K1C17_HUMAN
ID K1C17_HUMAN Reviewed; 432 AA.
AC Q04695; A5Z1M9; A5Z1N0; A5Z1N1; A5Z1N2; A6NDV6; A6NKQ2; Q6IP98; Q8N1P6;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Keratin, type I cytoskeletal 17;
DE AltName: Full=39.1;
DE AltName: Full=Cytokeratin-17;
DE Short=CK-17;
DE AltName: Full=Keratin-17;
DE Short=K17;
GN Name=KRT17;
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 [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=1281771;
RA Troyanovsky S.M., Leube R.E., Franke W.W.;
RT "Characterization of the human gene encoding cytokeratin 17 and its
RT expression pattern.";
RL Eur. J. Cell Biol. 59:127-137(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RX PubMed=1372562; DOI=10.1002/eji.1830220415;
RA Flohr T., Buwitt U., Bonnekoh B., Decker T., Boettger E.C.;
RT "Interferon-gamma regulates expression of a novel keratin class I gene.";
RL Eur. J. Immunol. 22:975-979(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PC2 ASP-109.
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Cervix, and Muscle;
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 [MRNA] OF 85-101, AND VARIANT PC2 ASP-92.
RX PubMed=7539673; DOI=10.1038/ng0395-273;
RA McLean W.H.I., Rugg E.L., Lunny D.P., Morley S.M., Lane E.B., Swensson O.,
RA Dopping-Hepenstal P.J.C., Griffiths W.A.D., Eady R.A.J., Higgins C.,
RA Navsaria H.A., Leigh I.M., Strachan T., Kunkeler L., Munro C.S.;
RT "Keratin 16 and keratin 17 mutations cause pachyonychia congenita.";
RL Nat. Genet. 9:273-278(1995).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 101-117; 152-168; 306-322 AND 331-347.
RA Shen Z., Chen L., Wang G., Liu Y.-F.;
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=2481679; DOI=10.1242/jcs.93.3.419;
RA Troyanovsky S.M., Guelstein V.I., Tchipysheva T.A., Krutovskikh V.A.,
RA Bannikov G.A.;
RT "Patterns of expression of keratin 17 in human epithelia: dependency on
RT cell position.";
RL J. Cell Sci. 93:419-426(1989).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=10651700; DOI=10.1046/j.1365-2133.2000.03246.x;
RA De Berker D., Wojnarowska F., Sviland L., Westgate G.E., Dawber R.P.,
RA Leigh I.M.;
RT "Keratin expression in the normal nail unit: markers of regional
RT differentiation.";
RL Br. J. Dermatol. 142:89-96(2000).
RN [10]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=10844551; DOI=10.1046/j.1523-1747.2000.00986.x;
RA McGowan K.M., Coulombe P.A.;
RT "Keratin 17 expression in the hard epithelial context of the hair and nail,
RT and its relevance for the pachyonychia congenita phenotype.";
RL J. Invest. Dermatol. 114:1101-1107(2000).
RN [11]
RP FUNCTION, AND INDUCTION.
RX PubMed=15795121; DOI=10.1016/j.jdermsci.2005.01.001;
RA Shen Z., Wang G., Fan J.-Y., Li W., Liu Y.-F.;
RT "HLA DR B1*04, *07-restricted epitopes on Keratin 17 for autoreactive T
RT cells in psoriasis.";
RL J. Dermatol. Sci. 38:25-39(2005).
RN [12]
RP INDUCTION.
RX PubMed=15608502; DOI=10.1159/000081685;
RA Bockelmann R., Horn T., Gollnick H., Bonnekoh B.;
RT "Interferon-gamma-dependent in vitro model for the putative keratin 17
RT autoimmune loop in psoriasis: exploration of pharmaco- and gene-therapeutic
RT effects.";
RL Skin Pharmacol. Physiol. 18:42-54(2005).
RN [13]
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 [14]
RP FUNCTION, INDUCTION, AND MUTAGENESIS OF ARG-103; GLU-106; ASN-109; ASN-154;
RP ILE-155; LEU-157; ASP-160; ASN-333; ARG-334; CYS-336 AND LEU-339.
RX PubMed=16713453; DOI=10.1016/j.jaad.2006.02.033;
RA Shen Z., Chen L., Liu Y.-F., Gao T.-W., Wang G., Fan X.-L., Fan J.-Y.,
RA Fan P.-S., Li C.-Y., Liu B., Dang Y.-P., Li C.-X.;
RT "Altered keratin 17 peptide ligands inhibit in vitro proliferation of
RT keratinocytes and T cells isolated from patients with psoriasis.";
RL J. Am. Acad. Dermatol. 54:992-1002(2006).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-32 AND SER-39, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, AND IDENTIFICATION BY
RP 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 [18]
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 [19]
RP PHOSPHORYLATION AT SER-44.
