ZO3_HUMAN - dbPTM
ZO3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZO3_HUMAN
UniProt AC O95049
Protein Name Tight junction protein ZO-3
Gene Name TJP3
Organism Homo sapiens (Human).
Sequence Length 919
Subcellular Localization Cell membrane
Peripheral membrane protein
Cytoplasmic side . Cell junction, tight junction . Nucleus . Exhibits predominant nuclear expression in proliferating cells but is exclusively junctionally expressed after confluence is reached (PubMed:23
Protein Description TJP1, TJP2, and TJP3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton. [PubMed: 16129888 The tight junction acts to limit movement of substances through the paracellular space and as a boundary between the compositionally distinct apical and basolateral plasma membrane domains of epithelial and endothelial cells. Binds and recruits PATJ to tight junctions where it connects and stabilizes apical and lateral components of tight junctions]
Protein Sequence MEELTIWEQHTATLSKDPRRGFGIAISGGRDRPGGSMVVSDVVPGGPAEGRLQTGDHIVMVNGVSMENATSAFAIQILKTCTKMANITVKRPRRIHLPATKASPSSPGRQDSDEDDGPQRVEEVDQGRGYDGDSSSGSGRSWDERSRRPRPGRRGRAGSHGRRSPGGGSEANGLALVSGFKRLPRQDVQMKPVKSVLVKRRDSEEFGVKLGSQIFIKHITDSGLAARHRGLQEGDLILQINGVSSQNLSLNDTRRLIEKSEGKLSLLVLRDRGQFLVNIPPAVSDSDSSPLEDISDLASELSQAPPSHIPPPPRHAQRSPEASQTDSPVESPRLRRESSVDSRTISEPDEQRSELPRESSYDIYRVPSSQSMEDRGYSPDTRVVRFLKGKSIGLRLAGGNDVGIFVSGVQAGSPADGQGIQEGDQILQVNDVPFQNLTREEAVQFLLGLPPGEEMELVTQRKQDIFWKMVQSRVGDSFYIRTHFELEPSPPSGLGFTRGDVFHVLDTLHPGPGQSHARGGHWLAVRMGRDLREQERGIIPNQSRAEQLASLEAAQRAVGVGPGSSAGSNARAEFWRLRGLRRGAKKTTQRSREDLSALTRQGRYPPYERVVLREASFKRPVVILGPVADIAMQKLTAEMPDQFEIAETVSRTDSPSKIIKLDTVRVIAEKDKHALLDVTPSAIERLNYVQYYPIVVFFIPESRPALKALRQWLAPASRRSTRRLYAQAQKLRKHSSHLFTATIPLNGTSDTWYQELKAIIREQQTRPIWTAEDQLDGSLEDNLDLPHHGLADSSADLSCDSRVNSDYETDGEGGAYTDGEGYTDGEGGPYTDVDDEPPAPALARSSEPVQADESQSPRDRGRISAHQGAQVDSRHPQGQWRQDSMRTYEREALKKKFMRVHDAESSDEDGYDWGPATDL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
27PhosphorylationRGFGIAISGGRDRPG
CCCCEEEECCCCCCC
26.6027251275
36PhosphorylationGRDRPGGSMVVSDVV
CCCCCCCCEEEEECC
17.8323312004
40PhosphorylationPGGSMVVSDVVPGGP
CCCCEEEEECCCCCC
17.1823312004
45PhosphorylationVVSDVVPGGPAEGRL
EEEECCCCCCCCCCC
43.0127251275
103PhosphorylationHLPATKASPSSPGRQ
CCCCCCCCCCCCCCC
27.2030278072
105PhosphorylationPATKASPSSPGRQDS
CCCCCCCCCCCCCCC
46.8226657352
106PhosphorylationATKASPSSPGRQDSD
CCCCCCCCCCCCCCC
34.4630278072
112PhosphorylationSSPGRQDSDEDDGPQ
CCCCCCCCCCCCCCC
34.2630278072
121PhosphorylationEDDGPQRVEEVDQGR
CCCCCCCCEEECCCC
6.5727251275
130PhosphorylationEVDQGRGYDGDSSSG
EECCCCCCCCCCCCC
