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Keratin, type I cytoskeletal 18 (Cell proliferation-inducing gene 46 protein) (Cytokeratin-18) (CK-18) (Keratin-18) (K18)

 K1C18_HUMAN             Reviewed;         430 AA.
P05783; Q53G38; Q5U0N8; Q9BW26;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
25-OCT-2017, entry version 200.
RecName: Full=Keratin, type I cytoskeletal 18;
AltName: Full=Cell proliferation-inducing gene 46 protein;
AltName: Full=Cytokeratin-18;
Short=CK-18;
AltName: Full=Keratin-18;
Short=K18;
Name=KRT18; Synonyms=CYK18; ORFNames=PIG46;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Placenta;
PubMed=2434380; DOI=10.1111/j.1432-0436.1986.tb00411.x;
Oshima R.G., Millan J.L., Cecena G.;
"Comparison of mouse and human keratin 18: a component of intermediate
filaments expressed prior to implantation.";
Differentiation 33:61-68(1986).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kim J.W.;
"Identification of a cell proliferation-inducing gene.";
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cervix, Colon, Pancreas, Placenta, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-167.
PubMed=2454392; DOI=10.1128/MCB.8.4.1540;
Kulesh D.A., Oshima R.G.;
"Cloning of the human keratin 18 gene and its expression in
nonepithelial mouse cells.";
Mol. Cell. Biol. 8:1540-1550(1988).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 7-430, AND TISSUE SPECIFICITY.
TISSUE=Vulva;
PubMed=2434381; DOI=10.1111/j.1432-0436.1986.tb00412.x;
Leube R.E., Bosch F.X., Romano V., Zimbelmann R., Hofler H.,
Franke W.W.;
"Cytokeratin expression in simple epithelia. III. Detection of mRNAs
encoding human cytokeratins nos. 8 and 18 in normal and tumor cells by
hybridization with cDNA sequences in vitro and in situ.";
Differentiation 33:69-85(1986).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 199-430, AND TISSUE SPECIFICITY.
TISSUE=Liver;
PubMed=2422083; DOI=10.1111/j.1432-0436.1986.tb00787.x;
Romano V., Hatzfeld M., Magin T.M., Zimbelmann R., Franke W.W.,
Maier G., Ponstingl H.;
"Cytokeratin expression in simple epithelia. I. Identification of mRNA
coding for human cytokeratin no. 18 by a cDNA clone.";
Differentiation 30:244-253(1986).
[9]
PARTIAL PROTEIN SEQUENCE.
TISSUE=Colon carcinoma;
PubMed=9150948; DOI=10.1002/elps.1150180344;
Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.;
"A two-dimensional gel database of human colon carcinoma proteins.";
Electrophoresis 18:605-613(1997).
[10]
GLYCOSYLATION.
PubMed=1371281;
Chou C.F., Smith A.J., Omary M.B.;
"Characterization and dynamics of O-linked glycosylation of human
cytokeratin 8 and 18.";
J. Biol. Chem. 267:3901-3906(1992).
[11]
FUNCTION, PHOSPHORYLATION AT SER-53, AND MUTAGENESIS OF SER-2; SER-7;
SER-10; SER-15; SER-18; SER-23; SER-30; SER-31; SER-34; SER-42;
SER-44; SER-47; SER-49; SER-51 AND SER-53.
PubMed=7523419; DOI=10.1083/jcb.127.1.161;
Ku N.O., Omary M.B.;
"Identification of the major physiologic phosphorylation site of human
keratin 18: potential kinases and a role in filament reorganization.";
J. Cell Biol. 127:161-171(1994).
[12]
GLYCOSYLATION AT SER-30; SER-31 AND SER-49, MUTAGENESIS OF SER-30;
SER-31 AND SER-49, CLEAVAGE OF INITIATOR METHIONINE, AND ACETYLATION
AT SER-2.
PubMed=7538124; DOI=10.1074/jbc.270.20.11820;
Ku N.-O., Omary M.B.;
"Identification and mutational analysis of the glycosylation sites of
human keratin 18.";
J. Biol. Chem. 270:11820-11827(1995).
[13]
FUNCTION, AND MUTAGENESIS OF ARG-90.
