K1C10_HUMAN
ID K1C10_HUMAN Reviewed; 584 AA.
AC P13645; Q14664; Q8N175;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 6.
DT 03-AUG-2022, entry version 220.
DE RecName: Full=Keratin, type I cytoskeletal 10;
DE AltName: Full=Cytokeratin-10;
DE Short=CK-10;
DE AltName: Full=Keratin-10;
DE Short=K10;
GN Name=KRT10; Synonyms=KPP;
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 SER-101 AND TYR-487.
RC TISSUE=Foreskin;
RX PubMed=2459124; DOI=10.1016/s0021-9258(19)37628-8;
RA Zhou X.M., Idler W.W., Steven A.C., Roop D.R., Steinert P.M.;
RT "The complete sequence of the human intermediate filament chain keratin 10.
RT Subdomainal divisions and model for folding of end domain sequences.";
RL J. Biol. Chem. 263:15584-15589(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT TYR-487.
RX PubMed=2464696; DOI=10.1016/0022-2836(88)90045-9;
RA Rieger M., Franke W.W.;
RT "Identification of an orthologous mammalian cytokeratin gene. High degree
RT of intron sequence conservation during evolution of human cytokeratin 10.";
RL J. Mol. Biol. 204:841-856(1988).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS SER-101 AND TYR-487.
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 130-584, AND VARIANT TYR-487.
RX PubMed=2448602; DOI=10.1007/bf00444680;
RA Darmon M.Y., Semat A., Darmon M.C., Vasseur M.;
RT "Sequence of a cDNA encoding human keratin No 10 selected according to
RT structural homologies of keratins and their tissue-specific expression.";
RL Mol. Biol. Rep. 12:277-283(1987).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 147-161, AND VARIANTS EHK HIS-156 AND
RP ASN-160.
RX PubMed=7507150; DOI=10.1111/1523-1747.ep12371723;
RA Rothnagel J.A., Longley M.A., Holder R.A., Kuster W., Roop D.R.;
RT "Prenatal diagnosis of epidermolytic hyperkeratosis by direct gene
RT sequencing.";
RL J. Invest. Dermatol. 102:13-16(1994).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 147-161, AND VARIANT EHK CYS-156.
RA Rothnagel J.J., Dominey A., Fisher M., Axtell S., Pittelkow M.,
RA Anton-Lamprecht I., Hohl D., Roop D.;
RT "Identification of mutational hot spots in the suprabasal keratin genes
RT from patients with epidermolytic hyperkeratosis.";
RL Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 197-584.
RX PubMed=1378806; DOI=10.1016/0378-1119(92)90521-p;
RA Tkachenko A.V., Buchman V.L., Bliskovsky V.V., Shvets Y.P., Kisselev L.L.;
RT "Exons I and VII of the gene (Ker10) encoding human keratin 10 undergo
RT structural rearrangements within repeats.";
RL Gene 116:245-251(1992).
RN [9]
RP PROTEIN SEQUENCE OF 180-184 AND 568-580.
RC TISSUE=Keratinocyte;
RX PubMed=1286667; DOI=10.1002/elps.11501301199;
RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
RA Vandekerckhove J.;
RT "Microsequences of 145 proteins recorded in the two-dimensional gel protein
RT database of normal human epidermal keratinocytes.";
RL Electrophoresis 13:960-969(1992).
RN [10]
RP INTERACTION WITH STAPHYLOCOCCUS AUREUS CLFB (MICROBIAL INFECTION),
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12427098; DOI=10.1046/j.1462-5822.2002.00231.x;
RA O'Brien L.M., Walsh E.J., Massey R.C., Peacock S.J., Foster T.J.;
RT "Staphylococcus aureus clumping factor B (ClfB) promotes adherence to human
RT type I cytokeratin 10: implications for nasal colonization.";
RL Cell. Microbiol. 4:759-770(2002).
RN [11]
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 [12]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH STAPHYLOCOCCUS AUREUS
RP CLFB (MICROBIAL INFECTION).
RX PubMed=15385531; DOI=10.1074/jbc.m408713200;
RA Walsh E.J., O'Brien L.M., Liang X., Hoeoek M., Foster T.J.;
RT "Clumping factor B, a fibrinogen-binding MSCRAMM (microbial surface
RT components recognizing adhesive matrix molecules) adhesin of Staphylococcus
RT aureus, also binds to the tail region of type I cytokeratin 10.";
RL J. Biol. Chem. 279:50691-50699(2004).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-42, AND
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 [14]
RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH S.PNEUMONIAE PSRP
RP (MICROBIAL INFECTION), SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19627498; DOI=10.1111/j.1365-2958.2009.06796.x;
RA Shivshankar P., Sanchez C., Rose L.F., Orihuela C.J.;
RT "The Streptococcus pneumoniae adhesin PsrP binds to keratin 10 on lung
RT cells.";
RL Mol. Microbiol. 73:663-679(2009).
