K2C5_HUMAN
ID K2C5_HUMAN Reviewed; 590 AA.
AC P13647; Q6PI71; Q6UBJ0; Q8TA91;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 3.
DT 03-AUG-2022, entry version 239.
DE RecName: Full=Keratin, type II cytoskeletal 5;
DE AltName: Full=58 kDa cytokeratin;
DE AltName: Full=Cytokeratin-5;
DE Short=CK-5;
DE AltName: Full=Keratin-5;
DE Short=K5;
DE AltName: Full=Type-II keratin Kb5;
GN Name=KRT5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ARG-79 AND THR-387.
RX PubMed=2456903; DOI=10.1089/dna.1.1988.7.337;
RA Eckert R.L., Rorke E.A.;
RT "The sequence of the human epidermal 58-kD (#5) type II keratin reveals an
RT absence of 5' upstream sequence conservation between coexpressed epidermal
RT keratins.";
RL DNA 7:337-345(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLU-197.
RX PubMed=2476664; DOI=10.1128/mcb.9.9.3685-3697.1989;
RA Lersch R., Stellmach V., Stocks X., Giudice G., Fuchs E.;
RT "Isolation, sequence, and expression of a human keratin K5 gene:
RT transcriptional regulation of keratins and insights into pairwise
RT control.";
RL Mol. Cell. Biol. 9:3685-3697(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-79 AND THR-387.
RX PubMed=10903910; DOI=10.1006/bbrc.2000.3110;
RA Whittock N.V., Eady R.A.J., McGrath J.A.;
RT "Genomic organization and amplification of the human epidermal type II
RT keratin genes K1 and K5.";
RL Biochem. Biophys. Res. Commun. 274:149-152(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLY-528 AND SER-543.
RC TISSUE=Brain, and Pancreas;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 83-590, AND VARIANT GLU-197.
RX PubMed=2447486; DOI=10.1128/mcb.8.1.486-493.1988;
RA Lersch R., Fuchs E.;
RT "Sequence and expression of a type II keratin, K5, in human epidermal
RT cells.";
RL Mol. Cell. Biol. 8:486-493(1988).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 186-256, AND VARIANT EBS2C THR-199.
RX PubMed=14723728; DOI=10.1111/j.1365-2230.2004.01434.x;
RA Xu Z., Dong H., Sun X., Zhu X., Yang Y.;
RT "A new keratin 5 mutation (K199T) in a family with Weber-Cockayne
RT epidermolysis bullosa simplex.";
RL Clin. Exp. Dermatol. 29:74-76(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 348-590, AND VARIANT SER-543.
RX PubMed=2455002; DOI=10.1111/1523-1747.ep12463286;
RA Galup C., Darmon M.Y.;
RT "Isolation and characterization of a cDNA clone coding for human epidermal
RT keratin K5. Sequence of the carboxyterminal half of this keratin.";
RL J. Invest. Dermatol. 91:39-42(1988).
RN [8]
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 [9]
RP INTERACTION WITH TCHP.
RX PubMed=15731013; DOI=10.1242/jcs.01667;
RA Nishizawa M., Izawa I., Inoko A., Hayashi Y., Nagata K., Yokoyama T.,
RA Usukura J., Inagaki M.;
RT "Identification of trichoplein, a novel keratin filament-binding protein.";
RL J. Cell Sci. 118:1081-1090(2005).
RN [10]
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 [11]
RP IDENTIFICATION IN A COMPLEX WITH KRT14, AND INTERACTION WITH KRT14 AND
RP 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 [12]
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 [13]
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 [14]
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 [15]
RP SUBUNIT.
RX PubMed=28899683; DOI=10.1016/j.jid.2017.08.035;
RA Yu X., Chen F., Ni C., Zhang G., Zheng L., Zhang J., Li C., Sandilands A.,
RA Yao Z., Li M.;
RT "A missense mutation within the helix termination motif of KRT25 causes
RT autosomal dominant woolly hair/hypotrichosis.";
RL J. Invest. Dermatol. 138:230-233(2018).
RN [16] {ECO:0000312|PDB:3TNU}
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 350-477 IN COMPLEX WITH KRT14, AND
RP SUBUNIT.
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 [17] {ECO:0000312|PDB:6JFV}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 379-476 IN COMPLEX WITH KRT14,
RP AND MUTAGENESIS OF GLU-399; GLN-411; ASN-412; GLU-422; GLU-437; GLN-440 AND
RP GLN-444.
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 [18]
RP VARIANT EBS2A GLY-475.
RX PubMed=1372711; DOI=10.1038/356244a0;
RA Lane E.B., Rugg E.L., Navsaria H.A., Leigh I.M., Heagerty A.H.M.,
RA Ishida-Yamamoto A., Eady R.A.J.;
RT "A mutation in the conserved helix termination peptide of keratin 5 in
RT hereditary skin blistering.";
RL Nature 356:244-246(1992).
RN [19]
RP VARIANT EBS2B PRO-463.
RX PubMed=7686424; DOI=10.1002/humu.1380020206;
RA Dong W., Ryynaenen M., Uitto J.;
RT "Identification of a leucine-to-proline mutation in the keratin 5 gene in a
RT family with the generalized Kobner type of epidermolysis bullosa simplex.";
RL Hum. Mutat. 2:94-102(1993).
RN [20]
RP VARIANT GLU-138.
RX PubMed=7684424; DOI=10.1111/1523-1747.ep12475671;
RA Wanner R., Foerster H.-H., Tilmans I., Mischke D.;
RT "Allelic variations of human keratins K4 and K5 provide polymorphic markers
RT within the type II keratin gene cluster on chromosome 12.";
RL J. Invest. Dermatol. 100:735-741(1993).
RN [21]
RP VARIANT EBS2A LYS-193.
