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 02-SEP-2026, entry version 229. 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 {ECO:0000312|HGNC:HGNC:6447}; 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 EPPK1 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 EPPK1 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 EPPK1 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 EPPK1 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 EPPK1 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 EPPK1 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 EPPK1 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 EPPK1 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 VARIANT EPPK1 GLN-163. 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 EPPK1 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 EPPK1 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 EPPK1 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 EPPK1 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 EPPK1 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 EPPK1 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 EPPK1 TYR-167 DELINS TRP-LEU. 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 EPPK1 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 EPPK1 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 EPPK1 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 EPPK1 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 EPPK1 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 EPPK1 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 EPPK1 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: Structural component of intermediate filaments in suprabasal CC keratinocytes of palmoplantar epidermis. Forms heteropolymers with a CC type II keratin, assembling into keratin intermediate filament networks CC that maintain the mechanical integrity of the palmoplantar epidermis. CC {ECO:0000269|PubMed:10218578, ECO:0000269|PubMed:7507869, CC ECO:0000269|PubMed:7512862}. CC -!- SUBUNIT: Heterodimers composed of one type I and one type II keratins; CC forms parallel coiled-coil heterodimers. Heterodimers associate in an CC antiparallel manner to form heterotetramers, which further assemble CC into higher-order keratin intermediate filaments. CC {ECO:0000250|UniProtKB:P02533}. 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: Palmoplantar keratoderma, epidermolytic, 1 (EPPK1) CC [MIM:144200]: A form of epidermolytic palmoplantar keratoderma, a CC 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. EPPK1 CC inheritance is autosomal dominant. {ECO:0000269|PubMed:10632938, CC ECO:0000269|PubMed:10844507, ECO:0000269|PubMed:12072061, CC ECO:0000269|PubMed:12192490, ECO:0000269|PubMed:12838553, CC ECO:0000269|PubMed:12926810, ECO:0000269|PubMed:14675368, CC ECO:0000269|PubMed:15099359, ECO:0000269|PubMed:15115518, CC ECO:0000269|PubMed:15605275, ECO:0000269|PubMed:16911293, CC ECO:0000269|PubMed:16961539, ECO:0000269|PubMed:19874353, CC ECO:0000269|PubMed:20964665, ECO:0000269|PubMed:21715251, CC ECO:0000269|PubMed:7511021, ECO:0000269|PubMed:7512862, CC ECO:0000269|PubMed:7516304, ECO:0000269|PubMed:7523529, CC ECO:0000269|PubMed:7532199, ECO:0000269|PubMed:8647270, CC ECO:0000269|PubMed:9204965, ECO:0000269|PubMed:9856842}. Note=The CC disease is caused by variants affecting the gene represented in this CC 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; 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_000226.4. DR AlphaFoldDB; P35527; -. DR SMR; P35527; -. DR BioGRID; 110055; 186. DR CORUM; P35527; -. DR FunCoup; P35527; 396. DR IntAct; P35527; 54. 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; P35527; 12 N-Linked glycans (2 sites). DR GlyCosmos; P35527; 2 sites, 12 glycans. DR GlyGen; P35527; 4 sites, 12 N-linked glycans (2 sites), 1 O-linked glycan (2 sites). DR iPTMnet; P35527; -. DR PhosphoSitePlus; P35527; -. DR SwissPalm; P35527; -. DR BioMuta; KRT9; -. DR DMDM; 239938886; -. DR jPOST; P35527; -. DR MassIVE; P35527; -. DR PaxDb; 9606-ENSP00000246662; -. DR PeptideAtlas; P35527; -. DR PRIDE; P35527; -. DR ProteomicsDB; 55077; -. DR TopDownProteomics; P35527; -. DR Antibodypedia; 1544; 224 antibodies from 31 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 AGR; HGNC:6447; -. DR ClinPGx; PA30235; -. 