ID K1C18_HUMAN Reviewed; 430 AA. AC P05783; Q53G38; Q5U0N8; Q9BW26; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 243. DE RecName: Full=Keratin, type I cytoskeletal 18; DE AltName: Full=Cell proliferation-inducing gene 46 protein; DE AltName: Full=Cytokeratin-18; DE Short=CK-18; DE AltName: Full=Keratin-18; DE Short=K18; GN Name=KRT18; Synonyms=CYK18; ORFNames=PIG46; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC TISSUE=Placenta; RX PubMed=2434380; DOI=10.1111/j.1432-0436.1986.tb00411.x; RA Oshima R.G., Millan J.L., Cecena G.; RT "Comparison of mouse and human keratin 18: a component of intermediate RT filaments expressed prior to implantation."; RL Differentiation 33:61-68(1986). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kim J.W.; RT "Identification of a cell proliferation-inducing gene."; RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Cervix, Colon, Pancreas, Placenta, and Uterus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-167. RX PubMed=2454392; DOI=10.1128/mcb.8.4.1540-1550.1988; RA Kulesh D.A., Oshima R.G.; RT "Cloning of the human keratin 18 gene and its expression in nonepithelial RT mouse cells."; RL Mol. Cell. Biol. 8:1540-1550(1988). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-430, AND TISSUE SPECIFICITY. RC TISSUE=Vulva; RX PubMed=2434381; DOI=10.1111/j.1432-0436.1986.tb00412.x; RA Leube R.E., Bosch F.X., Romano V., Zimbelmann R., Hofler H., Franke W.W.; RT "Cytokeratin expression in simple epithelia. III. Detection of mRNAs RT encoding human cytokeratins nos. 8 and 18 in normal and tumor cells by RT hybridization with cDNA sequences in vitro and in situ."; RL Differentiation 33:69-85(1986). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 199-430, AND TISSUE SPECIFICITY. RC TISSUE=Liver; RX PubMed=2422083; DOI=10.1111/j.1432-0436.1986.tb00787.x; RA Romano V., Hatzfeld M., Magin T.M., Zimbelmann R., Franke W.W., Maier G., RA Ponstingl H.; RT "Cytokeratin expression in simple epithelia. I. Identification of mRNA RT coding for human cytokeratin no. 18 by a cDNA clone."; RL Differentiation 30:244-253(1986). RN [9] RP PARTIAL PROTEIN SEQUENCE. RC TISSUE=Colon carcinoma; RX PubMed=9150948; DOI=10.1002/elps.1150180344; RA Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.; RT "A two-dimensional gel database of human colon carcinoma proteins."; RL Electrophoresis 18:605-613(1997). RN [10] RP GLYCOSYLATION. RX PubMed=1371281; DOI=10.1016/s0021-9258(19)50611-1; RA Chou C.F., Smith A.J., Omary M.B.; RT "Characterization and dynamics of O-linked glycosylation of human RT cytokeratin 8 and 18."; RL J. Biol. Chem. 267:3901-3906(1992). RN [11] RP FUNCTION, PHOSPHORYLATION AT SER-53, AND MUTAGENESIS OF SER-2; SER-7; RP SER-10; SER-15; SER-18; SER-23; SER-30; SER-31; SER-34; SER-42; SER-44; RP SER-47; SER-49; SER-51 AND SER-53. RX PubMed=7523419; DOI=10.1083/jcb.127.1.161; RA Ku N.O., Omary M.B.; RT "Identification of the major physiologic phosphorylation site of human RT keratin 18: potential kinases and a role in filament reorganization."; RL J. Cell Biol. 127:161-171(1994). RN [12] RP GLYCOSYLATION AT SER-30; SER-31 AND SER-49, MUTAGENESIS OF SER-30; SER-31 RP AND SER-49, CLEAVAGE OF INITIATOR METHIONINE, AND ACETYLATION AT SER-2. RX PubMed=7538124; DOI=10.1074/jbc.270.20.11820; RA Ku N.-O., Omary M.B.; RT "Identification and mutational analysis of the glycosylation sites of human RT keratin 18."; RL J. Biol. Chem. 270:11820-11827(1995). RN [13] RP FUNCTION, AND MUTAGENESIS OF ARG-90. RX PubMed=8522591; DOI=10.1083/jcb.131.5.1303; RA Ku N.O., Michie S., Oshima R.G., Omary M.B.; RT "Chronic hepatitis, hepatocyte fragility, and increased soluble RT phosphoglycokeratins in transgenic mice expressing a keratin 18 conserved RT arginine mutant."; RL J. Cell Biol. 131:1303-1314(1995). RN [14] RP PHOSPHORYLATION, AND INTERACTION WITH YWHAE; YWHAH AND YWHAZ. RX PubMed=8609167; DOI=10.1083/jcb.133.2.345; RA Liao J., Omary M.B.; RT "14-3-3 proteins associate with phosphorylated simple epithelial keratins RT during cell cycle progression and act as a solubility cofactor."; RL J. Cell Biol. 133:345-357(1996). RN [15] RP