| UniProt ID | K1C10_HUMAN | |
|---|---|---|
| UniProt AC | P13645 | |
| Protein Name | Keratin, type I cytoskeletal 10 | |
| Gene Name | KRT10 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 584 | |
| Subcellular Localization | Secreted, extracellular space . Localized on the surface of desquamated nasal epithelial cells. | |
| Protein Description | Plays a role in the establishment of the epidermal barrier on plantar skin.; (Microbial infection) Acts as a mediator of S.aureus adherence to desquamated nasal epithelial cells via clfB, and hence may play a role in nasal colonization.. | |
| Protein Sequence | MSVRYSSSKHYSSSRSGGGGGGGGCGGGGGVSSLRISSSKGSLGGGFSSGGFSGGSFSRGSSGGGCFGGSSGGYGGLGGFGGGSFRGSYGSSSFGGSYGGIFGGGSFGGGSFGGGSFGGGGFGGGGFGGGFGGGFGGDGGLLSGNEKVTMQNLNDRLASYLDKVRALEESNYELEGKIKEWYEKHGNSHQGEPRDYSKYYKTIDDLKNQILNLTTDNANILLQIDNARLAADDFRLKYENEVALRQSVEADINGLRRVLDELTLTKADLEMQIESLTEELAYLKKNHEEEMKDLRNVSTGDVNVEMNAAPGVDLTQLLNNMRSQYEQLAEQNRKDAEAWFNEKSKELTTEIDNNIEQISSYKSEITELRRNVQALEIELQSQLALKQSLEASLAETEGRYCVQLSQIQAQISALEEQLQQIRAETECQNTEYQQLLDIKIRLENEIQTYRSLLEGEGSSGGGGRGGGSFGGGYGGGSSGGGSSGGGHGGGHGGSSGGGYGGGSSGGGSSGGGYGGGSSSGGHGGSSSGGYGGGSSGGGGGGYGGGSSGGGSSSGGGYGGGSSSGGHKSSSSGSVGESSSKGPRY | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 2 | Phosphorylation | ------MSVRYSSSK ------CCCCCCCCC | 18.46 | - | |
| 11 | Phosphorylation | RYSSSKHYSSSRSGG CCCCCCCCCCCCCCC | 17.62 | 29083192 | |
| 12 | Phosphorylation | YSSSKHYSSSRSGGG CCCCCCCCCCCCCCC | 22.89 | 29083192 | |
| 13 | Phosphorylation | SSSKHYSSSRSGGGG CCCCCCCCCCCCCCC | 23.70 | 21712546 | |
| 14 | Phosphorylation | SSKHYSSSRSGGGGG CCCCCCCCCCCCCCC | 25.24 | 29083192 | |
| 16 | Phosphorylation | KHYSSSRSGGGGGGG CCCCCCCCCCCCCCC | 43.68 | 23927012 | |
| 32 | Phosphorylation | CGGGGGVSSLRISSS CCCCCCCCCEEEECC | 27.25 | 23927012 | |
| 33 | Phosphorylation | GGGGGVSSLRISSSK CCCCCCCCEEEECCC | 21.18 | 23927012 | |
| 37 | Phosphorylation | GVSSLRISSSKGSLG CCCCEEEECCCCCCC | 23.33 | 23186163 | |
| 38 | Phosphorylation | VSSLRISSSKGSLGG CCCEEEECCCCCCCC | 33.43 | 27966365 | |
| 39 | Phosphorylation | SSLRISSSKGSLGGG CCEEEECCCCCCCCC | 33.96 | 27966365 | |
| 42 | Phosphorylation | RISSSKGSLGGGFSS EEECCCCCCCCCCCC | 27.81 | 21082442 | |
| 48 | Phosphorylation | GSLGGGFSSGGFSGG CCCCCCCCCCCCCCC | 31.20 | 29083192 | |
| 49 | Phosphorylation | SLGGGFSSGGFSGGS CCCCCCCCCCCCCCC | 40.45 | 30087585 | |
| 53 | Phosphorylation | GFSSGGFSGGSFSRG CCCCCCCCCCCCCCC | 45.58 | 21815630 | |
| 56 | Phosphorylation | SGGFSGGSFSRGSSG CCCCCCCCCCCCCCC | 24.47 | 21815630 | |
