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Keratin, type I cytoskeletal 17 (39.1) (Cytokeratin-17) (CK-17) (Keratin-17) (K17)

 K1C17_HUMAN             Reviewed;         432 AA.
Q04695; A5Z1M9; A5Z1N0; A5Z1N1; A5Z1N2; A6NDV6; A6NKQ2; Q6IP98;
Q8N1P6;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
25-OCT-2017, entry version 180.
RecName: Full=Keratin, type I cytoskeletal 17;
AltName: Full=39.1;
AltName: Full=Cytokeratin-17;
Short=CK-17;
AltName: Full=Keratin-17;
Short=K17;
Name=KRT17;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
PubMed=1281771;
Troyanovsky S.M., Leube R.E., Franke W.W.;
"Characterization of the human gene encoding cytokeratin 17 and its
expression pattern.";
Eur. J. Cell Biol. 59:127-137(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
PubMed=1372562; DOI=10.1002/eji.1830220415;
Flohr T., Buwitt U., Bonnekoh B., Decker T., Boettger E.C.;
"Interferon-gamma regulates expression of a novel keratin class I
gene.";
Eur. J. Immunol. 22:975-979(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PC2
ASP-109.
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, Cervix, and Muscle;
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 [MRNA] OF 85-101, AND VARIANT PC2 ASP-92.
PubMed=7539673; DOI=10.1038/ng0395-273;
McLean W.H.I., Rugg E.L., Lunny D.P., Morley S.M., Lane E.B.,
Swensson O., Dopping-Hepenstal P.J.C., Griffiths W.A.D., Eady R.A.J.,
Higgins C., Navsaria H.A., Leigh I.M., Strachan T., Kunkeler L.,
Munro C.S.;
"Keratin 16 and keratin 17 mutations cause pachyonychia congenita.";
Nat. Genet. 9:273-278(1995).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 101-117; 152-168; 306-322 AND 331-347.
Shen Z., Chen L., Wang G., Liu Y.-F.;
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
[8]
TISSUE SPECIFICITY.
PubMed=2481679;
Troyanovsky S.M., Guelstein V.I., Tchipysheva T.A., Krutovskikh V.A.,
Bannikov G.A.;
"Patterns of expression of keratin 17 in human epithelia: dependency
on cell position.";
J. Cell Sci. 93:419-426(1989).
[9]
TISSUE SPECIFICITY.
PubMed=10651700; DOI=10.1046/j.1365-2133.2000.03246.x;
De Berker D., Wojnarowska F., Sviland L., Westgate G.E., Dawber R.P.,
Leigh I.M.;
"Keratin expression in the normal nail unit: markers of regional
differentiation.";
Br. J. Dermatol. 142:89-96(2000).
[10]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=10844551; DOI=10.1046/j.1523-1747.2000.00986.x;
McGowan K.M., Coulombe P.A.;
"Keratin 17 expression in the hard epithelial context of the hair and
nail, and its relevance for the pachyonychia congenita phenotype.";
J. Invest. Dermatol. 114:1101-1107(2000).
[11]
FUNCTION, AND INDUCTION.
PubMed=15795121; DOI=10.1016/j.jdermsci.2005.01.001;
Shen Z., Wang G., Fan J.-Y., Li W., Liu Y.-F.;
"HLA DR B1*04, *07-restricted epitopes on Keratin 17 for autoreactive
T cells in psoriasis.";
J. Dermatol. Sci. 38:25-39(2005).
[12]
INDUCTION.
PubMed=15608502; DOI=10.1159/000081685;
Bockelmann R., Horn T., Gollnick H., Bonnekoh B.;
"Interferon-gamma-dependent in vitro model for the putative keratin 17
autoimmune loop in psoriasis: exploration of pharmaco- and gene-
therapeutic effects.";
Skin Pharmacol. Physiol. 18:42-54(2005).
[13]
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).
[14]
FUNCTION, INDUCTION, AND MUTAGENESIS OF ARG-103; GLU-106; ASN-109;
ASN-154; ILE-155; LEU-157; ASP-160; ASN-333; ARG-334; CYS-336 AND
LEU-339.
PubMed=16713453; DOI=10.1016/j.jaad.2006.02.033;
Shen Z., Chen L., Liu Y.-F., Gao T.-W., Wang G., Fan X.-L., Fan J.-Y.,
Fan P.-S., Li C.-Y., Liu B., Dang Y.-P., Li C.-X.;
"Altered keratin 17 peptide ligands inhibit in vitro proliferation of
keratinocytes and T cells isolated from patients with psoriasis.";
J. Am. Acad. Dermatol. 54:992-1002(2006).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, 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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-32 AND SER-39,
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).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, 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).
[18]
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).
[19]
PHOSPHORYLATION AT SER-44.
