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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
103 | S-palmitoylation | VALVGAQCTNCVQDD HHHHCCCCCCCCCCC | 2.68 | 29097667 | |
106 | S-palmitoylation | VGAQCTNCVQDDTAK HCCCCCCCCCCCCHH | 1.24 | 29097667 | |
182 | S-palmitoylation | LGGALLCCSCPPREK HCCHHHHCCCCCCCC | 4.78 | 29097667 | |
184 | S-palmitoylation | GALLCCSCPPREKKY CHHHHCCCCCCCCCC | 3.16 | 29097667 | |
191 | Phosphorylation | CPPREKKYTATKVVY CCCCCCCCEEEEEEE | 16.81 | 26657352 | |
192 | Phosphorylation | PPREKKYTATKVVYS CCCCCCCEEEEEEEC | 36.41 | 26657352 | |
194 | Phosphorylation | REKKYTATKVVYSAP CCCCCEEEEEEECCC | 19.30 | 28857561 | |
195 | Ubiquitination | EKKYTATKVVYSAPR CCCCEEEEEEECCCC | 27.52 | - | |
198 | Phosphorylation | YTATKVVYSAPRSTG CEEEEEEECCCCCCC | 11.34 | 21945579 | |
199 | Phosphorylation | TATKVVYSAPRSTGP EEEEEEECCCCCCCC | 21.86 | 21945579 | |
203 | Phosphorylation | VVYSAPRSTGPGASL EEECCCCCCCCCCCC | 36.34 | 21945579 | |
204 | Phosphorylation | VYSAPRSTGPGASLG EECCCCCCCCCCCCC | 48.99 | 21945579 | |
209 | Phosphorylation | RSTGPGASLGTGYDR CCCCCCCCCCCCCCC | 32.99 | 21945579 | |
212 | Phosphorylation | GPGASLGTGYDRKDY CCCCCCCCCCCCCCC | 37.55 | 21945579 | |
214 | Phosphorylation | GASLGTGYDRKDYV- CCCCCCCCCCCCCC- | 16.65 | 21945579 | |
219 | Phosphorylation | TGYDRKDYV------ CCCCCCCCC------ | 15.87 | 27259358 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
192 | T | Phosphorylation | Kinase | PRKACA | P17612 | GPS |
192 | T | Phosphorylation | Kinase | PKA-FAMILY | - | GPS |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CLD3_HUMAN !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
CLD1_HUMAN | CLDN1 | physical | 12909588 | |
CLD5_HUMAN | CLDN5 | physical | 12909588 | |
ZO1_HUMAN | TJP1 | physical | 10601346 | |
A4_HUMAN | APP | physical | 21832049 |
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. |
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Phosphorylation | |
Reference | PubMed |
"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. |