RA Smith F.J.D., Morley S.M., Rugg E.L., Navsaria H.A., Leigh I.M.,
RA Eady R.A.J., Tidman M.J., Lane E.B.;
RT "Clustering of epidermolysis bullosa simplex mutations in relation to
RT disease phenotype: data from Weber-Cockayne EBS.";
RL J. Invest. Dermatol. 101:481A-481A(1993).
RN [22]
RP VARIANT EBS2C CYS-331.
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 [23]
RP VARIANT EBS2C SER-161.
RX PubMed=7688477; DOI=10.1073/pnas.90.15.7414;
RA Chan Y.-M., Yu Q.-C., Fine J.-D., Fuchs E.;
RT "The genetic basis of Weber-Cockayne epidermolysis bullosa simplex.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:7414-7418(1993).
RN [24]
RP VARIANTS EBS2C THR-327 AND LYS-329.
RX PubMed=7520042; DOI=10.1242/jcs.107.4.765;
RA Chan Y.-M., Yu Q.-C., LeBlanc-Straceski J., Christiano A., Pulkkinen L.,
RA Kucherlapati R.S., Uitto J., Fuchs E.;
RT "Mutations in the non-helical linker segment L1-2 of keratin 5 in patients
RT with Weber-Cockayne epidermolysis bullosa simplex.";
RL J. Cell Sci. 107:765-774(1994).
RN [25]
RP VARIANT EBS2B ASN-173.
RX PubMed=7534039;
RA Stephens K., Zlotogorski A., Smith L., Ehrlich P., Wijsman E.M.,
RA Livingston R.J., Sybert V.P.;
RT "Epidermolysis bullosa simplex: a keratin 5 mutation is a fully dominant
RT allele in epidermal cytoskeleton function.";
RL Am. J. Hum. Genet. 56:577-585(1995).
RN [26]
RP VARIANT EBS2C VAL-328.
RX PubMed=8595431; DOI=10.1093/hmg/4.10.1999;
RA Matsuki M., Hashimoto K., Yoshikawa K., Yasuno H., Yamanishi K.;
RT "Epidermolysis bullosa simplex (Weber-Cockayne) associated with a novel
RT missense mutation of Asp328 to Val in linker 12 domain of keratin 5.";
RL Hum. Mol. Genet. 4:1999-2000(1995).
RN [27]
RP VARIANTS EBS2C LYS-193 AND THR-327.
RX PubMed=8807337;
RX DOI=10.1002/(sici)1098-1004(1996)8:1<57::aid-humu8>3.0.co;2-m;
RA Humphries M.M., Mansergh F.C., Kiang A.-S., Jordan S.A., Sheils D.M.,
RA Martin M.J., Farrar G.J., Kenna P.F., Young M.M., Humphries P.;
RT "Three keratin gene mutations account for the majority of dominant simplex
RT epidermolysis bullosa cases within the population of Ireland.";
RL Hum. Mutat. 8:57-63(1996).
RN [28]
RP VARIANT EBS2A PHE-175.
RX PubMed=8757772; DOI=10.1111/1523-1747.ep12329741;
RA Nomura K., Shimizu H., Meng X., Umeki K., Tamai K., Sawamura D., Nagao K.,
RA Kawakami T., Nishikawa T., Hashimoto I.;
RT "A novel keratin K5 gene mutation in Dowling-Meara epidermolysis bullosa
RT simplex.";
RL J. Invest. Dermatol. 107:253-254(1996).
RN [29]
RP VARIANT EBS2F LEU-25.
RX PubMed=8799157; DOI=10.1073/pnas.93.17.9079;
RA Uttam J., Hutton M.E., Coulombe P.A., Anton-Lamprecht I., Yu Q.-C.,
RA Gedde-Dahl T. Jr., Fine J.-D., Fuchs E.;
RT "The genetic basis of epidermolysis bullosa simplex with mottled
RT pigmentation.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:9079-9084(1996).
RN [30]
RP VARIANTS EBS2A SER-176; SER-179 AND LYS-477.
RX PubMed=9036937; DOI=10.1111/1523-1747.ep12286486;
RA Stephens K., Ehrlich P., Weaver M., Le R., Spencer A., Sybert V.P.;
RT "Primers for exon-specific amplification of the KRT5 gene: identification
RT of novel and recurrent mutations in epidermolysis bullosa simplex
RT patients.";
RL J. Invest. Dermatol. 108:349-353(1997).
RN [31]
RP VARIANT EBS2A THR-467.
RX PubMed=9406827; DOI=10.1111/1523-1747.ep12341024;
RA Irvine A.D., McKenna K.E., Bingham A., Nevin N.C., Hughes A.E.;
RT "A novel mutation in the helix termination peptide of keratin 5 causing
RT epidermolysis bullosa simplex Dowling-Meara.";
RL J. Invest. Dermatol. 109:815-816(1997).
RN [32]
RP VARIANT EBS2B ALA-323.
RX PubMed=9740251; DOI=10.1046/j.1523-1747.1998.00308.x;
RA Galligan P., Listwan P., Siller G.M., Rothnagel J.A.;
RT "A novel mutation in the L12 domain of keratin 5 in the Koebner variant of
RT epidermolysis bullosa simplex.";
RL J. Invest. Dermatol. 111:524-527(1998).
RN [33]
RP VARIANTS EBS2C LEU-152; LYS-327 AND HIS-328.
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 [34]
RP VARIANT EBS2F LEU-25.
RX PubMed=10494094;
RX DOI=10.1002/(sici)1096-8628(19991008)86:4<376::aid-ajmg12>3.0.co;2-w;
RA Moog U., de Die-Smulders C.E.M., Scheffer H., van der Vlies P.,
RA Henquet C.J.M., Jonkman M.F.;
RT "Epidermolysis bullosa simplex with mottled pigmentation: clinical aspects
RT and confirmation of the P24L mutation in the KRT5 gene in further
RT patients.";
RL Am. J. Med. Genet. 86:376-379(1999).
RN [35]
RP VARIANT EBS2A SER-176, AND VARIANT EBS2B PRO-325.
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 [36]
RP VARIANT EBS2A PRO-181.
