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   04-NOV-2026, entry version 248.
DE   RecName: Full=Keratin, type I cytoskeletal 14;
DE   AltName: Full=Cytokeratin-14;
DE            Short=CK-14;
DE   AltName: Full=Keratin-14 {ECO:0000303|PubMed:1717157};
DE            Short=K14 {ECO:0000303|PubMed:7682883};
GN   Name=KRT14 {ECO:0000312|HGNC:HGNC:6416};
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 EBS1A 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 EBS1A 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 EBS1B 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 EBS1B 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   FUNCTION, AND INTERACTION WITH KRT5.
RX   PubMed=1694855; DOI=10.1083/jcb.111.1.153;
RA   Coulombe P.A., Fuchs E.;
RT   "Elucidating the early stages of keratin filament assembly.";
RL   J. Cell Biol. 111:153-169(1990).
RN   [12]
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   [13]
RP   INTERACTION WITH PKP1 AND PKP2.
RX   PubMed=10852826; DOI=10.1242/jcs.113.13.2471;
RA   Hofmann I., Mertens C., Brettel M., Nimmrich V., Schnoelzer M.,
RA   Herrmann H.;
RT   "Interaction of plakophilins with desmoplakin and intermediate filament
RT   proteins: an in vitro analysis.";
RL   J. Cell Sci. 113:2471-2483(2000).
RN   [14]
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   [15]
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   [16]
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   [17]
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   [18]
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   [19]
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   [20]
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   [21]
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   [22]
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   [23]
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   [24]
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   [25] {ECO:0000312|PDB:3TNU}
RP   X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH KRT5, DISULFIDE BOND, AND SUBCELLULAR
RP   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   [26] {ECO:0007744|PDB:6JFV}
RP   X-RAY CRYSTALLOGRAPHY OF MUTANT ALA-367 IN COMPLEX WITH KRT5, SUBCELLULAR
RP   LOCATION, AND MUTAGENESIS OF ARG-335; GLU-342; GLN-346; ARG-365; TYR-366
RP   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   [27]
RP   VARIANT EBS1B PRO-384, AND FUNCTION.
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   [28]
RP   VARIANT EBS1C 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   [29]
RP   VARIANT EBS1B 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   [30]
RP   VARIANT EBS1A 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   [31]
RP   VARIANT EBS1D 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   [32]
RP   VARIANT EBS1A 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   [33]
RP   VARIANTS EBS1C ILE-119; ASP-274; ASN-377 AND CYS-388, AND VARIANTS EBS1A
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   [34]
RP   VARIANT EBS1C 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   [35]
RP   VARIANT EBS1A 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   [36]
RP   VARIANT EBS1C 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   [37]
RP   VARIANT EBS1A 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   [38]
RP   VARIANT EBS1B HIS-415, AND VARIANT EBS1A 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   [39]
RP   VARIANT EBS1C ASN-116, VARIANT EBS1A SER-123, VARIANT EBS1B 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   [40]
RP   VARIANT EBS1A 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   [41]
RP   VARIANTS EBS1A CYS-125; HIS-125 AND GLN-419, VARIANTS EBS1B ASP-247 AND
RP   HIS-415, AND VARIANT EBS1C 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   [42]
RP   VARIANTS EBS1A CYS-125 AND HIS-415, AND VARIANT EBS1B 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   [43]
RP   VARIANT EBS1A THR-119, AND VARIANT EBS1B 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   [44]
RP   VARIANT EBS1C CYS-415, VARIANT EBS1A HIS-125, AND VARIANT EBS1D HIS-388.
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   [45]
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   [46]
RP   VARIANTS EBS1A PRO-130 AND GLN-419, AND VARIANT EBS1C 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   [47]
RP   VARIANTS EBS1A SER-128 DEL AND PRO-416, AND VARIANT EBS1C 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   [48]
RP   VARIANTS EBS1A LYS-123 AND GLY-125, AND VARIANT EBS1C 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   [49]
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   [50]
RP   VARIANT EBS1C VAL-119, AND VARIANTS EBS1A 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   [51]
RP   VARIANTS EBS1A LYS-123; CYS-125; HIS-125 AND PRO-417, VARIANTS EBS1B
RP   LEU-133; THR-272 AND PRO-384, AND VARIANTS EBS1C 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   [52]
RP   VARIANTS EBS1C ASN-377; THR-377; CYS-388; MET-408; GLU-411 DEL AND PHE-412,
RP   AND VARIANTS EBS1A SER-123; CYS-125; PRO-130; ARG-272 AND GLN-419.
