ID K2C1_HUMAN Reviewed; 644 AA. AC P04264; B2RA01; P85925; P86104; Q14720; Q6GSJ0; Q9H298; DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot. DT 26-MAY-2009, sequence version 6. DT 27-MAR-2024, entry version 254. DE RecName: Full=Keratin, type II cytoskeletal 1; DE AltName: Full=67 kDa cytokeratin; DE AltName: Full=Cytokeratin-1; DE Short=CK-1; DE AltName: Full=Hair alpha protein; DE AltName: Full=Keratin-1; DE Short=K1; DE AltName: Full=Type-II keratin Kb1; GN Name=KRT1; Synonyms=KRTA; 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 VARIANTS ASN-358 AND ARG-633. RX PubMed=2580302; DOI=10.1073/pnas.82.7.1896; RA Johnson L.D., Idler W.W., Zhou X.-M., Roop D.R., Steinert P.M.; RT "Structure of a gene for the human epidermal 67-kDa keratin."; RL Proc. Natl. Acad. Sci. U.S.A. 82:1896-1900(1985). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASN-358 AND ARG-633. RX PubMed=10903910; DOI=10.1006/bbrc.2000.3110; RA Whittock N.V., Eady R.A.J., McGrath J.A.; RT "Genomic organization and amplification of the human epidermal type II RT keratin genes K1 and K5."; RL Biochem. Biophys. Res. Commun. 274:149-152(2000). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INVOLVEMENT IN EPPK2, AND VARIANT RP ARG-633. RX PubMed=11286630; DOI=10.1046/j.1523-1747.2001.13041234.x; RA Hatsell S.J., Eady R.A.J., Wennerstrand L., Dopping-Hepenstal P.J., RA Leigh I.M., Munro C., Kelsell D.P.; RT "Novel splice site mutation in keratin 1 underlies mild epidermolytic RT palmoplantar keratoderma in three kindreds."; RL J. Invest. Dermatol. 116:606-609(2001). RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-633. RC TISSUE=Skin; 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 2-8. RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., RA Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass spectrometric RT identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [8] RP PROTEIN SEQUENCE OF 13-30; 66-82; 186-240; 258-276; 278-298; 344-355; RP 365-386; 396-403; 408-416; 418-432; 442-455 AND 461-588, METHYLATION AT RP ARG-82 AND LYS-276, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Ovarian carcinoma; RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.; RL Submitted (DEC-2008) to UniProtKB. RN [9] RP PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] OF 152-644, AND VARIANTS CYS-537 AND RP ARG-633. RX PubMed=2581964; DOI=10.1016/s0021-9258(18)88900-1; RA Steinert P.M., Parry D.A.D., Idler W.W., Johnson L.D., Steven A.C., RA Roop D.R.; RT "Amino acid sequences of mouse and human epidermal type II keratins of Mr RT 67,000 provide a systematic basis for the structural and functional RT diversity of the end domains of keratin intermediate filament subunits."; RL J. Biol. Chem. 260:7142-7149(1985). RN [10] RP PROTEIN SEQUENCE OF 377-386, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Fetal brain cortex; RA Lubec G., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [11] RP CITRULLINATION. RX PubMed=8780679; DOI=10.1006/bbrc.1996.1240; RA Senshu T., Kan S., Ogawa H., Manabe M., Asaga H.; RT "Preferential deimination of keratin K1 and filaggrin during the terminal RT differentiation of human epidermis."; RL Biochem. Biophys. Res. Commun. 225:712-719(1996). RN [12] RP INVOLVEMENT IN IHCM. RX PubMed=11286616; DOI=10.1046/j.1523-1747.2001.01292.x; RA Sprecher E., Ishida-Yamamoto A., Becker O.M., Marekov L.N., Miller C.J., RA Steinert P.M., Neldner K., Richard G.; RT "Evidence for novel functions of the keratin tail emerging from a mutation RT causing ichthyosis hystrix."; RL J. Invest. Dermatol. 116:511-519(2001). RN [13] RP CITRULLINATION. RX PubMed=11841545; DOI=10.1046/j.0022-202x.2001.01671.x; RA Ishida-Yamamoto A., Senshu T., Eady R.A.J., Takahashi H., Shimizu H., RA Akiyama M., Iizuka H.; RT "Sequential reorganization of cornified cell keratin filaments involving RT filaggrin-mediated compaction and keratin 1 deimination."; RL J. Invest. Dermatol. 118:282-287(2002). RN [14] RP INVOLVEMENT IN SPPK3. RX PubMed=11982762; DOI=10.1046/j.1523-1747.2002.01750.x; RA Whittock N.V., Smith F.J., Wan H., Mallipeddi R., Griffiths W.A.D., RA Dopping-Hepenstal P.J., Ashton G.H.S., Eady R.A.J., McLean W.H.I., RA McGrath J.A.; RT "Frameshift mutation in the V2 domain of human keratin 1 results in striate RT palmoplantar keratoderma."; RL J. Invest. Dermatol. 118:838-844(2002). RN [15] 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 [16] RP INTERACTION WITH EPPK1. RX PubMed=16923132; DOI=10.1111/j.1346-8138.2006.00127.x; RA Wang W., Sumiyoshi H., Yoshioka H., Fujiwara S.; RT "Interactions between epiplakin and intermediate filaments."; RL J. Dermatol. 