FUNCTION, CLEAVAGE BY CASPASES, AND MUTAGENESIS OF SER-53 AND ASP-238. RX PubMed=9298992; DOI=10.1083/jcb.138.6.1379; RA Caulin C., Salvesen G.S., Oshima R.G.; RT "Caspase cleavage of keratin 18 and reorganization of intermediate RT filaments during epithelial cell apoptosis."; RL J. Cell Biol. 138:1379-1394(1997). RN [16] RP FUNCTION, INTERACTION WITH YWHAE AND YWHAZ, PHOSPHORYLATION AT SER-34, AND RP MUTAGENESIS OF SER-34 AND SER-53. RX PubMed=9524113; DOI=10.1093/emboj/17.7.1892; RA Ku N.O., Liao J., Omary M.B.; RT "Phosphorylation of human keratin 18 serine 33 regulates binding to 14-3-3 RT proteins."; RL EMBO J. 17:1892-1906(1998). RN [17] RP INTERACTION WITH PNN. RX PubMed=10809736; DOI=10.1074/jbc.275.20.14910; RA Shi J., Sugrue S.P.; RT "Dissection of protein linkage between keratins and pinin, a protein with RT dual location at desmosome-intermediate filament complex and in the RT nucleus."; RL J. Biol. Chem. 275:14910-14915(2000). RN [18] RP INTERACTION WITH DNAJB6. RX PubMed=10954706; DOI=10.1074/jbc.m003492200; RA Izawa I., Nishizawa M., Ohtakara K., Ohtsuka K., Inada H., Inagaki M.; RT "Identification of Mrj, a DnaJ/Hsp40 family protein, as a keratin 8/18 RT filament regulatory protein."; RL J. Biol. Chem. 275:34521-34527(2000). RN [19] RP INTERACTION WITH PKP1; PKP2 AND KRT8. RX PubMed=10852826; DOI=10.1242/jcs.113.13.2471; RA Hofmann I., Mertens C., Brettel M., Nimmrich V., Schnoelzer M., RA Herrmann H.; RT "Interaction of plakophilins with desmoplakin and intermediate filament RT proteins: an in vitro analysis."; RL J. Cell Sci. 113:2471-2483(2000). RN [20] RP INTERACTION WITH TRADD. RX PubMed=11684708; DOI=10.1083/jcb.200103078; RA Inada H., Izawa I., Nishizawa M., Fujita E., Kiyono T., Takahashi T., RA Momoi T., Inagaki M.; RT "Keratin attenuates tumor necrosis factor-induced cytotoxicity through RT association with TRADD."; RL J. Cell Biol. 155:415-426(2001). RN [21] RP ASSOCIATION WITH KRT8. RX PubMed=14756564; DOI=10.1021/bi035072s; RA Waseem A., Karsten U., Leigh I.M., Purkis P., Waseem N.H., Lane E.B.; RT "Conformational changes in the rod domain of human keratin 8 following RT heterotypic association with keratin 18 and its implication for filament RT stability."; RL Biochemistry 43:1283-1295(2004). RN [22] RP PHOSPHORYLATION AT SER-34 AND SER-53. RX PubMed=15368451; DOI=10.1002/hep.20277; RA Toivola D.M., Ku N.O., Resurreccion E.Z., Nelson D.R., Wright T.L., RA Omary M.B.; RT "Keratin 8 and 18 hyperphosphorylation is a marker of progression of human RT liver disease."; RL Hepatology 40:459-466(2004). RN [23] RP FUNCTION, INTERACTION WITH MUTATED CFTR, AND SUBCELLULAR LOCATION. RX PubMed=15529338; DOI=10.1002/pmic.200400850; RA Davezac N., Tondelier D., Lipecka J., Fanen P., Demaugre F., Debski J., RA Dadlez M., Schrattenholz A., Cahill M.A., Edelman A.; RT "Global proteomic approach unmasks involvement of keratins 8 and 18 in the RT delivery of cystic fibrosis transmembrane conductance regulator RT (CFTR)/deltaF508-CFTR to the plasma membrane."; RL Proteomics 4:3833-3844(2004). RN [24] RP INTERACTION WITH TCHP. RX PubMed=15731013; DOI=10.1242/jcs.01667; RA Nishizawa M., Izawa I., Inoko A., Hayashi Y., Nagata K., Yokoyama T., RA Usukura J., Inagaki M.; RT "Identification of trichoplein, a novel keratin filament-binding protein."; RL J. Cell Sci. 118:1081-1090(2005). RN [25] RP INTERACTION WITH HEPATITIS C VIRUS CORE PROTEIN (MICROBIAL INFECTION). RX PubMed=15846844; DOI=10.1002/pmic.200401093; RA Kang S.-M., Shin M.-J., Kim J.-H., Oh J.