RX PubMed=22006917; DOI=10.1074/jbc.m111.302042;
RA Pan X., Kane L.A., Van Eyk J.E., Coulombe P.A.;
RT "Type I keratin 17 protein is phosphorylated on serine 44 by p90 ribosomal
RT protein S6 kinase 1 (RSK1) in a growth- and stress-dependent fashion.";
RL J. Biol. Chem. 286:42403-42413(2011).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-13; SER-32; SER-39;
RP THR-110 AND SER-323, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-15; LYS-399 AND LYS-419, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [22]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-15; LYS-399; LYS-400 AND LYS-419,
RP AND IDENTIFICATION BY MASS 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 [23]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-15 AND LYS-399, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [24]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-15; LYS-278; LYS-399; LYS-400 AND
RP LYS-419, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [25]
RP VARIANTS PC2 SER-92 AND ASP-98, AND VARIANTS SM HIS-92 AND HIS-94.
RX PubMed=9008238; DOI=10.1111/1523-1747.ep12335315;
RA Smith F.J.D., Corden L.D., Rugg E.L., Ratnavel R., Leigh I.M., Moss C.,
RA Tidman M.J., Hohl D., Huber M., Kunkeler L., Munro C.S., Lane E.B.,
RA McLean W.H.I.;
RT "Missense mutations in keratin 17 cause either pachyonychia congenita type
RT 2 or a phenotype resembling steatocystoma multiplex.";
RL J. Invest. Dermatol. 108:220-223(1997).
RN [26]
RP VARIANTS PC2 SER-92 AND CYS-94, AND VARIANT SM CYS-94.
RX PubMed=9767294; DOI=10.1046/j.1365-2133.1998.02413.x;
RA Covello S.P., Smith F.J.D., Sillevis Smitt J.H., Paller A.S., Munro C.S.,
RA Jonkman M.F., Uitto J., McLean W.H.I.;
RT "Keratin 17 mutations cause either steatocystoma multiplex or pachyonychia
RT congenita type 2.";
RL Br. J. Dermatol. 139:475-480(1998).
RN [27]
RP VARIANT PC2 THR-88.
RX PubMed=10571744; DOI=10.1046/j.1523-1747.1999.00762.x;
RA Celebi J.T., Tanzi E.L., Yao Y.J., Michael E.J., Peacocke M.;
RT "Mutation report: identification of a germline mutation in keratin 17 in a
RT family with pachyonychia congenita type 2.";
RL J. Invest. Dermatol. 113:848-850(1999).
RN [28]
RP VARIANTS PC2 94-PRO--TYR-98 DEL; PRO-94 AND GLN-95.
RX PubMed=11348474; DOI=10.1046/j.1523-1747.2001.01335.x;
RA Smith F.J.D., Coleman C.M., Bayoumy N.M., Tenconi R., Nelson J., David A.,
RA McLean W.H.I.;
RT "Novel keratin 17 mutations in pachyonychia congenita type 2.";
RL J. Invest. Dermatol. 116:806-808(2001).
RN [29]
RP VARIANTS PC2 PRO-95; SER-97 DEL AND PRO-99.
RX PubMed=11886499; DOI=10.1046/j.0022-202x.2001.01565.x;
RA Terrinoni A., Smith F.J.D., Didona B., Canzona F., Paradisi M., Huber M.,
RA Hohl D., David A., Verloes A., Leigh I.M., Munro C.S., Melino G.,
RA McLean W.H.I.;
RT "Novel and recurrent mutations in the genes encoding keratins K6a, K16 and
RT K17 in 13 cases of pachyonychia congenita.";
RL J. Invest. Dermatol. 117:1391-1396(2001).
RN [30]
RP VARIANT PC2 MET-102.
RX PubMed=11874497; DOI=10.1046/j.0022-202x.2001.01701.x;
RA Hashiguchi T., Yotsumoto S., Shimada H., Terasaki K., Setoyama M.,
RA Kobayashi K., Saheki T., Kanzaki T.;
RT "A novel point mutation in the keratin 17 gene in a Japanese case of
RT pachyonychia congenita type 2.";
RL J. Invest. Dermatol. 118:545-547(2002).