33:518-527(2006). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=16529377; DOI=10.1094/mpmi-19-0150; RA Smith J.A., Blanchette R.A., Burnes T.A., Jacobs J.J., Higgins L., RA Witthuhn B.A., David A.J., Gillman J.H.; RT "Proteomic comparison of needles from blister rust-resistant and RT susceptible Pinus strobus seedlings reveals upregulation of putative RT disease resistance proteins."; RL Mol. Plant Microbe Interact. 19:150-160(2006). RN [18] RP FUNCTION, INTERACTION WITH RACK1 AND ITGB1, SUBCELLULAR LOCATION, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=17956333; DOI=10.1042/bst0351292; RA Chuang N.N., Huang C.C.; RT "Interaction of integrin beta1 with cytokeratin 1 in neuroblastoma NMB7 RT cells."; RL Biochem. Soc. Trans. 35:1292-1294(2007). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=18602030; DOI=10.1016/j.jprot.2008.06.004; RA Islam M.A., Sturrock R.N., Ekramoddoullah A.K.M.; RT "A proteomics approach to identify proteins differentially expressed in RT Douglas-fir seedlings infected by Phellinus sulphurascens."; RL J. Proteomics 71:425-438(2008). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, 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 [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [22] RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Xylem; RX PubMed=19412582; DOI=10.1007/s12010-009-8620-1; RA Basha S.M., Mazhar H., Vasanthaiah H.K.N.; RT "Proteomics approach to identify unique xylem sap proteins in Pierce's RT disease-tolerant Vitis species."; RL Appl. Biochem. Biotechnol. 160:932-944(2010). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-66 AND SER-344, AND RP IDENTIFICATION BY 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 [24] 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 [25] RP FUNCTION, AND INTERACTION WITH C1QBP. RX PubMed=21544310; DOI=10.1160/th10-09-0591; RA Pixley R.A., Espinola R.G., Ghebrehiwet B., Joseph K., Kao A., Bdeir K., RA Cines D.B., Colman R.W.; RT "Interaction of high-molecular-weight kininogen with endothelial cell RT binding proteins suPAR, gC1qR and cytokeratin 1 determined by surface RT plasmon resonance (BiaCore)."; RL Thromb. Haemost. 105:1053-1059(2011). RN [26] RP CORRECTION OF SPECIES OF ORIGIN. RX PubMed=23895828; DOI=10.1016/j.jprot.2013.07.009; RA Nawrot R., Barylski J., Schulze W.X.; RT "Incorrectly annotated keratin derived peptide sequences lead to misleading RT MS/MS data interpretation."; RL J. Proteomics 91:270-273(2013). RN [27] RP INTERACTION WITH PLEC AND KRT10. RX PubMed=24940650; DOI=10.1038/jid.2014.255; RA Bouameur J.E., Favre B., Fontao L., Lingasamy P., Begre N., Borradori L.; RT "Interaction of plectin with keratins 5 and 14: dependence on several RT plectin domains and keratin quaternary structure."; RL J. Invest. Dermatol. 134:2776-2783(2014). RN [28] 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 [29] 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 [30] RP SUBCELLULAR LOCATION, AND INDUCTION BY ATRA. RX PubMed=32179842; DOI=10.1038/s41598-020-61640-9; RA Aldehlawi H., Usman S., Lalli A., Ahmad F., Williams G., Teh M.T., RA Waseem A.; RT "Serum lipids, retinoic acid and phenol red differentially regulate RT expression of keratins K1, K10 and K2 in cultured keratinocytes."; RL Sci. Rep. 10:4829-4829(2020). RN [31] {ECO:0007744|PDB:4ZRY} RP X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 370-489 IN COMPLEX WITH KRT10, RP AND SUBUNIT. RX PubMed=27595935; DOI=10.1016/j.jid.2016.08.018; RA Bunick C.G., Milstone L.M.; RT "The X-Ray Crystal Structure of the Keratin1-Keratin 10 Helix 2B RT Heterodimer Reveals Molecular Surface Properties and Biochemical Insights RT into Human Skin Disease."; RL J. Invest. Dermatol. 137:142-150(2017). RN [32] RP VARIANT EHK1 PRO-161. RX PubMed=1381288; DOI=10.1016/0092-8674(92)90315-4; RA Chipev C.C., Korge B.P., Markova N., Bale S.J., Digiovanna J.J., RA Compton J.G., Steinert P.M.; RT "A leucine-->proline mutation in the H1 subdomain of keratin 1 causes RT epidermolytic hyperkeratosis."; RL Cell 70:821-828(1992). RN [33] RP VARIANT ALLELE 1B 560-GLY--TYR-566 DEL. RX PubMed=1281859; DOI=10.1111/1523-1747.ep12614149; RA Korge B.P., Compton J.G., Steinert P.M., Mischke D.; RT "The two size alleles of human keratin 1 are due to a deletion in the RT glycine-rich carboxyl-terminal V2 subdomain."; RL J. Invest. Dermatol. 