RN [15]
RP INVOLVEMENT IN CRIE.
RX PubMed=20798280; DOI=10.1126/science.1192280;
RA Choate K.A., Lu Y., Zhou J., Choi M., Elias P.M., Farhi A.,
RA Nelson-Williams C., Crumrine D., Williams M.L., Nopper A.J., Bree A.,
RA Milstone L.M., Lifton R.P.;
RT "Mitotic recombination in patients with ichthyosis causes reversion of
RT dominant mutations in KRT10.";
RL Science 330:94-97(2010).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-16; SER-42; SER-53;
RP SER-56 AND SER-170, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP IDENTIFICATION IN A COMPLEX WITH KRT1, AND INTERACTION WITH KRT1 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 [19]
RP INTERACTION WITH S.PNEUMONIAE PSRP (MICROBIAL INFECTION).
RX PubMed=24430336; DOI=10.1098/rsob.130090;
RA Schulte T., Lofling J., Mikaelsson C., Kikhney A., Hentrich K.,
RA Diamante A., Ebel C., Normark S., Svergun D., Henriques-Normark B.,
RA Achour A.;
RT "The basic keratin 10-binding domain of the virulence-associated
RT pneumococcal serine-rich protein PsrP adopts a novel MSCRAMM fold.";
RL Open Biol. 4:130090-130090(2014).
RN [20]
RP ERRATUM OF PUBMED:24430336.
RX DOI=10.1098/rsob.140172;
RA Schulte T., Lofling J., Mikaelsson C., Kikhney A., Hentrich K.,
RA Diamante A., Ebel C., Normark S., Svergun D., Henriques-Normark B.,
RA Achour A.;
RL Open Biol. 4:140172-140172(2014).
RN [21]
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 [22]
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 [23]
RP SUBCELLULAR LOCATION, AND INDUCTION BY ATRA.
RX PubMed=32179842; DOI=10.1038/s41598-020-61640-9;
RA Aldehlawi H., Usman S., Lalli A., Ahmad F., Williams G., Teh M.T.,
RA Waseem A.;
RT "Serum lipids, retinoic acid and phenol red differentially regulate
RT expression of keratins K1, K10 and K2 in cultured keratinocytes.";
RL Sci. Rep. 10:4829-4829(2020).
RN [24] {ECO:0007744|PDB:3ASW}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 473-487 IN COMPLEX WITH
RP STAPHYLOCOCCUS AUREUS CLFB.
RA Ganesh V.K., Barbu E.M., Deivanayagam C.C.S., Le B., Anderson A.,
RA Matsuka Y., Lin S.L., Foster T.J., Narayana S.L., Hook M.;
RT "Structural and biochemical characterization of ClfB:ligand interactions.";
RL Submitted (DEC-2010) to the PDB data bank.
RN [25] {ECO:0007744|PDB:4F1Z}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 499-512 IN COMPLEX WITH
RP STAPHYLOCOCCUS AUREUS CLFB, AND INTERACTION WITH STAPHYLOCOCCUS AUREUS
RP CLFB.
RX PubMed=22719251; DOI=10.1371/journal.ppat.1002751;
RA Xiang H., Feng Y., Wang J., Liu B., Chen Y., Liu L., Deng X., Yang M.;
RT "Crystal structures reveal the multi-ligand binding mechanism of
RT Staphylococcus aureus ClfB.";
RL PLoS Pathog. 8:e1002751-e1002751(2012).
RN [26] {ECO:0007744|PDB:4ZRY}
RP X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 337-456 IN COMPLEX WITH KRT1,
RP SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=27595935; DOI=10.1016/j.jid.2016.08.018;
RA Bunick C.G., Milstone L.M.;
RT "The X-Ray Crystal Structure of the Keratin1-Keratin 10 Helix 2B
RT Heterodimer Reveals Molecular Surface Properties and Biochemical Insights
RT into Human Skin Disease.";
RL J. Invest. Dermatol. 137:142-150(2017).
RN [27]
RP VARIANT EHK HIS-156.
RX PubMed=1381287; DOI=10.1016/0092-8674(92)90314-3;
RA Cheng J., Syder A.J., Yu Q.-C., Letai A., Paller A.S., Fuchs E.;
RT "The genetic basis of epidermolytic hyperkeratosis: a disorder of
RT differentiation-specific epidermal keratin genes.";
RL Cell 70:811-819(1992).
RN [28]
RP VARIANTS.
