K1C9_HUMAN
ID K1C9_HUMAN Reviewed; 623 AA.
AC P35527; O00109; Q0IJ47; Q14665;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 3.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Keratin, type I cytoskeletal 9;
DE AltName: Full=Cytokeratin-9;
DE Short=CK-9;
DE AltName: Full=Keratin-9;
DE Short=K9;
GN Name=KRT9;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Foot sole tissue;
RX PubMed=7507869; DOI=10.1111/j.1432-0436.1993.tb00033.x;
RA Langbein L., Heid H.W., Moll I., Franke W.W.;
RT "Molecular characterization of the body site-specific human epidermal
RT cytokeratin 9: cDNA cloning, amino acid sequence, and tissue specificity of
RT gene expression.";
RL Differentiation 55:57-72(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS EPPK LYS-161; GLN-163 AND
RP TRP-163.
RX PubMed=7512862; DOI=10.1038/ng0294-174;
RA Reis A., Hennies H.-C., Langbein L., Digweed M., Mischke D., Dreschler M.,
RA Schroek E., Royer-Pokora B., Franke W.W., Sperling K., Kuester W.;
RT "Keratin 9 gene mutations in epidermolytic palmoplantar keratoderma
RT (EPPK).";
RL Nat. Genet. 6:174-179(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [4]
RP PROTEIN SEQUENCE OF 14-29, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V.;
RL Submitted (AUG-2005) to UniProtKB.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 147-372, AND VARIANT EPPK GLN-163.
RX PubMed=8647270; DOI=10.1016/0014-5793(96)00393-6;
RA Kobayashi S., Tanaka T., Matsuyoshi N., Imamura S.;
RT "Keratin 9 point mutation in the pedigree of epidermolytic hereditary
RT palmoplantar keratoderma perturbs keratin intermediate filament network
RT formation.";
RL FEBS Lett. 386:149-155(1996).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 157-623.
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 [7]
RP PROTEIN SEQUENCE OF 450-466.
RX PubMed=2140676; DOI=10.1016/0006-291x(90)91140-n;
RA Rosen E.M., Meromsky L., Romero R., Setter E., Goldberg I.;
RT "Human placenta contains an epithelial scatter protein.";
RL Biochem. Biophys. Res. Commun. 168:1082-1088(1990).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF ARG-163.
RX PubMed=10218578; DOI=10.1016/s0014-5793(99)00233-1;
RA Kobayashi S., Kore-eda S., Tanaka T.;
RT "Demonstration of the pathogenic effect of point mutated keratin 9 in
RT vivo.";
RL FEBS Lett. 447:39-43(1999).
RN [9]
RP INDUCTION.
RX PubMed=10201533; DOI=10.1046/j.1523-1747.1999.00544.x;
RA Yamaguchi Y., Itami S., Tarutani M., Hosokawa K., Miura H., Yoshikawa K.;
RT "Regulation of keratin 9 in nonpalmoplantar keratinocytes by palmoplantar
RT fibroblasts through epithelial-mesenchymal interactions.";
RL J. Invest. Dermatol. 112:483-488(1999).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [11]
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 [12]
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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [15]
RP VARIANTS EPPK VAL-157 AND PRO-172.
RX PubMed=7516304; DOI=10.1007/bf00201564;
RA Hennies H.-C., Zehender D., Kunze J., Kuester W., Reis A.;
RT "Keratin 9 gene mutational heterogeneity in patients with epidermolytic
RT palmoplantar keratoderma.";
RL Hum. Genet. 93:649-654(1994).
RN [16]
RP VARIANT EPPK SER-161.
RX PubMed=7523529; DOI=10.1111/1523-1747.ep12395570;
RA Bonifas J.M., Matsumura K., Chen M.A., Berth-Jones J., Hutchinson P.E.,
RA Zloczower M., Fritsch P.O., Epstein E.H. Jr.;
RT "Mutations of keratin 9 in two families with palmoplantar epidermolytic
RT hyperkeratosis.";
RL J. Invest. Dermatol. 103:474-477(1994).
