K1C14_HUMAN
ID K1C14_HUMAN Reviewed; 472 AA.
AC P02533; Q14715; Q53XY3; Q9BUE3; Q9UBN2; Q9UBN3; Q9UCY4;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 4.
DT 03-AUG-2022, entry version 228.
DE RecName: Full=Keratin, type I cytoskeletal 14;
DE AltName: Full=Cytokeratin-14;
DE Short=CK-14;
DE AltName: Full=Keratin-14;
DE Short=K14;
GN Name=KRT14;
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].
RX PubMed=6210150; DOI=10.1016/0092-8674(84)90456-2;
RA Marchuk D., McCrohon S., Fuchs E.;
RT "Remarkable conservation of structure among intermediate filament genes.";
RL Cell 39:491-498(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT TYR-63.
RX PubMed=2580298; DOI=10.1073/pnas.82.6.1609;
RA Marchuk D., McCrohon S., Fuchs E.;
RT "Complete sequence of a gene encoding a human type I keratin: sequences
RT homologous to enhancer elements in the regulatory region of the gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:1609-1613(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS TYR-63 AND THR-94.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS TYR-63 AND THR-94.
RC TISSUE=Brain, Pancreas, and 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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 64-472.
RC TISSUE=Epidermis;
RX PubMed=6186381; DOI=10.1016/0092-8674(82)90424-x;
RA Hanukoglu I., Fuchs E.;
RT "The cDNA sequence of a human epidermal keratin: divergence of sequence but
RT conservation of structure among intermediate filament proteins.";
RL Cell 31:243-252(1982).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 117-132, AND VARIANT DM-EBS ASP-129.
RX PubMed=8601736; DOI=10.1111/1523-1747.ep12342985;
RA Chan Y.-M., Cheng J., Gedde-Dahl T. Jr., Niemi K.M., Fuchs E.;
RT "Genetic analysis of a severe case of Dowling-Meara epidermolysis bullosa
RT simplex.";
RL J. Invest. Dermatol. 106:327-334(1996).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 118-126, AND VARIANTS DM-EBS PHE-122;
RP CYS-125 AND HIS-125.
RX PubMed=1717157; DOI=10.1016/0092-8674(91)90051-y;
RA Coulombe P.A., Hutton M.E., Letai A., Hebert A., Paller A.S., Fuchs E.;
RT "Point mutations in human keratin 14 genes of epidermolysis bullosa simplex
RT patients: genetic and functional analyses.";
RL Cell 66:1301-1311(1991).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 118-126, AND VARIANT K-EBS PHE-122.
RX PubMed=7526926; DOI=10.1093/hmg/3.7.1171;
RA Yamanishi K., Matsuki M., Konishi K., Yasuno H.;
RT "A novel mutation of Leu122 to Phe at a highly conserved hydrophobic
RT residue in the helix initiation motif of keratin 14 in epidermolysis
RT bullosa simplex.";
RL Hum. Mol. Genet. 3:1171-1172(1994).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 352-424, AND VARIANT K-EBS THR-413.
RA Fujiwara H.;
RT "A novel mutation of cytokeratin 14 in a Japanese epidermolysis bullosa
RT simplex family.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP TISSUE SPECIFICITY.
RX PubMed=9457912; DOI=10.1046/j.1523-1747.1998.00097.x;
RA Bowden P.E., Hainey S.D., Parker G., Jones D.O., Zimonjic D., Popescu N.,
RA Hodgins M.B.;
RT "Characterization and chromosomal localization of human hair-specific
RT keratin genes and comparative expression during the hair growth cycle.";
RL J. Invest. Dermatol. 110:158-164(1998).
RN [12]
RP INTERACTION WITH TRADD.
RX PubMed=11684708; DOI=10.1083/jcb.200103078;
RA Inada H., Izawa I., Nishizawa M., Fujita E., Kiyono T., Takahashi T.,
RA Momoi T., Inagaki M.;
RT "Keratin attenuates tumor necrosis factor-induced cytotoxicity through
RT association with TRADD.";
RL J. Cell Biol. 155:415-426(2001).
RN [13]
RP FUNCTION, INTERACTION WITH KERATIN FILAMENTS, AND SUBCELLULAR LOCATION.
RX PubMed=11724817; DOI=10.1083/jcb.200104063;
RA Bousquet O., Ma L., Yamada S., Gu C., Idei T., Takahashi K., Wirtz D.,
RA Coulombe P.A.;
RT "The nonhelical tail domain of keratin 14 promotes filament bundling and
RT enhances the mechanical properties of keratin intermediate filaments in
RT vitro.";
RL J. Cell Biol. 155:747-754(2001).
RN [14]
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 [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [16]
RP 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 [17]
RP IDENTIFICATION IN A COMPLEX WITH KRT5, AND INTERACTION WITH KRT5 AND PLEC.
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 [18]
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 [19]
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 [20]
RP TISSUE SPECIFICITY.
RX PubMed=26758872; DOI=10.1093/hmg/ddw001;
RA Allen E.H., Courtney D.G., Atkinson S.D., Moore J.E., Mairs L.,
RA Poulsen E.T., Schiroli D., Maurizi E., Cole C., Hickerson R.P., James J.,
RA Murgatroyd H., Smith F.J., MacEwen C., Enghild J.J., Nesbit M.A.,
RA Leslie Pedrioli D.M., McLean W.H., Moore C.B.;
RT "Keratin 12 missense mutation induces the unfolded protein response and
RT apoptosis in Meesmann epithelial corneal dystrophy.";
RL Hum. Mol. Genet. 25:1176-1191(2016).
RN [21]
RP UBIQUITINATION BY THE BCR(KLHL24) COMPLEX, AND INTERACTION WITH KLHL24.
RX PubMed=27798626; DOI=10.1038/ng.3701;
RA Lin Z., Li S., Feng C., Yang S., Wang H., Ma D., Zhang J., Gou M., Bu D.,
RA Zhang T., Kong X., Wang X., Sarig O., Ren Y., Dai L., Liu H., Zhang J.,
RA Li F., Hu Y., Padalon-Brauch G., Vodo D., Zhou F., Chen T., Deng H.,
RA Sprecher E., Yang Y., Tan X.;
RT "Stabilizing mutations of KLHL24 ubiquitin ligase cause loss of keratin 14
RT and human skin fragility.";
RL Nat. Genet. 48:1508-1516(2016).
