disease	Defects in TJP2 are involved in familial hypercholanemia (FHCA) [MIM:607748]. FHCA is a disorder characterized by elevated serum bile acid concentrations, itching, and fat malabsorption. Ref.22
Sequence similarities	Belongs to the MAGUK family. Contains 1 guanylate kinase-like domain. Contains 3 PDZ (DHR) domains. Contains 1 SH3 domain.
Sequence caution	The sequence AAA61300.1 differs from that shown. Reason: Frameshift at positions 1086, 1092 and 1095.

Ontologies

Keywords
Cellular component	Cell junction Cell membrane Membrane Nucleus Tight junction
Coding sequence diversity	Alternative promoter usage Alternative splicing Polymorphism
Disease	Disease mutation
Domain	Repeat SH3 domain
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Cellular component	adherens junction Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from direct assay. Source: HPA nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell tight junction Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	guanylate kinase activity Traceable author statement. Source: ProtInc protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TRAF6	Q9Y4K3	1	EBI-1042602,EBI-359276
YWHAB	P31946	1	EBI-1042602,EBI-359815
YWHAG	P61981	1	EBI-1042602,EBI-359832
YWHAQ	P27348	1	EBI-1042602,EBI-359854
YWHAZ	P63104	1	EBI-1042602,EBI-347088

Alternative products

This entry describes 5 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]

Isoform A1 (identifier: Q9UDY2-1)

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.

Note: Produced by alternative promoter usage.

Isoform A2 (identifier: Q9UDY2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     961-1108: Missing.

Note: Produced by alternative splicing of isoform A1.

Isoform A3 (identifier: Q9UDY2-5)

The sequence of this isoform differs from the canonical sequence as follows:
     961-993: SIRKPSPEPRAQMRRAASSDQLRDNSPPPAFKP → VRRGRPRAGTGEPGVFLALSWTAVCSGCCGRHS
     994-1190: Missing.

Note: Produced by alternative splicing of isoform A1.

Isoform C1 (identifier: Q9UDY2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: Missing.

Note: Produced by alternative promoter usage.

Isoform C2 (identifier: Q9UDY2-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: Missing.
     961-1108: Missing.

Note: Produced by alternative splicing of isoform C1.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1190