99:697-702(1992). RN [34] RP VARIANT EHK1 GLN-490. RX PubMed=1380725; DOI=10.1126/science.257.5073.1128; RA Rothnagel J.A., Dominey A.M., Dempsey L.D., Longley M.A., Greenhalgh D.A., RA Gagne T.A., Huber M., Frenk E., Hohl D., Roop D.R.; RT "Mutations in the rod domains of keratins 1 and 10 in epidermolytic RT hyperkeratosis."; RL Science 257:1128-1130(1992). RN [35] RP VARIANT EHK1 CYS-482. RX PubMed=7512983; DOI=10.1172/jci117132; RA Syder A.J., Yu Q.-C., Paller A.S., Giudice G., Pearson R., Fuchs E.; RT "Genetic mutations in the K1 and K10 genes of patients with epidermolytic RT hyperkeratosis. Correlation between location and disease severity."; RL J. Clin. Invest. 93:1533-1542(1994). RN [36] RP VARIANTS EHK1 GLY-155; SER-188 AND PRO-193. RX PubMed=7507151; DOI=10.1111/1523-1747.ep12371725; RA Yang J.-M., Chipev C.C., Digiovanna J.J., Bale S.J., Marekov L.N., RA Steinert P.M., Compton J.G.; RT "Mutations in the H1 and 1A domains in the keratin 1 gene in epidermolytic RT hyperkeratosis."; RL J. Invest. Dermatol. 102:17-23(1994). RN [37] RP VARIANTS EHK1 PRO-186 AND SER-188. RX PubMed=7507152; DOI=10.1111/1523-1747.ep12371726; RA McLean W.H.I., Eady R.A.J., Dopping-Hepenstal P.J.C., McMillan J.R., RA Leigh I.M., Navsaria H.A., Higgins C., Harper J.I., Paige D.G., RA Morley S.M.; RT "Mutations in the rod 1A domain of keratins 1 and 10 in bullous congenital RT ichthyosiform erythroderma (BCIE)."; RL J. Invest. Dermatol. 102:24-30(1994). RN [38] RP VARIANT NEPPK ILE-74. RX PubMed=7528239; DOI=10.1111/1523-1747.ep12412771; RA Kimonis V., DiGiovanna J.J., Yang J.-M., Doyle S.Z., Bale S.J., RA Compton J.G.; RT "A mutation in the V1 end domain of keratin 1 in non-epidermolytic palmar- RT plantar keratoderma."; RL J. Invest. Dermatol. 103:764-769(1994). RN [39] RP VARIANT EHK1 VAL-340. RX PubMed=9856846; DOI=10.1046/j.1523-1747.1998.00389.x; RA Kremer H., Lavrijsen A.P., McLean W.H.I., Lane E.B., Melchers D., RA Ruiter D.J., Mariman E.C., Steijlen P.M.; RT "An atypical form of bullous congenital ichthyosiform erythroderma is RT caused by a mutation in the L12 linker region of keratin 1."; RL J. Invest. Dermatol. 111:1224-1226(1998). RN [40] RP VARIANTS AEI2 PHE-479 AND THR-479. RX PubMed=10053007; DOI=10.1086/302278; RA Sybert V.P., Francis J.S., Corden L.D., Smith L.T., Weaver M., Stephens K., RA McLean W.H.I.; RT "Cyclic ichthyosis with epidermolytic hyperkeratosis: a phenotype conferred RT by mutations in the 2B domain of keratin K1."; RL Am. J. Hum. Genet. 64:732-738(1999). RN [41] RP VARIANT EHK1 THR-188. RX PubMed=10232403; DOI=10.1111/j.1600-0625.1999.tb00359.x; RA Arin M.J., Longley M.A., Kuster W., Huber M., Hohl D., Rothnagel J.A., RA Roop D.R.; RT "An asparagine to threonine substitution in the 1A domain of keratin 1: a RT novel mutation that causes epidermolytic hyperkeratosis."; RL Exp. Dermatol. 8:124-127(1999). RN [42] RP VARIANT AEI2 PHE-479. RX PubMed=10597140; DOI=10.1111/j.1600-0625.1999.tb00309.x; RA Michael E.J., Schneiderman P., Grossman M.E., Christiano A.M.; RT "Epidermolytic hyperkeratosis with polycyclic psoriasiform plaques RT resulting from a mutation in the keratin 1 gene."; RL Exp. Dermatol. 8:501-503(1999). RN [43] RP VARIANT EHK1 PRO-214. RX PubMed=10844506; DOI=10.1046/j.1365-2230.2000.00625.x; RA Cserhalmi-Friedman P.B., Squeo R., Gordon D., Garzon M., Schneiderman P., RA Grossman M.E., Christiano A.M.; RT "Epidermolytic hyperkeratosis in a Hispanic family resulting from a RT mutation in the keratin 1 gene."; RL Clin. Exp. Dermatol. 25:241-243(2000). RN [44] RP VARIANT EHK1 THR-479. RX PubMed=10688370; DOI=10.1034/j.1600-0625.2000.009001016.x; RA Arin M.J., Longley M.A., Epstein E.H. Jr., Rothnagel J.A., Roop D.R.; RT "Identification of a novel mutation in keratin 1 in a family with RT epidermolytic hyperkeratosis."; RL Exp. Dermatol. 9:16-19(2000). RN [45] RP VARIANT EHK1 ASP-155. RX PubMed=11531804; DOI=10.1046/j.1365-2133.2001.04327.x; RA Whittock N.V., Ashton G.H.S., Griffiths W.A.D., Eady R.A.J., McGrath J.A.; RT "New mutations in keratin 1 that cause bullous congenital ichthyosiform RT erythroderma and keratin 2e that cause ichthyosis bullosa of Siemens."; RL Br. J. Dermatol. 145:330-335(2001). RN [46] RP VARIANTS PALMOPLANTAR KERATODERMA 176-VAL--LYS-197 DEL AND 459-ALA--GLN-466 RP DEL. RX PubMed=12406346; DOI=10.1046/j.1523-1747.2002.00186.x; RA Terron-Kwiatkowski A., Paller A.S., Compton J., Atherton D.J., McLean W.H., RA Irvine A.D.; RT "Two cases of primarily palmoplantar keratoderma associated with novel RT mutations in keratin 1."; RL J. Invest. Dermatol. 