RN [22]
RP SUBCELLULAR LOCATION.
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 [23] {ECO:0000312|PDB:3TNU}
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 295-422 IN COMPLEX WITH KRT5,
RP DISULFIDE BOND, AND SUBCELLULAR LOCATION.
RX PubMed=22705788; DOI=10.1038/nsmb.2330;
RA Lee C.H., Kim M.S., Chung B.M., Leahy D.J., Coulombe P.A.;
RT "Structural basis for heteromeric assembly and perinuclear organization of
RT keratin filaments.";
RL Nat. Struct. Mol. Biol. 19:707-715(2012).
RN [24] {ECO:0007744|PDB:6JFV}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 327-421 OF MUTANT ALA-367 IN
RP COMPLEX WITH KRT5, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-335;
RP GLU-342; GLN-346; ARG-365; TYR-366 AND GLN-372.
RX PubMed=31995743; DOI=10.1016/j.str.2020.01.002;
RA Lee C.H., Kim M.S., Li S., Leahy D.J., Coulombe P.A.;
RT "Structure-Function Analyses of a Keratin Heterotypic Complex Identify
RT Specific Keratin Regions Involved in Intermediate Filament Assembly.";
RL Structure 28:355-362.e4(2020).
RN [25]
RP VARIANT K-EBS PRO-384.
RX PubMed=1720261; DOI=10.1126/science.1720261;
RA Bonifas J.M., Rothman A.L., Epstein E.H. Jr.;
RT "Epidermolysis bullosa simplex: evidence in two families for keratin gene
RT abnormalities.";
RL Science 254:1202-1205(1991).
RN [26]
RP VARIANT WC-EBS GLU-375 DEL.
RX PubMed=7506606; DOI=10.1093/hmg/2.11.1971;
RA Chen M.A., Bonifas J.M., Matsumura K., Blumenfeld A., Epstein E.H. Jr.;
RT "A novel three-nucleotide deletion in the helix 2B region of keratin 14 in
RT epidermolysis bullosa simplex: delta E375.";
RL Hum. Mol. Genet. 2:1971-1972(1993).
RN [27]
RP VARIANT K-EBS ARG-272.
RX PubMed=7682883; DOI=10.1002/humu.1380020107;
RA Humphries M.M., Sheils D.M., Farrar G.J., Kumar-Singh R., Kenna P.F.,
RA Mansergh F.C., Jordan S.A., Young M.M., Humphries P.;
RT "A mutation (Met-->Arg) in the type I keratin (K14) gene responsible for
RT autosomal dominant epidermolysis bullosa simplex.";
RL Hum. Mutat. 2:37-42(1993).
RN [28]
RP VARIANT DM-EBS HIS-125.
RX PubMed=7688405; DOI=10.1111/1523-1747.ep12365079;
RA Stephens K., Sybert V.P., Wijsman E.M., Ehrlich P., Spencer A.;
RT "A keratin 14 mutational hot spot for epidermolysis bullosa simplex,
RT Dowling-Meara: implications for diagnosis.";
RL J. Invest. Dermatol. 101:240-243(1993).
RN [29]
RP VARIANT EBSB1 ALA-144.
RX PubMed=7526933; DOI=10.1038/ng0493-327;
RA Hovnanian A., Pollack E., Hilal L., Rochat A., Prost C., Barrandon Y.,
RA Goossens M.;
RT "A missense mutation in the rod domain of keratin 14 associated with
RT recessive epidermolysis bullosa simplex.";
RL Nat. Genet. 3:327-331(1993).
RN [30]
RP VARIANT WC-EBS MET-270.
RX PubMed=7506097; DOI=10.1038/ng1193-294;
RA Rugg E.L., Morley S.M., Smith F.J.D., Boxer M., Tidman M.J., Navsaria H.A.,
RA Leigh I.M., Lane E.B.;
RT "Missing links: Weber-Cockayne keratin mutations implicate the L12 linker
RT domain in effective cytoskeleton function.";
RL Nat. Genet. 5:294-300(1993).
RN [31]
RP VARIANTS WC-EBS ILE-119; ASP-274; ASN-377 AND CYS-388, AND VARIANTS DM-EBS
RP ARG-120; CYS-125 AND SER-125.
RX PubMed=7561171; DOI=10.1111/1523-1747.ep12323846;
RA Chen H., Bonifas J.M., Matsumura K., Ikeda S., Leyden W.A.,
RA Epstein E.H. Jr.;
RT "Keratin 14 gene mutations in patients with epidermolysis bullosa
RT simplex.";
RL J. Invest. Dermatol. 105:629-632(1995).
RN [32]
RP VARIANT WC-EBS ILE-119.
RX PubMed=9284105; DOI=10.1111/1523-1747.ep12336051;
RA Hu Z.L., Smith L., Martins S., Bonifas J.M., Chen H., Epstein E.H. Jr.;
RT "Partial dominance of a keratin 14 mutation in epidermolysis bullosa
RT simplex: increased severity of disease in a homozygote.";
RL J. Invest. Dermatol. 109:360-364(1997).
RN [33]
RP VARIANT DM-EBS THR-119.
RX PubMed=9804355; DOI=10.1046/j.1523-1747.1998.00388.x;
RA Shemanko C.S., Mellerio J.E., Tidman M.J., Lane E.B., Eady R.A.J.;
RT "Severe palmo-plantar hyperkeratosis in Dowling-Meara epidermolysis bullosa
RT simplex caused by a mutation in the keratin 14 gene (KRT14).";
RL J. Invest. Dermatol. 111:893-895(1998).
RN [34]
RP VARIANT WC-EBS GLY-273.
RX PubMed=9804357; DOI=10.1046/j.1523-1747.1998.00374.x;
RA Mueller F.B., Kuester W., Bruckner-Tuderman L., Korge B.P.;
RT "Novel K5 and K14 mutations in German patients with the Weber-Cockayne
RT variant of epidermolysis bullosa simplex.";
RL J. Invest. Dermatol. 111:900-902(1998).
RN [35]
RP VARIANT DM-EBS CYS-125.
RX PubMed=10583131; DOI=10.1046/j.1365-2133.1999.03124.x;
RA Sasaki Y., Shimizu H., Akiyama M., Hiraoka Y., Takizawa Y., Yamada S.,
RA Morishima Y., Yamanishi K., Aiso S., Nishikawa T.;
RT "A recurrent keratin 14 mutation in Dowling-Meara epidermolysis bullosa
RT simplex.";
RL Br. J. Dermatol. 141:747-748(1999).