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 [37]
RP VARIANT EBS2C GLU-328.
RX PubMed=10782015; DOI=10.1159/000022921;
RA Liovic M., Podrumac B., Dragos V., Vouk K., Komel R.;
RT "K5 D328E: a novel missense mutation in the linker 12 domain of keratin 5
RT associated with epidermolysis bullosa simplex (Weber-Cockayne).";
RL Hum. Hered. 50:234-236(2000).
RN [38]
RP VARIANT EBS2B LEU-186.
RX PubMed=11407988; DOI=10.1046/j.1523-1747.2001.01334.x;
RA Liovic M., Stojan J., Bowden P.E., Gibbs D., Vahlquist A., Lane E.B.,
RA Komel R.;
RT "A novel keratin 5 mutation (K5V186L) in a family with EBS-K: a
RT conservative substitution can lead to development of different disease
RT phenotypes.";
RL J. Invest. Dermatol. 116:964-969(2001).
RN [39]
RP VARIANTS EBS2D LYS-170 AND LYS-418.
RX PubMed=11973334; DOI=10.1074/jbc.m200974200;
RA Yasukawa K., Sawamura D., McMillan J.R., Nakamura H., Shimizu H.;
RT "Dominant and recessive compound heterozygous mutations in epidermolysis
RT bullosa simplex demonstrate the role of the stutter region in keratin
RT intermediate filament assembly.";
RL J. Biol. Chem. 277:23670-23674(2002).
RN [40]
RP VARIANTS EBS2C LYS-167; PRO-311 AND ASP-324.
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 [41]
RP VARIANTS EBS2C GLU-404 AND ASP-438, AND VARIANTS EBS2A LYS-475 AND LYS-477.
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 [42]
RP INVOLVEMENT IN EBS2E.
RX PubMed=12925204; DOI=10.1046/j.1523-1747.2003.12424.x;
RA Gu L.-H., Kim S.-C., Ichiki Y., Park J., Nagai M., Kitajima Y.;
RT "A usual frameshift and delayed termination codon mutation in keratin 5
RT causes a novel type of epidermolysis bullosa simplex with migratory
RT circinate erythema.";
RL J. Invest. Dermatol. 121:482-485(2003).
RN [43]
RP VARIANT EBS2C GLY-328.
RX PubMed=15347343; DOI=10.1111/j.1365-2230.2004.01565.x;
RA Li J.-G., Feng J., Xiao S.-X., Ai Y.-L., Wang J.-M., Peng Z.-H.;
RT "A new mutation in the linker 12 domain of keratin 5 in a Chinese family
RT with Weber-Cockayne epidermolysis bullosa simplex.";
RL Clin. Exp. Dermatol. 29:539-541(2004).
RN [44]
RP VARIANT EBS2C SER-177.
RX PubMed=15140024; DOI=10.1111/j.0906-6705.2004.00171.x;
RA Liovic M., Bowden P.E., Marks R., Komel R.;
RT "A mutation (N177S) in the structurally conserved helix initiation peptide
RT motif of keratin 5 causes a mild EBS phenotype.";
RL Exp. Dermatol. 13:332-334(2004).
RN [45]
RP INVOLVEMENT IN DDD1.
RX PubMed=16465624; DOI=10.1086/500850;
RA Betz R.C., Planko L., Eigelshoven S., Hanneken S., Pasternack S.M.,
RA Buessow H., Bogaert K.V., Wenzel J., Braun-Falco M., Ruetten A.,
RA Rogers M.A., Ruzicka T., Noethen M.M., Magin T.M., Kruse R.;
RT "Loss-of-function mutations in the keratin 5 gene lead to Dowling-Degos
RT disease.";
RL Am. J. Hum. Genet. 78:510-519(2006).
RN [46]
RP VARIANTS EBS2C LEU-25; VAL-158 AND SER-352, VARIANTS EBS2B ASP-143;
RP MET-186; LEU-186; PRO-191 AND ASP-517, VARIANTS EBS2A SER-176; LYS-475 AND
RP LYS-477, AND VARIANT EBS2F LEU-25.
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 [47]
RP VARIANTS EBS2A LYS-168; PRO-169 AND PRO-469, AND VARIANTS EBS2C LYS-190 AND
RP HIS-331.
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 [48]
RP VARIANTS EBS2C GLU-186; LYS-193; PRO-321; VAL-328 AND THR-428, VARIANTS
RP EBS2A SER-165 AND LYS-477, VARIANT EBS2F LEU-25, AND VARIANT EBS2B PRO-463.
RX PubMed=21623745; DOI=10.1111/j.1365-2133.2011.10428.x;
RA Garcia M., Santiago J.L., Terron A., Hernandez-Martin A., Vicente A.,
RA Fortuny C., De Lucas R., Lopez J.C., Cuadrado-Corrales N., Holguin A.,
RA Illera N., Duarte B., Sanchez-Jimeno C., Llames S., Garcia E., Ayuso C.,
RA Martinez-Santamaria L., Castiglia D., De Luca N., Torrelo A., Mechan D.,
RA Baty D., Zambruno G., Escamez M.J., Del Rio M.;
RT "Two novel recessive mutations in KRT14 identified in a cohort of 21
RT Spanish families with epidermolysis bullosa simplex.";
RL Br. J. Dermatol. 165:683-692(2011).
CC -!- FUNCTION: Required for the formation of keratin intermediate filaments
CC in the basal epidermis and maintenance of the skin barrier in response
CC to mechanical stress (By similarity). Regulates the recruitment of
CC Langerhans cells to the epidermis, potentially by modulation of the
CC abundance of macrophage chemotactic cytokines, macrophage inflammatory
CC cytokines and CTNND1 localization in keratinocytes (By similarity).
CC {ECO:0000250|UniProtKB:Q922U2}.