1190

Tight junction protein ZO-2

PRO_0000094543

Regions

Domain

33 – 120

88

PDZ 1

Domain

307 – 385

79

PDZ 2

Domain

509 – 590

82

PDZ 3

Domain

604 – 669

66

SH3

Domain

678 – 876

199

Guanylate kinase-like

Compositional bias

1162 – 1165

4

Poly-Glu

Amino acid modifications

Modified residue

130

1

Phosphoserine Ref.12 Ref.17

Modified residue

168

1

Phosphoserine Ref.16

Modified residue

170

1

Phosphoserine Ref.12 Ref.17 Ref.16 Ref.10

Modified residue

174

1

Phosphoserine Ref.17 Ref.16 Ref.10

Modified residue

192

1

Phosphoserine Ref.12

Modified residue

244

1

Phosphoserine Ref.12 Ref.17 Ref.16 Ref.10

Modified residue

261

1

Phosphotyrosine Ref.14

Modified residue

265

1

Phosphotyrosine By similarity

Modified residue

266

1

Phosphoserine Ref.17 Ref.16 Ref.9 Ref.13

Modified residue

296

1

Phosphoserine Ref.9

Modified residue

394

1

Phosphoserine Ref.12

Modified residue

398

1

Phosphoserine Ref.12 Ref.17

Modified residue

400

1

Phosphoserine Ref.12 Ref.17

Modified residue

415

1

Phosphoserine Ref.16 Ref.10

Modified residue

440

1

Phosphoserine Ref.12

Modified residue

441

1

Phosphoserine Ref.12

Modified residue

445

1

Phosphothreonine Ref.12

Modified residue

455

1

Phosphothreonine Ref.17

Modified residue

574

1

Phosphotyrosine Ref.11

Modified residue

702

1

Phosphoserine Ref.16

Modified residue

920

1

Phosphoserine Ref.17

Modified residue

925

1

Phosphothreonine Ref.17

Modified residue

933

1

Phosphothreonine Ref.17

Modified residue

966

1

Phosphoserine Ref.16

Modified residue

978

1

Phosphoserine Ref.17 Ref.16

Modified residue

986

1

Phosphoserine Ref.12 Ref.17 Ref.16

Modified residue

1067

1

Phosphoserine Ref.17

Modified residue

1068

1

Phosphoserine Ref.17

Modified residue

1118

1

Phosphotyrosine Ref.14

Modified residue

1131

1

Phosphothreonine Ref.17 Ref.15

Modified residue

1159

1

Phosphoserine Ref.17 Ref.16 Ref.9 Ref.18

Natural variations

Alternative sequence

1 – 23

23

Missing in isoform C1 and isoform C2.

VSP_006953

Alternative sequence

961 – 1108

148

Missing in isoform A2 and isoform C2.

VSP_003149

Alternative sequence

961 – 993

33

SIRKP…PAFKP → VRRGRPRAGTGEPGVFLALS WTAVCSGCCGRHS in isoform A3.

VSP_007835

Alternative sequence

994 – 1190

197

Missing in isoform A3.

VSP_007836

Natural variant

48

1

V → A in FHCA. Ref.22

VAR_016004

Natural variant

482

1

E → D: dbSNP rs2309428. Ref.4 Ref.5

VAR_030798

Natural variant

668

1

M → I: dbSNP rs34774441.

VAR_046675

Natural variant

711

1

S → P: dbSNP rs35797487.

VAR_046676

Natural variant

822

1

K → N: dbSNP rs1049624. Ref.1

VAR_046677

Natural variant

829

1

N → D: dbSNP rs1049625. Ref.1

VAR_046678

Experimental info

Sequence conflict

411

1

N → T in AAA61300. Ref.1

Sequence conflict

411

1

N → T in AAM28524. Ref.3

Sequence conflict

782

1

I → V in AAA61300. Ref.1

Sequence conflict

782

1

I → V in AAM28524. Ref.3

Sequence conflict

808

1

P → S in AAA61300. Ref.1

Sequence conflict

812 – 814

3

FFN → SFT in AAA61300. Ref.1

Sequence conflict

834

1

K → N in AAA61300. Ref.1

Sequence conflict

842

1

Q → H in AAA61300. Ref.1

Sequence conflict

996

1

P → S in AAA61300. Ref.1

Sequence conflict

1136

1

S → N in AAB41794. Ref.8

Sequence conflict

1155 – 1158

4

GSYG → RSFC in AAB41794. Ref.8

Sequence conflict

1165 – 1167

3

EYR → IRS Ref.8

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1190

Helix Strand Turn

Details...