RN [36]
RP VARIANT K-EBS HIS-415, AND VARIANT DM-EBS GLN-419.
RA Hut P.H.L., van der Vlies P., Jonkman M.F., Shimizu H., Buys C.H.C.M.,
RA Scheffer H.;
RT "Genomic keratin 14 mutation detection in epidermolysis bullosa simplex.";
RL Eur. J. Hum. Genet. Suppl. 7:121-121(1999).
RN [37]
RP VARIANT WC-EBS ASN-116, VARIANT DM-EBS SER-123, VARIANT K-EBS PRO-143,
RP VARIANT THR-94, AND SEQUENCE REVISION TO 25 AND 43.
RX PubMed=9989794; DOI=10.1046/j.1523-1747.1999.00495.x;
RA Soerensen C.B., Ladekjaer-Mikkelsen A.-S., Andresen B.S., Brandrup F.,
RA Veien N.K., Buus S.K., Anton-Lamprecht I., Kruse T.A., Jensen P.K.A.,
RA Eiberg H., Bolund L., Gregersen N.;
RT "Identification of novel and known mutations in the genes for keratin 5 and
RT 14 in Danish patients with epidermolysis bullosa simplex: correlation
RT between genotype and phenotype.";
RL J. Invest. Dermatol. 112:184-190(1999).
RN [38]
RP VARIANT DM-EBS HIS-125.
RX PubMed=10730767; DOI=10.1046/j.1365-2133.2000.03304.x;
RA Shemanko C.S., Horn H.M., Keohane S.G., Hepburn N., Kerr A.I.G.,
RA Atherton D.J., Tidman M.J., Lane E.B.;
RT "Laryngeal involvement in the Dowling-Meara variant of epidermolysis
RT bullosa simplex with keratin mutations of severely disruptive potential.";
RL Br. J. Dermatol. 142:315-320(2000).
RN [39]
RP VARIANTS DM-EBS CYS-125; HIS-125 AND GLN-419, VARIANTS K-EBS ASP-247 AND
RP HIS-415, AND VARIANT WC-EBS LYS-422.
RX PubMed=10733662; DOI=10.1046/j.1523-1747.2000.00928.x;
RA Hut P.H.L., van der Vlies P., Jonkman M.F., Verlind E., Shimizu H.,
RA Buys C.H.C.M., Scheffer H.;
RT "Exempting homologous pseudogene sequences from polymerase chain reaction
RT amplification allows genomic keratin 14 hotspot analysis.";
RL J. Invest. Dermatol. 114:616-619(2000).
RN [40]
RP VARIANTS DM-EBS CYS-125 AND HIS-415, AND VARIANT K-EBS PRO-134.
RX PubMed=10820403;
RX DOI=10.1002/(sici)1097-0223(200005)20:5<371::aid-pd818>3.0.co;2-5;
RA Rugg E.L., Baty D., Shemanko C.S., Magee G., Polak S., Bergman R.,
RA Kadar T., Boxer M., Falik-Zaccai T., Borochowitz Z., Lane E.B.;
RT "DNA based prenatal testing for the skin blistering disorder epidermolysis
RT bullosa simplex.";
RL Prenat. Diagn. 20:371-377(2000).
RN [41]
RP VARIANT DM-EBS THR-119, AND VARIANT K-EBS VAL-119.
RX PubMed=11710919; DOI=10.1046/j.0022-202x.2001.01508.x;
RA Cummins R.E., Klingberg S., Wesley J., Rogers M., Zhao Y., Murrell D.F.;
RT "Keratin 14 point mutations at codon 119 of helix 1A resulting in different
RT epidermolysis bullosa simplex phenotypes.";
RL J. Invest. Dermatol. 117:1103-1107(2001).
RN [42]
RP VARIANTS WC-EBS HIS-388 AND CYS-415, AND VARIANT DM-EBS HIS-125.
RX PubMed=12707098; DOI=10.1001/archderm.139.4.498;
RA Ciubotaru D., Bergman R., Baty D., Indelman M., Pfendner E., Petronius D.,
RA Moualem H., Kanaan M., Ben Amitai D., McLean W.H.I., Uitto J., Sprecher E.;
RT "Epidermolysis bullosa simplex in Israel: clinical and genetic features.";
RL Arch. Dermatol. 139:498-505(2003).
RN [43]
RP ERRATUM OF PUBMED:12707098.
RA Ciubotaru D., Bergman R., Baty D., Indelman M., Pfendner E., Petronius D.,
RA Moualem H., Kanaan M., Ben Amitai D., McLean W.H.I., Uitto J., Sprecher E.;
RL Arch. Dermatol. 139:1084-1084(2003).
RN [44]
RP VARIANTS DM-EBS PRO-130 AND GLN-419, AND VARIANT WC-EBS MET-408.
RX PubMed=12655565; DOI=10.1002/humu.9124;
RA Schuilenga-Hut P.H.L., Vlies P., Jonkman M.F., Waanders E., Buys C.H.C.M.,
RA Scheffer H.;
RT "Mutation analysis of the entire keratin 5 and 14 genes in patients with
RT epidermolysis bullosa simplex and identification of novel mutations.";
RL Hum. Mutat. 21:447-447(2003).
RN [45]
RP VARIANTS DM-EBS SER-128 DEL AND PRO-416, AND VARIANT WC-EBS CYS-148.
RX PubMed=12603865; DOI=10.1046/j.1523-1747.2003.12052.x;
RA Wood P., Baty D.U., Lane E.B., McLean W.H.I.;
RT "Long-range polymerase chain reaction for specific full-length
RT amplification of the human keratin 14 gene and novel keratin 14 mutations
RT in epidermolysis bullosa simplex patients.";
RL J. Invest. Dermatol. 120:495-497(2003).
RN [46]
RP VARIANTS DM-EBS LYS-123 AND GLY-125, AND VARIANT WC-EBS LEU-133.
RX PubMed=14987259; DOI=10.1111/j.0906-6705.2004.0120.x;
RA Csikos M., Szalai Z., Becker K., Sebok B., Schneider I., Horvath A.,
RA Karpati S.;
RT "Novel keratin 14 gene mutations in patients from Hungary with
RT epidermolysis bullosa simplex.";
RL Exp. Dermatol. 13:185-191(2004).
RN [47]
RP INVOLVEMENT IN NFJS, AND INVOLVEMENT IN DPR.
