K2C1_HUMAN
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 03-AUG-2022, entry version 245.
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 NEPPK, 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 EHK 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 EHK 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 EHK 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 EHK 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 EHK 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 EHK 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 AEI 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 EHK 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 AEI 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 EHK 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 EHK 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 EHK 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 VAL-176--LYS-197 DEL AND ALA-459--466-GLN
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 EHK 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 EHK 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).
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 (EHK) [MIM:113800]: An autosomal
CC dominant skin disorder characterized by widespread blistering and an
CC ichthyotic erythroderma at birth that persist into adulthood.
CC Histologically there is a diffuse epidermolytic degeneration in the
CC lower spinous layer of the epidermis. Within a few weeks from birth,
CC erythroderma and blister formation diminish and hyperkeratoses develop.
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:11286630, ECO:0000269|PubMed:7528239}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- DISEASE: Ichthyosis annular epidermolytic (AEI) [MIM:607602]: A skin
CC disorder resembling bullous congenital ichthyosiform erythroderma.
CC Affected individuals present with bullous ichthyosis in early childhood
CC and hyperkeratotic lichenified plaques in the flexural areas and
CC extensor surfaces at later ages. The feature that distinguishes AEI
CC from BCIE is dramatic episodes of flares of annular polycyclic plaques
CC with scale, which coalesce to involve most of the body surface and can
CC persist for several weeks or even months. {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 -!- 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=Human Intermediate Filament Mutation Database;
CC URL="http://www.interfil.org";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Keratin-1 entry;
CC URL="https://en.wikipedia.org/wiki/Keratin_1";
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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; 179.
DR ComplexPortal; CPX-5662; Keratin-1 - Keratin-10 dimer complex.
DR IntAct; P04264; 72.
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 GlyGen; P04264; 4 sites, 3 N-linked glycans (1 site), 1 O-linked glycan (3 sites).
DR iPTMnet; P04264; -.
DR PhosphoSitePlus; P04264; -.
DR SwissPalm; P04264; -.
DR BioMuta; KRT1; -.
DR DMDM; 238054406; -.
DR REPRODUCTION-2DPAGE; P04264; -.
DR SWISS-2DPAGE; P04264; -.
DR EPD; P04264; -.
DR jPOST; P04264; -.
DR MassIVE; P04264; -.
DR PaxDb; P04264; -.
DR PeptideAtlas; P04264; -.
DR PRIDE; P04264; -.
DR ProteomicsDB; 51694; -.
DR Antibodypedia; 3686; 1237 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 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; 607602; phenotype.
DR MIM; 607654; 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; IRMSGEC; -.
DR OrthoDB; 824246at2759; -.
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; 16 hits in 1072 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 tissues.
DR Genevisible; P04264; HS.
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 GO; GO:0001895; P:retina homeostasis; HEP:UniProtKB.
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 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 PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
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 EHK; dbSNP:rs57959072)"
FT /evidence="ECO:0000269|PubMed:11531804"
FT /id="VAR_017820"
FT VARIANT 155
FT /note="V -> G (in EHK; dbSNP:rs57959072)"
FT /evidence="ECO:0000269|PubMed:7507151"
FT /id="VAR_003853"
FT VARIANT 161
FT /note="L -> P (in EHK; 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 EHK; dbSNP:rs60022878)"
FT /evidence="ECO:0000269|PubMed:7507152"
FT /id="VAR_003855"
FT VARIANT 188
FT /note="N -> K (in EHK; 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 EHK; 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 EHK; severe; dbSNP:rs58928370)"
FT /evidence="ECO:0000269|PubMed:10232403"
FT /id="VAR_017822"
FT VARIANT 193
FT /note="S -> P (in EHK; dbSNP:rs60937700)"
FT /evidence="ECO:0000269|PubMed:7507151"
FT /id="VAR_003857"
FT VARIANT 214
FT /note="L -> P (in EHK; 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 EHK; 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 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 EHK; dbSNP:rs59089201)"
FT /evidence="ECO:0000269|PubMed:21271994"
FT /id="VAR_071986"
FT VARIANT 479
FT /note="I -> F (in AEI; 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 AEI and EHK; 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 EHK; dbSNP:rs58420087)"
FT /evidence="ECO:0000269|PubMed:7512983"
FT /id="VAR_017827"
FT VARIANT 485
FT /note="L -> P (in EHK; dbSNP:rs267607430)"
FT /evidence="ECO:0000269|PubMed:21271994"
FT /id="VAR_071987"
FT VARIANT 486
FT /note="L -> P (in EHK; 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 EHK; dbSNP:rs60279707)"
FT /evidence="ECO:0000269|PubMed:21271994"
FT /id="VAR_071988"
FT VARIANT 490
FT /note="E -> Q (in EHK; 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