RX   PubMed=21375516; DOI=10.1111/j.1365-2133.2010.10146.x;
RA   Bolling M.C., Lemmink H.H., Jansen G.H., Jonkman M.F.;
RT   "Mutations in KRT5 and KRT14 cause epidermolysis bullosa simplex in 75% of
RT   the patients.";
RL   Br. J. Dermatol. 164:637-644(2011).
RN   [53]
RP   VARIANT EBS1D HIS-388.
RX   PubMed=22832485; DOI=10.1038/jid.2012.229;
RA   Padalon-Brauch G., Ben Amitai D., Vodo D., Harel A., Sarig O., Sprecher E.,
RA   Mashiah J.;
RT   "Digenic inheritance in epidermolysis bullosa simplex.";
RL   J. Invest. Dermatol. 132:2852-2854(2012).
RN   [54]
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).
RN   [55]
RP   VARIANTS EBS1A THR-119; SER-123; CYS-125; HIS-125 AND ASP-129, VARIANTS
RP   EBS1C MET-133; ALA-270; THR-272; THR-413 AND GLN-418, AND VARIANTS
RP   EPIDERMOLYSIS BULLOSA SIMPLEX LEU-125; CYS-388 AND GLU-411 DEL.
RX   PubMed=26432462; DOI=10.1007/s13353-015-0310-9;
RA   Wertheim-Tysarowska K., Oldak M., Giza A., Kutkowska-Kazmierczak A.,
RA   Sota J., Przybylska D., Wozniak K., Sniegorska D., Niepokoj K.,
RA   Sobczynska-Tomaszewska A., Rygiel A.M., Ploski R., Bal J., Kowalewski C.;
RT   "Novel sporadic and recurrent mutations in KRT5 and KRT14 genes in Polish
RT   epidermolysis bullosa simplex patients: further insights into epidemiology
RT   and genotype-phenotype correlation.";
RL   J. Appl. Genet. 57:175-181(2016).
RN   [56]
RP   TISSUE SPECIFICITY, AND INTERACTION WITH SNF.
RX   PubMed=36512409; DOI=10.1172/jci.insight.162041;
RA   Ievlev V., Lynch T.J., Freischlag K.W., Gries C.B., Shah A., Pai A.C.,
RA   Ahlers B.A., Park S., Engelhardt J.F., Parekh K.R.;
RT   "Krt14 and Krt15 differentially regulate regenerative properties and
RT   differentiation potential of airway basal cells.";
RL   JCI Insight 8:0-0(2023).
RN   [57]
RP   FUNCTION, PHOSPHORYLATION, MUTAGENESIS OF 39-SER--PRO-43 AND CYS-367, AND
RP   INTERACTION WITH SNF.
RX   PubMed=41511042; DOI=10.1083/jcb.202503046;
RA   Redmond C.J., Steiner S.N., Cohen E., Johnson C.N., Oezlue N.,
RA   Coulombe P.A.;
RT   "Keratin 15 promotes a progenitor cell state in basal keratinocytes of skin
RT   epidermis.";
RL   J. Cell Biol. 225:0-0(2026).
CC   -!- FUNCTION: Structural component of intermediate filaments in basal
CC       keratinocytes of stratified epithelia. Forms heteropolymers with type
CC       II keratin KRT5, contributing to the keratin intermediate filament
CC       network that confers mechanical strength and structural integrity to
CC       the basal layer of the epidermis and other stratified epithelial
CC       (PubMed:11724817, PubMed:1694855, PubMed:1720261, PubMed:41511042). The
CC       nonhelical tail domain is involved in promoting KRT5-KRT14 filaments to
CC       self-organize into large bundles and enhances the mechanical properties
CC       involved in resilience of keratin intermediate filaments in vitro
CC       (PubMed:11724817). Displays an antagonist role with KRT15 in basal
CC       epithelial cells, where KRT14 promotes cell differentiation while KRT15
CC       maintains the progenitor state and promotes proliferation and
CC       clonogenicity (PubMed:41511042). Promotes cell differentiation by
CC       retaining YAP1 in the cytoplasm of basal keratinocytes via regulatory
CC       residue C367 and stratifin/SNF interaction (PubMed:41511042).
