Search Results
Overview
| Uniprot ID | P04264 |
|---|---|
| Protein Name | Keratin, type II cytoskeletal 1 |
| Gene Name | KRT1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 185 | SREREQIKSLNNQFA |
| 197 | QFASFIDKVRFLEQQ |
| 211 | QNQVLQTKWELLQQV |
| 246 | RRRVDQLKSDQSRLD |
| 257 | SRLDSELKNMQDMVE |
| 288 | ENEFVTIKKDVDGAY |
| 289 | NEFVTIKKDVDGAYM |
| 355 | DSIIAEVKAQYEDIA |
| 364 | QYEDIAQKSKAEAES |
| 366 | EDIAQKSKAEAESLY |
| 376 | AESLYQSKYEELQIT |
| 395 | GDSVRNSKIEISELN |
| 416 | RSEIDNVKKQISNLQ |
| 417 | SEIDNVKKQISNLQQ |
| 438 | QRGENALKDAKNKLN |
| 455 | EDALQQAKEDLARLL |
Function
Structural component of intermediate filaments in suprabasal keratinocytes of stratified epithelia. Forms heteropolymers with a type I keratin, assembling into keratin intermediate filament networks that provide mechanical strength and structural stability to differentiating epidermal cells (PubMed:1381288). May regulate the activity of kinases such as PKC and SRC by interacting with integrin beta-1 (ITB1) and the receptor of activated protein C kinase 1 (RACK1) (PubMed:17956333, PubMed:21544310). In complex with C1QBP, acts as a high-affinity receptor for kininogen-1 (HMWK) (PubMed:21544310)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0072562 | blood microparticle |
| Cellular Component | GO:0001533 | cornified envelope |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005856 | cytoskeleton |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0005576 | extracellular region |
| Cellular Component | GO:0005615 | extracellular space |
| Cellular Component | GO:1904813 | ficolin-1-rich granule lumen |
| Cellular Component | GO:0045095 | keratin filament |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0005634 | nucleus |
| Molecular Function | GO:0030246 | carbohydrate binding |
| Molecular Function | GO:0046982 | protein heterodimerization activity |
| Molecular Function | GO:0038023 | signaling receptor activity |
| Molecular Function | GO:0030280 | structural constituent of skin epidermis |
| Biological Process | GO:0001867 | complement activation, lectin pathway |
| Biological Process | GO:0070268 | cornification |
| Biological Process | GO:0042730 | fibrinolysis |
| Biological Process | GO:0045109 | intermediate filament organization |
| Biological Process | GO:0031424 | keratinization |
| Biological Process | GO:0051290 | protein heterotetramerization |
| Biological Process | GO:0045765 | regulation of angiogenesis |
| Biological Process | GO:0006979 | response to oxidative stress |
Reference
[1] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.
[2] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.
[3] Yan M, Tu H, Tang S, Gai Z, Shi Q et al.. Lactylated Proteomic Analysis Reveals Functional Implications of Lysine Lactylation In Asthenozoospermia.. Mol Cell Proteomics 24(12):101439. 2025 Dec. PMID: 41192556.
[4] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.
[5] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.