PubMed=22006917; DOI=10.1074/jbc.M111.302042;
Pan X., Kane L.A., Van Eyk J.E., Coulombe P.A.;
"Type I keratin 17 protein is phosphorylated on serine 44 by p90
ribosomal protein S6 kinase 1 (RSK1) in a growth- and stress-dependent
fashion.";
J. Biol. Chem. 286:42403-42413(2011).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-13; SER-32;
SER-39; THR-110 AND SER-323, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
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).
[21]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-15; LYS-399 AND LYS-419, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[22]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-15; LYS-399; LYS-400 AND
LYS-419, 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).
[23]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-15 AND LYS-399, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[24]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-15; LYS-278; LYS-399;
LYS-400 AND LYS-419, 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).
[25]
VARIANTS PC2 SER-92 AND ASP-98, AND VARIANTS SM HIS-92 AND HIS-94.
PubMed=9008238; DOI=10.1111/1523-1747.ep12335315;
Smith F.J.D., Corden L.D., Rugg E.L., Ratnavel R., Leigh I.M.,
Moss C., Tidman M.J., Hohl D., Huber M., Kunkeler L., Munro C.S.,
Lane E.B., McLean W.H.I.;
"Missense mutations in keratin 17 cause either pachyonychia congenita
type 2 or a phenotype resembling steatocystoma multiplex.";
J. Invest. Dermatol. 108:220-223(1997).
[26]
VARIANTS PC2 SER-92 AND CYS-94, AND VARIANT SM CYS-94.
PubMed=9767294; DOI=10.1046/j.1365-2133.1998.02413.x;
Covello S.P., Smith F.J.D., Sillevis Smitt J.H., Paller A.S.,
Munro C.S., Jonkman M.F., Uitto J., McLean W.H.I.;
"Keratin 17 mutations cause either steatocystoma multiplex or
pachyonychia congenita type 2.";
Br. J. Dermatol. 139:475-480(1998).
[27]
VARIANT PC2 THR-88.
PubMed=10571744; DOI=10.1046/j.1523-1747.1999.00762.x;
Celebi J.T., Tanzi E.L., Yao Y.J., Michael E.J., Peacocke M.;
"Mutation report: identification of a germline mutation in keratin 17
in a family with pachyonychia congenita type 2.";
J. Invest. Dermatol. 113:848-850(1999).
[28]
VARIANTS PC2 94-PRO--TYR-98 DEL; PRO-94 AND GLN-95.
PubMed=11348474; DOI=10.1046/j.1523-1747.2001.01335.x;
Smith F.J.D., Coleman C.M., Bayoumy N.M., Tenconi R., Nelson J.,
David A., McLean W.H.I.;
"Novel keratin 17 mutations in pachyonychia congenita type 2.";
J. Invest. Dermatol. 116:806-808(2001).
[29]
VARIANTS PC2 PRO-95; SER-97 DEL AND PRO-99.
PubMed=11886499; DOI=10.1046/j.0022-202x.2001.01565.x;
Terrinoni A., Smith F.J.D., Didona B., Canzona F., Paradisi M.,
Huber M., Hohl D., David A., Verloes A., Leigh I.M., Munro C.S.,
Melino G., McLean W.H.I.;
"Novel and recurrent mutations in the genes encoding keratins K6a, K16
and K17 in 13 cases of pachyonychia congenita.";
J. Invest. Dermatol. 117:1391-1396(2001).
[30]
VARIANT PC2 MET-102.
PubMed=11874497; DOI=10.1046/j.0022-202x.2001.01701.x;
Hashiguchi T., Yotsumoto S., Shimada H., Terasaki K., Setoyama M.,
Kobayashi K., Saheki T., Kanzaki T.;
"A novel point mutation in the keratin 17 gene in a Japanese case of
pachyonychia congenita type 2.";
J. Invest. Dermatol. 118:545-547(2002).
[31]
VARIANT PC2 ASP-109.
PubMed=15102078; DOI=10.1111/j.0022-202X.2004.22408.x;
Xiao S.-X., Feng Y.-G., Ren X.-R., Tan S.-S., Li L., Wang J.-M.,
Shi Y.-Z.;
"A novel mutation in the second half of the keratin 17 1A domain in a
large pedigree with delayed-onset pachyonychia congenita type 2.";
J. Invest. Dermatol. 122:892-895(2004).
[32]
VARIANT PC2 MET-102.
PubMed=15795125; DOI=10.1016/j.jdermsci.2004.12.022;
Uchida T., Inaoki M., Makino E., Fujimoto W.;
"Identification of a recurrent mutation in keratin 17 in a Japanese
family with pachyonychia congenita type 2.";
J. Dermatol. Sci. 38:60-63(2005).
[33]
VARIANTS PC2 SER-92 AND PRO-388.