PubMed=8522591; DOI=10.1083/jcb.131.5.1303;
Ku N.O., Michie S., Oshima R.G., Omary M.B.;
"Chronic hepatitis, hepatocyte fragility, and increased soluble
phosphoglycokeratins in transgenic mice expressing a keratin 18
conserved arginine mutant.";
J. Cell Biol. 131:1303-1314(1995).
[14]
PHOSPHORYLATION, AND INTERACTION WITH YWHAE; YWHAH AND YWHAZ.
PubMed=8609167; DOI=10.1083/jcb.133.2.345;
Liao J., Omary M.B.;
"14-3-3 proteins associate with phosphorylated simple epithelial
keratins during cell cycle progression and act as a solubility
cofactor.";
J. Cell Biol. 133:345-357(1996).
[15]
FUNCTION, CLEAVAGE BY CASPASES, AND MUTAGENESIS OF SER-53 AND ASP-238.
PubMed=9298992; DOI=10.1083/jcb.138.6.1379;
Caulin C., Salvesen G.S., Oshima R.G.;
"Caspase cleavage of keratin 18 and reorganization of intermediate
filaments during epithelial cell apoptosis.";
J. Cell Biol. 138:1379-1394(1997).
[16]
FUNCTION, INTERACTION WITH YWHAE AND YWHAZ, PHOSPHORYLATION AT SER-34,
AND MUTAGENESIS OF SER-34 AND SER-53.
PubMed=9524113; DOI=10.1093/emboj/17.7.1892;
Ku N.O., Liao J., Omary M.B.;
"Phosphorylation of human keratin 18 serine 33 regulates binding to
14-3-3 proteins.";
EMBO J. 17:1892-1906(1998).
[17]
INTERACTION WITH PNN.
PubMed=10809736; DOI=10.1074/jbc.275.20.14910;
Shi J., Sugrue S.P.;
"Dissection of protein linkage between keratins and pinin, a protein
with dual location at desmosome-intermediate filament complex and in
the nucleus.";
J. Biol. Chem. 275:14910-14915(2000).
[18]
INTERACTION WITH DNAJB6.
PubMed=10954706; DOI=10.1074/jbc.M003492200;
Izawa I., Nishizawa M., Ohtakara K., Ohtsuka K., Inada H., Inagaki M.;
"Identification of Mrj, a DnaJ/Hsp40 family protein, as a keratin 8/18
filament regulatory protein.";
J. Biol. Chem. 275:34521-34527(2000).
[19]
INTERACTION WITH TRADD.
PubMed=11684708; DOI=10.1083/jcb.200103078;
Inada H., Izawa I., Nishizawa M., Fujita E., Kiyono T., Takahashi T.,
Momoi T., Inagaki M.;
"Keratin attenuates tumor necrosis factor-induced cytotoxicity through
association with TRADD.";
J. Cell Biol. 155:415-426(2001).
[20]
ASSOCIATION WITH KRT8.
PubMed=14756564; DOI=10.1021/bi035072s;
Waseem A., Karsten U., Leigh I.M., Purkis P., Waseem N.H., Lane E.B.;
"Conformational changes in the rod domain of human keratin 8 following
heterotypic association with keratin 18 and its implication for
filament stability.";
Biochemistry 43:1283-1295(2004).
[21]
PHOSPHORYLATION AT SER-34 AND SER-53.
PubMed=15368451; DOI=10.1002/hep.20277;
Toivola D.M., Ku N.O., Resurreccion E.Z., Nelson D.R., Wright T.L.,
Omary M.B.;
"Keratin 8 and 18 hyperphosphorylation is a marker of progression of
human liver disease.";
Hepatology 40:459-466(2004).
[22]
FUNCTION, INTERACTION WITH MUTATED CFTR, AND SUBCELLULAR LOCATION.
PubMed=15529338; DOI=10.1002/pmic.200400850;
Davezac N., Tondelier D., Lipecka J., Fanen P., Demaugre F.,
Debski J., Dadlez M., Schrattenholz A., Cahill M.A., Edelman A.;
"Global proteomic approach unmasks involvement of keratins 8 and 18 in
the delivery of cystic fibrosis transmembrane conductance regulator
(CFTR)/deltaF508-CFTR to the plasma membrane.";
Proteomics 4:3833-3844(2004).