RN [31]
RP VARIANT PC2 ASP-109.
RX PubMed=15102078; DOI=10.1111/j.0022-202x.2004.22408.x;
RA Xiao S.-X., Feng Y.-G., Ren X.-R., Tan S.-S., Li L., Wang J.-M., Shi Y.-Z.;
RT "A novel mutation in the second half of the keratin 17 1A domain in a large
RT pedigree with delayed-onset pachyonychia congenita type 2.";
RL J. Invest. Dermatol. 122:892-895(2004).
RN [32]
RP VARIANT PC2 MET-102.
RX PubMed=15795125; DOI=10.1016/j.jdermsci.2004.12.022;
RA Uchida T., Inaoki M., Makino E., Fujimoto W.;
RT "Identification of a recurrent mutation in keratin 17 in a Japanese family
RT with pachyonychia congenita type 2.";
RL J. Dermatol. Sci. 38:60-63(2005).
RN [33]
RP VARIANTS PC2 SER-92 AND PRO-388.
RX PubMed=16250206; DOI=10.1111/j.1087-0024.2005.10204.x;
RA Smith F.J., Liao H., Cassidy A.J., Stewart A., Hamill K.J., Wood P.,
RA Joval I., van Steensel M.A., Bjoerck E., Callif-Daley F., Pals G.,
RA Collins P., Leachman S.A., Munro C.S., McLean W.H.;
RT "The genetic basis of pachyonychia congenita.";
RL J. Investig. Dermatol. Symp. Proc. 10:21-30(2005).
RN [34]
RP VARIANT PC2 THR-88, AND VARIANT SM THR-88.
RX PubMed=16620218; DOI=10.1111/j.1346-8138.2006.00037.x;
RA Oh S.-W., Kim M.Y., Lee J.S., Kim S.-C.;
RT "Keratin 17 mutation in pachyonychia congenita type 2 patient with early
RT onset steatocystoma multiplex and Hutchinson-like tooth deformity.";
RL J. Dermatol. 33:161-164(2006).
RN [35]
RP VARIANT PC2 SER-92.
RX PubMed=17719747; DOI=10.1016/j.jdermsci.2007.07.003;
RA Liao H., Sayers J.M., Wilson N.J., Irvine A.D., Mellerio J.E., Baselga E.,
RA Bayliss S.J., Uliana V., Fimiani M., Lane E.B., McLean W.H., Leachman S.A.,
RA Smith F.J.;
RT "A spectrum of mutations in keratins K6a, K16 and K17 causing pachyonychia
RT congenita.";
RL J. Dermatol. Sci. 48:199-205(2007).
RN [36]
RP VARIANT PC2 LYS-88.
RX PubMed=18547302; DOI=10.1111/j.1365-2133.2008.08684.x;
RA Tsuda T., Ishikawa C., Nakagawa N., Konishi H., Tarutani M., Matsuki M.,
RA Yamanishi K.;
RT "A novel point mutation of keratin 17 (KRT17) in a Japanese family with
RT pachyonychia congenita type 2: an RNA-based genetic analysis using a single
RT hair bulb.";
RL Br. J. Dermatol. 159:730-732(2008).
RN [37]
RP VARIANTS PC2 SER-92 AND HIS-94.
RX PubMed=19470054; DOI=10.1111/j.1468-3083.2009.03180.x;
RA Wang J.F., Lu W.S., Sun L.D., Lv Y.M., Zhou F.S., Fang Q.Y., Tang H.Y.,
RA Cui Y., Yang S., Zhang X.J.;
RT "Novel missense mutation of keratin in Chinese family with steatocystoma
RT multiplex.";
RL J. Eur. Acad. Dermatol. Venereol. 23:723-724(2009).
RN [38]
RP VARIANTS PC2 92-ASN--LEU-99 DEL AND SER-92.
RX PubMed=21326300; DOI=10.1038/jid.2011.20;
RA Wilson N.J., Leachman S.A., Hansen C.D., McMullan A.C., Milstone L.M.,
RA Schwartz M.E., McLean W.H., Hull P.R., Smith F.J.;
RT "A large mutational study in pachyonychia congenita.";
RL J. Invest. Dermatol. 131:1018-1024(2011).
RN [39]
RP VARIANT PC2 ARG-388.
RX PubMed=23278621; DOI=10.1111/j.1365-4632.2010.04667.x;
RA Qiang W., Kaibo W., Tienan L., Guilan Z., Yueyang L., Ting X., Fangji S.;
RT "A novel mutation of keratin 17 gene in a pedigree with pachyonychia
RT congenita type 2.";
RL Int. J. Dermatol. 52:117-119(2013).