-W.; RT "Proteomic profiling of cellular proteins interacting with the hepatitis C RT virus core protein."; RL Proteomics 5:2227-2237(2005). RN [26] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [27] RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-53. RX PubMed=16424149; DOI=10.1124/jpet.105.097667; RA Lipecka J., Norez C., Bensalem N., Baudouin-Legros M., Planelles G., RA Becq F., Edelman A., Davezac N.; RT "Rescue of DeltaF508-CFTR (cystic fibrosis transmembrane conductance RT regulator) by curcumin: involvement of the keratin 18 network."; RL J. Pharmacol. Exp. Ther. 317:500-505(2006). RN [28] RP FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION, AND INDUCTION. RX PubMed=17213200; DOI=10.1074/jbc.m604068200; RA Wang L., Srinivasan S., Theiss A.L., Merlin D., Sitaraman S.V.; RT "Interleukin-6 induces keratin expression in intestinal epithelial cells: RT potential role of keratin-8 in interleukin-6-induced barrier function RT alterations."; RL J. Biol. Chem. 282:8219-8227(2007). RN [29] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17924679; DOI=10.1021/pr070152u; RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells RT and high confident phosphopeptide identification by cross-validation of RT MS/MS and MS/MS/MS spectra."; RL J. Proteome Res. 6:4150-4162(2007). RN [30] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [31] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-34; SER-42; SER-60; RP THR-302 AND SER-399, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [32] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-131 AND LYS-426, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [33] RP GLYCOSYLATION AT SER-30; SER-31 AND SER-49. RX PubMed=20729549; DOI=10.1074/jbc.m109.098996; RA Srikanth B., Vaidya M.M., Kalraiya R.D.; RT "O-GlcNAcylation determines the solubility, filament organization, and RT stability of keratins 8 and 18."; RL J. Biol. Chem. 285:34062-34071(2010). RN [34] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-15; SER-34; SER-42; RP SER-60; THR-65; SER-100; SER-319; SER-399 AND THR-404, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [35] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [36] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [37] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=22002106; DOI=10.1074/mcp.m111.013680; RA Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I.; RT "Systematic analysis of protein pools, isoforms, and modifications RT affecting turnover and subcellular localization."; RL Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012). RN [38] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [39] RP INTERACTION WITH FAM83H. RX PubMed=23902688; DOI=10.1242/jcs.129684; RA Kuga T., Kume H., Kawasaki N., Sato M., Adachi J., Shiromizu T., RA Hoshino I., Nishimori T., Matsubara H., Tomonaga T.; RT "A novel mechanism of keratin cytoskeleton organization through casein RT kinase Ialpha and FAM83H in colorectal cancer."; RL J. Cell Sci. 126:4721-4731(2013). RN [40] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-18; SER-34; SER-49; RP THR-52; SER-60; SER-93; SER-305; SER-319; SER-323 AND SER-399, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [41] RP IDENTIFICATION IN A COMPLEX WITH KRT8, AND INTERACTION WITH KRT8 AND PLEC. RX PubMed=24940650; DOI=10.1038/jid.2014.255; RA Bouameur J.E., Favre B., Fontao L., Lingasamy P., Begre N., Borradori L.; RT "Interaction of plectin with keratins 5 and 14: dependence on several RT plectin domains and keratin quaternary structure."; RL J. Invest. Dermatol. 134:2776-2783(2014). RN [42] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-65; SER-177; SER-305; RP SER-398; SER-399; SER-401 AND THR-404, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [43] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-45 AND ARG-55, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [44] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-426, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [45] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-81; LYS-247; LYS-370; LYS-372; RP LYS-417 AND LYS-426, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [46] RP VARIANT CIRRH LEU-128. RX PubMed=9011570; DOI=10.1172/jci119127; RA Ku N.-O., Wright T.L., Terrault N.A., Gish R., Omary M.B.; RT "Mutation of human keratin 18 in association with cryptogenic cirrhosis."; RL J. Clin. Invest. 99:19-23(1997). RN [47] RP VARIANTS CIRRH ALA-103; LEU-128; GLN-261 AND ARG-340, AND VARIANT THR-230. RX PubMed=12724528; DOI=10.1073/pnas.0936165100; RA Ku N.-O., Darling J.M., Krams S.M., Esquivel C.O., Keeffe E.B., RA Sibley R.K., Lee Y.M., Wright T.L., Omary M.B.; RT "Keratin 8 and 18 mutations are risk factors for developing liver disease RT of multiple etiologies."; RL Proc. Natl. Acad. Sci. U.S.A. 100:6063-6068(2003). CC -!