PubMed=16250206; DOI=10.1111/j.1087-0024.2005.10204.x;
Smith F.J., Liao H., Cassidy A.J., Stewart A., Hamill K.J., Wood P.,
Joval I., van Steensel M.A., Bjoerck E., Callif-Daley F., Pals G.,
Collins P., Leachman S.A., Munro C.S., McLean W.H.;
"The genetic basis of pachyonychia congenita.";
J. Investig. Dermatol. Symp. Proc. 10:21-30(2005).
[34]
VARIANT PC2 THR-88, AND VARIANT SM THR-88.
PubMed=16620218; DOI=10.1111/j.1346-8138.2006.00037.x;
Oh S.-W., Kim M.Y., Lee J.S., Kim S.-C.;
"Keratin 17 mutation in pachyonychia congenita type 2 patient with
early onset steatocystoma multiplex and Hutchinson-like tooth
deformity.";
J. Dermatol. 33:161-164(2006).
[35]
VARIANT PC2 SER-92.
PubMed=17719747; DOI=10.1016/j.jdermsci.2007.07.003;
Liao H., Sayers J.M., Wilson N.J., Irvine A.D., Mellerio J.E.,
Baselga E., Bayliss S.J., Uliana V., Fimiani M., Lane E.B.,
McLean W.H., Leachman S.A., Smith F.J.;
"A spectrum of mutations in keratins K6a, K16 and K17 causing
pachyonychia congenita.";
J. Dermatol. Sci. 48:199-205(2007).
[36]
VARIANT PC2 LYS-88.
PubMed=18547302; DOI=10.1111/j.1365-2133.2008.08684.x;
Tsuda T., Ishikawa C., Nakagawa N., Konishi H., Tarutani M.,
Matsuki M., Yamanishi K.;
"A novel point mutation of keratin 17 (KRT17) in a Japanese family
with pachyonychia congenita type 2: an RNA-based genetic analysis
using a single hair bulb.";
Br. J. Dermatol. 159:730-732(2008).
[37]
VARIANTS PC2 SER-92 AND HIS-94.
PubMed=19470054; DOI=10.1111/j.1468-3083.2009.03180.x;
Wang J.F., Lu W.S., Sun L.D., Lv Y.M., Zhou F.S., Fang Q.Y.,
Tang H.Y., Cui Y., Yang S., Zhang X.J.;
"Novel missense mutation of keratin in Chinese family with
steatocystoma multiplex.";
J. Eur. Acad. Dermatol. Venereol. 23:723-724(2009).
[38]
VARIANTS PC2 92-ASN--LEU-99 DEL AND SER-92.
PubMed=21326300; DOI=10.1038/jid.2011.20;
Wilson N.J., Leachman S.A., Hansen C.D., McMullan A.C., Milstone L.M.,
Schwartz M.E., McLean W.H., Hull P.R., Smith F.J.;
"A large mutational study in pachyonychia congenita.";
J. Invest. Dermatol. 131:1018-1024(2011).
[39]
VARIANT PC2 ARG-388.
PubMed=23278621; DOI=10.1111/j.1365-4632.2010.04667.x;
Qiang W., Kaibo W., Tienan L., Guilan Z., Yueyang L., Ting X.,
Fangji S.;
"A novel mutation of keratin 17 gene in a pedigree with pachyonychia
congenita type 2.";
Int. J. Dermatol. 52:117-119(2013).
[40]
VARIANT PC2 PRO-91.
PubMed=23855588; DOI=10.1111/1346-8138.12212;
Ichimiya M., Yamaguchi M., Nemoto K., Muto M.;
"Novel mutation (p.L91P, c.272T>C) of keratin 17 in a case with
pachyonychia congenita type 2.";
J. Dermatol. 40:757-758(2013).
-!- FUNCTION: Type I keratin involved in the formation and maintenance
of various skin appendages, specifically in determining shape and
orientation of hair (By similarity). Required for the correct
growth of hair follicles, in particular for the persistence of the
anagen (growth) state (By similarity). Modulates the function of
TNF-alpha in the specific context of hair cycling. Regulates
protein synthesis and epithelial cell growth through binding to
the adapter protein SFN and by stimulating Akt/mTOR pathway (By
similarity). Involved in tissue repair. May be a marker of basal
cell differentiation in complex epithelia and therefore indicative
of a certain type of epithelial "stem cells". Acts as a promoter
of epithelial proliferation by acting a regulator of immune
response in skin: promotes Th1/Th17-dominated immune environment
contributing to the development of basaloid skin tumors (By
similarity). May act as an autoantigen in the immunopathogenesis
of psoriasis, with certain peptide regions being a major target
for autoreactive T-cells and hence causing their proliferation.
{ECO:0000250|UniProtKB:Q9QWL7, ECO:0000269|PubMed:10844551,
ECO:0000269|PubMed:15795121, ECO:0000269|PubMed:16713453}.
-!- SUBUNIT: Heterodimer of a type I and a type II keratin. KRT17
associates with KRT6 isomers (KRT6A or KRT6B). Interacts with
TRADD and SFN (By similarity). {ECO:0000250}.