RN [40]
RP VARIANT PC2 PRO-91.
RX PubMed=23855588; DOI=10.1111/1346-8138.12212;
RA Ichimiya M., Yamaguchi M., Nemoto K., Muto M.;
RT "Novel mutation (p.L91P, c.272T>C) of keratin 17 in a case with
RT pachyonychia congenita type 2.";
RL J. Dermatol. 40:757-758(2013).
CC -!- FUNCTION: Type I keratin involved in the formation and maintenance of
CC various skin appendages, specifically in determining shape and
CC orientation of hair (By similarity). Required for the correct growth of
CC hair follicles, in particular for the persistence of the anagen
CC (growth) state (By similarity). Modulates the function of TNF-alpha in
CC the specific context of hair cycling. Regulates protein synthesis and
CC epithelial cell growth through binding to the adapter protein SFN and
CC by stimulating Akt/mTOR pathway (By similarity). Involved in tissue
CC repair. May be a marker of basal cell differentiation in complex
CC epithelia and therefore indicative of a certain type of epithelial
CC 'stem cells'. Acts as a promoter of epithelial proliferation by acting
CC a regulator of immune response in skin: promotes Th1/Th17-dominated
CC immune environment contributing to the development of basaloid skin
CC tumors (By similarity). May act as an autoantigen in the
CC immunopathogenesis of psoriasis, with certain peptide regions being a
CC major target for autoreactive T-cells and hence causing their
CC proliferation. {ECO:0000250|UniProtKB:Q9QWL7,
CC ECO:0000269|PubMed:10844551, ECO:0000269|PubMed:15795121,
CC ECO:0000269|PubMed:16713453}.
CC -!- SUBUNIT: Heterodimer of a type I and a type II keratin. KRT17
CC associates with KRT6 isomers (KRT6A or KRT6B). Interacts with TRADD and
CC SFN (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q04695; Q15834: CCDC85B; NbExp=2; IntAct=EBI-297873, EBI-739674;
CC Q04695; P26641: EEF1G; NbExp=2; IntAct=EBI-297873, EBI-351467;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9QWL7}.
CC -!- TISSUE SPECIFICITY: Expressed in the outer root sheath and medulla
CC region of hair follicle specifically from eyebrow and beard, digital
CC pulp, nail matrix and nail bed epithelium, mucosal stratified squamous
CC epithelia and in basal cells of oral epithelium, palmoplantar epidermis
CC and sweat and mammary glands. Also expressed in myoepithelium of
CC prostate, basal layer of urinary bladder, cambial cells of sebaceous
CC gland and in exocervix (at protein level).
CC {ECO:0000269|PubMed:10651700, ECO:0000269|PubMed:10844551,
CC ECO:0000269|PubMed:1281771, ECO:0000269|PubMed:2481679}.
CC -!- INDUCTION: Induced in damaged or stressed epidermis. Induced by the
CC cytokines interferon-gamma (IFN-gamma), tumor necrosis factor alpha
CC (TNF-alpha) and transforming growth factor-alpha (TGF-alpha), and by
CC the potent NF-kappa B inhibitor compounds Bay 11-7082 and Bay 11-7085.
CC Down-regulated by the drug Imatinib. {ECO:0000269|PubMed:1372562,
CC ECO:0000269|PubMed:15608502, ECO:0000269|PubMed:15795121,
CC ECO:0000269|PubMed:16713453}.
CC -!- PTM: Phosphorylation at Ser-44 occurs in a growth- and stress-dependent
CC fashion in skin keratinocytes, it has no effect on filament
CC organization. {ECO:0000269|PubMed:22006917}.
CC -!- DISEASE: Pachyonychia congenita 2 (PC2) [MIM:167210]: An autosomal
CC dominant ectodermal dysplasia characterized by hypertrophic nail
CC dystrophy resulting in onchyogryposis (thickening and increase in
CC curvature of the nail), palmoplantar keratoderma and hyperhidrosis,
CC follicular hyperkeratosis, multiple epidermal cysts, absent/sparse
CC eyebrow and body hair, and by the presence of natal teeth.