18.5222210691
134PhosphorylationGRGYDGDSSSGSGRS
CCCCCCCCCCCCCCC
31.7523909892
135PhosphorylationRGYDGDSSSGSGRSW
CCCCCCCCCCCCCCC
43.3823909892
136PhosphorylationGYDGDSSSGSGRSWD
CCCCCCCCCCCCCCC
40.7123909892
138PhosphorylationDGDSSSGSGRSWDER
CCCCCCCCCCCCCHH
32.7423909892
141PhosphorylationSSSGSGRSWDERSRR
CCCCCCCCCCHHCCC
42.2633259812
150PhosphorylationDERSRRPRPGRRGRA
CHHCCCCCCCCCCCC
44.4833259812
159PhosphorylationGRRGRAGSHGRRSPG
CCCCCCCCCCCCCCC
23.0622617229
164PhosphorylationAGSHGRRSPGGGSEA
CCCCCCCCCCCCCHH
26.9123927012
168PhosphorylationGRRSPGGGSEANGLA
CCCCCCCCCHHHCEE
28.3827251275
169PhosphorylationRRSPGGGSEANGLAL
CCCCCCCCHHHCEEE
36.4930266825
173PhosphorylationGGGSEANGLALVSGF
CCCCHHHCEEECCCC
21.2627251275
178PhosphorylationANGLALVSGFKRLPR
HHCEEECCCCCCCCC
39.0923090842
203PhosphorylationVLVKRRDSEEFGVKL
EEEECCCHHHHCCCC
36.9028355574
212PhosphorylationEFGVKLGSQIFIKHI
HHCCCCCCEEEEEEE
30.4620068231
220PhosphorylationQIFIKHITDSGLAAR
EEEEEEECCCCHHHH
24.6720068231
221PhosphorylationIFIKHITDSGLAARH
EEEEEECCCCHHHHH
39.8527251275
222PhosphorylationFIKHITDSGLAARHR
EEEEECCCCHHHHHC
27.3623312004
259UbiquitinationDTRRLIEKSEGKLSL
HHHHHHHHCCCCEEE
46.9829967540
260PhosphorylationTRRLIEKSEGKLSLL
HHHHHHHCCCCEEEE
38.5023312004
265PhosphorylationEKSEGKLSLLVLRDR
HHCCCCEEEEEEECC
24.1228348404
268UbiquitinationEGKLSLLVLRDRGQF
CCCEEEEEEECCCCE
5.1029967540
274PhosphorylationLVLRDRGQFLVNIPP
EEEECCCCEEEECCC
29.4227251275
319PhosphorylationPPRHAQRSPEASQTD
CCCCCCCCCCHHCCC
24.2428355574
323PhosphorylationAQRSPEASQTDSPVE
CCCCCCHHCCCCCCC
6.8630278072
325PhosphorylationRSPEASQTDSPVESP
CCCCHHCCCCCCCCH
51.4223927012
327PhosphorylationPEASQTDSPVESPRL
CCHHCCCCCCCCHHH
46.6030278072
328PhosphorylationEASQTDSPVESPRLR
CHHCCCCCCCCHHHH
43.4727251275
331PhosphorylationQTDSPVESPRLRRES
CCCCCCCCHHHHCCC
40.0130278072
332PhosphorylationTDSPVESPRLRRESS
CCCCCCCHHHHCCCC
55.7727251275
336PhosphorylationVESPRLRRESSVDSR
CCCHHHHCCCCCCCC
15.4327251275
338PhosphorylationSPRLRRESSVDSRTI
CHHHHCCCCCCCCCC
57.2725849741
339PhosphorylationPRLRRESSVDSRTIS
HHHHCCCCCCCCCCC
35.6325849741
340PhosphorylationRLRRESSVDSRTISE
HHHCCCCCCCCCCCC
43.2227251275
342PhosphorylationRRESSVDSRTISEPD
HCCCCCCCCCCCCCH
36.3825849741
344PhosphorylationESSVDSRTISEPDEQ
CCCCCCCCCCCCHHH
59.4123927012
346PhosphorylationSVDSRTISEPDEQRS
CCCCCCCCCCHHHHC
26.3123911959
347PhosphorylationVDSRTISEPDEQRSE
CCCCCCCCCHHHHCC
50.5427251275
352MethylationISEPDEQRSELPRES
CCCCHHHHCCCCCCC
33.57115367603
353PhosphorylationSEPDEQRSELPRESS
CCCHHHHCCCCCCCC
25.7823927012
355PhosphorylationPDEQRSELPRESSYD
CHHHHCCCCCCCCCC