119:966-971(2002). RN [47] RP VARIANTS EHK1 LYS-188 AND PRO-486. RX PubMed=12406348; DOI=10.1046/j.1523-1747.2002.00061.x; RA Lee D.-Y., Ahn K.-S., Lee C.-H., Rho N.-K., Lee J.-H., Lee E.-S., RA Steinert P.M., Yang J.-M.; RT "Two novel mutations in the keratin 1 gene in epidermolytic RT hyperkeratosis."; RL J. Invest. Dermatol. 119:976-977(2002). RN [48] RP VARIANTS EHK1 LYS-188; SER-188; GLN-478; THR-479; PRO-485; PRO-486 AND RP LYS-490. RX PubMed=21271994; DOI=10.1111/j.1365-2133.2010.10096.x; RA Arin M.J., Oji V., Emmert S., Hausser I., Traupe H., Krieg T., Grimberg G.; RT "Expanding the keratin mutation database: novel and recurrent mutations and RT genotype-phenotype correlations in 28 patients with epidermolytic RT ichthyosis."; RL Br. J. Dermatol. 164:442-447(2011). RN [49] RP VARIANT EPPK2 ASP-436, AND INVOLVEMENT IN EPPK2. RX PubMed=37122192; DOI=10.1111/1346-8138.16815; RA Nakamizo S., Murata T., Ishida Y., Aoki S., Sasaki T., Kubo A., RA Kabashima K.; RT "A Japanese case of Voerner-type palmoplantar keratoderma caused by a novel RT KRT1 variant."; RL J. Dermatol. 50:e307-e308(2023). CC -!- FUNCTION: May regulate the activity of kinases such as PKC and SRC via CC binding to integrin beta-1 (ITB1) and the receptor of activated protein CC C kinase 1 (RACK1). In complex with C1QBP is a high affinity receptor CC for kininogen-1/HMWK. {ECO:0000269|PubMed:17956333, CC ECO:0000269|PubMed:21544310}. CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins CC (PubMed:24940650, PubMed:27595935). Heterodimer with KRT10 CC (PubMed:24940650, PubMed:27595935). Two heterodimers of KRT1 and KRT10 CC form a heterotetramer (PubMed:27595935). Forms a heterodimer with CC KRT14; the interaction is more abundant in the absence of KRT5 (By CC similarity). Interacts with PLEC isoform 1C, when in a heterodimer with CC KRT10 (PubMed:24940650). Interacts with ITGB1 in the presence of RACK1 CC and SRC, and with RACK1 (PubMed:17956333). Interacts with C1QBP; the CC association represents a cell surface kininogen receptor CC (PubMed:21544310). Interacts with EPPK1; interaction is dependent of CC higher-order structure of intermediate filament (PubMed:16923132). CC {ECO:0000250|UniProtKB:P04104, ECO:0000269|PubMed:16923132, CC ECO:0000269|PubMed:17956333, ECO:0000269|PubMed:21544310, CC ECO:0000269|PubMed:24940650, ECO:0000269|PubMed:27595935}. CC -!- INTERACTION: CC P04264; Q9Y2J4: AMOTL2; NbExp=3; IntAct=EBI-298429, EBI-746752; CC P04264; O15552: FFAR2; NbExp=3; IntAct=EBI-298429, EBI-2833872; CC P04264; Q08379: GOLGA2; NbExp=6; IntAct=EBI-298429, EBI-618309; CC P04264; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-298429, EBI-5916454; CC P04264; Q96CS2: HAUS1; NbExp=3; IntAct=EBI-298429, EBI-2514791; CC P04264; Q9NP66: HMG20A; NbExp=3; IntAct=EBI-298429, EBI-740641; CC P04264; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-298429, EBI-10961706; CC P04264; P13645: KRT10; NbExp=5; IntAct=EBI-298429, EBI-465144; CC P04264; P13646: KRT13; NbExp=3; IntAct=EBI-298429, EBI-1223876; CC P04264; P02533: KRT14; NbExp=3; IntAct=EBI-298429, EBI-702178; CC P04264; P19012: KRT15; NbExp=7; IntAct=EBI-298429, EBI-739566; CC P04264; P08779: KRT16; NbExp=3; IntAct=EBI-298429, EBI-356410; CC P04264; P08727: KRT19; NbExp=3; IntAct=EBI-298429, EBI-742756; CC P04264; Q2M2I5: KRT24; NbExp=3; IntAct=EBI-298429, EBI-2952736; CC P04264; Q7Z3Z0: KRT25; NbExp=3; IntAct=EBI-298429, EBI-11980019; CC P04264; Q7Z3Y9: KRT26; NbExp=3; IntAct=EBI-298429, EBI-12084444; CC P04264; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-298429, EBI-3044087; CC P04264; Q7Z3Y7: KRT28; NbExp=5; IntAct=EBI-298429, EBI-11980489; CC P04264; Q15323: KRT31; NbExp=3; IntAct=EBI-298429, EBI-948001; CC P04264; Q14525: KRT33B; NbExp=7; IntAct=EBI-298429, EBI-1049638; CC P04264; O76011: KRT34; NbExp=3; IntAct=EBI-298429, EBI-1047093; CC P04264; Q92764: KRT35; NbExp=3; IntAct=EBI-298429, EBI-1058674; CC P04264; O76013-2: KRT36; NbExp=3; IntAct=EBI-298429, EBI-11958506; CC P04264; O76014: KRT37; NbExp=3; IntAct=EBI-298429, EBI-1045716; CC P04264; O76015: KRT38; NbExp=3; IntAct=EBI-298429, EBI-1047263; CC P04264; Q6A163: KRT39; NbExp=3; IntAct=EBI-298429, EBI-11958242; CC P04264; P37198: NUP62; NbExp=7; IntAct=EBI-298429, EBI-347978; CC P04264; Q6NUQ1: RINT1; NbExp=3; IntAct=EBI-298429, EBI-726876; CC P04264; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-298429, EBI-744081; CC P04264; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-298429, EBI-1105213; CC P04264; Q96MV1: TLCD4; NbExp=3; IntAct=EBI-298429, EBI-12947623; CC P04264; P14373: TRIM27; NbExp=4; IntAct=EBI-298429, EBI-719493; CC P04264; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-298429, EBI-2130429; CC P04264; Q01081: U2AF1; NbExp=3; IntAct=EBI-298429, EBI-632461; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17956333}. CC Cytoplasm {ECO:0000269|PubMed:32179842}. CC -!