RX PubMed=1371013; DOI=10.1073/pnas.89.3.910;
RA Korge B.P., Gan S.-Q., McBridge O.W., Mischke D., Steinert P.M.;
RT "Extensive size polymorphism of the human keratin 10 chain resides in the
RT C-terminal V2 subdomain due to variable numbers and sizes of glycine
RT loops.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:910-914(1992).
RN [29]
RP VARIANTS EHK HIS-156 AND SER-161.
RX PubMed=1380725; DOI=10.1126/science.257.5073.1128;
RA Rothnagel J.A., Dominey A.M., Dempsey L.D., Longley M.A., Greenhalgh D.A.,
RA Gagne T.A., Huber M., Frenk E., Hohl D., Roop D.R.;
RT "Mutations in the rod domains of keratins 1 and 10 in epidermolytic
RT hyperkeratosis.";
RL Science 257:1128-1130(1992).
RN [30]
RP VARIANTS EHK HIS-154; CYS-156; HIS-156; ASP-160 AND GLN-442.
RX PubMed=7508181;
RA Chipev C.C., Yang J.-M., Digiovanna J.J., Steinert P.M., Marekov L.,
RA Compton J.G., Bale S.J.;
RT "Preferential sites in keratin 10 that are mutated in epidermolytic
RT hyperkeratosis.";
RL Am. J. Hum. Genet. 54:179-190(1994).
RN [31]
RP VARIANTS EHK ARG-150; CYS-156 AND GLU-439, AND VARIANT SER-126.
RX PubMed=7512983; DOI=10.1172/jci117132;
RA Syder A.J., Yu Q.-C., Paller A.S., Giudice G., Pearson R., Fuchs E.;
RT "Genetic mutations in the K1 and K10 genes of patients with epidermolytic
RT hyperkeratosis. Correlation between location and disease severity.";
RL J. Clin. Invest. 93:1533-1542(1994).
RN [32]
RP VARIANTS EHK PRO-156 AND SER-156.
RX PubMed=7507152; DOI=10.1111/1523-1747.ep12371726;
RA McLean W.H.I., Eady R.A.J., Dopping-Hepenstal P.J.C., McMillan J.R.,
RA Leigh I.M., Navsaria H.A., Higgins C., Harper J.I., Paige D.G.,
RA Morley S.M.;
RT "Mutations in the rod 1A domain of keratins 1 and 10 in bullous congenital
RT ichthyosiform erythroderma (BCIE).";
RL J. Invest. Dermatol. 102:24-30(1994).
RN [33]
RP VARIANT EHK THR-150.
RX PubMed=7526210; DOI=10.1056/nejm199411243312103;
RA Paller A.S., Syder A.J., Chan Y.-M., Yu Q.-C., Hutton M.E., Tadini G.,
RA Fuchs E.;
RT "Genetic and clinical mosaicism in a type of epidermal nevus.";
RL N. Engl. J. Med. 331:1408-1415(1994).
RN [34]
RP VARIANT AEI GLU-422.
RX PubMed=9036939; DOI=10.1111/1523-1747.ep12286491;
RA Joh G.-Y., Traupe H., Metze D., Nashan D., Huber M., Hohl D., Longley M.A.,
RA Rothnagel J.A., Roop D.R.;
RT "A novel dinucleotide mutation in keratin 10 in the annular epidermolytic
RT ichthyosis variant of bullous congenital ichthyosiform erythroderma.";
RL J. Invest. Dermatol. 108:357-361(1997).
RN [35]
RP VARIANT AEI THR-446.
RX PubMed=9856845; DOI=10.1046/j.1523-1747.1998.00451.x;
RA Suga Y., Duncan K.O., Heald P.W., Roop D.R.;
RT "A novel helix termination mutation in keratin 10 in annular epidermolytic
RT ichthyosis, a variant of bullous congenital ichthyosiform erythroderma.";
RL J. Invest. Dermatol. 111:1220-1223(1998).
RN [36]
RP VARIANT EHK SER-160.
RX PubMed=10201536; DOI=10.1046/j.1523-1747.1999.00557.x;
RA Arin M.J., Longley M.A., Anton-Lamprecht I., Kurze G., Huber M., Hohl D.,
RA Rothnagel J.A., Roop D.R.;
RT "A novel substitution in keratin 10 in epidermolytic hyperkeratosis.";
RL J. Invest. Dermatol. 112:506-508(1999).
RN [37]
RP VARIANTS EHK ARG-150; THR-150; CYS-156; HIS-156 AND CYS-449.