RX PubMed=16960809; DOI=10.1086/507792;
RA Lugassy J., Itin P., Ishida-Yamamoto A., Holland K., Huson S., Geiger D.,
RA Hennies H.C., Indelman M., Bercovich D., Uitto J., Bergman R.,
RA McGrath J.A., Richard G., Sprecher E.;
RT "Naegeli-Franceschetti-Jadassohn syndrome and dermatopathia pigmentosa
RT reticularis: two allelic ectodermal dysplasias caused by dominant mutations
RT in KRT14.";
RL Am. J. Hum. Genet. 79:724-730(2006).
RN [48]
RP VARIANT WC-EBS VAL-119, AND VARIANTS DM-EBS HIS-125 AND CYS-125.
RX PubMed=16882168; DOI=10.1111/j.1365-2133.2006.07285.x;
RA Yasukawa K., Sawamura D., Goto M., Nakamura H., Jung S.-Y., Kim S.-C.,
RA Shimizu H.;
RT "Epidermolysis bullosa simplex in Japanese and Korean patients: genetic
RT studies in 19 cases.";
RL Br. J. Dermatol. 155:313-317(2006).
RN [49]
RP VARIANTS DM-EBS LYS-123; CYS-125; HIS-125 AND PRO-417, VARIANTS K-EBS
RP LEU-133; THR-272 AND PRO-384, AND VARIANTS WC-EBS PRO-211 AND GLU-411 DEL.
RX PubMed=16786515; DOI=10.1002/humu.9437;
RA Mueller F.B., Kuester W., Wodecki K., Almeida H. Jr., Bruckner-Tuderman L.,
RA Krieg T., Korge B.P., Arin M.J.;
RT "Novel and recurrent mutations in keratin KRT5 and KRT14 genes in
RT epidermolysis bullosa simplex: implications for disease phenotype and
RT keratin filament assembly.";
RL Hum. Mutat. 27:719-720(2006).
RN [50]
RP VARIANT GLN-418.
RX PubMed=24981776; DOI=10.1111/exd.12478;
RA Jankowski M., Wertheim-Tysarowska K., Jakubowski R., Sota J., Nowak W.,
RA Czajkowski R.;
RT "Novel KRT14 mutation causing epidermolysis bullosa simplex with variable
RT phenotype.";
RL Exp. Dermatol. 23:684-687(2014).
CC -!- FUNCTION: The nonhelical tail domain is involved in promoting KRT5-
CC KRT14 filaments to self-organize into large bundles and enhances the
CC mechanical properties involved in resilience of keratin intermediate
CC filaments in vitro. {ECO:0000269|PubMed:11724817}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins (By
CC similarity). Forms a disulfide-linked heterodimer (via 2B domains) with
CC KRT5 (via 2B domains) (PubMed:24940650, PubMed:22705788). Forms a
CC heterodimer with KRT1; the interaction is more abundant in the absence
CC of KRT5 (By similarity). Interacts with PLEC isoform 1C, when in a
CC heterodimer with KRT5 (PubMed:24940650). Interacts with TRADD and with
CC keratin filaments (PubMed:11684708). Associates with other type I
CC keratins (PubMed:11724817). Interacts with EPPK1 (By similarity).
CC Interacts with KLHL24 (PubMed:27798626). {ECO:0000250|UniProtKB:Q61781,
CC ECO:0000269|PubMed:11684708, ECO:0000269|PubMed:11724817,
CC ECO:0000269|PubMed:22705788, ECO:0000269|PubMed:24940650,
CC ECO:0000269|PubMed:27798626}.
CC -!- INTERACTION:
CC P02533; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-702178, EBI-11096309;
CC P02533; Q9P2A4: ABI3; NbExp=3; IntAct=EBI-702178, EBI-742038;
CC P02533; A2BDD9: AMOT; NbExp=3; IntAct=EBI-702178, EBI-17286414;
CC P02533; Q13515: BFSP2; NbExp=3; IntAct=EBI-702178, EBI-10229433;
CC P02533; Q8WZ74: CTTNBP2; NbExp=3; IntAct=EBI-702178, EBI-1774260;
CC P02533; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-702178, EBI-744099;
CC P02533; O95995: GAS8; NbExp=3; IntAct=EBI-702178, EBI-1052570;
CC P02533; O14964: HGS; NbExp=3; IntAct=EBI-702178, EBI-740220;
CC P02533; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-702178, EBI-14069005;
CC P02533; P04264: KRT1; NbExp=3; IntAct=EBI-702178, EBI-298429;
CC P02533; P12035: KRT3; NbExp=3; IntAct=EBI-702178, EBI-2430095;
CC P02533; P13647: KRT5; NbExp=8; IntAct=EBI-702178, EBI-702187;
CC P02533; P48668: KRT6C; NbExp=3; IntAct=EBI-702178, EBI-2564105;
CC P02533; Q14CN4: KRT72; NbExp=3; IntAct=EBI-702178, EBI-1221280;
CC P02533; Q8N1N4: KRT78; NbExp=3; IntAct=EBI-702178, EBI-1056564;
CC P02533; Q5XKE5: KRT79; NbExp=3; IntAct=EBI-702178, EBI-2514135;
CC P02533; Q6KB66-2: KRT80; NbExp=3; IntAct=EBI-702178, EBI-11999246;
CC P02533; Q14533: KRT81; NbExp=3; IntAct=EBI-702178, EBI-739648;
CC P02533; O43790: KRT86; NbExp=3; IntAct=EBI-702178, EBI-9996498;
CC P02533; O43482: OIP5; NbExp=3; IntAct=EBI-702178, EBI-536879;
CC P02533; Q13835-2: PKP1; NbExp=2; IntAct=EBI-702178, EBI-9087684;
CC P02533; P41219: PRPH; NbExp=3; IntAct=EBI-702178, EBI-752074;
CC P02533; Q3MIT2: PUS10; NbExp=3; IntAct=EBI-702178, EBI-11983583;
CC P02533; O00560: SDCBP; NbExp=3; IntAct=EBI-702178, EBI-727004;
CC P02533; Q969G3: SMARCE1; NbExp=3; IntAct=EBI-702178, EBI-455078;
CC P02533; P57075-2: UBASH3A; NbExp=3; IntAct=EBI-702178, EBI-7353612;
CC P02533; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-702178, EBI-739895;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11724817,
CC ECO:0000269|PubMed:31995743, ECO:0000269|PubMed:32179842}. Nucleus
CC {ECO:0000269|PubMed:11724817}. Note=Expressed in both as a filamentous
CC pattern. {ECO:0000269|PubMed:11724817}.