CC -!- SUBUNIT: Heterodimer of a type I and a type II keratin
CC (PubMed:22705788, PubMed:31995743). Heterodimer with type I keratin
CC KRT25 leading to the formation of keratin intermediate filament (KIF)
CC network (PubMed:28899683). Forms a heterodimer (via 2B domains) with
CC KRT14 (via 2B domains) (PubMed:24940650, PubMed:22705788,
CC PubMed:31995743). Interacts with PLEC isoform 1C, when in a heterodimer
CC with KRT14 (PubMed:24940650). Interacts with TCHP (PubMed:15731013).
CC Interacts with EPPK1 (By similarity). Interacts with AMELX (By
CC similarity). {ECO:0000250|UniProtKB:Q922U2,
CC ECO:0000269|PubMed:15731013, ECO:0000269|PubMed:22705788,
CC ECO:0000269|PubMed:24940650, ECO:0000269|PubMed:28899683,
CC ECO:0000269|PubMed:31995743}.
CC -!- INTERACTION:
CC P13647; P18054: ALOX12; NbExp=7; IntAct=EBI-702187, EBI-1633210;
CC P13647; Q0VD86: INCA1; NbExp=3; IntAct=EBI-702187, EBI-6509505;
CC P13647; Q9BVG8: KIFC3; NbExp=3; IntAct=EBI-702187, EBI-2125614;
CC P13647; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-702187, EBI-14069005;
CC P13647; P02533: KRT14; NbExp=8; IntAct=EBI-702187, EBI-702178;
CC P13647; P19012: KRT15; NbExp=6; IntAct=EBI-702187, EBI-739566;
CC P13647; P08779: KRT16; NbExp=3; IntAct=EBI-702187, EBI-356410;
CC P13647; P08727: KRT19; NbExp=3; IntAct=EBI-702187, EBI-742756;
CC P13647; Q2M2I5: KRT24; NbExp=3; IntAct=EBI-702187, EBI-2952736;
CC P13647; Q7Z3Z0: KRT25; NbExp=3; IntAct=EBI-702187, EBI-11980019;
CC P13647; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-702187, EBI-3044087;
CC P13647; Q7Z3Y7: KRT28; NbExp=3; IntAct=EBI-702187, EBI-11980489;
CC P13647; Q15323: KRT31; NbExp=6; IntAct=EBI-702187, EBI-948001;
CC P13647; Q92764: KRT35; NbExp=3; IntAct=EBI-702187, EBI-1058674;
CC P13647; O76015: KRT38; NbExp=6; IntAct=EBI-702187, EBI-1047263;
CC P13647; Q6A162: KRT40; NbExp=6; IntAct=EBI-702187, EBI-10171697;
CC P13647; Q13835-2: PKP1; NbExp=2; IntAct=EBI-702187, EBI-9087684;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q922U2}.
CC -!- TISSUE SPECIFICITY: Expressed in corneal epithelium (at protein level).
CC {ECO:0000269|PubMed:26758872}.
CC -!- PTM: Phosphorylated by CDK1, AURKB and Rho-kinase, phosphorylation is
CC regulated by the cell cycle (By similarity). Thr-24 phosphorylation,
CC mediated by CDK1, peaks during prometaphase or metaphase cells with
CC phosphorylated filamentous structures evident throughout the cytoplasm
CC during early mitosis (By similarity). CDK1 phosphorylates Thr-24 in
CC mitotic cells at the site of injury (By similarity).
CC {ECO:0000250|UniProtKB:Q922U2}.
CC -!- PTM: O-glycosylated. {ECO:0000250|UniProtKB:Q922U2}.
CC -!- DISEASE: Epidermolysis bullosa simplex 2A, generalized severe (EBS2A)
CC [MIM:619555]: 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. EBS2A is an autosomal
CC dominant, severe form characterized by extensive intra-epidermal
CC blistering from the time of birth with herpetiform marginal spreading
CC and central healing. Oral mucosal involvement, nail dystrophy,
CC onychogryposis, formation of milia, and palmoplantar hyperkeratosis are
CC common features. {ECO:0000269|PubMed:10730767,
CC ECO:0000269|PubMed:12655565, ECO:0000269|PubMed:1372711,
CC ECO:0000269|PubMed:16786515, ECO:0000269|PubMed:16882168,
CC ECO:0000269|PubMed:21623745, ECO:0000269|PubMed:8757772,
CC ECO:0000269|PubMed:9036937, ECO:0000269|PubMed:9406827,
CC ECO:0000269|PubMed:9989794, ECO:0000269|Ref.21}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: Epidermolysis bullosa simplex 2B, generalized intermediate
CC (EBS2B) [MIM:619588]: 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. EBS2B is an autosomal
CC dominant form characterized by generalized blistering manifesting at
CC birth. The tendency to blistering diminishes in adolescence, when it
CC may become localized to hands and feet. {ECO:0000269|PubMed:11407988,
CC ECO:0000269|PubMed:16882168, ECO:0000269|PubMed:21623745,
CC ECO:0000269|PubMed:7534039, ECO:0000269|PubMed:7686424,
CC ECO:0000269|PubMed:9740251, 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 2C, localized (EBS2C)
CC [MIM:619594]: 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. EBS2C is an autosomal
CC dominant form with intra-epidermal blistering after minor trauma mainly
CC restricted to hands and feet beginning in infancy. Nails may be thick
CC and dystrophic. {ECO:0000269|PubMed:10782015,
CC ECO:0000269|PubMed:12655565, ECO:0000269|PubMed:12707098,
CC ECO:0000269|PubMed:14723728, ECO:0000269|PubMed:15140024,
CC ECO:0000269|PubMed:15347343, ECO:0000269|PubMed:16786515,
CC ECO:0000269|PubMed:16882168, ECO:0000269|PubMed:21623745,
CC ECO:0000269|PubMed:7506097, ECO:0000269|PubMed:7520042,
CC ECO:0000269|PubMed:7688477, ECO:0000269|PubMed:8595431,
CC ECO:0000269|PubMed:8807337, ECO:0000269|PubMed:9804357}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Epidermolysis bullosa simplex 2D, generalized, intermediate or
CC severe, autosomal recessive (EBS2D) [MIM:619599]: A form of
CC epidermolysis bullosa, a genodermatosis characterized by recurrent
CC blistering and cleavage within basal keratinocytes, fragility of the
CC skin and mucosal epithelia, and erosions caused by minor mechanical
CC trauma. EBS2D is an autosomal recessive form characterized by
CC widespread intra-epidermal skin blistering and erosions from birth.