RX PubMed=21271994; DOI=10.1111/j.1365-2133.2010.10096.x;
RA Arin M.J., Oji V., Emmert S., Hausser I., Traupe H., Krieg T., Grimberg G.;
RT "Expanding the keratin mutation database: novel and recurrent mutations and
RT genotype-phenotype correlations in 28 patients with epidermolytic
RT ichthyosis.";
RL Br. J. Dermatol. 164:442-447(2011).
CC -!- FUNCTION: Plays a role in the establishment of the epidermal barrier on
CC plantar skin (By similarity). Involved in the maintenance of cell layer
CC development and keratin filament bundles in suprabasal cells of the
CC epithelium (By similarity). {ECO:0000250|UniProtKB:P02535}.
CC -!- FUNCTION: (Microbial infection) Acts as a mediator of S.aureus
CC adherence to desquamated nasal epithelial cells via clfB, and hence may
CC play a role in nasal colonization. {ECO:0000269|PubMed:15385531}.
CC -!- FUNCTION: (Microbial infection) Binds S.pneumoniae PsrP, mediating
CC adherence of the bacteria to lung cell lines. Reduction of levels of
CC KRT10 keratin decrease adherence, overexpression increases adherence.
CC Neither protein has to be glycosylated for the interaction to occur.
CC {ECO:0000269|PubMed:19627498}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC Heterodimer with KRT1 (PubMed:24940650, PubMed:27595935). Two
CC heterodimers of KRT1 and KRT10 form a heterotetramer (PubMed:27595935).
CC The KRT10 subunit in the heterotetramer is probably disulfide-linked
CC (PubMed:27595935). Interacts with PLEC isoform 1C, when in a
CC heterodimer with KRT1 (PubMed:24940650). {ECO:0000269|PubMed:24940650,
CC ECO:0000269|PubMed:27595935, ECO:0000303|PubMed:27595935}.
CC -!- SUBUNIT: (Microbial infection) Interacts (via C-terminal tail domain)
CC with the S.aureus clumping factor, clfB; this interaction probably
CC mediates S.aureus attachment to the keratinized squamous epithelial
CC cells from the nasal cavity. {ECO:0000269|PubMed:12427098,
CC ECO:0000269|PubMed:15385531, ECO:0000269|PubMed:22719251}.
CC -!- SUBUNIT: (Microbial infection) Interacts (via the C-terminal tail
CC domain) with S.pneumoniae serine-rich repeat protein PsrP; this
CC interaction probably mediates S.pneumoniae adherence to lung tissue and
CC subsequent pathogenesis. Neither protein has to be glycosylated for the
CC interaction to occur. {ECO:0000269|PubMed:19627498,
CC ECO:0000269|PubMed:24430336}.
CC -!- INTERACTION:
CC P13645; P04264: KRT1; NbExp=5; IntAct=EBI-465144, EBI-298429;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000269|PubMed:12427098}. Cell surface
CC {ECO:0000269|PubMed:19627498}. Cytoplasm {ECO:0000269|PubMed:32179842}.
CC -!- TISSUE SPECIFICITY: Seen in all suprabasal cell layers including
CC stratum corneum. Expressed on the surface of lung cell lines
CC (PubMed:19627498). Localized on the surface of desquamated nasal
CC epithelial cells (at protein level) (PubMed:12427098).
CC {ECO:0000269|PubMed:12427098, ECO:0000269|PubMed:19627498}.
CC -!- INDUCTION: Repressed in keratinocytes by all-trans retinoic acid
CC (ATRA), via reduction of mRNA stability. {ECO:0000269|PubMed:32179842}.
CC -!- POLYMORPHISM: A number of alleles are known that mainly differ in the
CC Gly-rich region (positions 490-560).
CC -!- DISEASE: Epidermolytic hyperkeratosis (EHK) [MIM:113800]: An autosomal
CC dominant skin disorder characterized by widespread blistering and an
CC ichthyotic erythroderma at birth that persist into adulthood.
CC Histologically there is a diffuse epidermolytic degeneration in the
CC lower spinous layer of the epidermis. Within a few weeks from birth,
CC erythroderma and blister formation diminish and hyperkeratoses develop.
CC {ECO:0000269|PubMed:10201536, ECO:0000269|PubMed:1380725,
CC ECO:0000269|PubMed:1381287, ECO:0000269|PubMed:21271994,
CC ECO:0000269|PubMed:7507150, ECO:0000269|PubMed:7507152,
CC ECO:0000269|PubMed:7508181, ECO:0000269|PubMed:7512983,
CC ECO:0000269|PubMed:7526210, ECO:0000269|Ref.7}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: Ichthyosis annular epidermolytic (AEI) [MIM:607602]: A skin
CC disorder resembling bullous congenital ichthyosiform erythroderma.