-!- INTERACTION:
Q15834:CCDC85B; NbExp=2; IntAct=EBI-297873, EBI-739674;
P26641:EEF1G; NbExp=2; IntAct=EBI-297873, EBI-351467;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9QWL7}.
-!- TISSUE SPECIFICITY: Expressed in the outer root sheath and medulla
region of hair follicle specifically from eyebrow and beard,
digital pulp, nail matrix and nail bed epithelium, mucosal
stratified squamous epithelia and in basal cells of oral
epithelium, palmoplantar epidermis and sweat and mammary glands.
Also expressed in myoepithelium of prostate, basal layer of
urinary bladder, cambial cells of sebaceous gland and in exocervix
(at protein level). {ECO:0000269|PubMed:10651700,
ECO:0000269|PubMed:10844551, ECO:0000269|PubMed:1281771,
ECO:0000269|PubMed:2481679}.
-!- INDUCTION: Induced in damaged or stressed epidermis. Induced by
the cytokines interferon-gamma (IFN-gamma), tumor necrosis factor
alpha (TNF-alpha) and transforming growth factor-alpha (TGF-
alpha), and by the potent NF-kappa B inhibitor compounds Bay 11-
7082 and Bay 11-7085. Down-regulated by the drug Imatinib.
{ECO:0000269|PubMed:1372562, ECO:0000269|PubMed:15608502,
ECO:0000269|PubMed:15795121, ECO:0000269|PubMed:16713453}.
-!- PTM: Phosphorylation at Ser-44 occurs in a growth- and stress-
dependent fashion in skin keratinocytes, it has no effect on
filament organization. {ECO:0000269|PubMed:22006917}.
-!- DISEASE: Pachyonychia congenita 2 (PC2) [MIM:167210]: An autosomal
dominant ectodermal dysplasia characterized by hypertrophic nail
dystrophy resulting in onchyogryposis (thickening and increase in
curvature of the nail), palmoplantar keratoderma and
hyperhidrosis, follicular hyperkeratosis, multiple epidermal
cysts, absent/sparse eyebrow and body hair, and by the presence of
natal teeth. {ECO:0000269|PubMed:10571744,
ECO:0000269|PubMed:11348474, ECO:0000269|PubMed:11874497,
ECO:0000269|PubMed:11886499, ECO:0000269|PubMed:15102078,
ECO:0000269|PubMed:15795125, ECO:0000269|PubMed:16250206,
ECO:0000269|PubMed:16620218, ECO:0000269|PubMed:16625196,
ECO:0000269|PubMed:17719747, ECO:0000269|PubMed:18547302,
ECO:0000269|PubMed:19470054, ECO:0000269|PubMed:21326300,
ECO:0000269|PubMed:23278621, ECO:0000269|PubMed:23855588,
ECO:0000269|PubMed:7539673, ECO:0000269|PubMed:9008238,
ECO:0000269|PubMed:9767294}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Steatocystoma multiplex (SM) [MIM:184500]: Disease
characterized by round or oval cystic tumors widely distributed on
the back, anterior trunk, arms, scrotum, and thighs.
{ECO:0000269|PubMed:16620218, ECO:0000269|PubMed:9008238,
ECO:0000269|PubMed:9767294}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Note=KRT16 and KRT17 are coexpressed only in pathological
situations such as metaplasias and carcinomas of the uterine
cervix and in psoriasis vulgaris.
-!- 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}.
-!- SEQUENCE CAUTION:
Sequence=AAH72018.1; Type=Frameshift; Positions=109; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Human Intermediate Filament Mutation Database;
URL="http://www.interfil.org";
-!- WEB RESOURCE: Name=Wikipedia; Note=Keratin-17 entry;
URL="https://en.wikipedia.org/wiki/Keratin_17";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; Z19574; CAA79626.1; -; Genomic_DNA.
EMBL; X62571; CAA44451.1; -; mRNA.
EMBL; AK095342; BAC04534.1; -; mRNA.
EMBL; AC022596; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL353997; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC000159; AAH00159.2; -; mRNA.
EMBL; BC011901; AAH11901.1; -; mRNA.
EMBL; BC056421; AAH56421.1; -; mRNA.
EMBL; BC072018; AAH72018.1; ALT_FRAME; mRNA.
EMBL; BC072019; AAH72019.1; -; mRNA.
EMBL; S78515; AAB34565.1; -; Genomic_DNA.
EMBL; EF608068; ABQ96595.1; -; mRNA.
EMBL; EF608069; ABQ96596.1; -; mRNA.
EMBL; EF608070; ABQ96597.1; -; mRNA.
EMBL; EF608071; ABQ96598.1; -; mRNA.
CCDS; CCDS11402.1; -.
PIR; S30433; S30433.
RefSeq; NP_000413.1; NM_000422.2.
UniGene; Hs.2785; -.
ProteinModelPortal; Q04695; -.
SMR; Q04695; -.
BioGrid; 110070; 36.
DIP; DIP-33093N; -.