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 OpenTargets; ENSG00000171403; -. DR Orphanet; 2199; Epidermolytic palmoplantar keratoderma. DR VEuPathDB; HostDB:ENSG00000171403; -. DR eggNOG; ENOG502QTM6; Eukaryota. DR GeneTree; ENSGT00940000162894; -. DR HOGENOM; CLU_012560_8_3_1; -. DR InParanoid; P35527; -. DR OMA; HQEEMSQ; -. DR OrthoDB; 2441647at2759; -. DR PAN-GO; P35527; 6 GO annotations based on evolutionary models. DR PhylomeDB; P35527; -. DR PathwayCommons; P35527; -. DR Reactome; R-HSA-6805567; Keratinization. DR Reactome; R-HSA-6809371; Formation of the cornified envelope. DR SignaLink; P35527; -. DR Agora; ENSG00000171403; -. DR BioGRID-ORCS; 3857; 9 hits in 1141 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 male germ line stem cell (sensu Vertebrata) in testis and 54 other cell types or tissues. DR ExpressionAtlas; P35527; baseline and differential. 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:0005576; C:extracellular region; 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:0030280; F:structural constituent of skin epidermis; IBA:GO_Central. 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:0002009; P:morphogenesis of an epithelium; IBA:GO_Central. DR GO; GO:0043588; P:skin development; IDA:UniProtKB. DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl. DR FunFam; 1.20.5.1160:FF:000002; Type I keratin 10; 1. DR FunFam; 1.20.5.170:FF:000002; Type I keratin KA11; 1. DR FunFam; 1.20.5.500:FF:000001; Type II keratin 23; 1. DR Gene3D; 1.20.5.170; -; 1. DR Gene3D; 1.20.5.500; Single helix bin; 1. DR Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1. DR InterPro; IPR018039; IF_conserved. DR InterPro; IPR039008; IF_rod_dom. DR InterPro; IPR002957; Keratin_I. DR PANTHER; PTHR23239; INTERMEDIATE FILAMENT; 1. DR PANTHER; PTHR23239:SF96; KERATIN, TYPE I CYTOSKELETAL 9; 1. DR Pfam; PF00038; Filament; 1. DR PRINTS; PR01248; TYPE1KERATIN. DR SMART; SM01391; Filament; 1. DR SUPFAM; SSF64593; Intermediate filament protein, coiled coil region; 2. DR PROSITE; PS00226; IF_ROD_1; 1. DR PROSITE; PS51842; IF_ROD_2; 1. PE 1: Evidence at protein level; KW Coiled coil; Direct protein sequencing; Disease variant; KW Intermediate filament; Keratin; Palmoplantar keratoderma; Phosphoprotein; KW Proteomics identification; 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 COMPBIAS 1..13 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 14..25 FT /note="Gly residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 471..496 FT /note="Gly residues" 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 EPPK1; dbSNP:rs59510579)" FT /evidence="ECO:0000269|PubMed:19874353" FT /id="VAR_071977" FT VARIANT 157 FT /note="M -> R (in EPPK1; dbSNP:rs59510579)" FT /evidence="ECO:0000269|PubMed:16961539" FT /id="VAR_036805" FT VARIANT 157 FT /note="M -> T (in EPPK1; 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 EPPK1; 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 EPPK1; dbSNP:rs28940896)" FT /evidence="ECO:0000269|PubMed:12838553" FT /id="VAR_035438" FT VARIANT 160 FT /note="L -> V (in EPPK1; dbSNP:rs28940896)" FT /evidence="ECO:0000269|PubMed:9204965" FT /id="VAR_010501" FT VARIANT 161 FT /note="N -> H (in EPPK1; 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 EPPK1; 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 EPPK1; dbSNP:rs57536312)" FT /evidence="ECO:0000269|PubMed:7512862" FT /id="VAR_003822" FT VARIANT 161 FT /note="N -> S (in EPPK1; 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 EPPK1; dbSNP:rs59296273)" FT /evidence="ECO:0000269|PubMed:7511021" FT /id="VAR_010503" FT VARIANT 163 FT /note="R -> P (in EPPK1; dbSNP:rs57758262)" FT /evidence="ECO:0000269|PubMed:15605275" FT /id="VAR_036808" FT VARIANT 163 FT /note="R -> Q (in EPPK1; 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 EPPK1; 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 EPPK1)" FT /evidence="ECO:0000269|PubMed:15099359" FT /id="VAR_036809" FT VARIANT 168 FT /note="L -> S (in EPPK1; dbSNP:rs61157095)" FT /evidence="ECO:0000269|PubMed:7532199" FT /id="VAR_003825" FT VARIANT 171 FT /note="V -> M (in EPPK1; dbSNP:rs57019720)" FT /evidence="ECO:0000269|PubMed:12072061" FT /id="VAR_035439" FT VARIANT 172 FT /note="Q -> P (in EPPK1; dbSNP:rs59878153)" FT /evidence="ECO:0000269|PubMed:7516304" FT /id="VAR_010504" FT VARIANT 406 FT /note="C -> R (in EPPK1; dbSNP:rs77688767)" FT /evidence="ECO:0000269|PubMed:20964665" FT /id="VAR_071978" FT VARIANT 454 FT /note="Y -> H (in EPPK1; dbSNP:rs267607420)" FT /evidence="ECO:0000269|PubMed:19874353" FT /id="VAR_071979" FT VARIANT 458 FT /note="L -> F (in EPPK1; dbSNP:rs58120120)" FT /evidence="ECO:0000269|PubMed:16911293" FT /id="VAR_036810" FT VARIANT 458 FT /note="L -> P (in EPPK1)" 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 //