CLD3_HUMAN - dbPTM
CLD3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CLD3_HUMAN
UniProt AC O15551
Protein Name Claudin-3
Gene Name CLDN3
Organism Homo sapiens (Human).
Sequence Length 220
Subcellular Localization Cell junction, tight junction . Cell membrane
Multi-pass membrane protein .
Protein Description Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity..
Protein Sequence MSMGLEITGTALAVLGWLGTIVCCALPMWRVSAFIGSNIITSQNIWEGLWMNCVVQSTGQMQCKVYDSLLALPQDLQAARALIVVAILLAAFGLLVALVGAQCTNCVQDDTAKAKITIVAGVLFLLAALLTLVPVSWSANTIIRDFYNPVVPEAQKREMGAGLYVGWAAAALQLLGGALLCCSCPPREKKYTATKVVYSAPRSTGPGASLGTGYDRKDYV
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
103S-palmitoylationVALVGAQCTNCVQDD
HHHHCCCCCCCCCCC
2.6829097667
106S-palmitoylationVGAQCTNCVQDDTAK
HCCCCCCCCCCCCHH
1.2429097667
182S-palmitoylationLGGALLCCSCPPREK
HCCHHHHCCCCCCCC
4.7829097667
184S-palmitoylationGALLCCSCPPREKKY
CHHHHCCCCCCCCCC
3.1629097667
191PhosphorylationCPPREKKYTATKVVY
CCCCCCCCEEEEEEE
16.8126657352
192PhosphorylationPPREKKYTATKVVYS
CCCCCCCEEEEEEEC
36.4126657352
194PhosphorylationREKKYTATKVVYSAP
CCCCCEEEEEEECCC
19.3028857561
195UbiquitinationEKKYTATKVVYSAPR
CCCCEEEEEEECCCC
27.52-
198PhosphorylationYTATKVVYSAPRSTG
CEEEEEEECCCCCCC
11.3421945579
199PhosphorylationTATKVVYSAPRSTGP
EEEEEEECCCCCCCC
21.8621945579
203PhosphorylationVVYSAPRSTGPGASL
EEECCCCCCCCCCCC
36.3421945579
204PhosphorylationVYSAPRSTGPGASLG
EECCCCCCCCCCCCC
48.9921945579
209PhosphorylationRSTGPGASLGTGYDR
CCCCCCCCCCCCCCC
32.9921945579
212PhosphorylationGPGASLGTGYDRKDY
CCCCCCCCCCCCCCC
37.5521945579
214PhosphorylationGASLGTGYDRKDYV-
CCCCCCCCCCCCCC-
16.6521945579
219PhosphorylationTGYDRKDYV------
CCCCCCCCC------
15.8727259358

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
192TPhosphorylationKinasePRKACAP17612
GPS
192TPhosphorylationKinasePKA-FAMILY-GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CLD3_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 CLD3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CLD1_HUMANCLDN1physical
12909588
CLD5_HUMANCLDN5physical
12909588
ZO1_HUMANTJP1physical
10601346
A4_HUMANAPPphysical
21832049

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 CLD3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-214 AND TYR-219, ANDMASS SPECTROMETRY.

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