CC Death may occur in the neonatal period. {ECO:0000269|PubMed:11973334}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- DISEASE: Epidermolysis bullosa simplex 2E, with migratory circinate
CC erythema (EBS2E) [MIM:609352]: A form of epidermolysis bullosa, a
CC genodermatosis characterized by recurrent blistering and cleavage
CC within basal keratinocytes, fragility of the skin and mucosal
CC epithelia, and erosions caused by minor mechanical trauma. EBS2E is an
CC autosomal dominant form in which multiple vesicles are present from
CC birth onward and acquire over time a typical migratory circinate
CC pattern on an erythematous background. Postinflammatory
CC hyperpigmentation develops gradually and may have a mottled pattern.
CC {ECO:0000269|PubMed:12925204}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Epidermolysis bullosa simplex 2F, with mottled pigmentation
CC (EBS2F) [MIM:131960]: 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. EBS2F is an autosomal
CC dominant form characterized by generalized skin blistering of
CC intermediate severity beginning at birth, with mottled or reticulate
CC pigmentation developing gradually. Focal keratoses of palms and soles
CC and dystrophic, thickened nails develop over time.
CC {ECO:0000269|PubMed:10494094, ECO:0000269|PubMed:16882168,
CC ECO:0000269|PubMed:21623745, ECO:0000269|PubMed:8799157}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Dowling-Degos disease 1 (DDD1) [MIM:179850]: An autosomal
CC dominant genodermatosis. Affected individuals develop a postpubertal
CC reticulate hyperpigmentation that is progressive and disfiguring, and
CC small hyperkeratotic dark brown papules that affect mainly the flexures
CC and great skin folds. Patients usually show no abnormalities of the
CC hair or nails. {ECO:0000269|PubMed:16465624}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: There are two types of cytoskeletal and microfibrillar
CC keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
CC -!- WEB RESOURCE: Name=Human Intermediate Filament Mutation Database;
CC URL="http://www.interfil.org";
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DR EMBL; M21389; AAA36143.1; -; mRNA.
DR EMBL; M28496; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF274874; AAF97931.1; -; Genomic_DNA.
DR EMBL; BC024292; AAH24292.1; -; mRNA.
DR EMBL; BC042132; AAH42132.1; -; mRNA.
DR EMBL; BC071906; AAH71906.1; -; mRNA.
DR EMBL; M19723; AAA36145.1; -; mRNA.
DR EMBL; AY373434; AAQ81588.1; -; mRNA.
DR CCDS; CCDS8830.1; -.
DR PIR; A29904; A29904.
DR RefSeq; NP_000415.2; NM_000424.3.
DR PDB; 3TNU; X-ray; 3.00 A; B=350-477.
DR PDB; 6JFV; X-ray; 2.60 A; B/D=379-476.
DR PDBsum; 3TNU; -.
DR PDBsum; 6JFV; -.
DR AlphaFoldDB; P13647; -.
DR SMR; P13647; -.
DR BioGRID; 110050; 120.
DR ComplexPortal; CPX-888; Keratin-5 - Keratin-14 dimer complex.
DR DIP; DIP-39N; -.
DR IntAct; P13647; 52.
DR MINT; P13647; -.
DR STRING; 9606.ENSP00000252242; -.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR Allergome; 415; Hom s 5.
DR GlyGen; P13647; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P13647; -.
DR PhosphoSitePlus; P13647; -.
DR SwissPalm; P13647; -.
DR BioMuta; KRT5; -.
DR DMDM; 143811411; -.
DR jPOST; P13647; -.
DR MassIVE; P13647; -.
DR PaxDb; P13647; -.
DR PeptideAtlas; P13647; -.
DR PRIDE; P13647; -.
DR ProteomicsDB; 52954; -.
DR Antibodypedia; 3501; 1541 antibodies from 50 providers.
DR CPTC; P13647; 2 antibodies.
DR DNASU; 3852; -.
DR Ensembl; ENST00000252242.9; ENSP00000252242.4; ENSG00000186081.12.
DR GeneID; 3852; -.
DR KEGG; hsa:3852; -.
DR MANE-Select; ENST00000252242.9; ENSP00000252242.4; NM_000424.4; NP_000415.2.
DR UCSC; uc001san.4; human.
DR CTD; 3852; -.
DR DisGeNET; 3852; -.
DR GeneCards; KRT5; -.
DR GeneReviews; KRT5; -.
DR HGNC; HGNC:6442; KRT5.
DR HPA; ENSG00000186081; Group enriched (esophagus, skin, vagina).
DR MalaCards; KRT5; -.
DR MIM; 131960; phenotype.
DR MIM; 148040; gene.
DR MIM; 179850; phenotype.
DR MIM; 609352; phenotype.
DR MIM; 619555; phenotype.
DR MIM; 619588; phenotype.
DR MIM; 619594; phenotype.
DR MIM; 619599; phenotype.
DR neXtProt; NX_P13647; -.
DR OpenTargets; ENSG00000186081; -.
DR Orphanet; 79399; Autosomal dominant generalized epidermolysis bullosa simplex, intermediate form.
DR Orphanet; 79396; Autosomal dominant generalized epidermolysis bullosa simplex, severe form.
DR Orphanet; 79145; Dowling-Degos disease.
DR Orphanet; 158681; Epidermolysis bullosa simplex with circinate migratory erythema.
DR Orphanet; 79397; Epidermolysis bullosa simplex with mottled pigmentation.