- FUNCTION: Involved in the uptake of thrombin-antithrombin complexes by CC hepatic cells (By similarity). When phosphorylated, plays a role in CC filament reorganization. Involved in the delivery of mutated CFTR to CC the plasma membrane. Together with KRT8, is involved in interleukin-6 CC (IL-6)-mediated barrier protection. {ECO:0000250, CC ECO:0000269|PubMed:15529338, ECO:0000269|PubMed:16424149, CC ECO:0000269|PubMed:17213200, ECO:0000269|PubMed:7523419, CC ECO:0000269|PubMed:8522591, ECO:0000269|PubMed:9298992, CC ECO:0000269|PubMed:9524113}. CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins. KRT18 CC associates with KRT8 (PubMed:10852826, PubMed:24940650). Interacts with CC PLEC isoform 1C, when in a heterodimer with KRT8 (PubMed:24940650). CC Interacts with the thrombin-antithrombin complex (By similarity). CC Interacts with PNN and mutated CFTR. Interacts with YWHAE, YWHAH and CC YWHAZ only when phosphorylated. Interacts with DNAJB6, TCHP and TRADD. CC Interacts with FAM83H (PubMed:23902688). Interacts with EPPK1 (By CC similarity). Interacts with PKP1 and PKP2 (PubMed:10852826). CC {ECO:0000250, ECO:0000250|UniProtKB:P05784, CC ECO:0000269|PubMed:10809736, ECO:0000269|PubMed:10852826, CC ECO:0000269|PubMed:10954706, ECO:0000269|PubMed:11684708, CC ECO:0000269|PubMed:15529338, ECO:0000269|PubMed:15731013, CC ECO:0000269|PubMed:23902688, ECO:0000269|PubMed:24940650, CC ECO:0000269|PubMed:8609167, ECO:0000269|PubMed:9524113}. CC -!- SUBUNIT: (Microbial infection) Interacts with hepatitis C virus/HCV CC core protein. {ECO:0000269|PubMed:15846844}. CC -!- INTERACTION: CC P05783; Q9NX04: AIRIM; NbExp=3; IntAct=EBI-297888, EBI-8643161; CC P05783; Q14457: BECN1; NbExp=2; IntAct=EBI-297888, EBI-949378; CC P05783; Q8IYE0-2: CCDC146; NbExp=3; IntAct=EBI-297888, EBI-10247802; CC P05783; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-297888, EBI-10175300; CC P05783; O75190: DNAJB6; NbExp=6; IntAct=EBI-297888, EBI-1053164; CC P05783; Q5JVL4: EFHC1; NbExp=3; IntAct=EBI-297888, EBI-743105; CC P05783; Q08379: GOLGA2; NbExp=7; IntAct=EBI-297888, EBI-618309; CC P05783; Q96CS2: HAUS1; NbExp=3; IntAct=EBI-297888, EBI-2514791; CC P05783; A0A0S2Z4Q4: HGS; NbExp=3; IntAct=EBI-297888, EBI-16429135; CC P05783; O14964: HGS; NbExp=7; IntAct=EBI-297888, EBI-740220; CC P05783; P42858: HTT; NbExp=6; IntAct=EBI-297888, EBI-466029; CC P05783; Q9Y6K9: IKBKG; NbExp=3; IntAct=EBI-297888, EBI-81279; CC P05783; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-297888, EBI-14069005; CC P05783; P02538: KRT6A; NbExp=3; IntAct=EBI-297888, EBI-702198; CC P05783; P48668: KRT6C; NbExp=4; IntAct=EBI-297888, EBI-2564105; CC P05783; Q3SY84: KRT71; NbExp=3; IntAct=EBI-297888, EBI-2952676; CC P05783; Q5XKE5: KRT79; NbExp=3; IntAct=EBI-297888, EBI-2514135; CC P05783; P05787: KRT8; NbExp=16; IntAct=EBI-297888, EBI-297852; CC P05783; Q14533: KRT81; NbExp=3; IntAct=EBI-297888, EBI-739648; CC P05783; O75022: LILRB3; NbExp=3; IntAct=EBI-297888, EBI-2830524; CC P05783; Q9BQ69: MACROD1; NbExp=7; IntAct=EBI-297888, EBI-5324932; CC P05783; P07196: NEFL; NbExp=3; IntAct=EBI-297888, EBI-475646; CC P05783; Q9Y5B8: NME7; NbExp=4; IntAct=EBI-297888, EBI-744782; CC P05783; Q13835-2: PKP1; NbExp=4; IntAct=EBI-297888, EBI-9087684; CC P05783; A0A0S2Z505: PSTPIP2; NbExp=3; IntAct=EBI-297888, EBI-16437709; CC P05783; Q9P2K3-2: RCOR3; NbExp=3; IntAct=EBI-297888, EBI-1504830; CC P05783; Q8N0S2: SYCE1; NbExp=3; IntAct=EBI-297888, EBI-6872807; CC P05783; Q8WW24: TEKT4; NbExp=3; IntAct=EBI-297888, EBI-750487; CC P05783; Q15628: TRADD; NbExp=11; IntAct=EBI-297888, EBI-359215; CC P05783; Q99816: TSG101; NbExp=4; IntAct=EBI-297888, EBI-346882; CC P05783; B7UM99: tir; Xeno; NbExp=5; IntAct=EBI-297888, EBI-2504426; CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250|UniProtKB:Q5BJY9}. CC Cytoplasm, perinuclear region. Nucleus, nucleolus CC {ECO:0000269|PubMed:22002106}. Cytoplasm CC {ECO:0000250|UniProtKB:Q5BJY9}. CC -!