- TISSUE SPECIFICITY: The source of this protein is neonatal foreskin. CC The 67-kDa type II keratins are expressed in terminally differentiating CC epidermis. CC -!- INDUCTION: Repressed in keratinocytes by all-trans retinoic acid CC (ATRA), via reduction of mRNA stability. {ECO:0000269|PubMed:32179842}. CC -!- PTM: Undergoes deimination of some arginine residues (citrullination). CC {ECO:0000269|PubMed:11841545, ECO:0000269|PubMed:8780679}. CC -!- POLYMORPHISM: There are two size variants of KRT1, termed allele 1A and CC allele 1B with allelic frequencies of 0.61 and 0.39. Allele 1B lacks 7 CC residues compared to allele 1A. CC -!- DISEASE: Epidermolytic hyperkeratosis 1 (EHK1) [MIM:113800]: A skin CC disorder characterized by widespread blistering and an ichthyotic CC erythroderma at birth that persist into adulthood. Histologically there CC is a diffuse epidermolytic degeneration in the lower spinous layer of CC the epidermis. Within a few weeks from birth, erythroderma and blister CC formation diminish and hyperkeratoses develop. EHK1 inheritance is CC autosomal dominant or autosomal recessive. CC {ECO:0000269|PubMed:10232403, ECO:0000269|PubMed:10688370, CC ECO:0000269|PubMed:10844506, ECO:0000269|PubMed:11531804, CC ECO:0000269|PubMed:12406348, ECO:0000269|PubMed:1380725, CC ECO:0000269|PubMed:1381288, ECO:0000269|PubMed:21271994, CC ECO:0000269|PubMed:7507151, ECO:0000269|PubMed:7507152, CC ECO:0000269|PubMed:7512983, ECO:0000269|PubMed:9856846}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Ichthyosis hystrix, Curth-Macklin type (IHCM) [MIM:146590]: A CC genodermatosis with severe verrucous hyperkeratosis. Affected CC individuals manifest congenital verrucous black scale on the scalp, CC neck, and limbs with truncal erythema, palmoplantar keratoderma and CC keratoses on the lips, ears, nipples and buttocks. CC {ECO:0000269|PubMed:11286616}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Keratoderma, palmoplantar, non-epidermolytic (NEPPK) CC [MIM:600962]: A dermatological disorder characterized by well- CC demarcated hyperkeratosis is present over the palms and soles. A red CC band is frequently present at the periphery of the keratosis. It is CC usually non-transgredient, with a sharp demarcation of the lesions at CC the wrists. {ECO:0000269|PubMed:7528239}. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC -!- DISEASE: Ichthyosis, annular epidermolytic, 2 (AEI2) [MIM:620148]: A CC form of annular epidermolytic ichthyosis, an autosomal dominant skin CC disorder characterized by polycyclic, migratory erythematous and scaly CC plaques. AEI2 patients manifest erythema and blistering of skin at CC birth that improves without scarring, as well as palmoplantar CC keratoderma. {ECO:0000269|PubMed:10053007, CC ECO:0000269|PubMed:10597140}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Keratoderma, palmoplantar, striate 3 (SPPK3) [MIM:607654]: A CC dermatological disorder characterized by thickening of the stratum CC corneum and epidermal layers on palms and soles. There is no CC involvement of non-palmoplantar skin, and both hair and nails are CC normal. {ECO:0000269|PubMed:11982762}. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC -!- DISEASE: Palmoplantar keratoderma, epidermolytic, 2 (EPPK2) CC [MIM:620411]: 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. EPPK2 CC is an autosomal dominant form in which hyperkeratosis is restricted to CC palms and soles and is apparent from birth or childhood. CC {ECO:0000269|PubMed:11286630, ECO:0000269|PubMed:37122192}. 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; 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 -!