Beta strand

306 – 311

6

Beta strand

315 – 317

3

Beta strand

321 – 332

12

Helix

337 – 341

5

Beta strand

349 – 353

5

Helix

363 – 372

10

Beta strand

375 – 381

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform A1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: BE2BE6F181467058	FASTA	1,190	133,972
	10 20 30 40 50 60 MPVRGDRGFP PRRELSGWLR APGMEELIWE QYTVTLQKDS KRGFGIAVSG GRDNPHFENG 70 80 90 100 110 120 ETSIVISDVL PGGPADGLLQ ENDRVVMVNG TPMEDVLHSF AVQQLRKSGK VAAIVVKRPR 130 140 150 160 170 180 KVQVAALQAS PPLDQDDRAF EVMDEFDGRS FRSGYSERSR LNSHGGRSRS WEDSPERGRP 190 200 210 220 230 240 HERARSRERD LSRDRSRGRS LERGLDQDHA RTRDRSRGRS LERGLDHDFG PSRDRDRDRS 250 260 270 280 290 300 RGRSIDQDYE RAYHRAYDPD YERAYSPEYR RGARHDARSR GPRSRSREHP HSRSPSPEPR 310 320 330 340 350 360 GRPGPIGVLL MKSRANEEYG LRLGSQIFVK EMTRTGLATK DGNLHEGDII LKINGTVTEN 370 380 390 400 410 420 MSLTDARKLI EKSRGKLQLV VLRDSQQTLI NIPSLNDSDS EIEDISEIES NRSFSPEERR 430 440 450 460 470 480 HQYSDYDYHS SSEKLKERPS SREDTPSRLS RMGATPTPFK STGDIAGTVV PETNKEPRYQ 490 500 510 520 530 540 EEPPAPQPKA APRTFLRPSP EDEAIYGPNT KMVRFKKGDS VGLRLAGGND VGIFVAGIQE 550 560 570 580 590 600 GTSAEQEGLQ EGDQILKVNT QDFRGLVRED AVLYLLEIPK GEMVTILAQS RADVYRDILA 610 620 630 640 650 660 CGRGDSFFIR SHFECEKETP QSLAFTRGEV FRVVDTLYDG KLGNWLAVRI GNELEKGLIP 670 680 690 700 710 720 NKSRAEQMAS VQNAQRDNAG DRADFWRMRG QRSGVKKNLR KSREDLTAVV SVSTKFPAYE 730 740 750 760 770 780 RVLLREAGFK RPVVLFGPIA DIAMEKLANE LPDWFQTAKT EPKDAGSEKS TGVVRLNTVR 790 800 810 820 830 840 QIIEQDKHAL LDVTPKAVDL LNYTQWFPIV IFFNPDSRQG VKTMRQRLNP TSNKSSRKLF 850 860 870 880 890 900 DQANKLKKTC AHLFTATINL NSANDSWFGS LKDTIQHQQG EAVWVSEGKM EGMDDDPEDR 910 920 930 940 950 960 MSYLTAMGAD YLSCDSRLIS DFEDTDGEGG AYTDNELDEP AEEPLVSSIT RSSEPVQHEE 970 980 990 1000 1010 1020 SIRKPSPEPR AQMRRAASSD QLRDNSPPPA FKPEPPKAKT QNKEESYDFS KSYEYKSNPS 1030 1040 1050 1060 1070 1080 AVAGNETPGA STKGYPPPVA AKPTFGRSIL KPSTPIPPQE GEEVGESSEE QDNAPKSVLG 1090 1100 1110 1120 1130 1140 KVKIFEKMDH KARLQRMQEL QEAQNARIEI AQKHPDIYAV PIKTHKPDPG TPQHTSSRPP 1150 1160 1170 1180 1190 EPQKAPSRPY QDTRGSYGSD AEEEEYRQQL SEHSKRGYYG QSARYRDTEL
	Isoform A2. Checksum: ECBAD3D0FA2BF09C	FASTA	1,042	117,659
	10 20 30 40 50 60 MPVRGDRGFP PRRELSGWLR APGMEELIWE QYTVTLQKDS KRGFGIAVSG GRDNPHFENG 70 80 90 100 110 120 ETSIVISDVL PGGPADGLLQ ENDRVVMVNG TPMEDVLHSF AVQQLRKSGK VAAIVVKRPR 130 140 150 160 170 180 KVQVAALQAS PPLDQDDRAF EVMDEFDGRS FRSGYSERSR LNSHGGRSRS WEDSPERGRP 190 200 210 220 230 240 HERARSRERD LSRDRSRGRS LERGLDQDHA RTRDRSRGRS LERGLDHDFG PSRDRDRDRS 250 260 270 280 290 300 RGRSIDQDYE RAYHRAYDPD YERAYSPEYR RGARHDARSR GPRSRSREHP HSRSPSPEPR 310 320 330 340 350 360 GRPGPIGVLL MKSRANEEYG LRLGSQIFVK EMTRTGLATK DGNLHEGDII LKINGTVTEN 370 380 390 400 410 420 MSLTDARKLI EKSRGKLQLV VLRDSQQTLI NIPSLNDSDS EIEDISEIES NRSFSPEERR 430 440 450 460 470 480 