Search Results

Overview

Uniprot IDP02538
Protein NameKeratin, type II cytoskeletal 6A
Gene NameKRT6A
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
168 AEEREQIKTLNNKFA
173 QIKTLNNKFASFIDK
180 KFASFIDKVRFLEQQ
189 RFLEQQNKVLETKWT
252 LVEDFKNKYEDEINK
259 KYEDEINKRTAAENE
467 VEIATYRKLLEGEEC

Function

Structural component of intermediate filaments in epithelial keratinocytes. Forms heteropolymers with the type I keratins KRT16 and KRT17, assembling into keratin intermediate filament networks that contributes to the structural integrity and stress resilience of stratified epithelia, particularly in epidermis, nail bed and oral mucosa (PubMed:11886499, PubMed:17719747, PubMed:7545493). Rapidly induced in wound-edge keratinocytes and participates in cytoskeletal reorganization during re-epithelialization (By similarity). Negatively regulates collective keratinocyte migration by stabilizing non-muscle myosin MYH9 and desmoplakin, thereby altering cell-cell and cell-matrix adhesion and reducing the speed and directionality of epithelial sheet movement during wound repair (By similarity). Also limits epithelial migration by inhibiting SRC activity during wound repair (By similarity). Required for normal palmoplantar, nail unit and oral mucosa integrity (PubMed:11886499, PubMed:17719747, PubMed:7545493)

Protein Sequence

10 MASTSTTIRS 20 HSSSRRGFSA 30 NSARLPGVSR 40 SGFSSVSVSR 50 SRGSGGLGGA 60 CGGAGFGSRS 70 LYGLGGSKRI 80 SIGGGSCAIS 90 GGYGSRAGGS 100 YGFGGAGSGF 110 GFGGGAGIGF 120 GLGGGAGLAG 130 GFGGPGFPVC 140 PPGGIQEVTV 150 NQSLLTPLNL 160 QIDPTIQRVR 170 AEEREQIKTL 180 NNKFASFIDK 190 VRFLEQQNKV 200 LETKWTLLQE 210 QGTKTVRQNL 220 EPLFEQYINN 230 LRRQLDSIVG 240 ERGRLDSELR 250 GMQDLVEDFK 260 NKYEDEINKR 270 TAAENEFVTL 280 KKDVDAAYMN 290 KVELQAKADT 300 LTDEINFLRA 310 LYDAELSQMQ 320 THISDTSVVL 330 SMDNNRNLDL 340 DSIIAEVKAQ 350 YEEIAQRSRA 360 EAESWYQTKY 370 EELQVTAGRH 380 GDDLRNTKQE 390 IAEINRMIQR 400 LRSEIDHVKK 410 QCANLQAAIA 420 DAEQRGEMAL 430 KDAKNKLEGL 440 EDALQKAKQD 450 LARLLKEYQE 460 LMNVKLALDV 470 EIATYRKLLE 480 GEECRLNGEG 490 VGQVNISVVQ 500 STVSSGYGGA 510 SGVGSGLGLG 520 GGSSYSYGSG 530 LGVGGGFSSS 540 SGRAIGGGLS 550 SVGGGSSTIK 560 YTTTSSSSRK SYKH

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0045111 intermediate filament cytoskeleton
Cellular Component GO:0045095 keratin filament
Cellular Component GO:0016020 membrane
Cellular Component GO:0005634 nucleus
Molecular Function GO:0005200 structural constituent of cytoskeleton
Molecular Function GO:0030280 structural constituent of skin epidermis
Biological Process GO:0061844 antimicrobial humoral immune response mediated by antimicrobial peptide
Biological Process GO:0030154 cell differentiation
Biological Process GO:0050830 defense response to Gram-positive bacterium
Biological Process GO:0045109 intermediate filament organization
Biological Process GO:0031424 keratinization
Biological Process GO:0031640 killing of cells of another organism
Biological Process GO:0002009 morphogenesis of an epithelium
Biological Process GO:2000536 negative regulation of entry of bacterium into host cell
Biological Process GO:0008284 positive regulation of cell population proliferation
Biological Process GO:0042060 wound healing

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.