K1C13_HUMAN
ID K1C13_HUMAN Reviewed; 458 AA.
AC P13646; Q53G54; Q6AZK5; Q8N240;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 4.
DT 03-AUG-2022, entry version 216.
DE RecName: Full=Keratin, type I cytoskeletal 13;
DE AltName: Full=Cytokeratin-13;
DE Short=CK-13;
DE AltName: Full=Keratin-13;
DE Short=K13;
GN Name=KRT13;
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] (ISOFORM 1), AND VARIANTS VAL-187 AND ALA-298.
RX PubMed=2475110; DOI=10.1016/0006-291x(89)90847-4;
RA Schulz P., Wachter E., Hochstrasser K., Wild A.G., Mischke D.;
RT "Sequence of a human keratin 13 specific cDNA encompassing coil 1B through
RT the 3' end.";
RL Biochem. Biophys. Res. Commun. 162:1522-1527(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SEQUENCE REVISION, PROTEIN SEQUENCE
RP OF 291-299, AND VARIANTS VAL-187 AND ALA-298.
RX PubMed=2477803; DOI=10.1093/nar/17.19.7984;
RA Mischke D., Schulz P., Wild A.G.;
RT "The N-, but not the C-terminal domains of human keratins 13 and 15 are
RT closely related.";
RL Nucleic Acids Res. 17:7984-7984(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, AND VARIANTS
RP VAL-187 AND ALA-298.
RX PubMed=2483837; DOI=10.1111/j.1432-0436.1989.tb00612.x;
RA Kuruc N., Leube R.E., Moll I., Bader B.L., Franke W.W.;
RT "Synthesis of cytokeratin 13, a component characteristic of internal
RT stratified epithelia, is not induced in human epidermal tumors.";
RL Differentiation 42:111-123(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 3), AND VARIANTS VAL-187 AND
RP ALA-298.
RX PubMed=9714826; DOI=10.1016/s0378-1119(98)00297-2;
RA Waseem A., Alam Y., Dogan B., White K.N., Leigh I.M., Waseem N.H.;
RT "Isolation, sequence and expression of the gene encoding human keratin
RT 13.";
RL Gene 215:269-279(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS VAL-187
RP AND ALA-298.
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS VAL-187
RP AND ALA-298.
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS VAL-187
RP AND ALA-298.
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 [9]
RP PROTEIN SEQUENCE OF 124-135; 176-222; 291-318 AND 416-429, PHOSPHORYLATION
RP AT SER-427, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., von Kriegsheim A.F., Kolch W.;
RL Submitted (OCT-2008) to UniProtKB.
RN [10]
RP GLYCOSYLATION.
RX PubMed=2474541; DOI=10.1016/s0021-9258(18)71636-0;
RA King I.A., Hounsell E.F.;
RT "Cytokeratin 13 contains O-glycosidically linked N-acetylglucosamine
RT residues.";
RL J. Biol. Chem. 264:14022-14028(1989).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [16]
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 [17]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-27 AND ARG-35, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [18]
RP VARIANT WSN2 PRO-119.
RX PubMed=7493031; DOI=10.1038/ng1295-453;
RA Richard G., de Laurenzi V., Didona B., Bale S.J., Compton J.G.;
RT "Keratin 13 point mutation underlies the hereditary mucosal epithelial
RT disorder white sponge nevus.";
RL Nat. Genet. 11:453-455(1995).
RN [19]
RP VARIANTS WSN2 THR-108 AND PRO-115.
RX PubMed=10561721; DOI=10.1111/j.1601-0825.1999.tb00097.x;
RA Rugg E.L., Magee G., Wilson N., Brandrup F., Hamburger J., Lane E.B.;
RT "Identification of two novel mutations in keratin 13 as the cause of white
RT sponge naevus.";
RL Oral Dis. 5:321-324(1999).
RN [20]
RP VARIANT WSN2 SER-112.
RX PubMed=11379896; DOI=10.1177/00220345010800031401;
RA Terrinoni A., Rugg E.L., Lane E.B., Melino G., Felix D.H., Munro C.S.,
RA McLean W.H.I.;
RT "A novel mutation in the keratin 13 gene causing oral white sponge nevus.";
RL J. Dent. Res. 80:919-923(2001).