CC {ECO:0000269|PubMed:10571744, ECO:0000269|PubMed:11348474,
CC ECO:0000269|PubMed:11874497, ECO:0000269|PubMed:11886499,
CC ECO:0000269|PubMed:15102078, ECO:0000269|PubMed:15795125,
CC ECO:0000269|PubMed:16250206, ECO:0000269|PubMed:16620218,
CC ECO:0000269|PubMed:16625196, ECO:0000269|PubMed:17719747,
CC ECO:0000269|PubMed:18547302, ECO:0000269|PubMed:19470054,
CC ECO:0000269|PubMed:21326300, ECO:0000269|PubMed:23278621,
CC ECO:0000269|PubMed:23855588, ECO:0000269|PubMed:7539673,
CC ECO:0000269|PubMed:9008238, ECO:0000269|PubMed:9767294}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Steatocystoma multiplex (SM) [MIM:184500]: Disease
CC characterized by round or oval cystic tumors widely distributed on the
CC back, anterior trunk, arms, scrotum, and thighs.
CC {ECO:0000269|PubMed:16620218, ECO:0000269|PubMed:9008238,
CC ECO:0000269|PubMed:9767294}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Note=KRT16 and KRT17 are coexpressed only in pathological
CC situations such as metaplasias and carcinomas of the uterine cervix and
CC in psoriasis vulgaris.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAH72018.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Human Intermediate Filament Mutation Database;
CC URL="http://www.interfil.org";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Keratin-17 entry;
CC URL="https://en.wikipedia.org/wiki/Keratin_17";
CC ---------------------------------------------------------------------------
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DR EMBL; Z19574; CAA79626.1; -; Genomic_DNA.
DR EMBL; X62571; CAA44451.1; -; mRNA.
DR EMBL; AK095342; BAC04534.1; -; mRNA.
DR EMBL; AC022596; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL353997; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000159; AAH00159.2; -; mRNA.
DR EMBL; BC011901; AAH11901.1; -; mRNA.
DR EMBL; BC056421; AAH56421.1; -; mRNA.
DR EMBL; BC072018; AAH72018.1; ALT_FRAME; mRNA.
DR EMBL; BC072019; AAH72019.1; -; mRNA.
DR EMBL; S78515; AAB34565.1; -; Genomic_DNA.
DR EMBL; EF608068; ABQ96595.1; -; mRNA.
DR EMBL; EF608069; ABQ96596.1; -; mRNA.
DR EMBL; EF608070; ABQ96597.1; -; mRNA.
DR EMBL; EF608071; ABQ96598.1; -; mRNA.
DR CCDS; CCDS11402.1; -.
DR PIR; S30433; S30433.
DR RefSeq; NP_000413.1; NM_000422.2.
DR AlphaFoldDB; Q04695; -.
DR SMR; Q04695; -.
DR BioGRID; 110070; 210.
DR DIP; DIP-33093N; -.
DR IntAct; Q04695; 29.
DR MINT; Q04695; -.
DR STRING; 9606.ENSP00000308452; -.
DR GlyGen; Q04695; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; Q04695; -.
DR MetOSite; Q04695; -.
DR PhosphoSitePlus; Q04695; -.
DR SwissPalm; Q04695; -.
DR BioMuta; KRT17; -.
DR DMDM; 547751; -.
DR SWISS-2DPAGE; Q04695; -.
DR CPTAC; CPTAC-1516; -.
DR CPTAC; CPTAC-1517; -.
DR EPD; Q04695; -.
DR jPOST; Q04695; -.
DR MassIVE; Q04695; -.
DR PaxDb; Q04695; -.
DR PeptideAtlas; Q04695; -.
DR PRIDE; Q04695; -.
DR ProteomicsDB; 58264; -.
DR TopDownProteomics; Q04695; -.
DR ABCD; Q04695; 2 sequenced antibodies.
DR Antibodypedia; 6491; 1230 antibodies from 46 providers.
DR DNASU; 3872; -.
DR Ensembl; ENST00000311208.13; ENSP00000308452.8; ENSG00000128422.18.
DR GeneID; 3872; -.
DR KEGG; hsa:3872; -.
DR MANE-Select; ENST00000311208.13; ENSP00000308452.8; NM_000422.3; NP_000413.1.
DR UCSC; uc002hxh.3; human.
DR CTD; 3872; -.
DR DisGeNET; 3872; -.
DR GeneCards; KRT17; -.
DR GeneReviews; KRT17; -.
DR HGNC; HGNC:6427; KRT17.
DR HPA; ENSG00000128422; Tissue enhanced (breast, skin, urinary bladder).
DR MalaCards; KRT17; -.
DR MIM; 148069; gene.
DR MIM; 167210; phenotype.