RN [17]
RP VARIANT EPPK TYR-161.
RX PubMed=7511021; DOI=10.1038/ng0194-106;
RA Torchard D., Blanchet-Bardon C., Serova O., Langbein L., Narod S.,
RA Janin N., Goguel A.F., Bernheim A., Franke W.W., Lenoir G.M., Feunteun J.;
RT "Epidermolytic palmoplantar keratoderma cosegregates with a keratin 9
RT mutation in a pedigree with breast and ovarian cancer.";
RL Nat. Genet. 6:106-110(1994).
RN [18]
RP VARIANTS EPPK TRP-163 AND SER-168.
RX PubMed=7532199; DOI=10.1111/1523-1747.ep12666018;
RA Rothnagel J.A., Wojcik S., Liefer K.M., Dominey A.M., Huber M., Hohl D.,
RA Roop D.R.;
RT "Mutations in the 1A domain of keratin 9 in patients with epidermolytic
RT palmoplantar keratoderma.";
RL J. Invest. Dermatol. 104:430-433(1995).
RN [19]
RP VARIANT EPPK VAL-160.
RX PubMed=9204965; DOI=10.1111/1523-1747.ep12276751;
RA Endo H., Hatamochi A., Shinkai H.;
RT "A novel mutation of a leucine residue in coil 1A of keratin 9 in
RT epidermolytic palmoplantar keratoderma.";
RL J. Invest. Dermatol. 109:113-115(1997).
RN [20]
RP VARIANTS EPPK THR-157; VAL-157 AND GLN-163.
RX PubMed=9856842; DOI=10.1046/j.1523-1747.1998.00445.x;
RA Covello S.P., Irvine A.D., McKenna K.E., Munro C.S., Nevin N.C.,
RA Smith F.J.D., Uitto J., McLean W.H.I.;
RT "Mutations in keratin K9 in kindreds with epidermolytic palmoplantar
RT keratoderma and epidemiology in Northern Ireland.";
RL J. Invest. Dermatol. 111:1207-1209(1998).
RN [21]
RP VARIANTS EPPK GLN-163 AND STOP-170.
RX PubMed=10632938; DOI=10.1046/j.1525-1470.1999.00111.x;
RA Szalai S., Szalai C., Becker K., Torok E.;
RT "Keratin 9 mutations in the coil 1A region in epidermolytic palmoplantar
RT keratoderma.";
RL Pediatr. Dermatol. 16:430-435(1999).
RN [22]
RP VARIANT EPPK TRP-163.
RX PubMed=10844507; DOI=10.1046/j.1365-2230.2000.00626.x;
RA Warmuth I., Cserhalmi-Friedman P.B., Schneiderman P., Grossman M.E.,
RA Christiano A.M.;
RT "Epidermolytic palmoplantar keratoderma in a Hispanic kindred resulting
RT from a mutation in the keratin 9 gene.";
RL Clin. Exp. Dermatol. 25:244-246(2000).
RN [23]
RP VARIANT EPPK ILE-161.
RX PubMed=12192490; DOI=10.1007/s00403-002-0328-9;
RA Kuster W., Reis A., Hennies H.C.;
RT "Epidermolytic palmoplantar keratoderma of Vorner: re-evaluation of
RT Vorner's original family and identification of a novel keratin 9
RT mutation.";
RL Arch. Dermatol. Res. 294:268-272(2002).
RN [24]
RP VARIANTS EPPK VAL-157; TRP-163; GLN-163 AND MET-171.
RX PubMed=12072061; DOI=10.1046/j.1365-2133.2002.04764.x;
RA Rugg E.L., Common J.E., Wilgoss A., Stevens H.P., Buchan J., Leigh I.M.,
RA Kelsell D.P.;
RT "Diagnosis and confirmation of epidermolytic palmoplantar keratoderma by
RT the identification of mutations in keratin 9 using denaturing high-
RT performance liquid chromatography.";
RL Br. J. Dermatol. 146:952-957(2002).