| 56 | O-linked_Glycosylation | SGGFSGGSFSRGSSG CCCCCCCCCCCCCCC | 24.47 | 26853435 | |
| 58 | O-linked_Glycosylation | GFSGGSFSRGSSGGG CCCCCCCCCCCCCCC | 37.11 | 26853435 | |
| 58 | Phosphorylation | GFSGGSFSRGSSGGG CCCCCCCCCCCCCCC | 37.11 | 29083192 | |
| 61 | Phosphorylation | GGSFSRGSSGGGCFG CCCCCCCCCCCCCCC | 25.38 | 27966365 | |
| 62 | Phosphorylation | GSFSRGSSGGGCFGG CCCCCCCCCCCCCCC | 44.26 | 21815630 | |
| 70 | Phosphorylation | GGGCFGGSSGGYGGL CCCCCCCCCCCCCCC | 26.62 | 25247763 | |
| 71 | Phosphorylation | GGCFGGSSGGYGGLG CCCCCCCCCCCCCCC | 39.24 | 23927012 | |
| 74 | Phosphorylation | FGGSSGGYGGLGGFG CCCCCCCCCCCCCCC | 16.14 | 27251275 | |
| 84 | Phosphorylation | LGGFGGGSFRGSYGS CCCCCCCCCCCCCCC | 18.29 | 23186163 | |
| 159 | Phosphorylation | NLNDRLASYLDKVRA CHHHHHHHHHHHHHH | 30.71 | 25106551 | |
| 160 | Phosphorylation | LNDRLASYLDKVRAL HHHHHHHHHHHHHHH | 17.20 | 26356563 | |
| 163 | Acetylation | RLASYLDKVRALEES HHHHHHHHHHHHHHC | 30.90 | 19608861 | |
| 163 | Ubiquitination | RLASYLDKVRALEES HHHHHHHHHHHHHHC | 30.90 | 19608861 | |
| 170 | Phosphorylation | KVRALEESNYELEGK HHHHHHHCCCCCCHH | 35.02 | 7512983 | |
| 172 | Phosphorylation | RALEESNYELEGKIK HHHHHCCCCCCHHHH | 31.04 | 22817900 | |
| 188 | Phosphorylation | WYEKHGNSHQGEPRD HHHHHCCCCCCCCCC | 23.06 | 24719451 | |
| 199 | Phosphorylation | EPRDYSKYYKTIDDL CCCCHHHHHHHHHHH | 12.31 | 22817900 | |
| 200 | Phosphorylation | PRDYSKYYKTIDDLK CCCHHHHHHHHHHHH | 12.85 | 22817900 | |
| 238 | Phosphorylation | ADDFRLKYENEVALR CCHHHHHHHCHHHHH | 28.69 | 22817900 | |
| 277 | Phosphorylation | EMQIESLTEELAYLK HHHHHHHHHHHHHHH | 36.37 | - | |
| 282 | Phosphorylation | SLTEELAYLKKNHEE HHHHHHHHHHHCCHH | 31.51 | - | |
| 284 | Sumoylation | TEELAYLKKNHEEEM HHHHHHHHHCCHHHH | 38.56 | - | |
| 284 | Ubiquitination | TEELAYLKKNHEEEM HHHHHHHHHCCHHHH | 38.56 | 22817900 | |
| 284 | Sumoylation | TEELAYLKKNHEEEM HHHHHHHHHCCHHHH | 38.56 | - | |
| 285 | Ubiquitination | EELAYLKKNHEEEMK HHHHHHHHCCHHHHH | 62.02 | 22817900 | |
| 298 | Phosphorylation | MKDLRNVSTGDVNVE HHHHCCCCCCCCCCC | 30.16 | 18691976 | |
| 299 | Phosphorylation | KDLRNVSTGDVNVEM HHHCCCCCCCCCCCC | 32.87 | 23186163 | |
| 325 | Phosphorylation | LNNMRSQYEQLAEQN HHHHHHHHHHHHHHH | 13.59 | 22817900 | |
| 334 | Ubiquitination | QLAEQNRKDAEAWFN HHHHHHHHHHHHHHH | 69.69 | 22817900 | |
| 343 | Ubiquitination | AEAWFNEKSKELTTE HHHHHHHHHHHHHHH | 68.85 | 29967540 | |
| 344 | Phosphorylation | EAWFNEKSKELTTEI HHHHHHHHHHHHHHC | 25.78 | - | |