DR MIM; 184500; phenotype.
DR neXtProt; NX_Q04695; -.
DR OpenTargets; ENSG00000128422; -.
DR Orphanet; 2309; Pachyonychia congenita.
DR Orphanet; 841; Sebocystomatosis.
DR PharmGKB; PA30214; -.
DR VEuPathDB; HostDB:ENSG00000128422; -.
DR eggNOG; ENOG502QTM6; Eukaryota.
DR GeneTree; ENSGT00940000160681; -.
DR HOGENOM; CLU_012560_8_1_1; -.
DR InParanoid; Q04695; -.
DR OMA; YYHTIED; -.
DR OrthoDB; 798081at2759; -.
DR PhylomeDB; Q04695; -.
DR TreeFam; TF332742; -.
DR PathwayCommons; Q04695; -.
DR Reactome; R-HSA-6805567; Keratinization.
DR Reactome; R-HSA-6809371; Formation of the cornified envelope.
DR SignaLink; Q04695; -.
DR SIGNOR; Q04695; -.
DR BioGRID-ORCS; 3872; 86 hits in 1029 CRISPR screens.
DR ChiTaRS; KRT17; human.
DR GeneWiki; Keratin_17; -.
DR GenomeRNAi; 3872; -.
DR Pharos; Q04695; Tbio.
DR PRO; PR:Q04695; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q04695; protein.
DR Bgee; ENSG00000128422; Expressed in gingival epithelium and 159 other tissues.
DR ExpressionAtlas; Q04695; baseline and differential.
DR Genevisible; Q04695; HS.
DR GO; GO:0001533; C:cornified envelope; IEA:Ensembl.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
DR GO; GO:0045095; C:keratin filament; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0030855; P:epithelial cell differentiation; IBA:GO_Central.
DR GO; GO:0031069; P:hair follicle morphogenesis; ISS:UniProtKB.
DR GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
DR GO; GO:0031424; P:keratinization; IEA:Ensembl.
DR GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
DR GO; GO:0051798; P:positive regulation of hair follicle development; IEA:Ensembl.
DR GO; GO:0045727; P:positive regulation of translation; IEA:Ensembl.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR002957; Keratin_I.
DR PANTHER; PTHR23239; PTHR23239; 1.
DR Pfam; PF00038; Filament; 1.
DR PRINTS; PR01248; TYPE1KERATIN.
DR SMART; SM01391; Filament; 1.
DR PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Disease variant; Ectodermal dysplasia;
KW Intermediate filament; Isopeptide bond; Keratin; Palmoplantar keratoderma;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..432
FT /note="Keratin, type I cytoskeletal 17"
FT /id="PRO_0000063664"
FT DOMAIN 84..395
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..83
FT /note="Head"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..120
FT /note="Coil 1A"
FT REGION 102..116
FT /note="Peptide epitope S1; induces T-cell and keratinocyte
FT proliferation and IFN-gamma production"
FT REGION 121..138
FT /note="Linker 1"
FT REGION 139..230
FT /note="Coil 1B"
FT REGION 153..167
FT /note="Peptide epitope S2; induces T-cell proliferation and
FT IFN-gamma production"
FT REGION 231..250
FT /note="Linker 12"
FT REGION 251..392
FT /note="Coil 2"
FT REGION 332..346
FT /note="Peptide epitope S4; induces T-cell and keratinocyte
FT proliferation and IFN-gamma production"
FT REGION 393..432
FT /note="Tail"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61414"
FT MOD_RES 32
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 39
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 44
FT /note="Phosphoserine; by RPS6KA1"
FT /evidence="ECO:0000269|PubMed:22006917"
FT MOD_RES 110
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 279
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6IFV3"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 15
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 15
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 278
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 399
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 399
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 400