DR Orphanet; 79400; Localized epidermolysis bullosa simplex.
DR PharmGKB; PA30230; -.
DR VEuPathDB; HostDB:ENSG00000186081; -.
DR eggNOG; ENOG502QURK; Eukaryota.
DR GeneTree; ENSGT00940000160458; -.
DR HOGENOM; CLU_012560_6_1_1; -.
DR InParanoid; P13647; -.
DR OMA; MHTHISD; -.
DR OrthoDB; 824246at2759; -.
DR PhylomeDB; P13647; -.
DR TreeFam; TF317854; -.
DR PathwayCommons; P13647; -.
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; P13647; -.
DR SIGNOR; P13647; -.
DR BioGRID-ORCS; 3852; 11 hits in 1077 CRISPR screens.
DR ChiTaRS; KRT5; human.
DR GeneWiki; Keratin_5; -.
DR GenomeRNAi; 3852; -.
DR Pharos; P13647; Tbio.
DR PRO; PR:P13647; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P13647; protein.
DR Bgee; ENSG00000186081; Expressed in lower esophagus mucosa and 130 other tissues.
DR ExpressionAtlas; P13647; baseline and differential.
DR Genevisible; P13647; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
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:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
DR GO; GO:0030280; F:structural constituent of skin epidermis; IBA:GO_Central.
DR GO; GO:0008544; P:epidermis development; TAS:ProtInc.
DR GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
DR GO; GO:0045107; P:intermediate filament polymerization; ISS:UniProtKB.
DR GO; GO:0031424; P:keratinization; IBA:GO_Central.
DR GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0032880; P:regulation of protein localization; ISS:UniProtKB.
DR GO; GO:0009612; P:response to mechanical stimulus; ISS:UniProtKB.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR032444; Keratin_2_head.
DR InterPro; IPR003054; Keratin_II.
DR Pfam; PF00038; Filament; 1.
DR Pfam; PF16208; Keratin_2_head; 1.
DR PRINTS; PR01276; TYPE2KERATIN.
DR SMART; SM01391; Filament; 1.
DR PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; Disease variant;
KW Epidermolysis bullosa; Intermediate filament; Keratin; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..590
FT /note="Keratin, type II cytoskeletal 5"
FT /id="PRO_0000063727"
FT DOMAIN 168..481
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..167
FT /note="Head"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..203
FT /note="Coil 1A"
FT REGION 204..222
FT /note="Linker 1"
FT REGION 223..315
FT /note="Coil 1B"
FT REGION 316..338
FT /note="Linker 12"
FT REGION 339..477
FT /note="Coil 2"
FT REGION 478..590
FT /note="Tail"
FT REGION 566..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 419
FT /note="Stutter"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P6Q2"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P6Q2"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q922U2"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q922U2"
FT MOD_RES 24
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q922U2"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q922U2"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P6Q2"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q922U2"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q922U2"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P6Q2"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P6Q2"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P6Q2"
FT MOD_RES 151
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q922U2"
FT VARIANT 25
FT /note="P -> L (in EBS2F; dbSNP:rs57499817)"
FT /evidence="ECO:0000269|PubMed:10494094,
FT ECO:0000269|PubMed:16882168, ECO:0000269|PubMed:21623745,
FT ECO:0000269|PubMed:8799157"
FT /id="VAR_010453"
FT VARIANT 79
FT /note="S -> R (in dbSNP:rs1065115)"
FT /evidence="ECO:0000269|PubMed:10903910,
FT ECO:0000269|PubMed:2456903"
FT /id="VAR_028763"
FT VARIANT 138
FT /note="G -> E (in dbSNP:rs11170164)"
FT /evidence="ECO:0000269|PubMed:7684424"
FT /id="VAR_003871"
FT VARIANT 143
FT /note="V -> D (in EBS2B; dbSNP:rs59851104)"
FT /evidence="ECO:0000269|PubMed:16882168"
FT /id="VAR_031640"
FT VARIANT 152
FT /note="P -> L (in EBS2C; dbSNP:rs60617604)"
FT /evidence="ECO:0000269|PubMed:9804357"
FT /id="VAR_010454"
FT VARIANT 158
FT /note="D -> V (in EBS2C; dbSNP:rs61222761)"
FT /evidence="ECO:0000269|PubMed:16882168"
FT /id="VAR_031641"
FT VARIANT 161
FT /note="I -> S (in EBS2C; dbSNP:rs58058996)"
FT /evidence="ECO:0000269|PubMed:7688477"
FT /id="VAR_003872"
FT VARIANT 165
