Search Results

Overview

Uniprot IDP05783
Protein NameKeratin, type I cytoskeletal 18
Gene NameKRT18
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
167 AADDFRVKYETELAM
187 NDIHGLRKVIDDTNI
214 KEELLFMKKNHEEEV
215 EELLFMKKNHEEEVK
247 PKSQDLAKIMADIRA
317 LDSMRNLKASLENSL
370 YEALLNIKVKLEAEI
372 ALLNIKVKLEAEIAT
407 NSMQTIQKTTTRRIV
417 TRRIVDGKVVSETND
426 VSETNDTKVLRH***

Function

Structural component of intermediate filaments in simple epithelial cells. Forms obligate heteropolymers with a type II keratin KRT8, mechanical stability and resilience to epithelial cells (PubMed:15529338, PubMed:26823019). KRT8/KRT18 filaments are involved in ARHGEF40-mediated actin stress fiber formation and tensional force-induced stress fiber formation and reinforcement (PubMed:26823019). Organization and orientation of KRT8/KRT18 filaments are responsible for the properly elongated morphology of epithelial tubules (By similarity). Also acts downstream of ROCK kinase activation as part of a positive feedback mechanism in response to cellular mechanical stress loading (PubMed:26823019). Involved in the uptake of thrombin-antithrombin complexes by hepatic cells (By similarity). When phosphorylated, plays a role in filament reorganization (PubMed:7523419, PubMed:8522591, PubMed:9298992, PubMed:9524113). Involved in the delivery of mutated CFTR to the plasma membrane (PubMed:15529338, PubMed:16424149). Involved in interleukin-6 (IL-6)-mediated barrier protection (PubMed:17213200)

Protein Sequence

10 MSFTTRSTFS 20 TNYRSLGSVQ 30 APSYGARPVS 40 SAASVYAGAG 50 GSGSRISVSR 60 STSFRGGMGS 70 GGLATGIAGG 80 LAGMGGIQNE 90 KETMQSLNDR 100 LASYLDRVRS 110 LETENRRLES 120 KIREHLEKKG 130 PQVRDWSHYF 140 KIIEDLRAQI 150 FANTVDNARI 160 VLQIDNARLA 170 ADDFRVKYET 180 ELAMRQSVEN 190 DIHGLRKVID 200 DTNITRLQLE 210 TEIEALKEEL 220 LFMKKNHEEE 230 VKGLQAQIAS 240 SGLTVEVDAP 250 KSQDLAKIMA 260 DIRAQYDELA 270 RKNREELDKY 280 WSQQIEESTT 290 VVTTQSAEVG 300 AAETTLTELR 310 RTVQSLEIDL 320 DSMRNLKASL 330 ENSLREVEAR 340 YALQMEQLNG 350 ILLHLESELA 360 QTRAEGQRQA 370 QEYEALLNIK 380 VKLEAEIATY 390 RRLLEDGEDF 400 NLGDALDSSN 410 SMQTIQKTTT 420 RRIVDGKVVS 430 ETNDTKVLRH

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005912 adherens junction
Cellular Component GO:0071944 cell periphery
Cellular Component GO:0034451 centriolar satellite
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005856 cytoskeleton
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005882 intermediate filament
Cellular Component GO:0045095 keratin filament
Cellular Component GO:0005815 microtubule organizing center
Cellular Component GO:0016363 nuclear matrix
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0048471 perinuclear region of cytoplasm
Molecular Function GO:0098641 cadherin binding involved in cell-cell adhesion
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0097110 scaffold protein binding
Molecular Function GO:0005198 structural molecule activity
Biological Process GO:0009653 anatomical structure morphogenesis
Biological Process GO:0043001 Golgi to plasma membrane protein transport
Biological Process GO:0045104 intermediate filament cytoskeleton organization
Biological Process GO:0043066 negative regulation of apoptotic process

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[3] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[4] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.

[5] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.

[6] 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.

[7] 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.

[8] 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.