RN [25]
RP VARIANT EPPK ILE-161.
RX PubMed=12926810; DOI=10.1080/00015550310016652;
RA Csikos M., Hollo P., Becker K., Racz E., Horvath A., Karpati S.;
RT "Novel N160I mutation of keratin 9 in a large pedigree from Hungary with
RT epidermolytic palmoplantar keratoderma.";
RL Acta Derm. Venereol. 83:303-305(2003).
RN [26]
RP VARIANT EPPK PHE-160.
RX PubMed=12838553; DOI=10.1002/ajmg.a.20090;
RA Lu Y., Guo C., Liu Q., Zhang X., Cheng L., Li J., Chen B., Gao G., Zhou H.,
RA Guo Y., Li Y., Gong Y.;
RT "A novel mutation of keratin 9 in epidermolytic palmoplantar keratoderma
RT combined with knuckle pads.";
RL Am. J. Med. Genet. A 120:345-349(2003).
RN [27]
RP VARIANTS EPPK HIS-161; SER-161 AND TRP-163.
RX PubMed=14675368; DOI=10.1111/j.0906-6705.2003.00012.x;
RA Lee J.-H., Ahn K.-S., Lee C.-H., Youn S.-J., Kim J.-W., Lee D.-Y.,
RA Lee E.-S., Steinert P.M., Yang J.-M.;
RT "Keratin 9 gene mutations in five Korean families with epidermolytic
RT palmoplantar keratoderma.";
RL Exp. Dermatol. 12:876-881(2003).
RN [28]
RP VARIANT EPPK TYR-167 DEL TRP-LEU INS.
RX PubMed=15099359; DOI=10.1111/j.0007-0963.2004.05865.x;
RA He X.-H., Zhang X.-N., Mao W., Chen H.-P., Xu L.-R., Chen H., He X.-L.,
RA Le Y.-P.;
RT "A novel mutation of keratin 9 in a large Chinese family with epidermolytic
RT palmoplantar keratoderma.";
RL Br. J. Dermatol. 150:647-651(2004).
RN [29]
RP VARIANT EPPK HIS-161.
RX PubMed=15115518; DOI=10.1111/j.1365-2230.2004.01497.x;
RA Lin J.-H., Lin M.-H., Yang M.-H., Chao S.-C.;
RT "A novel keratin 9 gene mutation (Asn160His) in a Taiwanese family with
RT epidermolytic palmoplantar keratoderma.";
RL Clin. Exp. Dermatol. 29:308-310(2004).
RN [30]
RP VARIANT EPPK PRO-163.
RX PubMed=15605275; DOI=10.1007/s00403-004-0534-8;
RA Kon A., Itagaki K., Yoneda K., Takagaki K.;
RT "A novel mutation of keratin 9 gene (R162P) in a Japanese family with
RT epidermolytic palmoplantar keratoderma.";
RL Arch. Dermatol. Res. 296:375-378(2005).
RN [31]
RP VARIANT EPPK PHE-458.
RX PubMed=16911293; DOI=10.1111/j.1365-2133.2006.07358.x;
RA Kon A., Ito N., Kudo Y., Nomura K., Yoneda K., Hanada K., Hashimoto I.,
RA Takagaki K.;
RT "L457F missense mutation within the 2B rod domain of keratin 9 in a
RT Japanese family with epidermolytic palmoplantar keratoderma.";
RL Br. J. Dermatol. 155:624-626(2006).
RN [32]
RP VARIANT EPPK ARG-157.
RX PubMed=16961539; DOI=10.1111/j.1365-4632.2006.02910.x;
RA Shimazu K., Tsunemi Y., Hattori N., Saeki H., Komine M., Adachi M.,
RA Tamaki K.;
RT "A novel keratin 9 gene mutation (Met156Arg) in a Japanese patient with
RT epidermolytic palmoplantar keratoderma.";
RL Int. J. Dermatol. 45:1128-1130(2006).
RN [33]
RP VARIANTS EPPK LYS-157; THR-157; GLN-163 AND HIS-454.