[23]
INTERACTION WITH TCHP.
PubMed=15731013; DOI=10.1242/jcs.01667;
Nishizawa M., Izawa I., Inoko A., Hayashi Y., Nagata K., Yokoyama T.,
Usukura J., Inagaki M.;
"Identification of trichoplein, a novel keratin filament-binding
protein.";
J. Cell Sci. 118:1081-1090(2005).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[25]
FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-53.
PubMed=16424149; DOI=10.1124/jpet.105.097667;
Lipecka J., Norez C., Bensalem N., Baudouin-Legros M., Planelles G.,
Becq F., Edelman A., Davezac N.;
"Rescue of DeltaF508-CFTR (cystic fibrosis transmembrane conductance
regulator) by curcumin: involvement of the keratin 18 network.";
J. Pharmacol. Exp. Ther. 317:500-505(2006).
[26]
FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION, AND INDUCTION.
PubMed=17213200; DOI=10.1074/jbc.M604068200;
Wang L., Srinivasan S., Theiss A.L., Merlin D., Sitaraman S.V.;
"Interleukin-6 induces keratin expression in intestinal epithelial
cells: potential role of keratin-8 in interleukin-6-induced barrier
function alterations.";
J. Biol. Chem. 282:8219-8227(2007).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17924679; DOI=10.1021/pr070152u;
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa
cells and high confident phosphopeptide identification by cross-
validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-34; SER-42;
SER-60; THR-302 AND SER-399, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[30]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-131 AND LYS-426, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[31]
GLYCOSYLATION AT SER-30; SER-31 AND SER-49.
PubMed=20729549; DOI=10.1074/jbc.M109.098996;
Srikanth B., Vaidya M.M., Kalraiya R.D.;
"O-GlcNAcylation determines the solubility, filament organization, and
stability of keratins 8 and 18.";
J. Biol. Chem. 285:34062-34071(2010).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-15; SER-34;
SER-42; SER-60; THR-65; SER-100; SER-319; SER-399 AND THR-404, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[33]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[34]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[35]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=22002106; DOI=10.1074/mcp.M111.013680;
Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I.;
"Systematic analysis of protein pools, isoforms, and modifications
affecting turnover and subcellular localization.";
Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012).
[36]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[37]
INTERACTION WITH FAM83H.
PubMed=23902688; DOI=10.1242/jcs.129684;
Kuga T., Kume H., Kawasaki N., Sato M., Adachi J., Shiromizu T.,
Hoshino I., Nishimori T., Matsubara H., Tomonaga T.;
"A novel mechanism of keratin cytoskeleton organization through casein
kinase Ialpha and FAM83H in colorectal cancer.";
J. Cell Sci. 126:4721-4731(2013).
[38]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-18; SER-34;
SER-49; THR-52; SER-60; SER-93; SER-305; SER-319; SER-323 AND SER-399,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[39]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-65; SER-177; SER-305;
SER-398; SER-399; SER-401 AND THR-404, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[40]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-45 AND ARG-55, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[41]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-426, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[42]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-81; LYS-247; LYS-370;
LYS-372; LYS-417 AND LYS-426, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[43]
VARIANT CIRRH LEU-128.
PubMed=9011570; DOI=10.1172/JCI119127;
Ku N.-O., Wright T.L., Terrault N.A., Gish R., Omary M.B.;
"Mutation of human keratin 18 in association with cryptogenic
cirrhosis.";
J. Clin. Invest. 99:19-23(1997).
[44]
VARIANTS CIRRH ALA-103; LEU-128; GLN-261 AND ARG-340, AND VARIANT
THR-230.
PubMed=12724528; DOI=10.1073/pnas.0936165100;
Ku N.-O., Darling J.M., Krams S.M., Esquivel C.O., Keeffe E.B.,
Sibley R.K., Lee Y.M., Wright T.L., Omary M.B.;
"Keratin 8 and 18 mutations are risk factors for developing liver
disease of multiple etiologies.";
Proc. Natl. Acad. Sci. U.S.A. 100:6063-6068(2003).