- TISSUE SPECIFICITY: Expressed in colon, placenta, liver and very weakly CC in exocervix. Increased expression observed in lymph nodes of breast CC carcinoma. {ECO:0000269|PubMed:17213200, ECO:0000269|PubMed:2422083, CC ECO:0000269|PubMed:2434380, ECO:0000269|PubMed:2434381}. CC -!- INDUCTION: By IL6/interleukin-6. {ECO:0000269|PubMed:17213200}. CC -!- PTM: Phosphorylation at Ser-34 increases during mitosis. CC Hyperphosphorylated at Ser-53 in diseased cirrhosis liver. CC Phosphorylation increases by IL-6. {ECO:0000269|PubMed:15368451, CC ECO:0000269|PubMed:16424149, ECO:0000269|PubMed:17213200, CC ECO:0000269|PubMed:7523419, ECO:0000269|PubMed:8609167, CC ECO:0000269|PubMed:9524113}. CC -!- PTM: Proteolytically cleaved by caspases during epithelial cell CC apoptosis. Cleavage occurs at Asp-238 by either caspase-3, caspase-6 or CC caspase-7. {ECO:0000269|PubMed:9298992}. CC -!- PTM: O-GlcNAcylation increases solubility, and decreases stability by CC inducing proteasomal degradation. CC -!- DISEASE: Cirrhosis (CIRRH) [MIM:215600]: A liver disease characterized CC by severe panlobular liver-cell swelling with Mallory body formation, CC prominent pericellular fibrosis, and marked deposits of copper. CC Clinical features include abdomen swelling, jaundice and pulmonary CC hypertension. {ECO:0000269|PubMed:12724528, CC ECO:0000269|PubMed:9011570}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- MISCELLANEOUS: There are two types of cytoskeletal and microfibrillar CC keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa). CC -!- SIMILARITY: Belongs to the intermediate filament family. CC {ECO:0000255|PROSITE-ProRule:PRU01188}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X12881; CAA31375.1; -; mRNA. DR EMBL; AY762101; AAX07828.1; -; mRNA. DR EMBL; BT019412; AAV38219.1; -; mRNA. DR EMBL; AK223093; BAD96813.1; -; mRNA. DR EMBL; BC000180; AAH00180.1; -; mRNA. DR EMBL; BC000698; AAH00698.1; -; mRNA. DR EMBL; BC004253; AAH04253.1; -; mRNA. DR EMBL; BC008636; AAH08636.1; -; mRNA. DR EMBL; BC020982; AAH20982.1; -; mRNA. DR EMBL; BC072017; AAH72017.1; -; mRNA. DR EMBL; AF179904; AAA59461.1; -; Genomic_DNA. DR EMBL; X12883; CAA31377.1; -; mRNA. DR EMBL; X12876; CAA31369.1; -; mRNA. DR CCDS; CCDS31809.1; -. DR PIR; S05481; S05481. DR RefSeq; NP_000215.1; NM_000224.2. DR RefSeq; NP_954657.1; NM_199187.1. DR AlphaFoldDB; P05783; -. DR SMR; P05783; -. DR BioGRID; 110073; 377. DR ComplexPortal; CPX-5661; Keratin-8 - Keratin-18 dimer complex. DR DIP; DIP-633N; -. DR IntAct; P05783; 119. DR MINT; P05783; -. DR STRING; 9606.ENSP00000373489; -. DR GlyConnect; 312; 3 N-Linked glycans (1 site), 1 O-GlcNAc glycan (2 sites). DR GlyCosmos; P05783; 7 sites, 3 glycans. DR GlyGen; P05783; 19 sites, 2 N-linked glycans (1 site), 2 O-linked glycans (18 sites). DR iPTMnet; P05783; -. DR MetOSite; P05783; -. DR PhosphoSitePlus; P05783; -. DR SwissPalm; P05783; -. DR BioMuta; KRT18; -. DR DMDM; 125083; -. DR CPTAC; CPTAC-1518; -. DR CPTAC; CPTAC-1519; -. DR EPD; P05783; -. DR jPOST; P05783; -. DR MassIVE; P05783; -. DR MaxQB; P05783; -. DR PaxDb; 9606-ENSP00000373487; -. DR PeptideAtlas; P05783; -. DR PRIDE; P05783; -. DR ProteomicsDB; 51857; -. DR TopDownProteomics; P05783; -. DR ABCD; P05783; 4 sequenced antibodies. DR Antibodypedia; 271; 4198 antibodies from 57 providers. DR DNASU; 3875; -. DR Ensembl; ENST00000388835.4; ENSP00000373487.3; ENSG00000111057.11. DR Ensembl; ENST00000388837.6; ENSP00000373489.2; ENSG00000111057.11. DR GeneID; 3875; -. DR KEGG; hsa:3875; -. DR MANE-Select; ENST00000388835.4; ENSP00000373487.3; NM_000224.3; NP_000215.1. DR UCSC; uc001sbe.4; human. DR AGR; HGNC:6430; -. DR CTD; 3875; -. DR DisGeNET; 3875; -. DR GeneCards; KRT18; -. DR HGNC; HGNC:6430; KRT18. DR HPA; ENSG00000111057; Low tissue specificity. DR MalaCards; KRT18; -. DR MIM; 148070; gene. DR MIM; 215600; phenotype. DR neXtProt; NX_P05783; -. DR OpenTargets; ENSG00000111057; -. DR PharmGKB; PA30217; -. DR VEuPathDB; HostDB:ENSG00000111057; -. DR eggNOG; ENOG502QUS8; Eukaryota. DR GeneTree; ENSGT00940000153309; -. DR InParanoid; P05783; -. DR OMA; REWGHYF; -. DR OrthoDB; 4640531at2759; -. DR PhylomeDB; P05783; -. DR TreeFam; TF332742; -. DR PathwayCommons; P05783; -. DR