34.0627251275
357MethylationEQRSELPRESSYDIY
HHHCCCCCCCCCCEE
31.45115367607
359PhosphorylationRSELPRESSYDIYRV
HCCCCCCCCCCEEEC
4.2226657352
360PhosphorylationSELPRESSYDIYRVP
CCCCCCCCCCEEECC
42.3328796482
361PhosphorylationELPRESSYDIYRVPS
CCCCCCCCCEEECCC
53.5828796482
364PhosphorylationRESSYDIYRVPSSQS
CCCCCCEEECCCCCC
59.6228796482
368PhosphorylationYDIYRVPSSQSMEDR
CCEEECCCCCCCCCC
66.0527273156
369PhosphorylationDIYRVPSSQSMEDRG
CEEECCCCCCCCCCC
5.2327273156
369O-linked_GlycosylationDIYRVPSSQSMEDRG
CEEECCCCCCCCCCC
5.2328580691
371PhosphorylationYRVPSSQSMEDRGYS
EECCCCCCCCCCCCC
69.8930278072
377PhosphorylationQSMEDRGYSPDTRVV
CCCCCCCCCCCCHHH
1.4727251275
378PhosphorylationSMEDRGYSPDTRVVR
CCCCCCCCCCCHHHH
11.5821815630
380PhosphorylationEDRGYSPDTRVVRFL
CCCCCCCCCHHHHHH
2.7927251275
381PhosphorylationDRGYSPDTRVVRFLK
CCCCCCCCHHHHHHC
21.1827794612
387PhosphorylationDTRVVRFLKGKSIGL
CCHHHHHHCCCCEEE
50.2127251275
479PhosphorylationSRVGDSFYIRTHFEL
HHCCCCEEEEEEEEE
4.04-
489PhosphorylationTHFELEPSPPSGLGF
EEEEECCCCCCCCCC
24.5926657352
492PhosphorylationELEPSPPSGLGFTRG
EECCCCCCCCCCCCC
7.5623312004
498PhosphorylationPSGLGFTRGDVFHVL
CCCCCCCCCCEEEEE
13.0127251275
518MethylationGPGQSHARGGHWLAV
CCCCCCCCCCCEEEE
3.3454560915
550PhosphorylationSRAEQLASLEAAQRA
CHHHHHHHHHHHHHH
41.1129743597
564PhosphorylationAVGVGPGSSAGSNAR
HHCCCCCCCCCHHHH
35.0223312004
565PhosphorylationVGVGPGSSAGSNARA
HCCCCCCCCCHHHHH
4.2825072903
568PhosphorylationGPGSSAGSNARAEFW
CCCCCCCHHHHHHHH
7.0425072903
573PhosphorylationAGSNARAEFWRLRGL
CCHHHHHHHHHHHHH
20.0627251275
587PhosphorylationLRRGAKKTTQRSRED
HHHHCCHHCCCCHHH
39.9427966365
588PhosphorylationRRGAKKTTQRSREDL
HHHCCHHCCCCHHHH
4.4926074081
591PhosphorylationAKKTTQRSREDLSAL
CCHHCCCCHHHHHHH
3.5730183078
596PhosphorylationQRSREDLSALTRQGR
CCCHHHHHHHHHCCC
55.2330278072
597PhosphorylationRSREDLSALTRQGRY
CCHHHHHHHHHCCCC
35.0027251275
599PhosphorylationREDLSALTRQGRYPP
HHHHHHHHHCCCCCC
54.1826074081
600PhosphorylationEDLSALTRQGRYPPY
HHHHHHHHCCCCCCH
57.1627251275
604PhosphorylationALTRQGRYPPYERVV
HHHHCCCCCCHHHHH
35.2726074081
607PhosphorylationRQGRYPPYERVVLRE
HCCCCCCHHHHHCCC
65.6326074081
616PhosphorylationRVVLREASFKRPVVI
HHHCCCCCCCCCEEE
28.0024719451
625PhosphorylationKRPVVILGPVADIAM
CCCEEEECHHHHHHH
5.3727251275
648PhosphorylationDQFEIAETVSRTDSP
CHHEEEEHHCCCCCC
34.4228348404
650PhosphorylationFEIAETVSRTDSPSK
HEEEEHHCCCCCCHH
27.8328348404
652PhosphorylationIAETVSRTDSPSKII
EEEHHCCCCCCHHEE
46.1123312004
654PhosphorylationETVSRTDSPSKIIKL
EHHCCCCCCHHEEEE
24.6125849741
656PhosphorylationVSRTDSPSKIIKLDT
HCCCCCCHHEEEEEE
31.8123312004