-!- FUNCTION: Involved in the uptake of thrombin-antithrombin
complexes by hepatic cells (By similarity). When phosphorylated,
plays a role in filament reorganization. Involved in the delivery
of mutated CFTR to the plasma membrane. Together with KRT8, is
involved in interleukin-6 (IL-6)-mediated barrier protection.
{ECO:0000250, ECO:0000269|PubMed:15529338,
ECO:0000269|PubMed:16424149, ECO:0000269|PubMed:17213200,
ECO:0000269|PubMed:7523419, ECO:0000269|PubMed:8522591,
ECO:0000269|PubMed:9298992, ECO:0000269|PubMed:9524113}.
-!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
KRT18 associates with KRT8. Interacts with the thrombin-
antithrombin complex (By similarity). Interacts with PNN, HCV core
protein and mutated CFTR. Interacts with YWHAE, YWHAH and YWHAZ
only when phosphorylated. Interacts with DNAJB6, TCHP and TRADD.
Interacts with FAM83H (PubMed:23902688). Interacts with EPPK1 (By
similarity). {ECO:0000250, ECO:0000250|UniProtKB:P05784,
ECO:0000269|PubMed:10809736, ECO:0000269|PubMed:10954706,
ECO:0000269|PubMed:11684708, ECO:0000269|PubMed:15529338,
ECO:0000269|PubMed:15731013, ECO:0000269|PubMed:23902688,
ECO:0000269|PubMed:8609167, ECO:0000269|PubMed:9524113}.
-!- INTERACTION:
Q14457:BECN1; NbExp=2; IntAct=EBI-297888, EBI-949378;
Q8IYE0-2:CCDC146; NbExp=3; IntAct=EBI-297888, EBI-10247802;
O75190:DNAJB6; NbExp=6; IntAct=EBI-297888, EBI-1053164;
Q08379:GOLGA2; NbExp=6; IntAct=EBI-297888, EBI-618309;
Q96CS2:HAUS1; NbExp=3; IntAct=EBI-297888, EBI-2514791;
O14964:HGS; NbExp=8; IntAct=EBI-297888, EBI-740220;
Q9Y6K9:IKBKG; NbExp=3; IntAct=EBI-297888, EBI-81279;
P48668:KRT6C; NbExp=4; IntAct=EBI-297888, EBI-2564105;
P05787:KRT8; NbExp=12; IntAct=EBI-297888, EBI-297852;
Q9Y5B8:NME7; NbExp=3; IntAct=EBI-297888, EBI-744782;
Q13835-2:PKP1; NbExp=4; IntAct=EBI-297888, EBI-9087684;
Q8N0S2:SYCE1; NbExp=3; IntAct=EBI-297888, EBI-6872807;
Q15628:TRADD; NbExp=11; IntAct=EBI-297888, EBI-359215;
Q99816:TSG101; NbExp=3; IntAct=EBI-297888, EBI-346882;
-!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Nucleus,
nucleolus.
-!- TISSUE SPECIFICITY: Expressed in colon, placenta, liver and very
weakly in exocervix. Increased expression observed in lymph nodes
of breast carcinoma. {ECO:0000269|PubMed:17213200,
ECO:0000269|PubMed:2422083, ECO:0000269|PubMed:2434380,
ECO:0000269|PubMed:2434381}.
-!- INDUCTION: By IL6/interleukin-6. {ECO:0000269|PubMed:17213200}.
-!- PTM: Phosphorylation at Ser-34 increases during mitosis.
Hyperphosphorylated at Ser-53 in diseased cirrhosis liver.
Phosphorylation increases by IL-6. {ECO:0000269|PubMed:15368451,
ECO:0000269|PubMed:16424149, ECO:0000269|PubMed:17213200,
ECO:0000269|PubMed:7523419, ECO:0000269|PubMed:8609167,
ECO:0000269|PubMed:9524113}.