HQYSDYDYHS SSEKLKERPS SREDTPSRLS RMGATPTPFK STGDIAGTVV PETNKEPRYQ 490 500 510 520 530 540 EEPPAPQPKA APRTFLRPSP EDEAIYGPNT KMVRFKKGDS VGLRLAGGND VGIFVAGIQE 550 560 570 580 590 600 GTSAEQEGLQ EGDQILKVNT QDFRGLVRED AVLYLLEIPK GEMVTILAQS RADVYRDILA 610 620 630 640 650 660 CGRGDSFFIR SHFECEKETP QSLAFTRGEV FRVVDTLYDG KLGNWLAVRI GNELEKGLIP 670 680 690 700 710 720 NKSRAEQMAS VQNAQRDNAG DRADFWRMRG QRSGVKKNLR KSREDLTAVV SVSTKFPAYE 730 740 750 760 770 780 RVLLREAGFK RPVVLFGPIA DIAMEKLANE LPDWFQTAKT EPKDAGSEKS TGVVRLNTVR 790 800 810 820 830 840 QIIEQDKHAL LDVTPKAVDL LNYTQWFPIV IFFNPDSRQG VKTMRQRLNP TSNKSSRKLF 850 860 870 880 890 900 DQANKLKKTC AHLFTATINL NSANDSWFGS LKDTIQHQQG EAVWVSEGKM EGMDDDPEDR 910 920 930 940 950 960 MSYLTAMGAD YLSCDSRLIS DFEDTDGEGG AYTDNELDEP AEEPLVSSIT RSSEPVQHEE 970 980 990 1000 1010 1020 EIAQKHPDIY AVPIKTHKPD PGTPQHTSSR PPEPQKAPSR PYQDTRGSYG SDAEEEEYRQ 1030 1040 QLSEHSKRGY YGQSARYRDT EL
	Isoform A3. Checksum: 9A6279A73851A6D3	FASTA	993	111,677
	10 20 30 40 50 60 MPVRGDRGFP PRRELSGWLR APGMEELIWE QYTVTLQKDS KRGFGIAVSG GRDNPHFENG 70 80 90 100 110 120 ETSIVISDVL PGGPADGLLQ ENDRVVMVNG TPMEDVLHSF AVQQLRKSGK VAAIVVKRPR 130 140 150 160 170 180 KVQVAALQAS PPLDQDDRAF EVMDEFDGRS FRSGYSERSR LNSHGGRSRS WEDSPERGRP 190 200 210 220 230 240 HERARSRERD LSRDRSRGRS LERGLDQDHA RTRDRSRGRS LERGLDHDFG PSRDRDRDRS 250 260 270 280 290 300 RGRSIDQDYE RAYHRAYDPD YERAYSPEYR RGARHDARSR GPRSRSREHP HSRSPSPEPR 310 320 330 340 350 360 GRPGPIGVLL MKSRANEEYG LRLGSQIFVK EMTRTGLATK DGNLHEGDII LKINGTVTEN 370 380 390 400 410 420 MSLTDARKLI EKSRGKLQLV VLRDSQQTLI NIPSLNDSDS EIEDISEIES NRSFSPEERR 430 440 450 460 470 480 HQYSDYDYHS SSEKLKERPS SREDTPSRLS RMGATPTPFK STGDIAGTVV PETNKEPRYQ 490 500 510 520 530 540 EEPPAPQPKA APRTFLRPSP EDEAIYGPNT KMVRFKKGDS VGLRLAGGND VGIFVAGIQE 550 560 570 580 590 600 GTSAEQEGLQ EGDQILKVNT QDFRGLVRED AVLYLLEIPK GEMVTILAQS RADVYRDILA 610 620 630 640 650 660 CGRGDSFFIR SHFECEKETP QSLAFTRGEV FRVVDTLYDG KLGNWLAVRI GNELEKGLIP 670 680 690 700 710 720 NKSRAEQMAS VQNAQRDNAG DRADFWRMRG QRSGVKKNLR KSREDLTAVV SVSTKFPAYE 730 740 750 760 770 780 RVLLREAGFK RPVVLFGPIA DIAMEKLANE LPDWFQTAKT EPKDAGSEKS TGVVRLNTVR 790 800 810 820 830 840 QIIEQDKHAL LDVTPKAVDL LNYTQWFPIV IFFNPDSRQG VKTMRQRLNP TSNKSSRKLF 850 860 870 880 890 900 DQANKLKKTC AHLFTATINL NSANDSWFGS LKDTIQHQQG EAVWVSEGKM EGMDDDPEDR 910 920 930 940 950 960 MSYLTAMGAD YLSCDSRLIS DFEDTDGEGG AYTDNELDEP AEEPLVSSIT RSSEPVQHEE 970 980 990 VRRGRPRAGT GEPGVFLALS WTAVCSGCCG RHS
	Isoform C1. Checksum: 08EC680BD978D8AA	FASTA	1,167	131,382