Reactome; R-HSA-6805567; Keratinization. DR Reactome; R-HSA-6809371; Formation of the cornified envelope. DR SignaLink; P05783; -. DR SIGNOR; P05783; -. DR BioGRID-ORCS; 3875; 105 hits in 1166 CRISPR screens. DR ChiTaRS; KRT18; human. DR GeneWiki; Keratin_18; -. DR GenomeRNAi; 3875; -. DR Pharos; P05783; Tbio. DR PRO; PR:P05783; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; P05783; Protein. DR Bgee; ENSG00000111057; Expressed in endometrium epithelium and 173 other cell types or tissues. DR ExpressionAtlas; P05783; baseline and differential. DR GO; GO:0005912; C:adherens junction; HDA:BHF-UCL. DR GO; GO:0071944; C:cell periphery; IEA:Ensembl. DR GO; GO:0034451; C:centriolar satellite; IDA:BHF-UCL. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005882; C:intermediate filament; IDA:BHF-UCL. DR GO; GO:0045095; C:keratin filament; IDA:UniProtKB. DR GO; GO:0005815; C:microtubule organizing center; IDA:BHF-UCL. DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0098641; F:cadherin binding involved in cell-cell adhesion; HDA:BHF-UCL. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IEA:Ensembl. DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IDA:UniProtKB. DR GO; GO:0097284; P:hepatocyte apoptotic process; IEA:Ensembl. DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; IDA:UniProtKB. DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB. DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IEA:Ensembl. DR Gene3D; 1.20.5.170; -; 1. DR Gene3D; 1.20.5.500; Single helix bin; 1. DR Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1. DR InterPro; IPR018039; IF_conserved. DR InterPro; IPR039008; IF_rod_dom. DR InterPro; IPR002957; Keratin_I. DR PANTHER; PTHR23239; INTERMEDIATE FILAMENT; 1. DR PANTHER; PTHR23239:SF349; KERATIN, TYPE I CYTOSKELETAL 18; 1. DR Pfam; PF00038; Filament; 1. DR PRINTS; PR01248; TYPE1KERATIN. DR SMART; SM01391; Filament; 1. DR SUPFAM; SSF64593; Intermediate filament protein, coiled coil region; 2. DR PROSITE; PS00226; IF_ROD_1; 1. DR PROSITE; PS51842; IF_ROD_2; 1. DR SWISS-2DPAGE; P05783; -. DR Genevisible; P05783; HS. PE 1: Evidence at protein level; KW Acetylation; Cell cycle; Coiled coil; Cytoplasm; Direct protein sequencing; KW Disease variant; Glycoprotein; Host-virus interaction; KW Intermediate filament; Isopeptide bond; Keratin; Methylation; Nucleus; KW Phosphoprotein; Reference proteome; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:7538124" FT CHAIN 2..430 FT /note="Keratin, type I cytoskeletal 18" FT /id="PRO_0000063666" FT DOMAIN 80..391 FT /note="IF rod" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188" FT REGION 2..79 FT /note="Head" FT REGION 70..373 FT /note="Necessary for interaction with PNN" FT /evidence="ECO:0000269|PubMed:10809736" FT REGION 77..128 FT /note="Interaction with TRADD" FT /evidence="ECO:0000269|PubMed:11684708" FT REGION 80..115 FT /note="Coil 1A" FT REGION 116..132 FT /note="Linker 1" FT REGION 133..224 FT /note="Coil 1B" FT REGION 225..248 FT /note="Linker 12" FT REGION 243..391 FT /note="Interaction with DNAJB6" FT /evidence="ECO:0000269|PubMed:10954706" FT REGION 249..387 FT /note="Coil 2" FT REGION 388..430 FT /note="Tail" FT SITE 238..239 FT /note="Cleavage; by caspase-3, caspase-6 or caspase-7" FT SITE 271 FT /note="Stutter" FT SITE 331 FT /note="Stutter" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000269|PubMed:7538124" FT MOD_RES 7 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 10 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 15 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17924679, FT ECO:0007744|PubMed:20068231" FT MOD_RES 18 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 30 FT /note="Phosphoserine; alternate" FT /evidence="ECO:0000250|UniProtKB:P05784" FT MOD_RES 31 FT /note="Phosphoserine; alternate" FT /evidence="ECO:0000250|UniProtKB:P05784" FT MOD_RES 34 FT /note="Phosphoserine; by CDK1" FT /evidence="ECO:0000269|PubMed:15368451, FT ECO:0000269|PubMed:9524113, ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 36 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P05784" FT MOD_RES 42 