CC       Contributes to airway basal cell differentiation after injury
CC       (PubMed:36512409). {ECO:0000269|PubMed:11724817,
CC       ECO:0000269|PubMed:1694855, ECO:0000269|PubMed:1720261,
CC       ECO:0000269|PubMed:36512409, ECO:0000269|PubMed:41511042}.
CC   -!- SUBUNIT: Heterodimers composed of type I and type II keratin; forms
CC       parallel coiled-coil heterodimers (PubMed:11724817, PubMed:1694855,
CC       PubMed:22705788, PubMed:24940650). Two heterodimers associate in an
CC       antiparallel manner to form heterotetramers, which further assemble
CC       into higher-order intermediate filaments (PubMed:1694855). Forms a
CC       disulfide-linked heterodimer (via 2B domains) with KRT5 (via 2B
CC       domains) (PubMed:1694855, PubMed:22705788, PubMed:24940650). 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). Interacts with EPPK1 (By
CC       similarity). Interacts with KLHL24 (PubMed:27798626). Interacts with
CC       PKP1 (via N-terminus) and PKP2 (PubMed:10852826). Interacts with
CC       SFN/stratifin; the interaction stabilizes SFN in the cytoplasm
CC       (PubMed:36512409, PubMed:41511042). {ECO:0000250|UniProtKB:Q61781,
CC       ECO:0000269|PubMed:10852826, ECO:0000269|PubMed:11684708,
CC       ECO:0000269|PubMed:11724817, ECO:0000269|PubMed:1694855,
CC       ECO:0000269|PubMed:22705788, ECO:0000269|PubMed:24940650,
CC       ECO:0000269|PubMed:27798626, ECO:0000269|PubMed:36512409,
CC       ECO:0000269|PubMed:41511042}.
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; Q15149: PLEC; NbExp=2; IntAct=EBI-702178, EBI-297903;
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). Expressed in gland ducts and in the myoepithelial
CC       cells of gland tubules and acini in pulmonary bronchus
CC       (PubMed:36512409). {ECO:0000269|PubMed:26758872,
CC       ECO:0000269|PubMed:36512409, 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   -!- PTM: Phosphorylated. {ECO:0000269|PubMed:41511042}.
CC   -!- DISEASE: Epidermolysis bullosa simplex 1A, generalized severe (EBS1A)
CC       [MIM:131760]: A form of epidermolysis bullosa simplex, a group of skin
CC       fragility disorders characterized by skin blistering due to cleavage
CC       within the basal layer of keratinocytes, and erosions caused by minor
CC       mechanical trauma. There is a broad spectrum of clinical severity
CC       ranging from minor blistering on the feet, to subtypes with
CC       extracutaneous involvement and a lethal outcome. EBS1A is an autosomal
CC       dominant form characterized by generalized intraepidermal skin
CC       blistering that begins and is very prominent at birth. EBS1A may be
CC       life-threatening in the first year of life. Tendency to blistering
CC       diminishes in adolescence. {ECO:0000269|PubMed:10583131,
CC       ECO:0000269|PubMed:10730767, ECO:0000269|PubMed:10733662,
CC       ECO:0000269|PubMed:10820403, ECO:0000269|PubMed:11710919,
CC       ECO:0000269|PubMed:12603865, ECO:0000269|PubMed:12655565,
CC       ECO:0000269|PubMed:12707098, ECO:0000269|PubMed:14987259,
CC       ECO:0000269|PubMed:16786515, ECO:0000269|PubMed:16882168,
CC       ECO:0000269|PubMed:1717157, ECO:0000269|PubMed:21375516,
CC       ECO:0000269|PubMed:26432462, ECO:0000269|PubMed:7506097,
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.38}. Note=The disease is
CC       caused by variants affecting the gene represented in this entry.
CC   -!- DISEASE: Epidermolysis bullosa simplex 1C, localized (EBS1C)
CC       [MIM:131800]: A form of epidermolysis bullosa simplex, a group of skin
CC       fragility disorders characterized by skin blistering due to cleavage
CC       within the basal layer of keratinocytes, and erosions caused by minor
CC       mechanical trauma. There is a broad spectrum of clinical severity
CC       ranging from minor blistering on the feet, to subtypes with
CC       extracutaneous involvement and a lethal outcome. EBS1C is an autosomal
CC       dominant form with intraepidermal blistering mainly restricted to hands
CC       and feet beginning in infancy. Nails may be thick and dystrophic.