-!- PTM: Proteolytically cleaved by caspases during epithelial cell
apoptosis. Cleavage occurs at Asp-238 by either caspase-3,
caspase-6 or caspase-7. {ECO:0000269|PubMed:9298992}.
-!- PTM: O-GlcNAcylation increases solubility, and decreases stability
by inducing proteasomal degradation.
-!- DISEASE: Cirrhosis (CIRRH) [MIM:215600]: A liver disease
characterized by severe panlobular liver-cell swelling with
Mallory body formation, prominent pericellular fibrosis, and
marked deposits of copper. Clinical features include abdomen
swelling, jaundice and pulmonary hypertension.
{ECO:0000269|PubMed:12724528, ECO:0000269|PubMed:9011570}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- MISCELLANEOUS: There are two types of cytoskeletal and
microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to
basic; 56-70 kDa).
-!- SIMILARITY: Belongs to the intermediate filament family.
{ECO:0000255|PROSITE-ProRule:PRU01188}.
-!- WEB RESOURCE: Name=Human Intermediate Filament Mutation Database;
URL="http://www.interfil.org";
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EMBL; X12881; CAA31375.1; -; mRNA.
EMBL; AY762101; AAX07828.1; -; mRNA.
EMBL; BT019412; AAV38219.1; -; mRNA.
EMBL; AK223093; BAD96813.1; -; mRNA.
EMBL; BC000180; AAH00180.1; -; mRNA.
EMBL; BC000698; AAH00698.1; -; mRNA.
EMBL; BC004253; AAH04253.1; -; mRNA.
EMBL; BC008636; AAH08636.1; -; mRNA.
EMBL; BC020982; AAH20982.1; -; mRNA.
EMBL; BC072017; AAH72017.1; -; mRNA.
EMBL; AF179904; AAA59461.1; -; Genomic_DNA.
EMBL; X12883; CAA31377.1; -; mRNA.
EMBL; X12876; CAA31369.1; -; mRNA.
CCDS; CCDS31809.1; -.
PIR; S05481; S05481.
RefSeq; NP_000215.1; NM_000224.2.
RefSeq; NP_954657.1; NM_199187.1.
UniGene; Hs.406013; -.
ProteinModelPortal; P05783; -.
SMR; P05783; -.
BioGrid; 110073; 92.
DIP; DIP-633N; -.
IntAct; P05783; 73.
MINT; MINT-215967; -.
STRING; 9606.ENSP00000373487; -.
iPTMnet; P05783; -.
PhosphoSitePlus; P05783; -.
SwissPalm; P05783; -.
UniCarbKB; P05783; -.
BioMuta; KRT18; -.
DMDM; 125083; -.
SWISS-2DPAGE; P05783; -.
EPD; P05783; -.
MaxQB; P05783; -.
PaxDb; P05783; -.
PeptideAtlas; P05783; -.
PRIDE; P05783; -.
TopDownProteomics; P05783; -.
DNASU; 3875; -.
Ensembl; ENST00000388835; ENSP00000373487; ENSG00000111057.
Ensembl; ENST00000388837; ENSP00000373489; ENSG00000111057.
GeneID; 3875; -.
KEGG; hsa:3875; -.
UCSC; uc001sbe.4; human.
CTD; 3875; -.
DisGeNET; 3875; -.
EuPathDB; HostDB:ENSG00000111057.10; -.
GeneCards; KRT18; -.
H-InvDB; HIX0040371; -.
HGNC; HGNC:6430; KRT18.
HPA; CAB000008; -.
HPA; CAB000030; -.
HPA; HPA001605; -.
MalaCards; KRT18; -.
MIM; 148070; gene.
MIM; 215600; phenotype.
neXtProt; NX_P05783; -.
OpenTargets; ENSG00000111057; -.
PharmGKB; PA30217; -.
eggNOG; ENOG410IEYR; Eukaryota.
eggNOG; ENOG4111DJ8; LUCA.
GeneTree; ENSGT00900000140814; -.
HOGENOM; HOG000230975; -.
HOVERGEN; HBG013015; -.
InParanoid; P05783; -.
KO; K07604; -.
OMA; RAKYEKM; -.
OrthoDB; EOG091G0A3U; -.
