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 | ||
* 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. |
loading...
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. |