| 348 | Phosphorylation | NEKSKELTTEIDNNI HHHHHHHHHHCHHCH | 24.39 | 29083192 | |
| 349 | Phosphorylation | EKSKELTTEIDNNIE HHHHHHHHHCHHCHH | 43.50 | 29083192 | |
| 363 | Phosphorylation | EQISSYKSEITELRR HHHHHCHHHHHHHHH | 26.46 | 23403867 | |
| 392 | Phosphorylation | LKQSLEASLAETEGR HHHHHHHHHHHHCCC | 20.80 | 21815630 | |
| 430 | Phosphorylation | AETECQNTEYQQLLD HHHHHCCHHHHHHHH | 15.36 | - | |
| 451 | Phosphorylation | NEIQTYRSLLEGEGS HHHHHHHHHHCCCCC | 27.22 | 23186163 | |
| 458 | Phosphorylation | SLLEGEGSSGGGGRG HHHCCCCCCCCCCCC | 22.85 | 21815630 | |
| 459 | Phosphorylation | LLEGEGSSGGGGRGG HHCCCCCCCCCCCCC | 52.92 | 21815630 | |
| 535 | Phosphorylation | GGYGGGSSGGGGGGY CCCCCCCCCCCCCCC | 44.74 | - | |
| 546 | Phosphorylation | GGGYGGGSSGGGSSS CCCCCCCCCCCCCCC | 29.14 | - | |
| 557 | Phosphorylation | GSSSGGGYGGGSSSG CCCCCCCCCCCCCCC | 18.84 | - | |
| 568 | Phosphorylation | SSSGGHKSSSSGSVG CCCCCCCCCCCCCCC | 29.76 | 29083192 | |
| 569 | Phosphorylation | SSGGHKSSSSGSVGE CCCCCCCCCCCCCCC | 33.07 | 29083192 | |
| 570 | Phosphorylation | SGGHKSSSSGSVGES CCCCCCCCCCCCCCC | 45.89 | 24719451 | |
| 571 | Phosphorylation | GGHKSSSSGSVGESS CCCCCCCCCCCCCCC | 36.71 | 21815630 | |
| 573 | Phosphorylation | HKSSSSGSVGESSSK CCCCCCCCCCCCCCC | 28.97 | 21815630 | |
| 577 | Phosphorylation | SSGSVGESSSKGPRY CCCCCCCCCCCCCCC | 33.70 | 24532841 | |
| 578 | Phosphorylation | SGSVGESSSKGPRY- CCCCCCCCCCCCCC- | 31.59 | - | |
| 579 | Phosphorylation | GSVGESSSKGPRY-- CCCCCCCCCCCCC-- | 51.41 | - | |
| 584 | Phosphorylation | SSSKGPRY------- CCCCCCCC------- | 26.49 | - |
| 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 K1C10_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of K1C10_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 K1C10_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| AKT1_HUMAN | AKT1 | physical | 11585925 | |
| KPCZ_HUMAN | PRKCZ | physical | 11585925 | |
| K2C1_HUMAN | KRT1 | physical | 22939629 | |
| K22E_HUMAN | KRT2 | physical | 22939629 | |
| K1C16_HUMAN | KRT16 | physical | 26344197 | |
| K2C1B_HUMAN | KRT77 | physical | 26344197 | |
| TRY1_HUMAN | PRSS1 | physical | 26344197 |
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| 113800 | Epidermolytic hyperkeratosis (EHK) | |||||
| 607602 | Ichthyosis annular epidermolytic (AEI) | |||||
| 609165 | Erythroderma, ichthyosiform, congenital reticular (CRIE) | |||||
| 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 |
| "Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-42, AND MASSSPECTROMETRY. | |