CC       {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:21375516,
CC       ECO:0000269|PubMed:26432462, ECO:0000269|PubMed:7506606,
CC       ECO:0000269|PubMed:7561171, ECO:0000269|PubMed:9284105,
CC       ECO:0000269|PubMed:9804357, ECO:0000269|PubMed:9989794}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- DISEASE: Epidermolysis bullosa simplex 1B, generalized intermediate
CC       (EBS1B) [MIM:131900]: A form of epidermolysis bullosa simplex, a group
CC       of skin fragility disorders characterized by skin blistering due to
CC       cleavage within the basal layer of keratinocytes, and erosions caused
CC       by minor mechanical trauma. There is a broad spectrum of clinical
CC       severity ranging from minor blistering on the feet, to subtypes with
CC       extracutaneous involvement and a lethal outcome. EBS1B is an autosomal
CC       dominant form characterized by generalized intraepidermal blistering
CC       beginning at birth. The tendency to blistering diminishes in
CC       adolescence, when it may become localized to hands and feet.
CC       {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.38}. Note=The disease is caused by
CC       variants affecting the gene represented in this entry.
CC   -!- DISEASE: Epidermolysis bullosa simplex 1D, generalized, intermediate or
CC       severe, autosomal recessive (EBS1D) [MIM:601001]: A form of
CC       epidermolysis bullosa simplex, a group of skin fragility disorders
CC       characterized by skin blistering due to cleavage within the basal layer
CC       of keratinocytes, and erosions caused by minor mechanical trauma. There
CC       is a broad spectrum of clinical severity ranging from minor blistering
CC       on the feet, to subtypes with extracutaneous involvement and a lethal
CC       outcome. EBS1D is an autosomal recessive form characterized by
CC       blistering beginning at birth or early childhood. In some patients
CC       hands and feet are primarily affected, and in others blistering
CC       anywhere on the body may occur. In some patients the condition improves
CC       with age. {ECO:0000269|PubMed:12707098, ECO:0000269|PubMed:22832485,
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}.
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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_000517.3; NM_000526.5.
DR   PDB; 3TNU; X-ray; 3.00 A; A=295-422.
DR   PDB; 6JFV; X-ray; 2.60 A; A/C=327-421.
DR   PDB; 9VHF; NMR; -; A=120-144.
DR   PDB; 9VHO; NMR; -; A=120-144.
DR   PDB; 9VHS; NMR; -; A=120-144.
DR   PDB; 9VHX; NMR; -; A=120-144.
DR   AlphaFoldDB; P02533; -.
DR   SMR; P02533; -.
DR   BioGRID; 110059; 206.
DR   ComplexPortal; CPX-888; Keratin-5 - Keratin-14 dimer complex.
DR   CORUM; P02533; -.
DR   DIP; DIP-33874N; -.
DR   FunCoup; P02533; 423.
DR   IntAct; P02533; 87.
DR   NDEx; IQUERY-CP-KRT14; 3 NDEx IQuery Curated Pathways.
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; 9606-ENSP00000167586; -.
DR   PeptideAtlas; P02533; -.
DR   PRIDE; P02533; -.
DR   ProteomicsDB; 51528; -.
DR   Antibodypedia; 3600; 1643 antibodies from 55 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   AGR; HGNC:6416; -.
DR   ClinPGx; PA30203; -.
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   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   VEuPathDB; HostDB:ENSG00000186847; -.
DR   eggNOG; ENOG502R8V7; Eukaryota.
DR   GeneTree; ENSGT00940000154602; -.
DR   HOGENOM; CLU_012560_8_1_1; -.
DR   InParanoid; P02533; -.
DR   OMA; ATYRLHC; -.
DR   OrthoDB; 2441647at2759; -.
DR   PAN-GO; P02533; 6 GO annotations based on evolutionary models.
DR   PhylomeDB; P02533; -.
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   Reactome; R-HSA-9725554; Differentiation of Keratinocytes in Interfollicular Epidermis in Mammalian Skin.
DR   Reactome; R-HSA-9927432; Developmental Lineage of Mammary Gland Myoepithelial Cells.
DR   SignaLink; P02533; -.
DR   SIGNOR; P02533; -.
DR   Agora; ENSG00000186847; -.
DR   BioGRID-ORCS; 3861; 17 hits in 1123 CRISPR screens.
DR   ChiTaRS; KRT14; human.