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 400
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 419
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 419
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:28112733"
FT VARIANT 88
FT /note="M -> K (in PC2; dbSNP:rs28928898)"
FT /evidence="ECO:0000269|PubMed:18547302"
FT /id="VAR_072441"
FT VARIANT 88
FT /note="M -> T (in PC2 and SM; dbSNP:rs28928898)"
FT /evidence="ECO:0000269|PubMed:10571744,
FT ECO:0000269|PubMed:16620218"
FT /id="VAR_010512"
FT VARIANT 91
FT /note="L -> P (in PC2)"
FT /evidence="ECO:0000269|PubMed:23855588"
FT /id="VAR_072442"
FT VARIANT 92..99
FT /note="Missing (in PC2)"
FT /evidence="ECO:0000269|PubMed:21326300"
FT /id="VAR_072443"
FT VARIANT 92
FT /note="N -> D (in PC2; dbSNP:rs28928896)"
FT /evidence="ECO:0000269|PubMed:7539673"
FT /id="VAR_003847"
FT VARIANT 92
FT /note="N -> H (in SM; dbSNP:rs28928896)"
FT /evidence="ECO:0000269|PubMed:9008238"
FT /id="VAR_003848"
FT VARIANT 92
FT /note="N -> S (in PC2; dbSNP:rs59151893)"
FT /evidence="ECO:0000269|PubMed:16250206,
FT ECO:0000269|PubMed:17719747, ECO:0000269|PubMed:19470054,
FT ECO:0000269|PubMed:21326300, ECO:0000269|PubMed:9008238,
FT ECO:0000269|PubMed:9767294"
FT /id="VAR_003849"
FT VARIANT 94..98
FT /note="Missing (in PC2)"
FT /id="VAR_017069"
FT VARIANT 94
FT /note="R -> C (in PC2 and SM; dbSNP:rs58730926)"
FT /evidence="ECO:0000269|PubMed:9767294"
FT /id="VAR_010513"
FT VARIANT 94
FT /note="R -> H (in SM AND PC2; dbSNP:rs28928897)"
FT /evidence="ECO:0000269|PubMed:19470054,
FT ECO:0000269|PubMed:9008238"
FT /id="VAR_003850"
FT VARIANT 94
FT /note="R -> P (in PC2; dbSNP:rs28928897)"
FT /evidence="ECO:0000269|PubMed:11348474"
FT /id="VAR_017068"
FT VARIANT 95
FT /note="L -> P (in PC2; dbSNP:rs28928899)"
FT /evidence="ECO:0000269|PubMed:11886499"
FT /id="VAR_017071"
FT VARIANT 95
FT /note="L -> Q (in PC2; dbSNP:rs28928899)"
FT /evidence="ECO:0000269|PubMed:11348474"
FT /id="VAR_017070"
FT VARIANT 97
FT /note="Missing (in PC2)"
FT /evidence="ECO:0000269|PubMed:11886499"
FT /id="VAR_017072"
FT VARIANT 98
FT /note="Y -> D (in PC2; dbSNP:rs28933088)"
FT /evidence="ECO:0000269|PubMed:9008238"
FT /id="VAR_003851"
FT VARIANT 99
FT /note="L -> P (in PC2; dbSNP:rs28933089)"
FT /evidence="ECO:0000269|PubMed:11886499"
FT /id="VAR_017073"
FT VARIANT 102
FT /note="V -> M (in PC2; dbSNP:rs59977263)"
FT /evidence="ECO:0000269|PubMed:11874497,
FT ECO:0000269|PubMed:15795125"
FT /id="VAR_017074"
FT VARIANT 109
FT /note="N -> D (in PC2; dbSNP:rs267607412)"
FT /evidence="ECO:0000269|PubMed:15102078,
FT ECO:0000269|PubMed:16625196"
FT /id="VAR_037083"
FT VARIANT 388
FT /note="L -> P (in PC2; dbSNP:rs56690581)"
FT /evidence="ECO:0000269|PubMed:16250206"
FT /id="VAR_072444"
FT VARIANT 388
FT /note="L -> R (in PC2)"
FT /evidence="ECO:0000269|PubMed:23278621"
FT /id="VAR_072445"
FT MUTAGEN 103
FT /note="R->A: Down-regulates both proliferation of psoriatic
FT T-cells and IFN-gamma production; suppresses keratinocyte
FT growth when part of the altered peptide epitope S1."
FT /evidence="ECO:0000269|PubMed:16713453"
FT MUTAGEN 106
FT /note="E->A: Down-regulates proliferation of psoriatic T-
FT cells and IFN-gamma production when part of the altered
FT peptide epitope S1."
FT /evidence="ECO:0000269|PubMed:16713453"
FT MUTAGEN 109
FT /note="N->A: No significant effect on T-cell proliferation
FT or IFN-gamma production when part of the altered peptide
FT epitope S1."
FT /evidence="ECO:0000269|PubMed:16713453"
FT MUTAGEN 154
FT /note="N->A: No significant effect on T-cell proliferation
FT but reduces IFN-gamma production when part of the altered
FT peptide epitope S2."