CC -!- TISSUE SPECIFICITY: Expressed in the corneal epithelium (at protein
CC level) (PubMed:26758872). Detected in the basal layer, lowered within
CC the more apically located layers specifically in the stratum spinosum,
CC stratum granulosum but is not detected in stratum corneum. Strongly
CC expressed in the outer root sheath of anagen follicles but not in the
CC germinative matrix, inner root sheath or hair (PubMed:9457912). Found
CC in keratinocytes surrounding the club hair during telogen
CC (PubMed:9457912). {ECO:0000269|PubMed:26758872,
CC ECO:0000269|PubMed:9457912}.
CC -!- PTM: A disulfide bond is formed between rather than within filaments
CC and promotes the formation of a keratin filament cage around the
CC nucleus. {ECO:0000250|UniProtKB:Q61781}.
CC -!- PTM: Ubiquitinated by the BCR(KLHL24) E3 ubiquitin ligase complex.
CC {ECO:0000269|PubMed:27798626}.
CC -!- DISEASE: Epidermolysis bullosa simplex, Dowling-Meara type (DM-EBS)
CC [MIM:131760]: A severe form of intraepidermal epidermolysis bullosa
CC characterized by generalized herpetiform blistering, milia formation,
CC dystrophic nails, and mucous membrane involvement.
CC {ECO:0000269|PubMed:10583131, ECO:0000269|PubMed:10730767,
CC ECO:0000269|PubMed:10733662, ECO:0000269|PubMed:10820403,
CC ECO:0000269|PubMed:11710919, ECO:0000269|PubMed:12603865,
CC ECO:0000269|PubMed:12655565, ECO:0000269|PubMed:12707098,
CC ECO:0000269|PubMed:14987259, ECO:0000269|PubMed:16786515,
CC ECO:0000269|PubMed:16882168, ECO:0000269|PubMed:1717157,
CC ECO:0000269|PubMed:7561171, ECO:0000269|PubMed:7688405,
CC ECO:0000269|PubMed:8601736, ECO:0000269|PubMed:9804355,
CC ECO:0000269|PubMed:9989794, ECO:0000269|Ref.36}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: Epidermolysis bullosa simplex, Weber-Cockayne type (WC-EBS)
CC [MIM:131800]: A form of intraepidermal epidermolysis bullosa
CC characterized by blistering limited to palmar and plantar areas of the
CC skin. {ECO:0000269|PubMed:10733662, ECO:0000269|PubMed:12603865,
CC ECO:0000269|PubMed:12655565, ECO:0000269|PubMed:12707098,
CC ECO:0000269|PubMed:14987259, ECO:0000269|PubMed:16786515,
CC ECO:0000269|PubMed:16882168, ECO:0000269|PubMed:7506097,
CC ECO:0000269|PubMed:7506606, ECO:0000269|PubMed:7561171,
CC ECO:0000269|PubMed:9284105, ECO:0000269|PubMed:9804357,
CC ECO:0000269|PubMed:9989794}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Epidermolysis bullosa simplex, Koebner type (K-EBS)
CC [MIM:131900]: A form of intraepidermal epidermolysis bullosa
CC characterized by generalized skin blistering. The phenotype is not
CC fundamentally distinct from the Dowling-Meara type, although it is less
CC severe. {ECO:0000269|PubMed:10733662, ECO:0000269|PubMed:10820403,
CC ECO:0000269|PubMed:11710919, ECO:0000269|PubMed:16786515,
CC ECO:0000269|PubMed:1720261, ECO:0000269|PubMed:7526926,
CC ECO:0000269|PubMed:7682883, ECO:0000269|PubMed:9989794,
CC ECO:0000269|Ref.10, ECO:0000269|Ref.36}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- DISEASE: Epidermolysis bullosa simplex, autosomal recessive 1 (EBSB1)
CC [MIM:601001]: A form of epidermolysis bullosa, a genodermatosis
CC characterized by recurrent blistering and cleavage within basal
CC keratinocytes, fragility of the skin and mucosal epithelia, and
CC erosions caused by minor mechanical trauma.
CC {ECO:0000269|PubMed:7526933}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Naegeli-Franceschetti-Jadassohn syndrome (NFJS) [MIM:161000]:
CC A rare autosomal dominant form of ectodermal dysplasia. The cardinal
CC features are absence of dermatoglyphics (fingerprints), reticular
CC cutaneous hyperpigmentation (starting at about the age of 2 years
CC without a preceding inflammatory stage), palmoplantar keratoderma,
CC hypohidrosis with diminished sweat gland function and discomfort
CC provoked by heat, nail dystrophy, and tooth enamel defects.
CC {ECO:0000269|PubMed:16960809}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Dermatopathia pigmentosa reticularis (DPR) [MIM:125595]: A
CC rare ectodermal dysplasia characterized by lifelong persistent
CC reticulate hyperpigmentation, non-cicatricial alopecia, and nail
CC dystrophy. Variable features include adermatoglyphia, hypohidrosis or
CC hyperhidrosis, and palmoplantar hyperkeratosis.
CC {ECO:0000269|PubMed:16960809}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: There are two types of cytoskeletal and microfibrillar
CC keratin: I (acidic; 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 -!- WEB RESOURCE: Name=Human Intermediate Filament Mutation Database;
CC URL="http://www.interfil.org";
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DR EMBL; J00124; AAB59562.1; -; Genomic_DNA.
DR EMBL; BT007186; AAP35850.1; -; mRNA.
DR EMBL; AC019349; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002690; AAH02690.1; -; mRNA.
DR EMBL; BC019097; AAH19097.1; -; mRNA.
DR EMBL; BC042437; AAH42437.1; -; mRNA.
DR EMBL; BC094830; AAH94830.1; -; mRNA.
DR EMBL; D28807; BAA05967.1; -; Genomic_DNA.
DR EMBL; AF186085; AAF04034.1; -; Genomic_DNA.
DR EMBL; AF186086; AAF04035.1; -; Genomic_DNA.
DR EMBL; AF186087; AAF04036.1; -; Genomic_DNA.
DR EMBL; AF186088; AAF04037.1; -; Genomic_DNA.