	10 20 30 40 50 60 MEELIWEQYT VTLQKDSKRG FGIAVSGGRD NPHFENGETS IVISDVLPGG PADGLLQEND 70 80 90 100 110 120 RVVMVNGTPM EDVLHSFAVQ QLRKSGKVAA IVVKRPRKVQ VAALQASPPL DQDDRAFEVM 130 140 150 160 170 180 DEFDGRSFRS GYSERSRLNS HGGRSRSWED SPERGRPHER ARSRERDLSR DRSRGRSLER 190 200 210 220 230 240 GLDQDHARTR DRSRGRSLER GLDHDFGPSR DRDRDRSRGR SIDQDYERAY HRAYDPDYER 250 260 270 280 290 300 AYSPEYRRGA RHDARSRGPR SRSREHPHSR SPSPEPRGRP GPIGVLLMKS RANEEYGLRL 310 320 330 340 350 360 GSQIFVKEMT RTGLATKDGN LHEGDIILKI NGTVTENMSL TDARKLIEKS RGKLQLVVLR 370 380 390 400 410 420 DSQQTLINIP SLNDSDSEIE DISEIESNRS FSPEERRHQY SDYDYHSSSE KLKERPSSRE 430 440 450 460 470 480 DTPSRLSRMG ATPTPFKSTG DIAGTVVPET NKEPRYQEEP PAPQPKAAPR TFLRPSPEDE 490 500 510 520 530 540 AIYGPNTKMV RFKKGDSVGL RLAGGNDVGI FVAGIQEGTS AEQEGLQEGD QILKVNTQDF 550 560 570 580 590 600 RGLVREDAVL YLLEIPKGEM VTILAQSRAD VYRDILACGR GDSFFIRSHF ECEKETPQSL 610 620 630 640 650 660 AFTRGEVFRV VDTLYDGKLG NWLAVRIGNE LEKGLIPNKS RAEQMASVQN AQRDNAGDRA 670 680 690 700 710 720 DFWRMRGQRS GVKKNLRKSR EDLTAVVSVS TKFPAYERVL LREAGFKRPV VLFGPIADIA 730 740 750 760 770 780 MEKLANELPD WFQTAKTEPK DAGSEKSTGV VRLNTVRQII EQDKHALLDV TPKAVDLLNY 790 800 810 820 830 840 TQWFPIVIFF NPDSRQGVKT MRQRLNPTSN KSSRKLFDQA NKLKKTCAHL FTATINLNSA 850 860 870 880 890 900 NDSWFGSLKD TIQHQQGEAV WVSEGKMEGM DDDPEDRMSY LTAMGADYLS CDSRLISDFE 910 920 930 940 950 960 DTDGEGGAYT DNELDEPAEE PLVSSITRSS EPVQHEESIR KPSPEPRAQM RRAASSDQLR 970 980 990 1000 1010 1020 DNSPPPAFKP EPPKAKTQNK EESYDFSKSY EYKSNPSAVA GNETPGASTK GYPPPVAAKP 1030 1040 1050 1060 1070 1080 TFGRSILKPS TPIPPQEGEE VGESSEEQDN APKSVLGKVK IFEKMDHKAR LQRMQELQEA 1090 1100 1110 1120 1130 1140 QNARIEIAQK HPDIYAVPIK THKPDPGTPQ HTSSRPPEPQ KAPSRPYQDT RGSYGSDAEE 1150 1160 EEYRQQLSEH SKRGYYGQSA RYRDTEL
	Isoform C2. Checksum: DC790A47F4F210A3	FASTA	1,019	115,069
	10 20 30 40 50 60 MEELIWEQYT VTLQKDSKRG FGIAVSGGRD NPHFENGETS IVISDVLPGG PADGLLQEND 70 80 90 100 110 120 RVVMVNGTPM EDVLHSFAVQ QLRKSGKVAA IVVKRPRKVQ VAALQASPPL DQDDRAFEVM 130 140 150 160 170 180 DEFDGRSFRS GYSERSRLNS HGGRSRSWED SPERGRPHER ARSRERDLSR DRSRGRSLER 190 200 210 220 230 240 GLDQDHARTR DRSRGRSLER GLDHDFGPSR DRDRDRSRGR SIDQDYERAY HRAYDPDYER 250 260 270 280 290 300 AYSPEYRRGA RHDARSRGPR SRSREHPHSR SPSPEPRGRP GPIGVLLMKS RANEEYGLRL 310 320 330 340 350 360 GSQIFVKEMT RTGLATKDGN LHEGDIILKI NGTVTENMSL TDARKLIEKS RGKLQLVVLR 370 380 390 400 410 420 DSQQTLINIP SLNDSDSEIE DISEIESNRS FSPEERRHQY SDYDYHSSSE KLKERPSSRE 430 440 450 460 470 480 DTPSRLSRMG ATPTPFKSTG DIAGTVVPET NKEPRYQEEP PAPQPKAAPR TFLRPSPEDE 490 500 510 520 530 540 AIYGPNTKMV RFKKGDSVGL RLAGGNDVGI FVAGIQEGTS AEQEGLQEGD QILKVNTQDF 550 560 570 580 590 600 RGLVREDAVL YLLEIPKGEM VTILAQSRAD VYRDILACGR GDSFFIRSHF ECEKETPQSL 610 620 630 640 650 660 AFTRGEVFRV VDTLYDGKLG NWLAVRIGNE LEKGLIPNKS RAEQMASVQN AQRDNAGDRA 670 680 690 700 710 720 DFWRMRGQRS GVKKNLRKSR EDLTAVVSVS TKFPAYERVL LREAGFKRPV VLFGPIADIA 730 740 750 760 770 780 MEKLANELPD WFQTAKTEPK DAGSEKSTGV VRLNTVRQII EQDKHALLDV TPKAVDLLNY 790 800 810 820 830 840 TQWFPIVIFF NPDSRQGVKT MRQRLNPTSN KSSRKLFDQA NKLKKTCAHL FTATINLNSA 850 860 870 880 890 900 NDSWFGSLKD TIQHQQGEAV WVSEGKMEGM DDDPEDRMSY LTAMGADYLS CDSRLISDFE 910 920 930 940 950 960 DTDGEGGAYT DNELDEPAEE PLVSSITRSS EPVQHEEEIA QKHPDIYAVP IKTHKPDPGT 970 980 990 1000 1010 PQHTSSRPPE PQKAPSRPYQ DTRGSYGSDA EEEEYRQQLS EHSKRGYYGQ SARYRDTEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Friedreich ataxia region: characterization of two novel genes and reduction of the critical region to 300 kb." Duclos F., Rodius F., Wrogemann K., Mandel J.