PhylomeDB; P05783; -.
TreeFam; TF332742; -.
Reactome; R-HSA-6805567; Keratinization.
Reactome; R-HSA-6809371; Formation of the cornified envelope.
SignaLink; P05783; -.
SIGNOR; P05783; -.
ChiTaRS; KRT18; human.
GeneWiki; Keratin_18; -.
GenomeRNAi; 3875; -.
PMAP-CutDB; P05783; -.
PRO; PR:P05783; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000111057; -.
CleanEx; HS_KRT18; -.
ExpressionAtlas; P05783; baseline and differential.
Genevisible; P05783; HS.
GO; GO:0071944; C:cell periphery; IEA:Ensembl.
GO; GO:0005913; C:cell-cell adherens junction; IDA:BHF-UCL.
GO; GO:0034451; C:centriolar satellite; IDA:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005882; C:intermediate filament; IDA:BHF-UCL.
GO; GO:0045095; C:keratin filament; IDA:UniProtKB.
GO; GO:0005815; C:microtubule organizing center; IDA:BHF-UCL.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0098641; F:cadherin binding involved in cell-cell adhesion; IDA:BHF-UCL.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0070268; P:cornification; TAS:Reactome.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0043000; P:Golgi to plasma membrane CFTR protein transport; IDA:UniProtKB.
GO; GO:0097284; P:hepatocyte apoptotic process; IEA:Ensembl.
GO; GO:0045104; P:intermediate filament cytoskeleton organization; IDA:UniProtKB.
GO; GO:0031424; P:keratinization; TAS:Reactome.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IEA:Ensembl.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR001664; IF.
InterPro; IPR018039; Intermediate_filament_CS.
InterPro; IPR027695; Keratin-18.
InterPro; IPR002957; Keratin_I.
PANTHER; PTHR23239; PTHR23239; 1.
PANTHER; PTHR23239:SF35; PTHR23239:SF35; 1.
Pfam; PF00038; Filament; 1.
PRINTS; PR01248; TYPE1KERATIN.
SMART; SM01391; Filament; 1.
PROSITE; PS00226; IF_ROD_1; 1.
PROSITE; PS51842; IF_ROD_2; 1.
1: Evidence at protein level;
Acetylation; Cell cycle; Coiled coil; Complete proteome; Cytoplasm;
Direct protein sequencing; Disease mutation; Glycoprotein;
Host-virus interaction; Intermediate filament; Isopeptide bond;
Keratin; Methylation; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:7538124}.
CHAIN 2 430 Keratin, type I cytoskeletal 18.
/FTId=PRO_0000063666.
DOMAIN 80 391 IF rod. {ECO:0000255|PROSITE-
ProRule:PRU01188}.
REGION 2 79 Head.
REGION 70 373 Necessary for interaction with PNN.
{ECO:0000269|PubMed:10809736}.
REGION 77 128 Interaction with TRADD.
{ECO:0000269|PubMed:11684708}.
REGION 80 115 Coil 1A.
REGION 116 132 Linker 1.
REGION 133 224 Coil 1B.
REGION 225 248 Linker 12.
REGION 243 391 Interaction with DNAJB6.
{ECO:0000269|PubMed:10954706}.
REGION 249 387 Coil 2.
REGION 388 430 Tail.
SITE 238 239 Cleavage; by caspase-3, caspase-6 or
caspase-7.
SITE 271 271 Stutter.
SITE 331 331 Stutter.
MOD_RES 2 2 N-acetylserine.
{ECO:0000269|PubMed:7538124}.
MOD_RES 7 7 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 10 10 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 15 15 Phosphoserine.
{ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:20068231}.
MOD_RES 18 18 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 30 30 Phosphoserine; alternate.
{ECO:0000250|UniProtKB:P05784}.
MOD_RES 31 31 Phosphoserine; alternate.
{ECO:0000250|UniProtKB:P05784}.
MOD_RES 34 34 Phosphoserine; by CDK1.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:15368451,
ECO:0000269|PubMed:9524113}.
MOD_RES 36 36 Phosphotyrosine.
{ECO:0000250|UniProtKB:P05784}.