- CAUTION: A peptide corresponding to residues 278 to 289 was isolated as CC part of plant proteomics studies and was originally thought to be of CC plant origin (PubMed:18602030, PubMed:19412582, PubMed:16529377). CC However, it was later shown that it is likely to be human type II CC keratin, a common contaminant in proteomic analyzes (PubMed:23895828). CC {ECO:0000305|PubMed:23895828}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Keratin-1 entry; CC URL="https://en.wikipedia.org/wiki/Keratin_1"; 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; M98776; AAB47721.1; -; Genomic_DNA. DR EMBL; AF237621; AAF60327.1; -; Genomic_DNA. DR EMBL; AF304164; AAG41947.1; -; Genomic_DNA. DR EMBL; AK313986; BAG36698.1; -; mRNA. DR EMBL; AC055716; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC063697; AAH63697.1; -; mRNA. DR EMBL; M10938; AAA36153.1; -; mRNA. DR CCDS; CCDS8836.1; -. DR PIR; A22940; KRHU2. DR RefSeq; NP_006112.3; NM_006121.3. DR PDB; 4ZRY; X-ray; 3.30 A; B=370-489. DR PDB; 6E2J; X-ray; 2.39 A; A=226-331. DR PDB; 6UUI; X-ray; 2.07 A; C=370-489. DR PDBsum; 4ZRY; -. DR PDBsum; 6E2J; -. DR PDBsum; 6UUI; -. DR AlphaFoldDB; P04264; -. DR SMR; P04264; -. DR BioGRID; 110046; 214. DR ComplexPortal; CPX-5662; Keratin-1 - Keratin-10 dimer complex. DR IntAct; P04264; 76. DR MINT; P04264; -. DR STRING; 9606.ENSP00000252244; -. DR DrugBank; DB09130; Copper. DR DrugBank; DB01593; Zinc. DR DrugBank; DB14487; Zinc acetate. DR GlyConnect; 1952; 3 N-Linked glycans (1 site). DR GlyCosmos; P04264; 4 sites, 4 glycans. DR GlyGen; P04264; 7 sites, 3 N-linked glycans (1 site), 2 O-linked glycans (6 sites). DR iPTMnet; P04264; -. DR PhosphoSitePlus; P04264; -. DR SwissPalm; P04264; -. DR BioMuta; KRT1; -. DR DMDM; 238054406; -. DR REPRODUCTION-2DPAGE; P04264; -. DR EPD; P04264; -. DR jPOST; P04264; -. DR MassIVE; P04264; -. DR PaxDb; 9606-ENSP00000252244; -. DR PeptideAtlas; P04264; -. DR PRIDE; P04264; -. DR ProteomicsDB; 51694; -. DR Antibodypedia; 3686; 1316 antibodies from 40 providers. DR DNASU; 3848; -. DR Ensembl; ENST00000252244.3; ENSP00000252244.3; ENSG00000167768.4. DR GeneID; 3848; -. DR KEGG; hsa:3848; -. DR MANE-Select; ENST00000252244.3; ENSP00000252244.3; NM_006121.4; NP_006112.3. DR UCSC; uc001sau.1; human. DR AGR; HGNC:6412; -. DR CTD; 3848; -. DR DisGeNET; 3848; -. DR GeneCards; KRT1; -. DR HGNC; HGNC:6412; KRT1. DR HPA; ENSG00000167768; Tissue enriched (skin). DR MalaCards; KRT1; -. DR MIM; 113800; phenotype. DR MIM; 139350; gene. DR MIM; 146590; phenotype. DR MIM; 600962; phenotype. DR MIM; 607654; phenotype. DR MIM; 620148; phenotype. DR MIM; 620411; phenotype. DR neXtProt; NX_P04264; -. DR OpenTargets; ENSG00000167768; -. DR Orphanet; 281139; Annular epidermolytic ichthyosis. DR Orphanet; 312; Autosomal dominant epidermolytic ichthyosis. DR Orphanet; 281190; Congenital reticular ichthyosiform erythroderma. DR Orphanet; 2199; Epidermolytic palmoplantar keratoderma. DR Orphanet; 79503; Ichthyosis hystrix of Curth-Macklin. DR Orphanet; 530838; KRT1-related diffuse nonepidermolytic keratoderma. DR Orphanet; 538574; Palmoplantar keratoderma-hereditary motor and sensory neuropathy syndrome. DR Orphanet; 50942; Striate palmoplantar keratoderma. DR PharmGKB; PA30199; -. DR VEuPathDB; HostDB:ENSG00000167768; -. DR eggNOG; ENOG502QQIF; Eukaryota. DR GeneTree; ENSGT00940000162175; -. DR HOGENOM; CLU_012560_6_0_1; -. DR InParanoid; P04264; -. DR OMA; FGMAPGK; -. DR OrthoDB; 4640531at2759; -. DR PhylomeDB; P04264; -. DR TreeFam; TF317854; -. DR PathwayCommons; P04264; -. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR Reactome; R-HSA-6805567; Keratinization. DR Reactome; R-HSA-6809371; Formation of the cornified envelope. DR SignaLink; P04264; -. DR SIGNOR; P04264; -. DR BioGRID-ORCS; 3848; 21 hits in 1152 CRISPR screens. DR ChiTaRS; KRT1; human. DR GeneWiki; Keratin_1; -. DR GenomeRNAi; 3848; -. DR Pharos; P04264; Tbio. DR PRO; PR:P04264; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; P04264; Protein. DR Bgee; ENSG00000167768; Expressed in upper leg skin and 108 other cell types or tissues. DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB. DR GO; GO:0001533; C:cornified envelope; IDA:CAFA. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005856; C:cytoskeleton; TAS:ProtInc. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB. DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome. DR GO; GO:0045095; C:keratin filament; IPI:ComplexPortal. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; HDA:UniProtKB. DR GO; GO:0030246; F:carbohydrate binding; IPI:UniProtKB. DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB. DR GO; GO:0038023; F:signaling receptor activity; NAS:UniProtKB. DR GO; GO:0030280; F:structural constituent of skin epidermis; IDA:CAFA. DR GO; GO:0001867; P:complement activation, lectin pathway; IPI:UniProtKB. DR GO; GO:0061436; P:establishment of skin barrier; IEA:Ensembl. DR GO; GO:0042730; P:fibrinolysis; NAS:UniProtKB. DR GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central. DR GO; GO:0031424; P:keratinization; IBA:GO_Central. DR GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl. DR GO; GO:0018149; P:peptide cross-linking; IDA:CAFA. DR GO; GO:0051290; P:protein heterotetramerization; IDA:UniProtKB. DR GO; GO:0045765; P:regulation of angiogenesis; NAS:UniProtKB. DR GO; GO:0006979; P:response to oxidative stress; NAS:UniProtKB. 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; IPR032449; Keratin_2_1_tail. DR InterPro; IPR032444; Keratin_2_head. DR InterPro; IPR003054; Keratin_II. DR PANTHER; PTHR45616; GATA-TYPE DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR45616:SF33; KERATIN, TYPE II CYTOSKELETAL 1; 1. DR Pfam; PF00038; Filament; 1. DR Pfam; PF16208; Keratin_2_head; 1. DR Pfam; PF16210; Keratin_2_tail; 1. DR PRINTS; PR01276; TYPE2KERATIN. DR SMART; SM01391; Filament; 1. DR SUPFAM; SSF64593; Intermediate filament protein, coiled coil region; 3. DR PROSITE; PS00226; IF_ROD_1; 1. DR PROSITE; PS51842; IF_ROD_2; 1. DR SWISS-2DPAGE; P04264; -. DR Genevisible; P04264; HS. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Citrullination; Coiled coil; Cytoplasm; KW Direct protein sequencing; Disease variant; Ichthyosis; KW Intermediate filament; Keratin; Membrane; Methylation; KW Palmoplantar keratoderma; Phosphoprotein; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:12665801" FT CHAIN 2..644 FT /note="Keratin, type II cytoskeletal 1" FT /id="PRO_0000063709" FT DOMAIN 180..493 FT /note="IF rod" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188" FT REGION 2..179 FT /note="Head" FT REGION 22..47 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 180..215 FT /note="Coil 1A" FT REGION 216..234 FT /note="Linker 1" FT REGION 235..326 FT /note="Coil 1B" FT REGION 327..350 FT /note="Linker 12" FT REGION 351..489 FT /note="Coil 2" FT REGION 489..523 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 490..644 FT /note="Tail" FT REGION 568..644 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 22..42 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 497..515 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 602..644 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 433 FT /note="Stutter" FT MOD_RES 12 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:P04104" FT MOD_RES 18 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P04104" FT MOD_RES 21 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231" FT MOD_RES 45 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:P04104" FT MOD_RES 66 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:20068231" FT MOD_RES 82 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000269|Ref.8" FT MOD_RES 276 FT /note="N6,N6-dimethyllysine" FT /evidence="ECO:0000269|Ref.8" FT MOD_RES 344 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 518 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:P04104" FT MOD_RES 588 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:P04104" FT VARIANT 74 FT /note="K -> I (in NEPPK; dbSNP:rs57977969)" FT /evidence="ECO:0000269|PubMed:7528239" FT /id="VAR_017819" FT VARIANT 155 FT /note="V -> D (in EHK1; dbSNP:rs57959072)" FT /evidence="ECO:0000269|PubMed:11531804" FT /id="VAR_017820" FT VARIANT 155 FT /note="V -> G (in EHK1; dbSNP:rs57959072)" FT /evidence="ECO:0000269|PubMed:7507151" FT /id="VAR_003853" FT VARIANT 161 FT /note="L -> P (in EHK1; dbSNP:rs57695159)" FT /evidence="ECO:0000269|PubMed:1381288" FT /id="VAR_003854" FT VARIANT 176..197 FT /note="Missing (in palmoplantar keratoderma; and mild FT ichthyosis largely limited to the flexural areas)" FT /id="VAR_038627" FT VARIANT 186 FT /note="S -> P (in EHK1; dbSNP:rs60022878)" FT /evidence="ECO:0000269|PubMed:7507152" FT /id="VAR_003855" FT VARIANT 188 FT /note="N -> K (in EHK1; dbSNP:rs59429455)" FT /evidence="ECO:0000269|PubMed:12406348, FT ECO:0000269|PubMed:21271994" FT /id="VAR_017821" FT VARIANT 188 FT /note="N -> S (in EHK1; dbSNP:rs58928370)" FT /evidence="ECO:0000269|PubMed:21271994, FT ECO:0000269|PubMed:7507151, ECO:0000269|PubMed:7507152" FT /id="VAR_003856" FT VARIANT 188 FT /note="N -> T (in EHK1; severe; dbSNP:rs58928370)" FT /evidence="ECO:0000269|PubMed:10232403" FT /id="VAR_017822" FT VARIANT 193 FT /note="S -> P (in EHK1; dbSNP:rs60937700)" FT /evidence="ECO:0000269|PubMed:7507151" FT /id="VAR_003857" FT VARIANT 214 FT /note="L -> P (in EHK1; dbSNP:rs61549035)" FT /evidence="ECO:0000269|PubMed:10844506" FT /id="VAR_017823" FT VARIANT 312 FT /note="I -> V" FT /id="VAR_003858" FT VARIANT 330 FT /note="I -> T" FT /id="VAR_003859" FT VARIANT 340 FT /note="D -> V (in EHK1; dbSNP:rs58062863)" FT /evidence="ECO:0000269|PubMed:9856846" FT /id="VAR_017824" FT VARIANT 358 FT /note="Y -> N (in dbSNP:rs1050872)" FT /evidence="ECO:0000269|PubMed:10903910, FT ECO:0000269|PubMed:2580302" FT /id="VAR_003860" FT VARIANT 436 FT /note="A -> D (in EPPK2; uncertain significance)" FT /evidence="ECO:0000269|PubMed:37122192" FT /id="VAR_088636" FT VARIANT 454 FT /note="A -> S (in dbSNP:rs17678945)" FT /id="VAR_038628" FT VARIANT 459..466 FT /note="Missing (in palmoplantar keratoderma; and mild FT ichthyosis largely limited to the flexural areas)" FT /id="VAR_038629" FT VARIANT 478 FT /note="E -> Q (in EHK1; dbSNP:rs59089201)" FT /evidence="ECO:0000269|PubMed:21271994" FT /id="VAR_071986" FT VARIANT 479 FT /note="I -> F (in AEI2; dbSNP:rs61218439)" FT /evidence="ECO:0000269|PubMed:10053007, FT ECO:0000269|PubMed:10597140" FT /id="VAR_017825" FT VARIANT 479 FT /note="I -> T (in AEI2 and EHK1; dbSNP:rs57837128)" FT /evidence="ECO:0000269|PubMed:10053007, FT ECO:0000269|PubMed:10688370, ECO:0000269|PubMed:21271994" FT /id="VAR_017826" FT VARIANT 482 FT /note="Y -> C (in EHK1; dbSNP:rs58420087)" FT /evidence="ECO:0000269|PubMed:7512983" FT /id="VAR_017827" FT VARIANT 485 FT /note="L -> P (in EHK1; dbSNP:rs267607430)" FT /evidence="ECO:0000269|PubMed:21271994" FT /id="VAR_071987" FT VARIANT 486 FT /note="L -> P (in EHK1; dbSNP:rs56914602)" FT /evidence="ECO:0000269|PubMed:12406348, FT ECO:0000269|PubMed:21271994" FT /id="VAR_017828" FT VARIANT 490 FT /note="E -> K (in EHK1; dbSNP:rs60279707)" FT /evidence="ECO:0000269|PubMed:21271994" FT /id="VAR_071988" FT VARIANT 490 FT /note="E -> Q (in EHK1; dbSNP:rs60279707)" FT /evidence="ECO:0000269|PubMed:1380725" FT /id="VAR_003861" FT VARIANT 537 FT /note="G -> C" FT /evidence="ECO:0000269|PubMed:2581964" FT /id="VAR_003862" FT VARIANT 560..566 FT /note="Missing (in allele 1B)" FT /evidence="ECO:0000269|PubMed:1281859" FT /id="VAR_003864" FT VARIANT 633 FT /note="K -> R (in dbSNP:rs14024)" FT /evidence="ECO:0000269|PubMed:10903910, FT ECO:0000269|PubMed:11286630, ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:2580302, ECO:0000269|PubMed:2581964" FT /id="VAR_003863" FT CONFLICT 201 FT /note="L -> M (in Ref. 9; AAA36153)" FT /evidence="ECO:0000305" FT CONFLICT 206 FT /note="Q -> K (in Ref. 9; AAA36153)" FT /evidence="ECO:0000305" FT CONFLICT 238 FT /note="L -> S (in Ref. 9; AAA36153)" FT /evidence="ECO:0000305" FT CONFLICT 344..345 FT /note="SL -> QF (in Ref. 9; AAA36153)" FT /evidence="ECO:0000305" FT CONFLICT 403 FT /note="R -> H (in Ref. 4; BAG36698)" FT /evidence="ECO:0000305" FT CONFLICT 404 FT /note="V -> M (in Ref. 9; AAA36153)" FT /evidence="ECO:0000305" FT CONFLICT 447 FT /note="L -> M (in Ref. 9; AAA36153)" FT /evidence="ECO:0000305" FT CONFLICT 463 FT /note="R -> C (in Ref. 9; AAA36153)" FT /evidence="ECO:0000305" FT CONFLICT 466 FT /note="Q -> H (in Ref. 9; AAA36153)" FT /evidence="ECO:0000305" FT CONFLICT 504 FT /note="S -> T (in Ref. 9; AAA36153)" FT /evidence="ECO:0000305" FT CONFLICT 511..512 FT /note="TI -> SM (in Ref. 9; AAA36153)" FT /evidence="ECO:0000305" FT CONFLICT 564 FT /note="G -> S (in Ref. 9; AAA36153)" FT /evidence="ECO:0000305" FT CONFLICT 613 FT /note="I -> S (in Ref. 9; AAA36153)" FT /evidence="ECO:0000305" FT CONFLICT 638 FT /note="T -> S (in Ref. 9; AAA36153)" FT /evidence="ECO:0000305" FT HELIX 228..330 FT /evidence="ECO:0007829|PDB:6E2J" FT HELIX 384..488 FT /evidence="ECO:0007829|PDB:6UUI" SQ SEQUENCE 644 AA; 66039 MW; CE5DDE97388F5017 CRC64; MSRQFSSRSG YRSGGGFSSG SAGIINYQRR TTSSSTRRSG GGGGRFSSCG GGGGSFGAGG GFGSRSLVNL GGSKSISISV ARGGGRGSGF GGGYGGGGFG GGGFGGGGFG GGGIGGGGFG GFGSGGGGFG GGGFGGGGYG GGYGPVCPPG GIQEVTINQS LLQPLNVEID PEIQKVKSRE REQIKSLNNQ FASFIDKVRF LEQQNQVLQT KWELLQQVDT STRTHNLEPY FESFINNLRR RVDQLKSDQS RLDSELKNMQ DMVEDYRNKY EDEINKRTNA ENEFVTIKKD VDGAYMTKVD LQAKLDNLQQ EIDFLTALYQ AELSQMQTQI SETNVILSMD NNRSLDLDSI IAEVKAQYED IAQKSKAEAE SLYQSKYEEL QITAGRHGDS VRNSKIEISE LNRVIQRLRS EIDNVKKQIS NLQQSISDAE QRGENALKDA KNKLNDLEDA LQQAKEDLAR LLRDYQELMN TKLALDLEIA TYRTLLEGEE SRMSGECAPN VSVSVSTSHT TISGGGSRGG GGGGYGSGGS SYGSGGGSYG SGGGGGGGRG SYGSGGSSYG SGGGSYGSGG GGGGHGSYGS GSSSGGYRGG SGGGGGGSSG GRGSGGGSSG GSIGGRGSSS GGVKSSGGSS SVKFVSTTYS GVTR //