663PhosphorylationSKIIKLDTVRVIAEK
HHEEEEEEEEEEEEC
2.4728348404
679PhosphorylationKHALLDVTPSAIERL
CCEEECCCHHHHHHC
19.0621406692
681PhosphorylationALLDVTPSAIERLNY
EEECCCHHHHHHCCC
2.6121406692
717PhosphorylationRQWLAPASRRSTRRL
HHHHCHHCHHHHHHH
20.8828348404
725PhosphorylationRRSTRRLYAQAQKLR
HHHHHHHHHHHHHHH
40.1428152594
778PhosphorylationAEDQLDGSLEDNLDL
HHHHCCCCCCCCCCC
34.4228348404
787PhosphorylationEDNLDLPHHGLADSS
CCCCCCCCCCCCCCC
52.4527251275
793PhosphorylationPHHGLADSSADLSCD
CCCCCCCCCCCCCCC
13.5028348404
794PhosphorylationHHGLADSSADLSCDS
CCCCCCCCCCCCCCC
46.6928348404
803PhosphorylationDLSCDSRVNSDYETD
CCCCCCCCCCCCCCC
21.3727251275
805PhosphorylationSCDSRVNSDYETDGE
CCCCCCCCCCCCCCC
21.1629802988
814PhosphorylationYETDGEGGAYTDGEG
CCCCCCCCCCCCCCC
35.7827251275
845PhosphorylationPAPALARSSEPVQAD
CCCCCCCCCCCCCCC
32.4529396449
846PhosphorylationAPALARSSEPVQADE
CCCCCCCCCCCCCCC
35.6829396449
854PhosphorylationEPVQADESQSPRDRG
CCCCCCCCCCHHHHC
33.3122617229
855PhosphorylationPVQADESQSPRDRGR
CCCCCCCCCHHHHCC
18.8927251275
856PhosphorylationVQADESQSPRDRGRI
CCCCCCCCHHHHCCC
3.8619664994
863PhosphorylationSPRDRGRISAHQGAQ
CHHHHCCCCHHCCCC
6.8627251275
864PhosphorylationPRDRGRISAHQGAQV
HHHHCCCCHHCCCCC
54.5328348404
873PhosphorylationHQGAQVDSRHPQGQW
HCCCCCCCCCCCCCC
61.8527251275
884PhosphorylationQGQWRQDSMRTYERE
CCCCCHHHHHHHHHH
46.5024670416
893PhosphorylationRTYEREALKKKFMRV
HHHHHHHHHHHHCCH
27.2527251275
905PhosphorylationMRVHDAESSDEDGYD
CCHHCCCCCCCCCCC
46.5525159151
906PhosphorylationRVHDAESSDEDGYDW
CHHCCCCCCCCCCCC
30.7923927012
911PhosphorylationESSDEDGYDWGPATD
CCCCCCCCCCCCCCC
5.3323663014
914PhosphorylationDEDGYDWGPATDL--
CCCCCCCCCCCCC--
3.0027251275
915PhosphorylationEDGYDWGPATDL---
CCCCCCCCCCCC---
20.4227251275
917PhosphorylationGYDWGPATDL-----
CCCCCCCCCC-----
12.0523927012
919PhosphorylationDWGPATDL-------
CCCCCCCC-------
44.8218669648
920PhosphorylationWGPATDL--------
CCCCCCC--------
36.2018669648
925PhosphorylationDL-------------
CC-------------
22.3518669648

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of ZO3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZO3_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of ZO3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
INADL_HUMANINADLphysical
12021270
ZO1_HUMANTJP1physical
10575001

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZO3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164, AND MASSSPECTROMETRY.
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164; SER-919 ANDSER-920, AND MASS SPECTROMETRY.

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