CC Affected individuals present with bullous ichthyosis in early childhood
CC and hyperkeratotic lichenified plaques in the flexural areas and
CC extensor surfaces at later ages. The feature that distinguishes AEI
CC from BCIE is dramatic episodes of flares of annular polycyclic plaques
CC with scale, which coalesce to involve most of the body surface and can
CC persist for several weeks or even months. {ECO:0000269|PubMed:9036939,
CC ECO:0000269|PubMed:9856845}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Erythroderma, ichthyosiform, congenital reticular (CRIE)
CC [MIM:609165]: A rare skin condition characterized by slowly enlarging
CC islands of normal skin surrounded by erythematous ichthyotic patches in
CC a reticulated pattern. The condition starts in infancy as a lamellar
CC ichthyosis, with small islands of normal skin resembling confetti
CC appearing in late childhood and at puberty. Histopathologic findings
CC include band-like parakeratosis, psoriasiform acanthosis, and
CC vacuolization of keratinocytes with binucleated cells in the upper
CC epidermis, sometimes associated with amyloid deposition in the dermis.
CC Ultrastructural abnormalities include perinuclear shells formed from a
CC network of fine filaments in the upper epidermis.
CC {ECO:0000269|PubMed:20798280}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: There are two types of cytoskeletal and microfibrillar
CC keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA59468.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Human Intermediate Filament Mutation Database;
CC URL="http://www.interfil.org";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Keratin-10 entry;
CC URL="https://en.wikipedia.org/wiki/Keratin_10";
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DR EMBL; J04029; AAA60544.1; -; mRNA.
DR EMBL; X14487; CAA32649.1; -; Genomic_DNA.
DR EMBL; AC090283; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC034697; AAH34697.1; -; mRNA.
DR EMBL; M19156; AAA59468.1; ALT_INIT; mRNA.
DR EMBL; L20218; AAB59438.1; -; Genomic_DNA.
DR EMBL; L20219; AAB59439.1; -; Genomic_DNA.
DR EMBL; M77663; AAA59199.1; -; mRNA.
DR CCDS; CCDS11377.1; -.
DR PIR; A31994; A31994.
DR PIR; S02158; KRHU0.
DR RefSeq; NP_000412.3; NM_000421.3.
DR PDB; 3ASW; X-ray; 2.60 A; B=473-487.
DR PDB; 4F1Z; X-ray; 2.30 A; Q=499-512.
DR PDB; 4ZRY; X-ray; 3.30 A; A=337-456.
DR PDB; 6E2J; X-ray; 2.39 A; B=195-296.
DR PDB; 6EC0; X-ray; 2.98 A; B=195-296.
DR PDB; 6UUI; X-ray; 2.07 A; X=337-456.
DR PDBsum; 3ASW; -.
DR PDBsum; 4F1Z; -.
DR PDBsum; 4ZRY; -.
DR PDBsum; 6E2J; -.
DR PDBsum; 6EC0; -.
DR PDBsum; 6UUI; -.
DR AlphaFoldDB; P13645; -.
DR SMR; P13645; -.
DR BioGRID; 110056; 137.
DR ComplexPortal; CPX-5662; Keratin-1 - Keratin-10 dimer complex.
DR IntAct; P13645; 43.
DR MINT; P13645; -.
DR STRING; 9606.ENSP00000269576; -.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR GlyGen; P13645; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; P13645; -.
DR PhosphoSitePlus; P13645; -.
DR SwissPalm; P13645; -.
DR BioMuta; KRT10; -.
DR DMDM; 269849769; -.
DR REPRODUCTION-2DPAGE; P13645; -.
DR SWISS-2DPAGE; P13645; -.
DR CPTAC; non-CPTAC-2680; -.
DR EPD; P13645; -.
DR jPOST; P13645; -.
DR MassIVE; P13645; -.
DR PaxDb; P13645; -.
DR PeptideAtlas; P13645; -.
DR PRIDE; P13645; -.
DR ProteomicsDB; 52950; -.
DR TopDownProteomics; P13645; -.
DR Antibodypedia; 1606; 1550 antibodies from 45 providers.
DR DNASU; 3858; -.
DR Ensembl; ENST00000269576.6; ENSP00000269576.5; ENSG00000186395.9.
DR GeneID; 3858; -.
DR KEGG; hsa:3858; -.
DR MANE-Select; ENST00000269576.6; ENSP00000269576.5; NM_000421.5; NP_000412.4.
DR UCSC; uc002hvi.4; human.
DR CTD; 3858; -.
DR DisGeNET; 3858; -.
DR GeneCards; KRT10; -.
DR HGNC; HGNC:6413; KRT10.