DR EMBL; AF186089; AAF04038.1; -; Genomic_DNA.
DR EMBL; AF186090; AAF04039.1; -; Genomic_DNA.
DR CCDS; CCDS11400.1; -.
DR PIR; A26763; KRHUE.
DR RefSeq; NP_000517.2; NM_000526.4.
DR PDB; 3TNU; X-ray; 3.00 A; A=295-422.
DR PDB; 6JFV; X-ray; 2.60 A; A/C=327-421.
DR PDBsum; 3TNU; -.
DR PDBsum; 6JFV; -.
DR AlphaFoldDB; P02533; -.
DR SMR; P02533; -.
DR BioGRID; 110059; 134.
DR ComplexPortal; CPX-888; Keratin-5 - Keratin-14 dimer complex.
DR DIP; DIP-33874N; -.
DR IntAct; P02533; 65.
DR MINT; P02533; -.
DR STRING; 9606.ENSP00000167586; -.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR GlyGen; P02533; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P02533; -.
DR PhosphoSitePlus; P02533; -.
DR SwissPalm; P02533; -.
DR BioMuta; KRT14; -.
DR DMDM; 229463044; -.
DR jPOST; P02533; -.
DR MassIVE; P02533; -.
DR PaxDb; P02533; -.
DR PeptideAtlas; P02533; -.
DR PRIDE; P02533; -.
DR ProteomicsDB; 51528; -.
DR Antibodypedia; 3600; 1290 antibodies from 49 providers.
DR DNASU; 3861; -.
DR Ensembl; ENST00000167586.7; ENSP00000167586.6; ENSG00000186847.6.
DR GeneID; 3861; -.
DR KEGG; hsa:3861; -.
DR MANE-Select; ENST00000167586.7; ENSP00000167586.6; NM_000526.5; NP_000517.3.
DR UCSC; uc002hxf.3; human.
DR CTD; 3861; -.
DR DisGeNET; 3861; -.
DR GeneCards; KRT14; -.
DR GeneReviews; KRT14; -.
DR HGNC; HGNC:6416; KRT14.
DR HPA; ENSG00000186847; Tissue enriched (skin).
DR MalaCards; KRT14; -.
DR MIM; 125595; phenotype.
DR MIM; 131760; phenotype.
DR MIM; 131800; phenotype.
DR MIM; 131900; phenotype.
DR MIM; 148066; gene.
DR MIM; 161000; phenotype.
DR MIM; 601001; phenotype.
DR neXtProt; NX_P02533; -.
DR OpenTargets; ENSG00000186847; -.
DR Orphanet; 79399; Autosomal dominant generalized epidermolysis bullosa simplex, intermediate form.
DR Orphanet; 79396; Autosomal dominant generalized epidermolysis bullosa simplex, severe form.
DR Orphanet; 89838; Autosomal recessive generalized epidermolysis bullosa simplex.
DR Orphanet; 86920; Dermatopathia pigmentosa reticularis.
DR Orphanet; 79397; Epidermolysis bullosa simplex with mottled pigmentation.
DR Orphanet; 79400; Localized epidermolysis bullosa simplex.
DR Orphanet; 69087; Naegeli-Franceschetti-Jadassohn syndrome.
DR PharmGKB; PA30203; -.
DR VEuPathDB; HostDB:ENSG00000186847; -.
DR eggNOG; ENOG502R8V7; Eukaryota.
DR GeneTree; ENSGT00940000154602; -.
DR HOGENOM; CLU_012560_8_1_1; -.
DR InParanoid; P02533; -.
DR OMA; YWATIND; -.
DR OrthoDB; 798081at2759; -.
DR PhylomeDB; P02533; -.
DR TreeFam; TF332742; -.
DR PathwayCommons; P02533; -.
DR Reactome; R-HSA-446107; Type I hemidesmosome assembly.
DR Reactome; R-HSA-6805567; Keratinization.
DR Reactome; R-HSA-6809371; Formation of the cornified envelope.
DR SignaLink; P02533; -.
DR SIGNOR; P02533; -.
DR BioGRID-ORCS; 3861; 17 hits in 1045 CRISPR screens.
DR ChiTaRS; KRT14; human.
DR GeneWiki; Keratin_14; -.
DR GenomeRNAi; 3861; -.
DR Pharos; P02533; Tbio.
DR PRO; PR:P02533; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P02533; protein.
DR Bgee; ENSG00000186847; Expressed in gingival epithelium and 120 other tissues.
DR Genevisible; P02533; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
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:0005882; C:intermediate filament; IDA:BHF-UCL.
DR GO; GO:0045095; C:keratin filament; IDA:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:1990254; F:keratin filament binding; IPI:UniProtKB.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
DR GO; GO:0007568; P:aging; IDA:UniProtKB.
DR GO; GO:0008544; P:epidermis development; TAS:ProtInc.
DR GO; GO:0030855; P:epithelial cell differentiation; IBA:GO_Central.
DR GO; GO:0042633; P:hair cycle; IDA:UniProtKB.
DR GO; GO:0045110; P:intermediate filament bundle assembly; IMP:UniProtKB.
DR GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
DR DisProt; DP02605; -.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR002957; Keratin_I.
DR PANTHER; PTHR23239; PTHR23239; 1.
DR Pfam; PF00038; Filament; 1.
DR PRINTS; PR01248; TYPE1KERATIN.
DR SMART; SM01391; Filament; 1.