-L., Koenig M. Hum. Mol. Genet. 3:909-914(1994) [PubMed: 7951235] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A1), VARIANTS ASN-822 AND ASP-829. Tissue: Brain.
[2]	"Organization and expression of the human zo-2 gene (tjp-2) in normal and neoplastic tissues." Chlenski A., Ketels K.V., Korovaitseva G.I., Talamonti M.S., Oyasu R., Scarpelli D.G. Biochim. Biophys. Acta 1493:319-324(2000) [PubMed: 11018256] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS A1; C1; A2 AND C2), ALTERNATIVE PROMOTER USAGE. Tissue: Pancreas.
[3]	"LIM protein KyoT2 interacts with human tight junction protein ZO-2-i3." Yan H.H., Rong L., Qiang S., Jian W., Peng Z., Hua H., Hui Z.W. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A3).
[4]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed: 15164053] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASP-482.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A1), VARIANT ASP-482. Tissue: Testis.
[6]	"Tight junction protein ZO-2 is differentially expressed in normal pancreatic ducts compared to human pancreatic adenocarcinoma." Chlenski A., Ketels K.V., Tsao M.-S., Talamonti M.S., Anderson M.R., Oyasu R., Scarpelli D.G. Int. J. Cancer 82:137-144(1999) [PubMed: 10360833] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 1-104 (ISOFORMS A1 AND C1). Tissue: Pancreas.
[7]	"Zo-2 gene alternative promoters in normal and neoplastic human pancreatic duct cells." Chlenski A., Ketels K.V., Engeriser J.L., Talamonti M.S., Tsao M.-S., Koutnikova H., Oyasu R., Scarpelli D.G. Int. J. Cancer 83:349-358(1999) [PubMed: 10495427] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE (ISOFORMS A1 AND C1), ALTERNATIVE PROMOTER USAGE. Tissue: Pancreas.
[8]	Adams L.D., Werny I., Schwartz S.M. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE OF 1047-1167. Tissue: Aortic smooth muscle.
[9]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266; SER-296 AND SER-1159, MASS SPECTROMETRY. Tissue: Epithelium.
[10]	"Global phosphoproteome of HT-29 human colon adenocarcinoma cells." Kim J.-E., Tannenbaum S.R., White F.M. J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170; SER-174; SER-244 AND SER-415, MASS SPECTROMETRY.
[11]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-574, MASS SPECTROMETRY.
[12]	"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-130; SER-170; SER-192; SER-244; SER-394; SER-398; SER-400; SER-440; SER-441; THR-445 AND SER-986, MASS SPECTROMETRY. Tissue: Epithelium.