DR   EvolutionaryTrace; P02533; -.
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 121 other cell types or tissues.
DR   GO; GO:0045178; C:basal part of cell; IEA:Ensembl.
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:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
DR   GO; GO:0045095; C:keratin filament; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; IPI:UniProtKB.
DR   GO; GO:1990254; F:keratin filament binding; IPI:UniProtKB.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IDA:UniProt.
DR   GO; GO:0030280; F:structural constituent of skin epidermis; IBA:GO_Central.
DR   GO; GO:0008544; P:epidermis development; TAS:ProtInc.
DR   GO; GO: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   GO; GO:0030216; P:keratinocyte differentiation; IBA:GO_Central.
DR   GO; GO:0002009; P:morphogenesis of an epithelium; IBA:GO_Central.
DR   GO; GO:0045618; P:positive regulation of keratinocyte differentiation; ISS:UniProtKB.
DR   DisProt; DP02605; -.
DR   FunFam; 1.20.5.1160:FF:000002; Type I keratin 10; 1.
DR   FunFam; 1.20.5.170:FF:000002; Type I keratin KA11; 1.
DR   FunFam; 1.20.5.500:FF:000001; Type II keratin 23; 1.
DR   Gene3D; 1.20.5.170; -; 1.
DR   Gene3D; 1.20.5.500; Single helix bin; 1.
DR   Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1.
DR   InterPro; IPR018039; IF_conserved.
DR   InterPro; IPR039008; IF_rod_dom.
DR   InterPro; IPR002957; Keratin_I.
DR   PANTHER; PTHR23239; INTERMEDIATE FILAMENT; 1.
DR   PANTHER; PTHR23239:SF368; KERATIN, TYPE I CYTOSKELETAL 14; 1.
DR   Pfam; PF00038; Filament; 1.
DR   PRINTS; PR01248; TYPE1KERATIN.
DR   SMART; SM01391; Filament; 1.
DR   SUPFAM; SSF64593; Intermediate filament protein, coiled coil region; 2.
DR   SUPFAM; SSF46579; Prefoldin; 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   Proteomics identification; 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        427..445
FT                   /note="Low complexity"
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 EBS1C; dbSNP:rs59271739)"
FT                   /evidence="ECO:0000269|PubMed:9989794"
FT                   /id="VAR_010438"
FT   VARIANT         119
FT                   /note="M -> I (in EBS1C; 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 EBS1A; dbSNP:rs28928893)"
FT                   /evidence="ECO:0000269|PubMed:11710919,
FT                   ECO:0000269|PubMed:26432462, ECO:0000269|PubMed:9804355"
FT                   /id="VAR_010440"
FT   VARIANT         119
FT                   /note="M -> V (in EBS1B and EBS1C; 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 EBS1A; dbSNP:rs60993843)"
FT                   /evidence="ECO:0000269|PubMed:7561171"
FT                   /id="VAR_010441"
FT   VARIANT         122
FT                   /note="L -> F (in EBS1A and EBS1B; 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 EBS1A; 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 EBS1A; dbSNP:rs60171927)"
FT                   /evidence="ECO:0000269|PubMed:21375516,
FT                   ECO:0000269|PubMed:26432462, ECO:0000269|PubMed:9989794"
FT                   /id="VAR_010443"
FT   VARIANT         125
FT                   /note="R -> C (in EBS1A; 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:21375516,
FT                   ECO:0000269|PubMed:26432462, ECO:0000269|PubMed:7561171"
FT                   /id="VAR_003837"
FT   VARIANT         125
FT                   /note="R -> G (in EBS1A; dbSNP:rs60399023)"
FT                   /evidence="ECO:0000269|PubMed:14987259"
FT                   /id="VAR_023721"
FT   VARIANT         125
FT                   /note="R -> H (in EBS1A; 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:26432462,
FT                   ECO:0000269|PubMed:7688405"
FT                   /id="VAR_003838"
FT   VARIANT         125
FT                   /note="R -> L (found in a patient with epidermolysis
FT                   bullosa simplex with unspecified subtype; likely
FT                   pathogenic; dbSNP:rs58330629)"
FT                   /evidence="ECO:0000269|PubMed:26432462"