FT /note="R -> S (in EBS2A; dbSNP:rs267607456)"
FT /evidence="ECO:0000269|PubMed:21623745"
FT /id="VAR_071630"
FT VARIANT 167
FT /note="E -> K (in EBS2C; dbSNP:rs57378129)"
FT /evidence="ECO:0000269|PubMed:12707098"
FT /id="VAR_026536"
FT VARIANT 168
FT /note="E -> K (in EBS2A; dbSNP:rs58619430)"
FT /evidence="ECO:0000269|PubMed:16786515"
FT /id="VAR_027722"
FT VARIANT 169
FT /note="R -> P (in EBS2A; dbSNP:rs60720877)"
FT /evidence="ECO:0000269|PubMed:16786515"
FT /id="VAR_027723"
FT VARIANT 170
FT /note="E -> K (in EBS2D; dbSNP:rs59115483)"
FT /evidence="ECO:0000269|PubMed:11973334"
FT /id="VAR_026537"
FT VARIANT 173
FT /note="K -> N (in EBS2B; dbSNP:rs58163069)"
FT /evidence="ECO:0000269|PubMed:7534039"
FT /id="VAR_010455"
FT VARIANT 175
FT /note="L -> F (in EBS2A; dbSNP:rs57890479)"
FT /evidence="ECO:0000269|PubMed:8757772"
FT /id="VAR_010456"
FT VARIANT 176
FT /note="N -> S (in EBS2A; dbSNP:rs59092197)"
FT /evidence="ECO:0000269|PubMed:16882168,
FT ECO:0000269|PubMed:9036937, ECO:0000269|PubMed:9989794"
FT /id="VAR_010457"
FT VARIANT 177
FT /note="N -> S (in EBS2C; dbSNP:rs61495052)"
FT /evidence="ECO:0000269|PubMed:15140024"
FT /id="VAR_026538"
FT VARIANT 179
FT /note="F -> S (in EBS2A; dbSNP:rs57781042)"
FT /evidence="ECO:0000269|PubMed:9036937"
FT /id="VAR_010458"
FT VARIANT 181
FT /note="S -> P (in EBS2A; with laryngeal involvement;
FT dbSNP:rs60715293)"
FT /evidence="ECO:0000269|PubMed:10730767"
FT /id="VAR_010459"
FT VARIANT 186
FT /note="V -> E (in EBS2C; dbSNP:rs267607457)"
FT /evidence="ECO:0000269|PubMed:21623745"
FT /id="VAR_071631"
FT VARIANT 186
FT /note="V -> L (in EBS2B; dbSNP:rs121912475)"
FT /evidence="ECO:0000269|PubMed:11407988,
FT ECO:0000269|PubMed:16882168"
FT /id="VAR_013829"
FT VARIANT 186
FT /note="V -> M (in EBS2B; dbSNP:rs121912475)"
FT /evidence="ECO:0000269|PubMed:16882168"
FT /id="VAR_031642"
FT VARIANT 190
FT /note="E -> K (in EBS2C; requires 2 nucleotide
FT substitutions; dbSNP:rs58976397)"
FT /evidence="ECO:0000269|PubMed:16786515"
FT /id="VAR_027724"
FT VARIANT 191
FT /note="Q -> P (in EBS2B; dbSNP:rs57751134)"
FT /evidence="ECO:0000269|PubMed:16882168"
FT /id="VAR_031643"
FT VARIANT 193
FT /note="N -> K (in EBS2A and EBS2C; dbSNP:rs60586163)"
FT /evidence="ECO:0000269|PubMed:21623745,
FT ECO:0000269|PubMed:8807337, ECO:0000269|Ref.21"
FT /id="VAR_003873"
FT VARIANT 197
FT /note="D -> E (in dbSNP:rs641615)"
FT /evidence="ECO:0000269|PubMed:2447486,
FT ECO:0000269|PubMed:2476664"
FT /id="VAR_028764"
FT VARIANT 199
FT /note="K -> T (in EBS2C; dbSNP:rs58766676)"
FT /evidence="ECO:0000269|PubMed:14723728"
FT /id="VAR_026539"
FT VARIANT 232
FT /note="S -> N (in dbSNP:rs200333163)"
FT /id="VAR_028765"
FT VARIANT 311
FT /note="L -> P (in EBS2C; dbSNP:rs59864957)"
FT /evidence="ECO:0000269|PubMed:12707098"
FT /id="VAR_026540"
FT VARIANT 321
FT /note="T -> P (in EBS2C)"
FT /evidence="ECO:0000269|PubMed:21623745"
FT /id="VAR_071632"
FT VARIANT 323
FT /note="V -> A (in EBS2B; dbSNP:rs59840738)"
FT /evidence="ECO:0000269|PubMed:9740251"
FT /id="VAR_010460"
FT VARIANT 324
FT /note="V -> D (in EBS2C; dbSNP:rs59335325)"
FT /evidence="ECO:0000269|PubMed:12707098"
FT /id="VAR_026541"
FT VARIANT 325
FT /note="L -> P (in EBS2B; dbSNP:rs58107458)"
FT /evidence="ECO:0000269|PubMed:9989794"
FT /id="VAR_010461"
FT VARIANT 327
FT /note="M -> K (in EBS2C; dbSNP:rs58072617)"
FT /evidence="ECO:0000269|PubMed:9804357"
FT /id="VAR_010462"
FT VARIANT 327
FT /note="M -> T (in EBS2C; dbSNP:rs58072617)"
FT /evidence="ECO:0000269|PubMed:7520042,
FT ECO:0000269|PubMed:8807337"
FT /id="VAR_003874"
FT VARIANT 328
FT /note="D -> E (in EBS2C; dbSNP:rs59464425)"
FT /evidence="ECO:0000269|PubMed:10782015"
FT /id="VAR_026542"
FT VARIANT 328
FT /note="D -> G (in EBS2C; dbSNP:rs57142010)"
FT /evidence="ECO:0000269|PubMed:15347343"
FT /id="VAR_026543"
FT VARIANT 328
FT /note="D -> H (in EBS2C; dbSNP:rs56790237)"
FT /evidence="ECO:0000269|PubMed:9804357"
FT /id="VAR_010463"
FT VARIANT 328
FT /note="D -> V (in EBS2C; dbSNP:rs57142010)"
FT /evidence="ECO:0000269|PubMed:21623745,
FT ECO:0000269|PubMed:8595431"
FT /id="VAR_010464"
FT VARIANT 329
FT /note="N -> K (in EBS2C; dbSNP:rs59730172)"
FT /evidence="ECO:0000269|PubMed:7520042"
FT /id="VAR_010465"
FT VARIANT 331
FT /note="R -> C (in EBS2C; dbSNP:rs61297109)"
FT /evidence="ECO:0000269|PubMed:7506097"
FT /id="VAR_003875"