RX PubMed=19874353; DOI=10.1111/j.1365-2230.2009.03700.x;
RA Shimomura Y., Wajid M., Weiser J., Kraemer L., Christiano A.M.;
RT "Mutations in the keratin 9 gene in Pakistani families with epidermolytic
RT palmoplantar keratoderma.";
RL Clin. Exp. Dermatol. 35:759-764(2010).
RN [34]
RP VARIANT EPPK ARG-406.
RX PubMed=20964665; DOI=10.1111/j.1365-4632.2009.04295.x;
RA Wang K., He C.D., Song F., Liu J., Chen H.D.;
RT "A novel mutation of the keratin 9 gene in a Chinese family with
RT epidermolytic palmoplantar keratoderma.";
RL Int. J. Dermatol. 49:1342-1344(2010).
RN [35]
RP VARIANT EPPK PRO-458.
RX PubMed=21715251; DOI=10.1684/ejd.2011.1458;
RA Du Z.F., Wei W., Wang Y.F., Chen X.L., Chen C.Y., Liu W.T., Lu J.J.,
RA Mao L.G., Xu C.M., Fang H., Zhang X.N.;
RT "A novel mutation within the 2B rod domain of keratin 9 in a Chinese
RT pedigree with epidermolytic palmoplantar keratoderma combined with knuckle
RT pads and camptodactyly.";
RL Eur. J. Dermatol. 21:675-679(2011).
CC -!- FUNCTION: May serve an important special function either in the mature
CC palmar and plantar skin tissue or in the morphogenetic program of the
CC formation of these tissues. Plays a role in keratin filament assembly.
CC {ECO:0000269|PubMed:10218578, ECO:0000269|PubMed:7507869}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC -!- TISSUE SPECIFICITY: Expressed in the terminally differentiated
CC epidermis of palms and soles. {ECO:0000269|PubMed:7507869}.
CC -!- INDUCTION: Induced by intrinsic regulatory mechanisms and by extrinsic
CC signals from a subset of dermal palmoplantar fibroblasts.
CC {ECO:0000269|PubMed:10201533}.
CC -!- DISEASE: Keratoderma, palmoplantar, epidermolytic (EPPK) [MIM:144200]:
CC A dermatological disorder characterized by diffuse thickening of the
CC epidermis on the entire surface of palms and soles sharply bordered
CC with erythematous margins. Some patients may present knuckle pads,
CC thick pads of skin appearing over the proximal phalangeal joints.
CC {ECO:0000269|PubMed:10632938, ECO:0000269|PubMed:10844507,
CC ECO:0000269|PubMed:12072061, ECO:0000269|PubMed:12192490,
CC ECO:0000269|PubMed:12838553, ECO:0000269|PubMed:12926810,
CC ECO:0000269|PubMed:14675368, ECO:0000269|PubMed:15099359,
CC ECO:0000269|PubMed:15115518, ECO:0000269|PubMed:15605275,
CC ECO:0000269|PubMed:16911293, ECO:0000269|PubMed:16961539,
CC ECO:0000269|PubMed:19874353, ECO:0000269|PubMed:20964665,
CC ECO:0000269|PubMed:21715251, ECO:0000269|PubMed:7511021,
CC ECO:0000269|PubMed:7512862, ECO:0000269|PubMed:7516304,
CC ECO:0000269|PubMed:7523529, ECO:0000269|PubMed:7532199,
CC ECO:0000269|PubMed:8647270, ECO:0000269|PubMed:9204965,
CC ECO:0000269|PubMed:9856842}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: There are two types of cytoskeletal and microfibrillar
CC keratin, I (acidic) and II (neutral to basic) (40-55 and 56-70 kDa,
CC respectively).
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
CC -!- CAUTION: Was originally thought to be a 60 kDa chain of placental
CC scatter protein. {ECO:0000305|PubMed:2140676}.
CC -!- WEB RESOURCE: Name=Human Intermediate Filament Mutation Database;
CC URL="http://www.interfil.org";
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DR EMBL; Z29074; CAA82315.1; -; mRNA.