DR PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; Disease variant; Disulfide bond;
KW Ectodermal dysplasia; Epidermolysis bullosa; Intermediate filament;
KW Keratin; Nucleus; Palmoplantar keratoderma; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..472
FT /note="Keratin, type I cytoskeletal 14"
FT /id="PRO_0000063653"
FT DOMAIN 115..426
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..114
FT /note="Head"
FT REGION 115..150
FT /note="Coil 1A"
FT REGION 151..168
FT /note="Linker 1"
FT REGION 169..260
FT /note="Coil 1B"
FT REGION 261..283
FT /note="Linker 12"
FT REGION 284..422
FT /note="Coil 2"
FT REGION 423..472
FT /note="Tail"
FT REGION 425..472
FT /note="Interaction with Type I keratins and keratin
FT filaments"
FT REGION 426..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..472
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 364
FT /note="Stutter"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61781"
FT DISULFID 367
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:22705788"
FT VARIANT 63
FT /note="C -> Y (in dbSNP:rs6503640)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:2580298, ECO:0000269|Ref.3"
FT /id="VAR_055347"
FT VARIANT 94
FT /note="A -> T (in dbSNP:rs3826550)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9989794, ECO:0000269|Ref.3"
FT /id="VAR_010437"
FT VARIANT 116
FT /note="K -> N (in WC-EBS; dbSNP:rs59271739)"
FT /evidence="ECO:0000269|PubMed:9989794"
FT /id="VAR_010438"
FT VARIANT 119
FT /note="M -> I (in WC-EBS at heterozygosity; more severe
FT phenotype is associated with homozygosity;
FT dbSNP:rs57358989)"
FT /evidence="ECO:0000269|PubMed:7561171,
FT ECO:0000269|PubMed:9284105"
FT /id="VAR_010439"
FT VARIANT 119
FT /note="M -> T (in DM-EBS; dbSNP:rs28928893)"
FT /evidence="ECO:0000269|PubMed:11710919,
FT ECO:0000269|PubMed:9804355"
FT /id="VAR_010440"
FT VARIANT 119
FT /note="M -> V (in K-EBS and WC-EBS; dbSNP:rs61263401)"
FT /evidence="ECO:0000269|PubMed:11710919,
FT ECO:0000269|PubMed:16882168"
FT /id="VAR_023719"
FT VARIANT 120
FT /note="Q -> R (in DM-EBS; dbSNP:rs60993843)"
FT /evidence="ECO:0000269|PubMed:7561171"
FT /id="VAR_010441"
FT VARIANT 122
FT /note="L -> F (in DM-EBS and K-EBS; dbSNP:rs59110575)"
FT /evidence="ECO:0000269|PubMed:1717157,
FT ECO:0000269|PubMed:7526926"
FT /id="VAR_010442"
FT VARIANT 123
FT /note="N -> K (in DM-EBS; dbSNP:rs3826549)"
FT /evidence="ECO:0000269|PubMed:14987259,
FT ECO:0000269|PubMed:16786515"
FT /id="VAR_023720"
FT VARIANT 123
FT /note="N -> S (in DM-EBS; dbSNP:rs60171927)"
FT /evidence="ECO:0000269|PubMed:9989794"
FT /id="VAR_010443"
FT VARIANT 125
FT /note="R -> C (in DM-EBS; dbSNP:rs60399023)"
FT /evidence="ECO:0000269|PubMed:10583131,
FT ECO:0000269|PubMed:10733662, ECO:0000269|PubMed:10820403,
FT ECO:0000269|PubMed:16786515, ECO:0000269|PubMed:16882168,
FT ECO:0000269|PubMed:1717157, ECO:0000269|PubMed:7561171"
FT /id="VAR_003837"
FT VARIANT 125
FT /note="R -> G (in DM-EBS; dbSNP:rs60399023)"
FT /evidence="ECO:0000269|PubMed:14987259"
FT /id="VAR_023721"
FT VARIANT 125
FT /note="R -> H (in DM-EBS; dbSNP:rs58330629)"
FT /evidence="ECO:0000269|PubMed:10730767,
FT ECO:0000269|PubMed:10733662, ECO:0000269|PubMed:12707098,
FT ECO:0000269|PubMed:16786515, ECO:0000269|PubMed:16882168,
FT ECO:0000269|PubMed:1717157, ECO:0000269|PubMed:7688405"
FT /id="VAR_003838"
FT VARIANT 125
FT /note="R -> S (in DM-EBS)"
FT /evidence="ECO:0000269|PubMed:7561171"
FT /id="VAR_010444"
FT VARIANT 128
FT /note="Missing (in DM-EBS)"
FT /evidence="ECO:0000269|PubMed:12603865"
FT /id="VAR_031634"
FT VARIANT 129
FT /note="Y -> D (in DM-EBS; dbSNP:rs60470268)"
FT /evidence="ECO:0000269|PubMed:8601736"
FT /id="VAR_010445"
FT VARIANT 130
FT /note="L -> P (in DM-EBS; dbSNP:rs57522245)"
FT /evidence="ECO:0000269|PubMed:12655565"
FT /id="VAR_023722"
FT VARIANT 133
FT /note="V -> A (in dbSNP:rs56798071)"
FT /id="VAR_033496"
FT VARIANT 133
FT /note="V -> L (in WC-EBS and K-EBS; dbSNP:rs61027685)"
FT /evidence="ECO:0000269|PubMed:14987259,
FT ECO:0000269|PubMed:16786515"
FT /id="VAR_023723"
FT VARIANT 134
FT /note="R -> P (in K-EBS; dbSNP:rs61540016)"
FT /evidence="ECO:0000269|PubMed:10820403"
FT /id="VAR_031635"
FT VARIANT 143
FT /note="L -> P (in K-EBS; dbSNP:rs61326242)"
FT /evidence="ECO:0000269|PubMed:9989794"
FT /id="VAR_010446"
FT VARIANT 144
FT /note="E -> A (in EBSB1; dbSNP:rs57121345)"
FT /evidence="ECO:0000269|PubMed:7526933"
FT /id="VAR_003839"
FT VARIANT 148
FT /note="R -> C (in WC-EBS; dbSNP:rs58378809)"
FT /evidence="ECO:0000269|PubMed:12603865"
FT /id="VAR_031636"
FT VARIANT 211
FT /note="R -> P (in WC-EBS; dbSNP:rs60589227)"
FT /evidence="ECO:0000269|PubMed:16786515"
FT /id="VAR_027718"
FT VARIANT 215
FT /note="E -> K (in dbSNP:rs11551755)"
FT /id="VAR_049784"