DR HPA; ENSG00000186395; Tissue enriched (skin).
DR MalaCards; KRT10; -.
DR MIM; 113800; phenotype.
DR MIM; 148080; gene.
DR MIM; 607602; phenotype.
DR MIM; 609165; phenotype.
DR neXtProt; NX_P13645; -.
DR OpenTargets; ENSG00000186395; -.
DR Orphanet; 281139; Annular epidermolytic ichthyosis.
DR Orphanet; 312; Autosomal dominant epidermolytic ichthyosis.
DR Orphanet; 512103; Autosomal recessive epidermolytic ichthyosis.
DR Orphanet; 281190; Congenital reticular ichthyosiform erythroderma.
DR PharmGKB; PA30200; -.
DR VEuPathDB; HostDB:ENSG00000186395; -.
DR eggNOG; ENOG502QV0B; Eukaryota.
DR GeneTree; ENSGT00940000160849; -.
DR HOGENOM; CLU_012560_8_3_1; -.
DR InParanoid; P13645; -.
DR OMA; QGQPRDY; -.
DR OrthoDB; 798081at2759; -.
DR PhylomeDB; P13645; -.
DR TreeFam; TF332742; -.
DR PathwayCommons; P13645; -.
DR Reactome; R-HSA-6805567; Keratinization.
DR Reactome; R-HSA-6809371; Formation of the cornified envelope.
DR SignaLink; P13645; -.
DR SIGNOR; P13645; -.
DR BioGRID-ORCS; 3858; 254 hits in 1086 CRISPR screens.
DR ChiTaRS; KRT10; human.
DR GeneWiki; Keratin_10; -.
DR GenomeRNAi; 3858; -.
DR Pharos; P13645; Tbio.
DR PRO; PR:P13645; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P13645; protein.
DR Bgee; ENSG00000186395; Expressed in upper leg skin and 205 other tissues.
DR ExpressionAtlas; P13645; baseline and differential.
DR Genevisible; P13645; HS.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0001533; C:cornified envelope; IDA:CAFA.
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:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0005882; C:intermediate filament; NAS:UniProtKB.
DR GO; GO:0045095; C:keratin filament; IPI:ComplexPortal.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0030280; F:structural constituent of skin epidermis; IDA:CAFA.
DR GO; GO:0008544; P:epidermis development; IBA:GO_Central.
DR GO; GO:0030855; P:epithelial cell differentiation; IBA:GO_Central.
DR GO; GO:0030216; P:keratinocyte differentiation; IEP:UniProtKB.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IBA:GO_Central.
DR GO; GO:0018149; P:peptide cross-linking; IDA:CAFA.
DR GO; GO:0045684; P:positive regulation of epidermis development; ISS:UniProtKB.
DR GO; GO:0051290; P:protein heterotetramerization; IDA:UniProtKB.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR002957; Keratin_I.
DR PANTHER; PTHR23239; PTHR23239; 1.
DR Pfam; PF00038; Filament; 1.
DR PRINTS; PR01248; TYPE1KERATIN.
DR SMART; SM01391; Filament; 1.
DR PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; Direct protein sequencing;
KW Disease variant; Disulfide bond; Ichthyosis; Intermediate filament;
KW Keratin; Phosphoprotein; Reference proteome; Secreted.