IntAct; Q04695; 16.
MINT; MINT-256746; -.
STRING; 9606.ENSP00000308452; -.
iPTMnet; Q04695; -.
PhosphoSitePlus; Q04695; -.
SwissPalm; Q04695; -.
BioMuta; KRT17; -.
DMDM; 547751; -.
SWISS-2DPAGE; Q04695; -.
EPD; Q04695; -.
PaxDb; Q04695; -.
PeptideAtlas; Q04695; -.
PRIDE; Q04695; -.
TopDownProteomics; Q04695; -.
DNASU; 3872; -.
Ensembl; ENST00000311208; ENSP00000308452; ENSG00000128422.
GeneID; 3872; -.
KEGG; hsa:3872; -.
UCSC; uc002hxh.3; human.
CTD; 3872; -.
DisGeNET; 3872; -.
EuPathDB; HostDB:ENSG00000128422.15; -.
GeneCards; KRT17; -.
GeneReviews; KRT17; -.
H-InvDB; HIX0059686; -.
HGNC; HGNC:6427; KRT17.
HPA; CAB000029; -.
HPA; HPA000452; -.
HPA; HPA000453; -.
HPA; HPA000539; -.
HPA; HPA045062; -.
MalaCards; KRT17; -.
MIM; 148069; gene.
MIM; 167210; phenotype.
MIM; 184500; phenotype.
neXtProt; NX_Q04695; -.
OpenTargets; ENSG00000128422; -.
Orphanet; 2309; Pachyonychia congenita.
Orphanet; 841; Sebocystomatosis.
PharmGKB; PA30214; -.
eggNOG; ENOG410IFTF; Eukaryota.
eggNOG; ENOG410Y9IV; LUCA.
GeneTree; ENSGT00900000140820; -.
HOVERGEN; HBG013015; -.
InParanoid; Q04695; -.
KO; K07604; -.
OMA; QYHRTIE; -.
OrthoDB; EOG091G087I; -.
PhylomeDB; Q04695; -.
TreeFam; TF332742; -.
Reactome; R-HSA-6805567; Keratinization.
Reactome; R-HSA-6809371; Formation of the cornified envelope.
GeneWiki; Keratin_17; -.
GenomeRNAi; 3872; -.
PMAP-CutDB; Q04695; -.
PRO; PR:Q04695; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000128422; -.
ExpressionAtlas; Q04695; baseline and differential.
Genevisible; Q04695; HS.
GO; GO:0071944; C:cell periphery; IEA:Ensembl.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005882; C:intermediate filament; TAS:ProtInc.
GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
GO; GO:0042289; F:MHC class II protein binding; IPI:UniProtKB.
GO; GO:0032395; F:MHC class II receptor activity; IDA:UniProtKB.
GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
GO; GO:0070268; P:cornification; TAS:Reactome.
GO; GO:0008544; P:epidermis development; TAS:ProtInc.
GO; GO:0031069; P:hair follicle morphogenesis; ISS:UniProtKB.
GO; GO:0045109; P:intermediate filament organization; IEA:Ensembl.
GO; GO:0031424; P:keratinization; TAS:Reactome.
GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
GO; GO:0051798; P:positive regulation of hair follicle development; IEA:Ensembl.
GO; GO:0045727; P:positive regulation of translation; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; IMP:UniProtKB.
InterPro; IPR001664; IF.
InterPro; IPR018039; Intermediate_filament_CS.
InterPro; IPR002957; Keratin_I.
PANTHER; PTHR23239; PTHR23239; 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;
Coiled coil; Complete proteome; Cytoplasm; Disease mutation;
Ectodermal dysplasia; Intermediate filament; Isopeptide bond; Keratin;
Methylation; Palmoplantar keratoderma; Phosphoprotein;
Reference proteome; Ubl conjugation.
CHAIN 1 432 Keratin, type I cytoskeletal 17.
/FTId=PRO_0000063664.
DOMAIN 84 395 IF rod. {ECO:0000255|PROSITE-
ProRule:PRU01188}.
REGION 1 83 Head.
REGION 84 120 Coil 1A.
REGION 102 116 Peptide epitope S1; induces T-cell and
keratinocyte proliferation and IFN-gamma
production.
REGION 121 138 Linker 1.
REGION 139 230 Coil 1B.
REGION 153 167 Peptide epitope S2; induces T-cell
proliferation and IFN-gamma production.
REGION 231 250 Linker 12.
REGION 251 392 Coil 2.
REGION 332 346 Peptide epitope S4; induces T-cell and
keratinocyte proliferation and IFN-gamma
production.
REGION 393 432 Tail.
MOD_RES 12 12 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 13 13 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 26 26 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P19001}.
MOD_RES 32 32 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 39 39 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 44 44 Phosphoserine; by RPS6KA1.
{ECO:0000269|PubMed:22006917}.
MOD_RES 72 72 Phosphoserine.
{ECO:0000250|UniProtKB:P19001}.