DR EMBL; S69510; AAC60619.1; -; mRNA.
DR EMBL; X75015; CAA52924.1; -; Genomic_DNA.
DR EMBL; AC019349; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB001594; BAA19418.1; -; mRNA.
DR EMBL; BC121170; AAI21171.1; -; mRNA.
DR CCDS; CCDS32654.1; -.
DR PIR; I37984; I37984.
DR RefSeq; NP_000217.2; NM_000226.3.
DR AlphaFoldDB; P35527; -.
DR SMR; P35527; -.
DR BioGRID; 110055; 116.
DR IntAct; P35527; 41.
DR MINT; P35527; -.
DR STRING; 9606.ENSP00000246662; -.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR GlyConnect; 1951; 12 N-Linked glycans (2 sites).
DR GlyGen; P35527; 3 sites, 12 N-linked glycans (2 sites), 1 O-linked glycan (1 site).
DR iPTMnet; P35527; -.
DR PhosphoSitePlus; P35527; -.
DR SwissPalm; P35527; -.
DR BioMuta; KRT9; -.
DR DMDM; 239938886; -.
DR DOSAC-COBS-2DPAGE; P35527; -.
DR EPD; P35527; -.
DR jPOST; P35527; -.
DR MassIVE; P35527; -.
DR PaxDb; P35527; -.
DR PeptideAtlas; P35527; -.
DR PRIDE; P35527; -.
DR ProteomicsDB; 55077; -.
DR TopDownProteomics; P35527; -.
DR Antibodypedia; 1544; 209 antibodies from 28 providers.
DR DNASU; 3857; -.
DR Ensembl; ENST00000246662.9; ENSP00000246662.4; ENSG00000171403.10.
DR GeneID; 3857; -.
DR KEGG; hsa:3857; -.
DR MANE-Select; ENST00000246662.9; ENSP00000246662.4; NM_000226.4; NP_000217.2.
DR UCSC; uc002hxe.5; human.
DR CTD; 3857; -.
DR DisGeNET; 3857; -.
DR GeneCards; KRT9; -.
DR HGNC; HGNC:6447; KRT9.
DR HPA; ENSG00000171403; Tissue enriched (lymphoid).
DR MalaCards; KRT9; -.
DR MIM; 144200; phenotype.
DR MIM; 149100; phenotype.
DR MIM; 607606; gene.
DR neXtProt; NX_P35527; -.
DR OpenTargets; ENSG00000171403; -.
DR Orphanet; 2199; Epidermolytic palmoplantar keratoderma.
DR PharmGKB; PA30235; -.
DR VEuPathDB; HostDB:ENSG00000171403; -.
DR eggNOG; ENOG502QTM6; Eukaryota.
DR GeneTree; ENSGT00940000162894; -.
DR HOGENOM; CLU_012560_8_3_1; -.
DR InParanoid; P35527; -.
DR OMA; TNEKSAM; -.
DR OrthoDB; 798081at2759; -.
DR PhylomeDB; P35527; -.
DR TreeFam; TF332742; -.
DR PathwayCommons; P35527; -.
DR Reactome; R-HSA-6805567; Keratinization.
DR Reactome; R-HSA-6809371; Formation of the cornified envelope.
DR SignaLink; P35527; -.
DR BioGRID-ORCS; 3857; 9 hits in 1063 CRISPR screens.
DR GeneWiki; Keratin_9; -.
DR GenomeRNAi; 3857; -.
DR Pharos; P35527; Tbio.
DR PRO; PR:P35527; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P35527; protein.
DR Bgee; ENSG00000171403; Expressed in penis and 52 other tissues.
DR ExpressionAtlas; P35527; baseline and differential.
DR Genevisible; P35527; HS.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0045095; C:keratin filament; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
DR GO; GO:0008544; P:epidermis development; TAS:ProtInc.
DR GO; GO:0030855; P:epithelial cell differentiation; IBA:GO_Central.