[13]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, MASS SPECTROMETRY. Tissue: Epithelium.
[14]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-261 AND TYR-1118, MASS SPECTROMETRY.
[15]	"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 THR-1131, MASS SPECTROMETRY.
[16]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168; SER-170; SER-174; SER-244; SER-266; SER-415; SER-702; SER-966; SER-978; SER-986 AND SER-1159, MASS SPECTROMETRY. Tissue: Platelet.
[17]	"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-130; SER-170; SER-174; SER-244; SER-266; SER-398; SER-400; THR-455; SER-920; THR-925; THR-933; SER-978; SER-986; SER-1067; SER-1068; THR-1131 AND SER-1159, MASS SPECTROMETRY.
[18]	"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1159, MASS SPECTROMETRY. Tissue: Liver.
[19]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[20]	"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.
[21]	"Domain-swapped dimerization of the second PDZ domain of ZO2 may provide a structural basis for the polymerization of claudins." Wu J., Yang Y., Zhang J., Ji P., Du W., Jiang P., Xie D., Huang H., Wu M., Zhang G., Wu J., Shi Y. J. Biol. Chem. 282:35988-35999(2007) [PubMed: 17897942] [Abstract] Cited for: STRUCTURE BY NMR OF 306-385, SUBUNIT.
[22]	"Complex inheritance of familial hypercholanemia with associated mutations in TJP2 and BAAT." Carlton V.E.H., Harris B.Z., Puffenberger E.G., Batta A.K., Knisely A.S., Robinson D.L., Strauss K.A., Shneider B.L., Lim W.A., Salen G., Morton D.H., Bull L.N. Nat. Genet. 34:91-96(2003) [PubMed: 12704386] [Abstract] Cited for: VARIANT FHCA ALA-48.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L27476 mRNA. Translation: AAA61300.1. Frameshift.
AF177533 , AF043195, AF043196, AF043197, AF177518, AF177519, AF177520, AF177521, AF177522, AF177523, AF177524, AF177525, AF177526, AF177527, AF177528, AF177529, AF177530, AF177531, AF177532 Genomic DNA. Translation: AAD20387.2.
AF177533 , AF043196, AF043197, AF177518, AF177519, AF177520, AF177521, AF177522, AF177523, AF177524, AF177525, AF177526, AF177527, AF177528, AF177529, AF177530, AF177531, AF177532 Genomic DNA. Translation: AAC02527.2.
AF177533 , AF043195, AF043196, AF043197, AF177518, AF177519, AF177520, AF177521, AF177522, AF177523, AF177524, AF177525, AF177526, AF177527, AF177528, AF177529, AF177532 Genomic DNA. Translation: AAD56218.2.
AF177533 , AF043196, AF043197, AF177518, AF177519, AF177520, AF177521, AF177522, AF177523, AF177524, AF177525, AF177526, AF177527, AF177528, AF177529, AF177532 Genomic DNA. Translation: AAD56219.2.
AF489824 mRNA. Translation: AAM28524.1.
AL358113 Genomic DNA. Translation: CAH70868.1.
BC027592 mRNA. Translation: AAH27592.1.
AF083892 mRNA. Translation: AAC33121.1.
AF083893 mRNA. Translation: AAC33122.1.
U84581 mRNA. Translation: AAB41794.1.