FT CHAIN 1..584
FT /note="Keratin, type I cytoskeletal 10"
FT /id="PRO_0000063642"
FT DOMAIN 146..460
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..145
FT /note="Head"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..181
FT /note="Coil 1A"
FT REGION 182..202
FT /note="Linker 1"
FT REGION 203..294
FT /note="Coil 1B"
FT REGION 295..317
FT /note="Linker 12"
FT REGION 318..456
FT /note="Coil 2"
FT REGION 453..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..584
FT /note="Tail"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT DISULFID 401
FT /note="Interchain"
FT /evidence="ECO:0000305|PubMed:27595935,
FT ECO:0007744|PDB:4ZRY"
FT VARIANT 101
FT /note="I -> S (in dbSNP:rs4261597)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:2459124"
FT /id="VAR_058202"
FT VARIANT 126
FT /note="G -> S (in dbSNP:rs77919366)"
FT /evidence="ECO:0000269|PubMed:21271994,
FT ECO:0000269|PubMed:7512983"
FT /id="VAR_010505"
FT VARIANT 150
FT /note="M -> R (in EHK; dbSNP:rs58901407)"
FT /evidence="ECO:0000269|PubMed:21271994,
FT ECO:0000269|PubMed:7512983"
FT /id="VAR_010506"
FT VARIANT 150
FT /note="M -> T (in EHK; also found in a patient with
FT hyperkeratotic epidermal nevi due to genetic mosaicism;
FT dbSNP:rs58901407)"
FT /evidence="ECO:0000269|PubMed:21271994,
FT ECO:0000269|PubMed:7526210"
FT /id="VAR_010507"
FT VARIANT 154
FT /note="N -> H (in EHK; dbSNP:rs57784225)"
FT /evidence="ECO:0000269|PubMed:7508181"
FT /id="VAR_003826"
FT VARIANT 156
FT /note="R -> C (in EHK; dbSNP:rs58852768)"
FT /evidence="ECO:0000269|PubMed:21271994,
FT ECO:0000269|PubMed:7508181, ECO:0000269|PubMed:7512983,
FT ECO:0000269|Ref.7"
FT /id="VAR_003828"
FT VARIANT 156
FT /note="R -> H (in EHK; dbSNP:rs58075662)"
FT /evidence="ECO:0000269|PubMed:1380725,
FT ECO:0000269|PubMed:1381287, ECO:0000269|PubMed:21271994,
FT ECO:0000269|PubMed:7507150, ECO:0000269|PubMed:7508181"
FT /id="VAR_003827"
FT VARIANT 156
FT /note="R -> P (in EHK; dbSNP:rs58075662)"
FT /evidence="ECO:0000269|PubMed:7507152"
FT /id="VAR_003829"
FT VARIANT 156
FT /note="R -> S (in EHK; dbSNP:rs58852768)"
FT /evidence="ECO:0000269|PubMed:7507152"
FT /id="VAR_003830"
FT VARIANT 160
FT /note="Y -> D (in EHK; severe phenotype; dbSNP:rs58414354)"
FT /evidence="ECO:0000269|PubMed:7508181"
FT /id="VAR_003831"
FT VARIANT 160
FT /note="Y -> N (in EHK; severe phenotype)"
FT /evidence="ECO:0000269|PubMed:7507150"
FT /id="VAR_010508"
FT VARIANT 160
FT /note="Y -> S (in EHK; severe phenotype; dbSNP:rs58735429)"
FT /evidence="ECO:0000269|PubMed:10201536"
FT /id="VAR_010509"
FT VARIANT 161
FT /note="L -> S (in EHK; dbSNP:rs60118264)"
FT /evidence="ECO:0000269|PubMed:1380725"
FT /id="VAR_003832"
FT VARIANT 422
FT /note="R -> E (in AEI; requires 2 nucleotide substitutions;
FT dbSNP:rs59075499)"
FT /evidence="ECO:0000269|PubMed:9036939"
FT /id="VAR_033145"
FT VARIANT 439
FT /note="K -> E (in EHK; mild phenotype; dbSNP:rs61434181)"
FT /evidence="ECO:0000269|PubMed:7512983"
FT /id="VAR_010510"
FT VARIANT 442
FT /note="L -> Q (in EHK; dbSNP:rs58026994)"
FT /evidence="ECO:0000269|PubMed:7508181"
FT /id="VAR_003833"
FT VARIANT 446
FT /note="I -> T (in AEI; dbSNP:rs62651994)"
FT /evidence="ECO:0000269|PubMed:9856845"
FT /id="VAR_010511"
FT VARIANT 449
FT /note="Y -> C (in EHK; dbSNP:rs267607383)"
FT /evidence="ECO:0000269|PubMed:21271994"
FT /id="VAR_071985"
FT VARIANT 487
FT /note="H -> Y (in dbSNP:rs17855579)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:2448602, ECO:0000269|PubMed:2459124,
FT ECO:0000269|PubMed:2464696"
FT /id="VAR_060723"
FT CONFLICT 9..11
FT /note="KHY -> SKQF (in Ref. 1; AAA60544)"
FT /evidence="ECO:0000305"
FT CONFLICT 24..31