DR GO; GO:0045109; P:intermediate filament organization; IMP:UniProtKB.
DR GO; GO:0043588; P:skin development; IDA:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; 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; Direct protein sequencing; Disease variant;
KW Intermediate filament; Keratin; Palmoplantar keratoderma; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..623
FT /note="Keratin, type I cytoskeletal 9"
FT /id="PRO_0000063640"
FT DOMAIN 153..465
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..152
FT /note="Head"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..188
FT /note="Coil 1A"
FT REGION 189..207
FT /note="Linker 1"
FT REGION 208..299
FT /note="Coil 1B"
FT REGION 300..322
FT /note="Linker 12"
FT REGION 323..461
FT /note="Coil 2"
FT REGION 462..623
FT /note="Tail"
FT REGION 462..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13645"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13645"
FT VARIANT 157
FT /note="M -> K (in EPPK; dbSNP:rs59510579)"
FT /evidence="ECO:0000269|PubMed:19874353"
FT /id="VAR_071977"
FT VARIANT 157
FT /note="M -> R (in EPPK; dbSNP:rs59510579)"
FT /evidence="ECO:0000269|PubMed:16961539"
FT /id="VAR_036805"
FT VARIANT 157
FT /note="M -> T (in EPPK; dbSNP:rs59510579)"
FT /evidence="ECO:0000269|PubMed:19874353,
FT ECO:0000269|PubMed:9856842"
FT /id="VAR_010499"
FT VARIANT 157
FT /note="M -> V (in EPPK; dbSNP:rs58597584)"
FT /evidence="ECO:0000269|PubMed:12072061,
FT ECO:0000269|PubMed:7516304, ECO:0000269|PubMed:9856842"
FT /id="VAR_010500"
FT VARIANT 160
FT /note="L -> F (in EPPK; with knuckle pads;
FT dbSNP:rs28940896)"
FT /evidence="ECO:0000269|PubMed:12838553"
FT /id="VAR_035438"
FT VARIANT 160
FT /note="L -> V (in EPPK; dbSNP:rs28940896)"
FT /evidence="ECO:0000269|PubMed:9204965"
FT /id="VAR_010501"
FT VARIANT 161
FT /note="N -> H (in EPPK; dbSNP:rs59296273)"
FT /evidence="ECO:0000269|PubMed:14675368,
FT ECO:0000269|PubMed:15115518"
FT /id="VAR_036806"
FT VARIANT 161
FT /note="N -> I (in EPPK; dbSNP:rs56707768)"
FT /evidence="ECO:0000269|PubMed:12192490,
FT ECO:0000269|PubMed:12926810"
FT /id="VAR_036807"
FT VARIANT 161
FT /note="N -> K (in EPPK; dbSNP:rs57536312)"
FT /evidence="ECO:0000269|PubMed:7512862"
FT /id="VAR_003822"
FT VARIANT 161
FT /note="N -> S (in EPPK; dbSNP:rs56707768)"
FT /evidence="ECO:0000269|PubMed:14675368,
FT ECO:0000269|PubMed:7523529"
FT /id="VAR_010502"
FT VARIANT 161
FT /note="N -> Y (in EPPK; dbSNP:rs59296273)"
FT /evidence="ECO:0000269|PubMed:7511021"
FT /id="VAR_010503"
FT VARIANT 163
FT /note="R -> P (in EPPK; dbSNP:rs57758262)"
FT /evidence="ECO:0000269|PubMed:15605275"
FT /id="VAR_036808"
FT VARIANT 163
FT /note="R -> Q (in EPPK; dbSNP:rs57758262)"