MOD_RES 110 110 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 323 323 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 15 15 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
CROSSLNK 15 15 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 278 278 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 399 399 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
CROSSLNK 399 399 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 400 400 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
CROSSLNK 400 400 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 419 419 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
CROSSLNK 419 419 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
VARIANT 88 88 M -> K (in PC2; dbSNP:rs28928898).
{ECO:0000269|PubMed:18547302}.
/FTId=VAR_072441.
VARIANT 88 88 M -> T (in PC2 and SM; dbSNP:rs28928898).
{ECO:0000269|PubMed:10571744,
ECO:0000269|PubMed:16620218}.
/FTId=VAR_010512.
VARIANT 91 91 L -> P (in PC2).
{ECO:0000269|PubMed:23855588}.
/FTId=VAR_072442.
VARIANT 92 99 Missing (in PC2).
{ECO:0000269|PubMed:21326300}.
/FTId=VAR_072443.
VARIANT 92 92 N -> D (in PC2; dbSNP:rs28928896).
{ECO:0000269|PubMed:7539673}.
/FTId=VAR_003847.
VARIANT 92 92 N -> H (in SM; dbSNP:rs28928896).
{ECO:0000269|PubMed:9008238}.
/FTId=VAR_003848.
VARIANT 92 92 N -> S (in PC2; dbSNP:rs59151893).
{ECO:0000269|PubMed:16250206,
ECO:0000269|PubMed:17719747,
ECO:0000269|PubMed:19470054,
ECO:0000269|PubMed:21326300,
ECO:0000269|PubMed:9008238,
ECO:0000269|PubMed:9767294}.
/FTId=VAR_003849.
VARIANT 94 98 Missing (in PC2).
/FTId=VAR_017069.
VARIANT 94 94 R -> C (in PC2 and SM; dbSNP:rs58730926).
{ECO:0000269|PubMed:9767294}.
/FTId=VAR_010513.
VARIANT 94 94 R -> H (in SM AND PC2; dbSNP:rs28928897).
{ECO:0000269|PubMed:19470054,
ECO:0000269|PubMed:9008238}.
/FTId=VAR_003850.
VARIANT 94 94 R -> P (in PC2; dbSNP:rs28928897).
{ECO:0000269|PubMed:11348474}.
/FTId=VAR_017068.
VARIANT 95 95 L -> P (in PC2; dbSNP:rs28928899).
{ECO:0000269|PubMed:11886499}.
/FTId=VAR_017071.
VARIANT 95 95 L -> Q (in PC2; dbSNP:rs28928899).
{ECO:0000269|PubMed:11348474}.
/FTId=VAR_017070.
VARIANT 97 97 Missing (in PC2).
{ECO:0000269|PubMed:11886499}.
/FTId=VAR_017072.
VARIANT 98 98 Y -> D (in PC2; dbSNP:rs28933088).
{ECO:0000269|PubMed:9008238}.
/FTId=VAR_003851.
VARIANT 99 99 L -> P (in PC2; dbSNP:rs28933089).
{ECO:0000269|PubMed:11886499}.
/FTId=VAR_017073.
VARIANT 102 102 V -> M (in PC2; dbSNP:rs59977263).
{ECO:0000269|PubMed:11874497,
ECO:0000269|PubMed:15795125}.
/FTId=VAR_017074.
VARIANT 109 109 N -> D (in PC2; dbSNP:rs267607412).
{ECO:0000269|PubMed:15102078,
ECO:0000269|PubMed:16625196}.
/FTId=VAR_037083.
VARIANT 388 388 L -> P (in PC2; dbSNP:rs56690581).
{ECO:0000269|PubMed:16250206}.
/FTId=VAR_072444.
VARIANT 388 388 L -> R (in PC2).
{ECO:0000269|PubMed:23278621}.
/FTId=VAR_072445.
MUTAGEN 103 103 R->A: Down-regulates both proliferation
of psoriatic T-cells and IFN-gamma
production; suppresses keratinocyte
growth when part of the altered peptide
epitope S1.
{ECO:0000269|PubMed:16713453}.
MUTAGEN 106 106 E->A: Down-regulates proliferation of
psoriatic T-cells and IFN-gamma
production when part of the altered
peptide epitope S1.
{ECO:0000269|PubMed:16713453}.
MUTAGEN 109 109 N->A: No significant effect on T-cell
proliferation or IFN-gamma production
when part of the altered peptide epitope
S1. {ECO:0000269|PubMed:16713453}.
MUTAGEN 154 154 N->A: No significant effect on T-cell
proliferation but reduces IFN-gamma
production when part of the altered
peptide epitope S2.
{ECO:0000269|PubMed:16713453}.
MUTAGEN 155 155 I->A: No significant effect on T-cell
proliferation but reduces IFN-gamma
production when part of the altered
peptide epitope S2.
{ECO:0000269|PubMed:16713453}.