FT /note="Missing (in Ref. 1; AAA60544)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="R -> H (in Ref. 2; CAA32649)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="S -> N (in Ref. 2; CAA32649)"
FT /evidence="ECO:0000305"
FT CONFLICT 181..184
FT /note="WYEK -> RYDQ (in Ref. 1; AAA60544)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="H -> R (in Ref. 1; AAA60544)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="S -> G (in Ref. 8; AAA59199)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="K -> Q (in Ref. 1; AAA60544)"
FT /evidence="ECO:0000305"
FT CONFLICT 279..280
FT /note="EL -> YV (in Ref. 5; AAA59468)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="H -> R (in Ref. 1; AAA60544)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="D -> H (in Ref. 1; AAA60544)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="V -> I (in Ref. 5; AAA59468)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="S -> N (in Ref. 1; AAA60544)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="F -> V (in Ref. 5; AAA59468)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="A -> R (in Ref. 5; AAA59468)"
FT /evidence="ECO:0000305"
FT CONFLICT 408
FT /note="Q -> H (in Ref. 2; CAA32649)"
FT /evidence="ECO:0000305"
FT CONFLICT 420
FT /note="Q -> E (in Ref. 1; AAA60544)"
FT /evidence="ECO:0000305"
FT CONFLICT 436
FT /note="L -> T (in Ref. 1; AAA60544)"
FT /evidence="ECO:0000305"
FT CONFLICT 451
FT /note="S -> G (in Ref. 8; AAA59199)"
FT /evidence="ECO:0000305"
FT CONFLICT 460..461
FT /note="GG -> RS (in Ref. 5; AAA59468)"
FT /evidence="ECO:0000305"
FT CONFLICT 477
FT /note="S -> T (in Ref. 5; AAA59468)"
FT /evidence="ECO:0000305"
FT CONFLICT 482
FT /note="S -> T (in Ref. 5; AAA59468)"
FT /evidence="ECO:0000305"
FT CONFLICT 487..490
FT /note="Missing (in Ref. 8; AAA59199)"
FT /evidence="ECO:0000305"
FT CONFLICT 491..516
FT /note="Missing (in Ref. 1; AAA60544)"
FT /evidence="ECO:0000305"
FT CONFLICT 503
FT /note="S -> T (in Ref. 5; AAA59468)"
FT /evidence="ECO:0000305"
FT CONFLICT 508
FT /note="S -> T (in Ref. 5; AAA59468)"
FT /evidence="ECO:0000305"
FT CONFLICT 513..519
FT /note="YGGGSSS -> LRGELH (in Ref. 5; AAA59468)"
FT /evidence="ECO:0000305"
FT CONFLICT 523..527
FT /note="GGSSS -> AHST (in Ref. 5; AAA59468)"
FT /evidence="ECO:0000305"
FT CONFLICT 524
FT /note="G -> GGSSSGGHGG (in Ref. 2; CAA32649)"
FT /evidence="ECO:0000305"
FT CONFLICT 534
FT /note="S -> N (in Ref. 5; AAA59468)"
FT /evidence="ECO:0000305"
FT CONFLICT 535
FT /note="S -> F (in Ref. 1; AAA60544)"
FT /evidence="ECO:0000305"
FT CONFLICT 542..546
FT /note="YGGGS -> LRGRH (in Ref. 5; AAA59468)"
FT /evidence="ECO:0000305"
FT CONFLICT 565
FT /note="G -> GGYGGGSSSGG (in Ref. 1; AAA60544)"
FT /evidence="ECO:0000305"
FT HELIX 195..295
FT /evidence="ECO:0007829|PDB:6E2J"
FT HELIX 350..454
FT /evidence="ECO:0007829|PDB:6UUI"
FT STRAND 479..481
FT /evidence="ECO:0007829|PDB:3ASW"
FT STRAND 483..486
FT /evidence="ECO:0007829|PDB:3ASW"
FT STRAND 500..508
FT /evidence="ECO:0007829|PDB:4F1Z"
SQ SEQUENCE 584 AA; 58827 MW; 4941ECD2AE46D417 CRC64;
MSVRYSSSKH YSSSRSGGGG GGGGCGGGGG VSSLRISSSK GSLGGGFSSG GFSGGSFSRG
SSGGGCFGGS SGGYGGLGGF GGGSFRGSYG SSSFGGSYGG IFGGGSFGGG SFGGGSFGGG
GFGGGGFGGG FGGGFGGDGG LLSGNEKVTM QNLNDRLASY LDKVRALEES NYELEGKIKE
WYEKHGNSHQ GEPRDYSKYY KTIDDLKNQI LNLTTDNANI LLQIDNARLA ADDFRLKYEN
EVALRQSVEA DINGLRRVLD ELTLTKADLE MQIESLTEEL AYLKKNHEEE MKDLRNVSTG
DVNVEMNAAP GVDLTQLLNN MRSQYEQLAE QNRKDAEAWF NEKSKELTTE IDNNIEQISS
YKSEITELRR NVQALEIELQ SQLALKQSLE ASLAETEGRY CVQLSQIQAQ ISALEEQLQQ
IRAETECQNT EYQQLLDIKI RLENEIQTYR SLLEGEGSSG GGGRGGGSFG GGYGGGSSGG
GSSGGGHGGG HGGSSGGGYG GGSSGGGSSG GGYGGGSSSG GHGGSSSGGY GGGSSGGGGG
GYGGGSSGGG SSSGGGYGGG SSSGGHKSSS SGSVGESSSK GPRY