FT                   /id="VAR_086617"
FT   VARIANT         125
FT                   /note="R -> S (in EBS1A; dbSNP:rs60399023)"
FT                   /evidence="ECO:0000269|PubMed:7561171"
FT                   /id="VAR_010444"
FT   VARIANT         128
FT                   /note="Missing (in EBS1A)"
FT                   /evidence="ECO:0000269|PubMed:12603865"
FT                   /id="VAR_031634"
FT   VARIANT         129
FT                   /note="Y -> D (in EBS1A; dbSNP:rs60470268)"
FT                   /evidence="ECO:0000269|PubMed:26432462,
FT                   ECO:0000269|PubMed:8601736"
FT                   /id="VAR_010445"
FT   VARIANT         130
FT                   /note="L -> P (in EBS1A; uncertain significance;
FT                   dbSNP:rs57522245)"
FT                   /evidence="ECO:0000269|PubMed:12655565,
FT                   ECO:0000269|PubMed:21375516"
FT                   /id="VAR_023722"
FT   VARIANT         133
FT                   /note="V -> A (in dbSNP:rs1555603282)"
FT                   /id="VAR_033496"
FT   VARIANT         133
FT                   /note="V -> L (in EBS1C and EBS1B; dbSNP:rs61027685)"
FT                   /evidence="ECO:0000269|PubMed:14987259,
FT                   ECO:0000269|PubMed:16786515"
FT                   /id="VAR_023723"
FT   VARIANT         133
FT                   /note="V -> M (in EBS1C; dbSNP:rs61027685)"
FT                   /evidence="ECO:0000269|PubMed:26432462"
FT                   /id="VAR_086618"
FT   VARIANT         134
FT                   /note="R -> P (in EBS1B; dbSNP:rs61540016)"
FT                   /evidence="ECO:0000269|PubMed:10820403"
FT                   /id="VAR_031635"
FT   VARIANT         143
FT                   /note="L -> P (in EBS1B; dbSNP:rs61326242)"
FT                   /evidence="ECO:0000269|PubMed:9989794"
FT                   /id="VAR_010446"
FT   VARIANT         144
FT                   /note="E -> A (in EBS1D; dbSNP:rs57121345)"
FT                   /evidence="ECO:0000269|PubMed:7526933"
FT                   /id="VAR_003839"
FT   VARIANT         148
FT                   /note="R -> C (in EBS1C; dbSNP:rs58378809)"
FT                   /evidence="ECO:0000269|PubMed:12603865"
FT                   /id="VAR_031636"
FT   VARIANT         211
FT                   /note="R -> P (in EBS1C; 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 EBS1B; dbSNP:rs147611635)"
FT                   /evidence="ECO:0000269|PubMed:10733662"
FT                   /id="VAR_010447"
FT   VARIANT         270
FT                   /note="V -> A (in EBS1C)"
FT                   /evidence="ECO:0000269|PubMed:26432462"
FT                   /id="VAR_086619"
FT   VARIANT         270
FT                   /note="V -> M (in EBS1A; dbSNP:rs58560979)"
FT                   /evidence="ECO:0000269|PubMed:7506097"
FT                   /id="VAR_086620"
FT   VARIANT         272
FT                   /note="M -> R (in EBS1B and EBS1A; dbSNP:rs61371557)"
FT                   /evidence="ECO:0000269|PubMed:21375516,
FT                   ECO:0000269|PubMed:7682883"
FT                   /id="VAR_003841"
FT   VARIANT         272
FT                   /note="M -> T (in EBS1B and EBS1C; dbSNP:rs61371557)"
FT                   /evidence="ECO:0000269|PubMed:16786515,
FT                   ECO:0000269|PubMed:26432462"
FT                   /id="VAR_027719"
FT   VARIANT         273
FT                   /note="D -> G (in EBS1C; dbSNP:rs59375065)"
FT                   /evidence="ECO:0000269|PubMed:9804357"
FT                   /id="VAR_010448"
FT   VARIANT         274
FT                   /note="A -> D (in EBS1C; dbSNP:rs58785777)"
FT                   /evidence="ECO:0000269|PubMed:7561171"
FT                   /id="VAR_010449"
FT   VARIANT         375
FT                   /note="Missing (in EBS1C; dbSNP:rs56974573)"
FT                   /evidence="ECO:0000269|PubMed:7506606"
FT                   /id="VAR_003842"
FT   VARIANT         377
FT                   /note="I -> N (in EBS1C; dbSNP:rs61536893)"
FT                   /evidence="ECO:0000269|PubMed:21375516,
FT                   ECO:0000269|PubMed:7561171"