IPI

IPI00003843.
IPI00216245.
IPI00216246.
IPI00332453.
IPI00797934.

PIR

I54378.

RefSeq

NP_004808.2.
NP_963923.1.

UniGene

Hs.50382

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2OSG	NMR	-	A/B	306-385	[»]

SMR

Q9UDY2. Positions 21-129.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9UDY2. 5 interactions.

PTM databases

PhosphoSite

Q9UDY2.

Proteomic databases

PRIDE

Q9UDY2.

Genome annotation databases

Ensembl

ENSG00000119139. Homo sapiens. [Contig view]

GeneID

9414.

KEGG

hsa:9414.

Organism-specific databases

GeneCards

GC09P070956.

H-InvDB

HIX0079048.

HGNC

HGNC:11828. TJP2.

HPA

CAB009228.
HPA001813.

MIM

607709. gene.
607748. phenotype.

PharmGKB

PA36533.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q9UDY2.

Enzyme and pathway databases

Reactome

REACT_578. Apoptosis.

Gene expression databases

ArrayExpress

Q9UDY2.

Bgee

Q9UDY2.

CleanEx

HS_TJP2.

GermOnline

ENSG00000119139. Homo sapiens.

Family and domain databases

InterPro

IPR008144. Guanylate_kin.
IPR008145. Guanylt/Ca.
IPR001478. PDZ/DHR/GLGF.
IPR011511. SH3_2.
IPR001452. SH3_domain.
IPR005417. ZonOcculdens.
IPR005419. ZonOcculS2.
[Graphical view]

Pfam

PF00625. Guanylate_kin. 1 hit.
PF00595. PDZ. 3 hits.
PF07653. SH3_2. 1 hit.
[Graphical view]

PRINTS

PR01597. ZONOCCLUDNS.
PR01599. ZONOCCLUDNS2.

SMART

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

ProtoNet

Search...

Other Resources

NextBio

35268.

SOURCE

Search...

Entry information

Entry name

ZO2_HUMAN

Accession

Primary (citable) accession number: Q9UDY2
Secondary accession number(s): Q15883 , Q5VXL0, Q8N756, Q8NI14, Q99839, Q9UDY0, Q9UDY1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	May 1, 2000
Last modified:	June 16, 2009
This is version 99 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)