MUTAGEN 157 157 L->A: Down-regulates proliferation of
psoriatic T-cells and IFN-gamma
production when part of the altered
peptide epitope S2.
{ECO:0000269|PubMed:16713453}.
MUTAGEN 160 160 D->A: No significant effect on T-cell
proliferation but reduces IFN-gamma
production when part of the altered
peptide epitope S4.
{ECO:0000269|PubMed:16713453}.
MUTAGEN 333 333 N->A: No significant effect on T-cell
proliferation but reduces IFN-gamma
production when part of the altered
peptide epitope S4.
{ECO:0000269|PubMed:16713453}.
MUTAGEN 334 334 R->A: No significant effect on T-cell
proliferation but can induce IFN-gamma
production when part of the altered
peptide epitope S2.
{ECO:0000269|PubMed:16713453}.
MUTAGEN 336 336 C->A: No significant effect on T-cell
proliferation but reduces IFN-gamma
production when part of the altered
peptide epitope S2.
{ECO:0000269|PubMed:16713453}.
MUTAGEN 339 339 L->A: Down-regulates both proliferation
of psoriatic T-cells and IFN-gamma
production; suppresses keratinocyte
growth when part of the altered peptide
epitope S4.
{ECO:0000269|PubMed:16713453}.
CONFLICT 30 30 R -> Q (in Ref. 4; AL353997/AC022596).
{ECO:0000305}.
CONFLICT 42 42 L -> P (in Ref. 4; AL353997/AC022596).
{ECO:0000305}.
CONFLICT 51 56 Missing (in Ref. 3; BAC04534).
{ECO:0000305}.
CONFLICT 51 51 T -> A (in Ref. 4; AL353997/AC022596).
{ECO:0000305}.
CONFLICT 72 72 S -> SS (in Ref. 4; AL353997).
{ECO:0000305}.
CONFLICT 73 74 FG -> SFE (in Ref. 4; AC022596).
{ECO:0000305}.
CONFLICT 74 74 G -> E (in Ref. 4; AL353997).
{ECO:0000305}.
CONFLICT 81 81 A -> V (in Ref. 4; AL353997/AC022596).
{ECO:0000305}.
CONFLICT 94 108 Missing (in Ref. 5; AAH72018).
{ECO:0000305}.
CONFLICT 137 137 T -> I (in Ref. 4; AL353997/AC022596).
{ECO:0000305}.
CONFLICT 145 147 ILT -> VGPA (in Ref. 4; AL353997).
{ECO:0000305}.
CONFLICT 158 158 Q -> H (in Ref. 4; AC022596).
{ECO:0000305}.
CONFLICT 159 159 I -> N (in Ref. 4; AL353997).
{ECO:0000305}.
CONFLICT 163 163 R -> H (in Ref. 4; AL353997/AC022596).
{ECO:0000305}.
CONFLICT 167 167 D -> A (in Ref. 4; AL353997/AC022596).
{ECO:0000305}.
CONFLICT 180 180 R -> C (in Ref. 4; AL353997/AC022596).
{ECO:0000305}.
CONFLICT 190 191 LR -> PC (in Ref. 4; AL353997/AC022596).
{ECO:0000305}.
CONFLICT 204 204 L -> P (in Ref. 4; AL353997).
{ECO:0000305}.
CONFLICT 207 207 Q -> H (in Ref. 4; AL353997/AC022596).
{ECO:0000305}.
CONFLICT 225 225 Missing (in Ref. 4; AL353997/AC022596).
{ECO:0000305}.
CONFLICT 229 229 L -> P (in Ref. 4; AL353997/AC022596).
{ECO:0000305}.
CONFLICT 242 242 D -> G (in Ref. 4; AL353997/AC022596).
{ECO:0000305}.
CONFLICT 258 258 D -> E (in Ref. 4; AL353997/AC022596).
{ECO:0000305}.
CONFLICT 305 305 R -> C (in Ref. 4; AL353997/AC022596).
{ECO:0000305}.
CONFLICT 337 337 V -> M (in Ref. 4; AL353997/AC022596).
{ECO:0000305}.
CONFLICT 352 352 Q -> R (in Ref. 4; AL353997/AC022596).
{ECO:0000305}.
CONFLICT 357 357 R -> L (in Ref. 4; AL353997/AC022596).
{ECO:0000305}.
CONFLICT 373 375 VKT -> MKM (in Ref. 4; AL353997/
AC022596). {ECO:0000305}.
CONFLICT 379 379 Q -> L (in Ref. 4; AL353997/AC022596).
{ECO:0000305}.
CONFLICT 382 382 A -> T (in Ref. 4; AL353997/AC022596).
{ECO:0000305}.
CONFLICT 385 385 R -> H (in Ref. 4; AL353997/AC022596).
{ECO:0000305}.
CONFLICT 395 404 LTQYKKEPVT -> FRMSESSPVS (in Ref. 4;
AC022596). {ECO:0000305}.
