| UniProt ID | K1C25_HUMAN | |
|---|---|---|
| UniProt AC | Q7Z3Z0 | |
| Protein Name | Keratin, type I cytoskeletal 25 | |
| Gene Name | KRT25 {ECO:0000312|HGNC:HGNC:30839} | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 450 | |
| Subcellular Localization | Cytoplasm . | |
| Protein Description | Essential for the proper assembly of type I and type II keratin protein complexes and formation of keratin intermediate filaments in the inner root sheath (irs) (By similarity). Plays a role in the cytoskeleton organization. [PubMed: 26902920] | |
| Protein Sequence | MSLRLSSASRRSCPRPTTGSLRLYGGGTSFGTGNSCGISGIGSGFSSAFGGSSSGGNTGGGNPCAGFTVNERGLLSGNEKVTMQNLNDRLASYLDSVHALEEANADLEQKIKGWYEKFGPGSCRGLDHDYSRYFPIIDDLKNQIIASTTSNANAVLQIDNARLTADDFRLKYENELALHQSVEADVNGLRRVLDEITLCRTDLEIQYETLSEEMTYLKKNHKEEMQVLQCAAGGNVNVEMNAAPGVDLTVLLNNMRAEYEALAEQNRRDAEAWFNEKSASLQQQISEDVGATTSARNELTEMKRTLQTLEIELQSLLATKHSLECSLTETESNYCAQLAQIQAQIGALEEQLHQVRTETEGQKLEYEQLLDIKLHLEKEIETYCLLIGGDDGACKSGGYKSKDYGSGNVGSQVKDPAKAIVVKKVLEEVDQRSKILTTRLHSLEEKSQSN | |
| 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 | ------MSLRLSSAS ------CCCCCCCCC | 23.38 | 29978859 | |
| 6 | Phosphorylation | --MSLRLSSASRRSC --CCCCCCCCCCCCC | 19.88 | 29978859 | |
| 7 | Phosphorylation | -MSLRLSSASRRSCP -CCCCCCCCCCCCCC | 34.55 | 29978859 | |
| 9 | Phosphorylation | SLRLSSASRRSCPRP CCCCCCCCCCCCCCC | 30.12 | 29978859 | |
| 115 | Phosphorylation | EQKIKGWYEKFGPGS HHHHHHHHHHHCCCC | 20.22 | - | |
| 147 | Phosphorylation | LKNQIIASTTSNANA HHCCEEEECCCCCCC | 23.08 | - | |
| 148 | Phosphorylation | KNQIIASTTSNANAV HCCEEEECCCCCCCE | 25.81 | - | |
| 149 | Phosphorylation | NQIIASTTSNANAVL CCEEEECCCCCCCEE | 19.93 | - | |
| 150 | Phosphorylation | QIIASTTSNANAVLQ CEEEECCCCCCCEEE | 33.75 | - | |
| 197 | Phosphorylation | RRVLDEITLCRTDLE HHHHHHHHEECCCCH | 20.12 | - | |
| 207 | Phosphorylation | RTDLEIQYETLSEEM CCCCHHHHHHHHHHH | 19.28 | 26657352 | |
| 209 | Phosphorylation | DLEIQYETLSEEMTY CCHHHHHHHHHHHHH | 30.56 | 26657352 | |
| 433 | Phosphorylation | LEEVDQRSKILTTRL HHHHHHHHHHHHHHH | 20.58 | 18669648 | |
| 437 | Phosphorylation | DQRSKILTTRLHSLE HHHHHHHHHHHHHHH | 17.22 | 18669648 | |
| 438 | Phosphorylation | QRSKILTTRLHSLEE HHHHHHHHHHHHHHH | 27.99 | 29978859 | |
| 442 | Phosphorylation | ILTTRLHSLEEKSQS HHHHHHHHHHHHHHC | 41.91 | 26160856 |
| 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 K1C25_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of K1C25_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 K1C25_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of K1C25_HUMAN !! | ||||
| 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 |
| "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-433; THR-437 ANDSER-442, AND MASS SPECTROMETRY. | |