FT /evidence="ECO:0000269|PubMed:10632938,
FT ECO:0000269|PubMed:12072061, ECO:0000269|PubMed:19874353,
FT ECO:0000269|PubMed:7512862, ECO:0000269|PubMed:8647270,
FT ECO:0000269|PubMed:9856842"
FT /id="VAR_003823"
FT VARIANT 163
FT /note="R -> W (in EPPK; dbSNP:rs59616921)"
FT /evidence="ECO:0000269|PubMed:10844507,
FT ECO:0000269|PubMed:12072061, ECO:0000269|PubMed:14675368,
FT ECO:0000269|PubMed:7512862, ECO:0000269|PubMed:7532199"
FT /id="VAR_003824"
FT VARIANT 167
FT /note="Y -> WL (in EPPK)"
FT /id="VAR_036809"
FT VARIANT 168
FT /note="L -> S (in EPPK; dbSNP:rs61157095)"
FT /evidence="ECO:0000269|PubMed:7532199"
FT /id="VAR_003825"
FT VARIANT 171
FT /note="V -> M (in EPPK; dbSNP:rs57019720)"
FT /evidence="ECO:0000269|PubMed:12072061"
FT /id="VAR_035439"
FT VARIANT 172
FT /note="Q -> P (in EPPK; dbSNP:rs59878153)"
FT /evidence="ECO:0000269|PubMed:7516304"
FT /id="VAR_010504"
FT VARIANT 406
FT /note="C -> R (in EPPK; dbSNP:rs77688767)"
FT /evidence="ECO:0000269|PubMed:20964665"
FT /id="VAR_071978"
FT VARIANT 454
FT /note="Y -> H (in EPPK; dbSNP:rs267607420)"
FT /evidence="ECO:0000269|PubMed:19874353"
FT /id="VAR_071979"
FT VARIANT 458
FT /note="L -> F (in EPPK; dbSNP:rs58120120)"
FT /evidence="ECO:0000269|PubMed:16911293"
FT /id="VAR_036810"
FT VARIANT 458
FT /note="L -> P (in EPPK)"
FT /evidence="ECO:0000269|PubMed:21715251"
FT /id="VAR_071980"
FT MUTAGEN 163
FT /note="R->QHA: Leads to aggregate formation."
FT /evidence="ECO:0000269|PubMed:10218578"
FT CONFLICT 12..13
FT /note="SR -> T (in Ref. 1; AAC60619 and 2; CAA52924)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="G -> R (in Ref. 1; AAC60619/CAA82315 and 2;
FT CAA52924)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="F -> L (in Ref. 1; AAC60619/CAA82315 and 2;
FT CAA52924)"
FT /evidence="ECO:0000305"
FT CONFLICT 157..170
FT /note="MQELNSRLASYLDK -> HLGAGSTPITASQP (in Ref. 6;
FT AAI21171)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 623 AA; 62064 MW; 45C833749B63873D CRC64;
MSCRQFSSSY LSRSGGGGGG GLGSGGSIRS SYSRFSSSGG GGGGGRFSSS SGYGGGSSRV
CGRGGGGSFG YSYGGGSGGG FSASSLGGGF GGGSRGFGGA SGGGYSSSGG FGGGFGGGSG
GGFGGGYGSG FGGFGGFGGG AGGGDGGILT ANEKSTMQEL NSRLASYLDK VQALEEANND
LENKIQDWYD KKGPAAIQKN YSPYYNTIDD LKDQIVDLTV GNNKTLLDID NTRMTLDDFR
IKFEMEQNLR QGVDADINGL RQVLDNLTME KSDLEMQYET LQEELMALKK NHKEEMSQLT
GQNSGDVNVE INVAPGKDLT KTLNDMRQEY EQLIAKNRKD IENQYETQIT QIEHEVSSSG
QEVQSSAKEV TQLRHGVQEL EIELQSQLSK KAALEKSLED TKNRYCGQLQ MIQEQISNLE
AQITDVRQEI ECQNQEYSLL LSIKMRLEKE IETYHNLLEG GQEDFESSGA GKIGLGGRGG
SGGSYGRGSR GGSGGSYGGG GSGGGYGGGS GSRGGSGGSY GGGSGSGGGS GGGYGGGSGG
GHSGGSGGGH SGGSGGNYGG GSGSGGGSGG GYGGGSGSRG GSGGSHGGGS GFGGESGGSY
GGGEEASGSG GGYGGGSGKS SHS