FT                   /id="VAR_010450"
FT   VARIANT         377
FT                   /note="I -> T (in EBS1C; uncertain significance;
FT                   dbSNP:rs61536893)"
FT                   /evidence="ECO:0000269|PubMed:21375516"
FT                   /id="VAR_086621"
FT   VARIANT         384
FT                   /note="L -> P (in EBS1B; 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 EBS1C; also found in a patient with
FT                   epidermolysis bullosa simplex with unspecified subtype;
FT                   dbSNP:rs59966597)"
FT                   /evidence="ECO:0000269|PubMed:21375516,
FT                   ECO:0000269|PubMed:26432462, ECO:0000269|PubMed:7561171"
FT                   /id="VAR_010451"
FT   VARIANT         388
FT                   /note="R -> H (in EBS1D; dbSNP:rs58645163)"
FT                   /evidence="ECO:0000269|PubMed:12707098,
FT                   ECO:0000269|PubMed:22832485"
FT                   /id="VAR_031637"
FT   VARIANT         408
FT                   /note="L -> M (in EBS1C; dbSNP:rs57200223)"
FT                   /evidence="ECO:0000269|PubMed:12655565,
FT                   ECO:0000269|PubMed:21375516"
FT                   /id="VAR_023724"
FT   VARIANT         411
FT                   /note="Missing (in EBS1C; also found in a patient with
FT                   epidermolysis bullosa simplex with unspecified subtype;
FT                   dbSNP:rs267607389)"
FT                   /evidence="ECO:0000269|PubMed:16786515,
FT                   ECO:0000269|PubMed:21375516, ECO:0000269|PubMed:26432462"
FT                   /id="VAR_027720"
FT   VARIANT         412
FT                   /note="I -> F (in EBS1C; uncertain significance;
FT                   dbSNP:rs267607403)"
FT                   /evidence="ECO:0000269|PubMed:21375516"
FT                   /id="VAR_086622"
FT   VARIANT         413
FT                   /note="A -> T (in EBS1B and EBS1C; uncertain significance;
FT                   dbSNP:rs59780231)"
FT                   /evidence="ECO:0000269|PubMed:26432462, ECO:0000269|Ref.10"
FT                   /id="VAR_023725"
FT   VARIANT         415
FT                   /note="Y -> C (in EBS1C; dbSNP:rs59442925)"
FT                   /evidence="ECO:0000269|PubMed:12707098"
FT                   /id="VAR_031638"
FT   VARIANT         415
FT                   /note="Y -> H (in EBS1B; dbSNP:rs58380626)"
FT                   /evidence="ECO:0000269|PubMed:10733662,
FT                   ECO:0000269|PubMed:10820403, ECO:0000269|Ref.38"
FT                   /id="VAR_003844"
FT   VARIANT         416
FT                   /note="R -> P (in EBS1A; dbSNP:rs60622724)"
FT                   /evidence="ECO:0000269|PubMed:12603865"
FT                   /id="VAR_031639"
FT   VARIANT         417
FT                   /note="R -> P (in EBS1A; dbSNP:rs61085704)"
FT                   /evidence="ECO:0000269|PubMed:16786515"
FT                   /id="VAR_027721"
FT   VARIANT         418
FT                   /note="L -> Q (in EBS1C)"
FT                   /evidence="ECO:0000269|PubMed:24981776,
FT                   ECO:0000269|PubMed:26432462"
FT                   /id="VAR_071705"
FT   VARIANT         419
FT                   /note="L -> Q (in EBS1A; dbSNP:rs57364972)"
FT                   /evidence="ECO:0000269|PubMed:10733662,
FT                   ECO:0000269|PubMed:12655565, ECO:0000269|PubMed:21375516,
FT                   ECO:0000269|Ref.38"
FT                   /id="VAR_003845"
FT   VARIANT         422
FT                   /note="E -> K (in EBS1C; dbSNP:rs58762773)"
FT                   /evidence="ECO:0000269|PubMed:10733662"
FT                   /id="VAR_010452"
FT   MUTAGEN         39..43
FT                   /note="SCRAP->GFGGG: Loss of SFN-YAP proximity."
FT                   /evidence="ECO:0000269|PubMed:41511042"
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         367
FT                   /note="C->A: Loss of SFN-YAP proximity."
FT                   /evidence="ECO:0000269|PubMed:41511042"
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
//