FT /evidence="ECO:0000269|PubMed:16713453"
FT MUTAGEN 155
FT /note="I->A: No significant effect on T-cell proliferation
FT but reduces IFN-gamma production when part of the altered
FT peptide epitope S2."
FT /evidence="ECO:0000269|PubMed:16713453"
FT MUTAGEN 157
FT /note="L->A: Down-regulates proliferation of psoriatic T-
FT cells and IFN-gamma production when part of the altered
FT peptide epitope S2."
FT /evidence="ECO:0000269|PubMed:16713453"
FT MUTAGEN 160
FT /note="D->A: No significant effect on T-cell proliferation
FT but reduces IFN-gamma production when part of the altered
FT peptide epitope S4."
FT /evidence="ECO:0000269|PubMed:16713453"
FT MUTAGEN 333
FT /note="N->A: No significant effect on T-cell proliferation
FT but reduces IFN-gamma production when part of the altered
FT peptide epitope S4."
FT /evidence="ECO:0000269|PubMed:16713453"
FT MUTAGEN 334
FT /note="R->A: No significant effect on T-cell proliferation
FT but can induce IFN-gamma production when part of the
FT altered peptide epitope S2."
FT /evidence="ECO:0000269|PubMed:16713453"
FT MUTAGEN 336
FT /note="C->A: No significant effect on T-cell proliferation
FT but reduces IFN-gamma production when part of the altered
FT peptide epitope S2."
FT /evidence="ECO:0000269|PubMed:16713453"
FT MUTAGEN 339
FT /note="L->A: Down-regulates both proliferation of psoriatic
FT T-cells and IFN-gamma production; suppresses keratinocyte
FT growth when part of the altered peptide epitope S4."
FT /evidence="ECO:0000269|PubMed:16713453"
FT CONFLICT 30
FT /note="R -> Q (in Ref. 4; AL353997/AC022596)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="L -> P (in Ref. 4; AL353997/AC022596)"
FT /evidence="ECO:0000305"
FT CONFLICT 51..56
FT /note="Missing (in Ref. 3; BAC04534)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="T -> A (in Ref. 4; AL353997/AC022596)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="S -> SS (in Ref. 4; AL353997)"
FT /evidence="ECO:0000305"
FT CONFLICT 73..74
FT /note="FG -> SFE (in Ref. 4; AC022596)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="G -> E (in Ref. 4; AL353997)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="A -> V (in Ref. 4; AL353997/AC022596)"
FT /evidence="ECO:0000305"
FT CONFLICT 94..108
FT /note="Missing (in Ref. 5; AAH72018)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="T -> I (in Ref. 4; AL353997/AC022596)"
FT /evidence="ECO:0000305"
FT CONFLICT 145..147
FT /note="ILT -> VGPA (in Ref. 4; AL353997)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="Q -> H (in Ref. 4; AC022596)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="I -> N (in Ref. 4; AL353997)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="R -> H (in Ref. 4; AL353997/AC022596)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="D -> A (in Ref. 4; AL353997/AC022596)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="R -> C (in Ref. 4; AL353997/AC022596)"
FT /evidence="ECO:0000305"
FT CONFLICT 190..191
FT /note="LR -> PC (in Ref. 4; AL353997/AC022596)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="L -> P (in Ref. 4; AL353997)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="Q -> H (in Ref. 4; AL353997/AC022596)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="Missing (in Ref. 4; AL353997/AC022596)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="L -> P (in Ref. 4; AL353997/AC022596)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="D -> G (in Ref. 4; AL353997/AC022596)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="D -> E (in Ref. 4; AL353997/AC022596)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="R -> C (in Ref. 4; AL353997/AC022596)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="V -> M (in Ref. 4; AL353997/AC022596)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="Q -> R (in Ref. 4; AL353997/AC022596)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="R -> L (in Ref. 4; AL353997/AC022596)"
FT /evidence="ECO:0000305"
FT CONFLICT 373..375
FT /note="VKT -> MKM (in Ref. 4; AL353997/AC022596)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="Q -> L (in Ref. 4; AL353997/AC022596)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="A -> T (in Ref. 4; AL353997/AC022596)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="R -> H (in Ref. 4; AL353997/AC022596)"
FT /evidence="ECO:0000305"
FT CONFLICT 395..404
FT /note="LTQYKKEPVT -> FRMSESSPVS (in Ref. 4; AC022596)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="R -> C (in Ref. 4; AL353997)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="R -> P (in Ref. 4; AL353997)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="H -> R (in Ref. 4; AL353997)"
FT /evidence="ECO:0000305"
SQ 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