MOD_RES 42 42 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 45 45 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 49 49 Phosphoserine; alternate.
{ECO:0000244|PubMed:23186163}.
MOD_RES 51 51 Phosphoserine; by MAPKAPK2 and MAPKAPK3.
{ECO:0000250|UniProtKB:P05784,
ECO:0000305}.
MOD_RES 52 52 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 53 53 Phosphoserine; by CAMK, PKC/PRKCE and
AURKA. {ECO:0000269|PubMed:15368451,
ECO:0000269|PubMed:16424149,
ECO:0000269|PubMed:7523419}.
MOD_RES 55 55 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 60 60 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 65 65 Phosphothreonine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 93 93 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 100 100 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 131 131 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 177 177 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 302 302 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 305 305 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 319 319 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 323 323 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 398 398 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 399 399 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 401 401 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 404 404 Phosphothreonine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 426 426 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
CARBOHYD 30 30 O-linked (GlcNAc) serine; alternate.
{ECO:0000269|PubMed:20729549,
ECO:0000269|PubMed:7538124}.
/FTId=CAR_000175.
CARBOHYD 31 31 O-linked (GlcNAc) serine; alternate.
{ECO:0000269|PubMed:20729549,
ECO:0000269|PubMed:7538124}.
/FTId=CAR_000193.
CARBOHYD 49 49 O-linked (GlcNAc) serine; alternate.
{ECO:0000269|PubMed:20729549,
ECO:0000269|PubMed:7538124}.
/FTId=CAR_000194.
CROSSLNK 81 81 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 247 247 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 370 370 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 372 372 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 417 417 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 426 426 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 426 426 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
VARIANT 103 103 T -> A (in CIRRH; dbSNP:rs61136606).
{ECO:0000269|PubMed:12724528}.
/FTId=VAR_023054.
VARIANT 128 128 H -> L (in CIRRH; interfers with the
ability to form normal filaments;
dbSNP:rs57758506).
{ECO:0000269|PubMed:12724528,
ECO:0000269|PubMed:9011570}.
/FTId=VAR_003852.
VARIANT 230 230 S -> T (in dbSNP:rs58472472).
{ECO:0000269|PubMed:12724528}.
/FTId=VAR_023055.
VARIANT 261 261 R -> Q (in CIRRH; dbSNP:rs57354642).
{ECO:0000269|PubMed:12724528}.
/FTId=VAR_023056.
VARIANT 340 340 G -> R (in CIRRH; dbSNP:rs57370769).
{ECO:0000269|PubMed:12724528}.
/FTId=VAR_023057.
MUTAGEN 2 2 S->A: No effect on phosphorylation; when
associated with A-7 and A-10.
{ECO:0000269|PubMed:7523419}.
MUTAGEN 7 7 S->A: No effect on phosphorylation; when
associated with A-2 and A-10.
{ECO:0000269|PubMed:7523419}.
MUTAGEN 10 10 S->A: No effect on phosphorylation; when
associated with A-2 and A-7.
{ECO:0000269|PubMed:7523419}.
MUTAGEN 15 15 S->A: No effect on phosphorylation; when
associated with A-18 and A-23. Abolishes
phosphorylation; when associated with A-
18; A-34; A-47; A-49; A-51 and A-53.
{ECO:0000269|PubMed:7523419}.
MUTAGEN 18 18 S->A: No effect on phosphorylation; when
associated with A-15 and A-23. Abolishes
phosphorylation; when associated with A-
15; A-34; A-47; A-49; A-51 and A-53.
{ECO:0000269|PubMed:7523419}.
MUTAGEN 23 23 S->A: No effect on phosphorylation; when
associated with A-15 and A-18.
{ECO:0000269|PubMed:7523419}.
MUTAGEN 30 30 S->A: No effect on phosphorylation; when
associated with A-31 and A-34, or with A-
31; A-44 and A-51. Abolishes
glycosylation but does not affect binding
to YWHAE and YWHAZ; when associated with
A-31 and A-49.
{ECO:0000269|PubMed:7523419,
ECO:0000269|PubMed:7538124}.