CONFLICT 406 406 R -> C (in Ref. 4; AL353997).
{ECO:0000305}.
CONFLICT 409 409 R -> P (in Ref. 4; AL353997).
{ECO:0000305}.
CONFLICT 428 428 H -> R (in Ref. 4; AL353997).
{ECO:0000305}.
SEQUENCE 432 AA; 48106 MW; 35B429243F47EB5C CRC64;
MTTSIRQFTS SSSIKGSSGL GGGSSRTSCR LSGGLGAGSC RLGSAGGLGS TLGGSSYSSC
YSFGSGGGYG SSFGGVDGLL AGGEKATMQN LNDRLASYLD KVRALEEANT ELEVKIRDWY
QRQAPGPARD YSQYYRTIEE LQNKILTATV DNANILLQID NARLAADDFR TKFETEQALR
LSVEADINGL RRVLDELTLA RADLEMQIEN LKEELAYLKK NHEEEMNALR GQVGGEINVE
MDAAPGVDLS RILNEMRDQY EKMAEKNRKD AEDWFFSKTE ELNREVATNS ELVQSGKSEI
SELRRTMQAL EIELQSQLSM KASLEGNLAE TENRYCVQLS QIQGLIGSVE EQLAQLRCEM
EQQNQEYKIL LDVKTRLEQE IATYRRLLEG EDAHLTQYKK EPVTTRQVRT IVEEVQDGKV
ISSREQVHQT TR


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E1427m ELISA kit CK-2e,Cytokeratin-2e,Epithelial keratin-2e,K2e,K2e,Keratin, type II cytoskeletal 2 epidermal,Keratin-2 epidermis,Keratin-2e,Krt2,Krt2-17,Krt2a,Mouse,Mus musculus,Type-II keratin Kb2 96T
E2288m 56 kDa cytokeratin,CK-10,Cytokeratin-10,K10,Keratin, type I cytoskeletal 10,Keratin, type I cytoskeletal 59 kDa,Keratin-10,Krt10,Krt1-10,Mouse,Mus musculus
U1231m CLIA CK-18,Cytokeratin endo B,Cytokeratin-18,K18,Keratin D,Keratin, type I cytoskeletal 18,Keratin-18,Kerd,Krt1-18,Krt18,Mouse,Mus musculus 96T
E1231m ELISA kit CK-18,Cytokeratin endo B,Cytokeratin-18,K18,Keratin D,Keratin, type I cytoskeletal 18,Keratin-18,Kerd,Krt1-18,Krt18,Mouse,Mus musculus 96T
E1231m ELISA CK-18,Cytokeratin endo B,Cytokeratin-18,K18,Keratin D,Keratin, type I cytoskeletal 18,Keratin-18,Kerd,Krt1-18,Krt18,Mouse,Mus musculus 96T
E2282h ELISA kit 67 kDa cytokeratin,CK-1,Cytokeratin-1,Hair alpha protein,Homo sapiens,Human,K1,Keratin, type II cytoskeletal 1,Keratin-1,KRT1,KRTA,Type-II keratin Kb1 96T
E2282h ELISA 67 kDa cytokeratin,CK-1,Cytokeratin-1,Hair alpha protein,Homo sapiens,Human,K1,Keratin, type II cytoskeletal 1,Keratin-1,KRT1,KRTA,Type-II keratin Kb1 96T
U2282h CLIA kit 67 kDa cytokeratin,CK-1,Cytokeratin-1,Hair alpha protein,Homo sapiens,Human,K1,Keratin, type II cytoskeletal 1,Keratin-1,KRT1,KRTA,Type-II keratin Kb1 96T
U2282h CLIA 67 kDa cytokeratin,CK-1,Cytokeratin-1,Hair alpha protein,Homo sapiens,Human,K1,Keratin, type II cytoskeletal 1,Keratin-1,KRT1,KRTA,Type-II keratin Kb1 96T
E2282h 67 kDa cytokeratin,CK-1,Cytokeratin-1,Hair alpha protein,Homo sapiens,Human,K1,Keratin, type II cytoskeletal 1,Keratin-1,KRT1,KRTA,Type-II keratin Kb1
E2287m ELISA CK-8,Cytokeratin endo A,Cytokeratin-8,K8,Keratin, type II cytoskeletal 8,Keratin-8,Krt2-8,Krt8,Mouse,Mus musculus,Type-II keratin Kb8 96T
U2287r CLIA kit CK-8,Cytokeratin endo A,Cytokeratin-8,K8,Keratin, type II cytoskeletal 8,Keratin-8,Krt2-8,Krt8,Rat,Rattus norvegicus,Type-II keratin Kb8 96T
E2287r ELISA CK-8,Cytokeratin endo A,Cytokeratin-8,K8,Keratin, type II cytoskeletal 8,Keratin-8,Krt2-8,Krt8,Rat,Rattus norvegicus,Type-II keratin Kb8 96T


 

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