FT VARIANT 331
FT /note="R -> H (in EBS2C; dbSNP:rs56729325)"
FT /evidence="ECO:0000269|PubMed:16786515"
FT /id="VAR_027725"
FT VARIANT 352
FT /note="R -> S (in EBS2C; dbSNP:rs59112594)"
FT /evidence="ECO:0000269|PubMed:16882168"
FT /id="VAR_031644"
FT VARIANT 387
FT /note="S -> T (in dbSNP:rs2669875)"
FT /evidence="ECO:0000269|PubMed:10903910,
FT ECO:0000269|PubMed:2456903"
FT /id="VAR_028766"
FT VARIANT 404
FT /note="K -> E (in EBS2C; dbSNP:rs60809982)"
FT /evidence="ECO:0000269|PubMed:12655565"
FT /id="VAR_023726"
FT VARIANT 418
FT /note="E -> K (in EBS2D; dbSNP:rs121912476)"
FT /evidence="ECO:0000269|PubMed:11973334"
FT /id="VAR_026544"
FT VARIANT 428
FT /note="A -> T (in EBS2C; dbSNP:rs267607458)"
FT /evidence="ECO:0000269|PubMed:21623745"
FT /id="VAR_071633"
FT VARIANT 438
FT /note="A -> D (in EBS2C; dbSNP:rs57845028)"
FT /evidence="ECO:0000269|PubMed:12655565"
FT /id="VAR_023727"
FT VARIANT 463
FT /note="L -> P (in EBS2B; dbSNP:rs57599352)"
FT /evidence="ECO:0000269|PubMed:21623745,
FT ECO:0000269|PubMed:7686424"
FT /id="VAR_003876"
FT VARIANT 467
FT /note="I -> T (in EBS2A; dbSNP:rs60271599)"
FT /evidence="ECO:0000269|PubMed:9406827"
FT /id="VAR_010466"
FT VARIANT 469
FT /note="T -> P (in EBS2A; dbSNP:rs60596287)"
FT /evidence="ECO:0000269|PubMed:16786515"
FT /id="VAR_027726"
FT VARIANT 475
FT /note="E -> G (in EBS2A; dbSNP:rs61348633)"
FT /evidence="ECO:0000269|PubMed:1372711"
FT /id="VAR_003877"
FT VARIANT 475
FT /note="E -> K (in EBS2A; dbSNP:rs57155193)"
FT /evidence="ECO:0000269|PubMed:12655565,
FT ECO:0000269|PubMed:16882168"
FT /id="VAR_023728"
FT VARIANT 477
FT /note="E -> K (in EBS2A; dbSNP:rs59190510)"
FT /evidence="ECO:0000269|PubMed:12655565,
FT ECO:0000269|PubMed:16882168, ECO:0000269|PubMed:21623745,
FT ECO:0000269|PubMed:9036937"
FT /id="VAR_010467"
FT VARIANT 517
FT /note="G -> D (in EBS2B; dbSNP:rs58608695)"
FT /evidence="ECO:0000269|PubMed:16882168"
FT /id="VAR_031645"
FT VARIANT 528
FT /note="S -> G (in dbSNP:rs11549950)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_028767"
FT VARIANT 543
FT /note="G -> S (in dbSNP:rs11549949)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:2455002"
FT /id="VAR_028768"
FT MUTAGEN 399
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 411
FT /note="Q->A: No effect on interaction with KRT14 or keratin
FT intermediate filament networks."
FT /evidence="ECO:0000269|PubMed:31995743"
FT MUTAGEN 412
FT /note="N->A: No effect on interaction with KRT14 or keratin
FT intermediate filament networks."
FT /evidence="ECO:0000269|PubMed:31995743"
FT MUTAGEN 422
FT /note="E->A: No effect on interaction with KRT14 or keratin
FT intermediate filament networks."
FT /evidence="ECO:0000269|PubMed:31995743"
FT MUTAGEN 437
FT /note="E->A: No effect on interaction with KRT14 or keratin
FT intermediate filament networks."
FT /evidence="ECO:0000269|PubMed:31995743"
FT MUTAGEN 440
FT /note="Q->A: No effect on interaction with KRT14 or keratin
FT intermediate filament networks."
FT /evidence="ECO:0000269|PubMed:31995743"
FT MUTAGEN 444
FT /note="Q->A: No effect on interaction with KRT14 or keratin
FT intermediate filament networks."
FT /evidence="ECO:0000269|PubMed:31995743"
FT CONFLICT 9..11
FT /note="FRS -> SGA (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="E -> Q (in Ref. 5; AAA36145)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="E -> H (in Ref. 5; AAA36145)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="H -> E (in Ref. 7)"
FT /evidence="ECO:0000305"
FT CONFLICT 558
FT /note="G -> S (in Ref. 2 and 5; AAA36145)"
FT /evidence="ECO:0000305"
FT HELIX 384..474
FT /evidence="ECO:0007829|PDB:6JFV"
SQ SEQUENCE 590 AA; 62378 MW; E9D5318E01F55145 CRC64;
MSRQSSVSFR SGGSRSFSTA SAITPSVSRT SFTSVSRSGG GGGGGFGRVS LAGACGVGGY
GSRSLYNLGG SKRISISTSG GSFRNRFGAG AGGGYGFGGG AGSGFGFGGG AGGGFGLGGG
AGFGGGFGGP GFPVCPPGGI QEVTVNQSLL TPLNLQIDPS IQRVRTEERE QIKTLNNKFA
SFIDKVRFLE QQNKVLDTKW TLLQEQGTKT VRQNLEPLFE QYINNLRRQL DSIVGERGRL
DSELRNMQDL VEDFKNKYED EINKRTTAEN EFVMLKKDVD AAYMNKVELE AKVDALMDEI
NFMKMFFDAE LSQMQTHVSD TSVVLSMDNN RNLDLDSIIA EVKAQYEEIA NRSRTEAESW
YQTKYEELQQ TAGRHGDDLR NTKHEISEMN RMIQRLRAEI DNVKKQCANL QNAIADAEQR
GELALKDARN KLAELEEALQ KAKQDMARLL REYQELMNTK LALDVEIATY RKLLEGEECR
LSGEGVGPVN ISVVTSSVSS GYGSGSGYGG GLGGGLGGGL GGGLAGGSSG SYYSSSSGGV
GLGGGLSVGG SGFSASSGRG LGVGFGSGGG SSSSVKFVST TSSSRKSFKS