MUTAGEN 31 31 S->A: No effect on phosphorylation; when
associated with A-30 and A-34, or with A-
30; A-44 and A-51. Abolishes
glycosylation but does not affect binding
to YWHAE and YWHAZ; when associated with
A-30 and A-49.
{ECO:0000269|PubMed:7523419,
ECO:0000269|PubMed:7538124}.
MUTAGEN 34 34 S->A: No effect on phosphorylation; when
associated with A-30 and A-31. Abolishes
phosphorylation; when associated with A-
15; A-18; A-47; A-49; A-51 and A-53.
Abolishes binding to YWHAE and YWHAZ; and
when associated with A-53.
{ECO:0000269|PubMed:7523419,
ECO:0000269|PubMed:9524113}.
MUTAGEN 34 34 S->D,E: Abolishes binding to YWHAE and
YWHAZ. {ECO:0000269|PubMed:7523419,
ECO:0000269|PubMed:9524113}.
MUTAGEN 42 42 S->A: No effect on phosphorylation; when
associated with A-44.
{ECO:0000269|PubMed:7523419}.
MUTAGEN 44 44 S->A: No effect on phosphorylation; when
associated with A-42, or with A-30; A-31
and A-51. {ECO:0000269|PubMed:7523419}.
MUTAGEN 47 47 S->A: No effect on phosphorylation; when
associated with A-49. Abolishes
phosphorylation; when associated with A-
49; A-51 and A-53, or with A-15; A-18; A-
34; A-49; A-51 and A-53.
{ECO:0000269|PubMed:7523419}.
MUTAGEN 49 49 S->A: No effect on phosphorylation; when
associated with A-47. Abolishes
phosphorylation; when associated with A-
47; A-51 and A-53, or with A-15; A-18; A-
34; A-47; A-51 and A-53. Abolishes
glycosylation but does not affect binding
to YWHAE and YWHAZ; when associated with
A-30 and A-31.
{ECO:0000269|PubMed:7523419,
ECO:0000269|PubMed:7538124}.
MUTAGEN 51 51 S->A: No effect on phosphorylation; when
associated with A-30; A-31 and A-47.
Abolishes phosphorylation; when
associated with A-47; A-49 and A-53, or
with A-15; A-18; A-34; A-47; A-49 and A-
53. {ECO:0000269|PubMed:7523419}.
MUTAGEN 53 53 S->A: Abolishes phosphorylation; when
associated with A-47; A-49 and A-51, or
with A-15; A-18; A-34; A-47; A-49 and A-
51. Abolishes binding to YWHAE and YWHAZ;
when associated with A-34. No effect on
caspase cleavage during apoptosis.
{ECO:0000269|PubMed:7523419,
ECO:0000269|PubMed:9298992,
ECO:0000269|PubMed:9524113}.
MUTAGEN 90 90 R->C,H: In transgenic mice, induces
marked disruption of liver and pancreas
keratin filament network. Increases
phosphorylation and glycosylation.
{ECO:0000269|PubMed:8522591}.
MUTAGEN 238 238 D->E: Prevents cleavage by caspase-6
during apoptosis. Induces aggregates of
keratin filaments in an altered
organization.
{ECO:0000269|PubMed:9298992}.
CONFLICT 168 168 Y -> H (in Ref. 5; AAH00698).
{ECO:0000305}.
CONFLICT 202 202 E -> Q (in Ref. 8; CAA31369).
{ECO:0000305}.
CONFLICT 208 208 E -> G (in Ref. 3; BAD96813).
{ECO:0000305}.
CONFLICT 246 246 A -> S (in Ref. 8; CAA31369).
{ECO:0000305}.
CONFLICT 309 309 D -> R (in Ref. 8; CAA31369).
{ECO:0000305}.
CONFLICT 312 312 S -> R (in Ref. 8; CAA31369).
{ECO:0000305}.
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


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20-272-192053 Cytokeratin 18 - Mouse monoclonal [C - 04] to Cytokeratin 18; Cytokeratin-18; CK-18; Keratin-18; K18; Cell proliferation-inducing gene 46 protein Monoclonal 0.1 mg


 

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