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES 45 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 49 FT /note="Phosphoserine; alternate" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 51 FT /note="Phosphoserine; by MAPKAPK2 and MAPKAPK3" FT /evidence="ECO:0000250|UniProtKB:P05784" FT MOD_RES 52 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 53 FT /note="Phosphoserine; by CAMK, PKC/PRKCE and AURKA" FT /evidence="ECO:0000269|PubMed:15368451, FT ECO:0000269|PubMed:16424149, ECO:0000269|PubMed:7523419" FT MOD_RES 55 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 60 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 65 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:24275569" FT MOD_RES 93 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 100 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 131 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 177 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 302 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 305 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 319 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 323 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 398 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 399 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 401 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 404 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:24275569" FT MOD_RES 426 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT CARBOHYD 30 FT /note="O-linked (GlcNAc) serine; alternate" FT /evidence="ECO:0000269|PubMed:20729549, FT ECO:0000269|PubMed:7538124" FT /id="CAR_000175" FT CARBOHYD 31 FT /note="O-linked (GlcNAc) serine; alternate" FT /evidence="ECO:0000269|PubMed:20729549, FT ECO:0000269|PubMed:7538124" FT /id="CAR_000193" FT CARBOHYD 49 FT /note="O-linked (GlcNAc) serine; alternate" FT /evidence="ECO:0000269|PubMed:20729549, FT ECO:0000269|PubMed:7538124" FT /id="CAR_000194" FT CROSSLNK 81 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 247 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 370 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 372 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 417 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 426 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 426 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:28112733" FT VARIANT 103 FT /note="T -> A (in CIRRH; dbSNP:rs61136606)" FT /evidence="ECO:0000269|PubMed:12724528" FT /id="VAR_023054" FT VARIANT 128 FT /note="H -> L (in CIRRH; interferes with the ability to FT form normal filaments; dbSNP:rs57758506)" FT /evidence="ECO:0000269|PubMed:12724528, FT ECO:0000269|PubMed:9011570" FT /id="VAR_003852" FT VARIANT 230 FT /note="S -> T (in dbSNP:rs58472472)" FT /evidence="ECO:0000269|PubMed:12724528" FT /id="VAR_023055" FT VARIANT 261 FT /note="R -> Q (in CIRRH; dbSNP:rs57354642)" FT /evidence="ECO:0000269|PubMed:12724528" FT /id="VAR_023056" FT VARIANT 340 FT /note="G -> R (in CIRRH; dbSNP:rs57370769)" FT /evidence="ECO:0000269|PubMed:12724528" FT /id="VAR_023057" FT MUTAGEN 2 FT /note="S->A: No effect on phosphorylation; when associated FT with A-7 and A-10." FT /evidence="ECO:0000269|PubMed:7523419" FT MUTAGEN 7 FT /note="S->A: No effect on phosphorylation; when associated FT with A-2 and A-10." FT /evidence="ECO:0000269|PubMed:7523419" FT MUTAGEN 10 FT /note="S->A: No effect on phosphorylation; when associated FT with A-2 and A-7." FT /evidence="ECO:0000269|PubMed:7523419" FT MUTAGEN 15 FT /note="S->A: No effect on phosphorylation; when associated FT with A-18 and A-23. Abolishes phosphorylation; when FT associated with A-18; A-34; A-47; A-49; A-51 and A-53." FT /evidence="ECO:0000269|PubMed:7523419" FT MUTAGEN 18 FT /note="S->A: No effect on phosphorylation; when associated FT with A-15 and A-23. Abolishes phosphorylation; when FT associated with A-15; A-34; A-47; A-49; A-51 and A-53." FT /evidence="ECO:0000269|PubMed:7523419" FT MUTAGEN 23 FT /note="S->A: No effect on phosphorylation; when associated FT with A-15 and A-18." FT /evidence="ECO:0000269|PubMed:7523419" FT MUTAGEN 30 FT /note="S->A: No effect on phosphorylation; when associated FT with A-31 and A-34, or with A-31; A-44 and A-51. Abolishes FT glycosylation but does not affect binding to YWHAE and FT YWHAZ; when associated with A-31 and A-49." FT /evidence="ECO:0000269|PubMed:7523419, FT ECO:0000269|PubMed:7538124" FT MUTAGEN 31 FT /note="S->A: No effect on phosphorylation; when associated FT with A-30 and A-34, or with A-30; A-44 and A-51. Abolishes FT glycosylation but does not affect binding to YWHAE and FT YWHAZ; when associated with A-30 and A-49." FT /evidence="ECO:0000269|PubMed:7523419, FT ECO:0000269|PubMed:7538124" FT MUTAGEN 34 FT /note="S->A: No effect on phosphorylation; when associated FT with A-30 and A-31. Abolishes phosphorylation; when FT associated with A-15; A-18; A-47; A-49; A-51 and A-53. FT Abolishes binding to YWHAE and YWHAZ; and when associated FT with A-53." FT /evidence="ECO:0000269|PubMed:7523419, FT ECO:0000269|PubMed:9524113" FT MUTAGEN 34 FT /note="S->D,E: Abolishes binding to YWHAE and YWHAZ." FT /evidence="ECO:0000269|PubMed:7523419, FT ECO:0000269|PubMed:9524113" FT MUTAGEN 42 FT /note="S->A: No effect on phosphorylation; when associated FT with A-44." FT /evidence="ECO:0000269|PubMed:7523419" FT MUTAGEN 44 FT /note="S->A: No effect on phosphorylation; when associated FT with A-42, or with A-30; A-31 and A-51." FT /evidence="ECO:0000269|PubMed:7523419" FT MUTAGEN 47 FT /note="S->A: No effect on phosphorylation; when associated FT with A-49. Abolishes phosphorylation; when associated with FT A-49; A-51 and A-53, or with A-15; A-18; A-34; A-49; A-51 FT and A-53." FT /evidence="ECO:0000269|PubMed:7523419" FT MUTAGEN 49 FT /note="S->A: No effect on phosphorylation; when associated FT with A-47. Abolishes phosphorylation; when associated with FT A-47; A-51 and A-53, or with A-15; A-18; A-34; A-47; A-51 FT and A-53. Abolishes glycosylation but does not affect FT binding to YWHAE and YWHAZ; when associated with A-30 and FT A-31." FT /evidence="ECO:0000269|PubMed:7523419, FT ECO:0000269|PubMed:7538124" FT MUTAGEN 51 FT /note="S->A: No effect on phosphorylation; when associated FT with A-30; A-31 and A-47. Abolishes phosphorylation; when FT associated with A-47; A-49 and A-53, or with A-15; A-18; FT A-34; A-47; A-49 and A-53." FT /evidence="ECO:0000269|PubMed:7523419" FT MUTAGEN 53 FT /note="S->A: Abolishes phosphorylation; when associated FT with A-47; A-49 and A-51, or with A-15; A-18; A-34; A-47; FT A-49 and A-51. Abolishes binding to YWHAE and YWHAZ; when FT associated with A-34. No effect on caspase cleavage during FT apoptosis." FT /evidence="ECO:0000269|PubMed:7523419, FT ECO:0000269|PubMed:9298992, ECO:0000269|PubMed:9524113" FT MUTAGEN 90 FT /note="R->C,H: In transgenic mice, induces marked FT disruption of liver and pancreas keratin filament network. FT Increases phosphorylation and glycosylation." FT /evidence="ECO:0000269|PubMed:8522591" FT MUTAGEN 238 FT /note="D->E: Prevents cleavage by caspase-6 during FT apoptosis. Induces aggregates of keratin filaments in an FT altered organization." FT /evidence="ECO:0000269|PubMed:9298992" FT CONFLICT 168 FT /note="Y -> H (in Ref. 5; AAH00698)" FT /evidence="ECO:0000305" FT CONFLICT 202 FT /note="E -> Q (in Ref. 8; CAA31369)" FT /evidence="ECO:0000305" FT CONFLICT 208 FT /note="E -> G (in Ref. 3; BAD96813)" FT /evidence="ECO:0000305" FT CONFLICT 246 FT /note="A -> S (in Ref. 8; CAA31369)" FT /evidence="ECO:0000305" FT CONFLICT 309 FT /note="D -> R (in Ref. 8; CAA31369)" FT /evidence="ECO:0000305" FT CONFLICT 312 FT /note="S -> R (in Ref. 8; CAA31369)" FT /evidence="ECO:0000305" SQ SEQUENCE 430 AA; 48058 MW; 1E5604C6BCC7A17A CRC64; MSFTTRSTFS TNYRSLGSVQ APSYGARPVS SAASVYAGAG GSGSRISVSR STSFRGGMGS GGLATGIAGG LAGMGGIQNE KETMQSLNDR LASYLDRVRS LETENRRLES KIREHLEKKG PQVRDWSHYF KIIEDLRAQI FANTVDNARI VLQIDNARLA ADDFRVKYET ELAMRQSVEN DIHGLRKVID DTNITRLQLE TEIEALKEEL LFMKKNHEEE VKGLQAQIAS SGLTVEVDAP KSQDLAKIMA DIRAQYDELA RKNREELDKY WSQQIEESTT VVTTQSAEVG AAETTLTELR RTVQSLEIDL DSMRNLKASL ENSLREVEAR YALQMEQLNG ILLHLESELA QTRAEGQRQA QEYEALLNIK VKLEAEIATY RRLLEDGEDF NLGDALDSSN SMQTIQKTTT RRIVDGKVVS ETNDTKVLRH //