FT VARIANT 247
FT /note="A -> D (in K-EBS; dbSNP:rs147611635)"
FT /evidence="ECO:0000269|PubMed:10733662"
FT /id="VAR_010447"
FT VARIANT 270
FT /note="V -> M (in WC-EBS; dbSNP:rs58560979)"
FT /evidence="ECO:0000269|PubMed:7506097"
FT /id="VAR_003840"
FT VARIANT 272
FT /note="M -> R (in K-EBS; dbSNP:rs61371557)"
FT /evidence="ECO:0000269|PubMed:7682883"
FT /id="VAR_003841"
FT VARIANT 272
FT /note="M -> T (in K-EBS; dbSNP:rs61371557)"
FT /evidence="ECO:0000269|PubMed:16786515"
FT /id="VAR_027719"
FT VARIANT 273
FT /note="D -> G (in WC-EBS; dbSNP:rs59375065)"
FT /evidence="ECO:0000269|PubMed:9804357"
FT /id="VAR_010448"
FT VARIANT 274
FT /note="A -> D (in WC-EBS; dbSNP:rs58785777)"
FT /evidence="ECO:0000269|PubMed:7561171"
FT /id="VAR_010449"
FT VARIANT 375
FT /note="Missing (in WC-EBS; dbSNP:rs56974573)"
FT /evidence="ECO:0000269|PubMed:7506606"
FT /id="VAR_003842"
FT VARIANT 377
FT /note="I -> N (in WC-EBS; dbSNP:rs61536893)"
FT /evidence="ECO:0000269|PubMed:7561171"
FT /id="VAR_010450"
FT VARIANT 384
FT /note="L -> P (in K-EBS; dbSNP:rs59629244)"
FT /evidence="ECO:0000269|PubMed:16786515,
FT ECO:0000269|PubMed:1720261"
FT /id="VAR_003843"
FT VARIANT 388
FT /note="R -> C (in WC-EBS; dbSNP:rs59966597)"
FT /evidence="ECO:0000269|PubMed:7561171"
FT /id="VAR_010451"
FT VARIANT 388
FT /note="R -> H (in WC-EBS; dbSNP:rs58645163)"
FT /evidence="ECO:0000269|PubMed:12707098"
FT /id="VAR_031637"
FT VARIANT 408
FT /note="L -> M (in WC-EBS; dbSNP:rs57200223)"
FT /evidence="ECO:0000269|PubMed:12655565"
FT /id="VAR_023724"
FT VARIANT 411
FT /note="Missing (in WC-EBS; dbSNP:rs267607389)"
FT /evidence="ECO:0000269|PubMed:16786515"
FT /id="VAR_027720"
FT VARIANT 413
FT /note="A -> T (in K-EBS; dbSNP:rs59780231)"
FT /evidence="ECO:0000269|Ref.10"
FT /id="VAR_023725"
FT VARIANT 415
FT /note="Y -> C (in WC-EBS; dbSNP:rs59442925)"
FT /evidence="ECO:0000269|PubMed:12707098"
FT /id="VAR_031638"
FT VARIANT 415
FT /note="Y -> H (in K-EBS; dbSNP:rs58380626)"
FT /evidence="ECO:0000269|PubMed:10733662,
FT ECO:0000269|PubMed:10820403, ECO:0000269|Ref.36"
FT /id="VAR_003844"
FT VARIANT 416
FT /note="R -> P (in DM-EBS; dbSNP:rs60622724)"
FT /evidence="ECO:0000269|PubMed:12603865"
FT /id="VAR_031639"
FT VARIANT 417
FT /note="R -> P (in DM-EBS; dbSNP:rs61085704)"
FT /evidence="ECO:0000269|PubMed:16786515"
FT /id="VAR_027721"
FT VARIANT 418
FT /note="L -> Q (probable disease-associated variant found in
FT epidermolysis bullosa simplex with variable phenotype)"
FT /evidence="ECO:0000269|PubMed:24981776"
FT /id="VAR_071705"
FT VARIANT 419
FT /note="L -> Q (in DM-EBS; dbSNP:rs57364972)"
FT /evidence="ECO:0000269|PubMed:10733662,
FT ECO:0000269|PubMed:12655565, ECO:0000269|Ref.36"
FT /id="VAR_003845"
FT VARIANT 422
FT /note="E -> K (in WC-EBS; dbSNP:rs58762773)"
FT /evidence="ECO:0000269|PubMed:10733662"
FT /id="VAR_010452"
FT MUTAGEN 335
FT /note="R->A: Increase in keratin-positive aggregates and
FT keratin intermediate filament networks that are very thin
FT and sparse with short filaments."
FT /evidence="ECO:0000269|PubMed:31995743"
FT MUTAGEN 342
FT /note="E->A: Increase in keratin-positive aggregates and
FT keratin intermediate filament networks that are very thin
FT and sparse with short filaments."
FT /evidence="ECO:0000269|PubMed:31995743"
FT MUTAGEN 346
FT /note="Q->A: Increase in keratin-positive aggregates and
FT keratin intermediate filament networks that are very thin
FT and sparse with short filaments."
FT /evidence="ECO:0000269|PubMed:31995743"
FT MUTAGEN 365
FT /note="R->A: No effect on interaction with KRT5 or keratin
FT intermediate filament networks."
FT /evidence="ECO:0000269|PubMed:31995743"
FT MUTAGEN 366
FT /note="Y->A: No effect on interaction with KRT5 or keratin
FT intermediate filament networks."
FT /evidence="ECO:0000269|PubMed:31995743"
FT MUTAGEN 372
FT /note="Q->A: No effect on interaction with KRT5 or keratin
FT intermediate filament networks."
FT /evidence="ECO:0000269|PubMed:31995743"
FT CONFLICT 26
FT /note="G -> A (in Ref. 1 and 2; AAB59562)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="S -> N (in Ref. 1 and 2; AAB59562)"
FT /evidence="ECO:0000305"
FT HELIX 329..417
FT /evidence="ECO:0007829|PDB:6JFV"
SQ SEQUENCE 472 AA; 51561 MW; 120BA30BA2F8E397 CRC64;
MTTCSRQFTS SSSMKGSCGI GGGIGGGSSR ISSVLAGGSC RAPSTYGGGL SVSSSRFSSG
GACGLGGGYG GGFSSSSSSF GSGFGGGYGG GLGAGLGGGF GGGFAGGDGL LVGSEKVTMQ
NLNDRLASYL DKVRALEEAN ADLEVKIRDW YQRQRPAEIK DYSPYFKTIE DLRNKILTAT
VDNANVLLQI DNARLAADDF RTKYETELNL RMSVEADING LRRVLDELTL ARADLEMQIE
SLKEELAYLK KNHEEEMNAL RGQVGGDVNV EMDAAPGVDL SRILNEMRDQ YEKMAEKNRK
DAEEWFFTKT EELNREVATN SELVQSGKSE ISELRRTMQN LEIELQSQLS MKASLENSLE
ETKGRYCMQL AQIQEMIGSV EEQLAQLRCE MEQQNQEYKI LLDVKTRLEQ EIATYRRLLE
GEDAHLSSSQ FSSGSQSSRD VTSSSRQIRT KVMDVHDGKV VSTHEQVLRT KN