RN [21]
RP VARIANT WSN2 PRO-111.
RX PubMed=14600690; DOI=10.1016/s1079-2104(03)00372-x;
RA Shibuya Y., Zhang J., Yokoo S., Umeda M., Komori T.;
RT "Constitutional mutation of keratin 13 gene in familial white sponge
RT nevus.";
RL Oral Surg. Oral Med. Oral Pathol. Oral Radiol. Endod. 96:561-565(2003).
RN [22]
RP VARIANT WSN2 HIS-114.
RX PubMed=18616775; DOI=10.1111/j.1365-2133.2008.08716.x;
RA Nishizawa A., Nakajima R., Nakano H., Sawamura D., Takayama K., Satoh T.,
RA Yokozeki H.;
RT "A de novo missense mutation in the keratin 13 gene in oral white sponge
RT naevus.";
RL Br. J. Dermatol. 159:974-975(2008).
RN [23]
RP VARIANT [LARGE SCALE ANALYSIS] VAL-187, AND IDENTIFICATION BY MASS
RP 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 [24]
RP VARIANTS WSN2 PRO-111 AND CYS-114.
RX PubMed=25606422; DOI=10.1016/j.mgene.2014.04.008;
RA Cai W., Chen Z., Jiang B., Yu F., Xu P., Wang M., Wan R., Liu J., Xue Z.,
RA Yang J., Liu S., Wang X.;
RT "Keratin 13 mutations associated with oral white sponge nevus in two
RT Chinese families.";
RL Meta Gene 2:374-383(2014).
RN [25]
RP VARIANT WSN2 ASP-118.
RX PubMed=29476668; DOI=10.4317/medoral.21437;
RA Kuerklue E., Oeztuerk S., Cassidy A.J., Ak G., Koray M., Cefle K.,
RA Palanduez S., Guellueoglu M.G., Tanyeri H., McLean W.H.;
RT "Clinical features and molecular genetic analysis in a Turkish family with
RT oral white sponge nevus.";
RL Med. Oral Patol. Oral Cir. Bucal. 23:e144-e150(2018).
CC -!- FUNCTION: Type 1 keratin (Probable). Maintains postnatal tongue mucosal
CC cell homeostasis and tissue organization in response to mechanical
CC stress, potentially via regulation of the G1/S phase cyclins CCNE1 and
CC CCNE2 (By similarity). {ECO:0000250|UniProtKB:P08730, ECO:0000305}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC {ECO:0000305}.
CC -!- INTERACTION:
CC P13646; P17661: DES; NbExp=3; IntAct=EBI-1223876, EBI-1055572;
CC P13646; P14136: GFAP; NbExp=6; IntAct=EBI-1223876, EBI-744302;
CC P13646; Q8IVS8: GLYCTK; NbExp=3; IntAct=EBI-1223876, EBI-748515;
CC P13646; A0A024R8L2: hCG_1987119; NbExp=3; IntAct=EBI-1223876, EBI-14103818;
CC P13646; A0A0S2Z4Q4: HGS; NbExp=3; IntAct=EBI-1223876, EBI-16429135;
CC P13646; O14964: HGS; NbExp=6; IntAct=EBI-1223876, EBI-740220;
CC P13646; Q86VS8: HOOK3; NbExp=3; IntAct=EBI-1223876, EBI-1777078;
CC P13646; P04264: KRT1; NbExp=3; IntAct=EBI-1223876, EBI-298429;
CC P13646; P35908: KRT2; NbExp=5; IntAct=EBI-1223876, EBI-1247312;
CC P13646; P19013: KRT4; NbExp=4; IntAct=EBI-1223876, EBI-2371606;
CC P13646; P02538: KRT6A; NbExp=8; IntAct=EBI-1223876, EBI-702198;
CC P13646; P04259: KRT6B; NbExp=3; IntAct=EBI-1223876, EBI-740907;
CC P13646; Q14CN4: KRT72; NbExp=3; IntAct=EBI-1223876, EBI-1221280;
CC P13646; Q7RTS7: KRT74; NbExp=3; IntAct=EBI-1223876, EBI-968660;
CC P13646; O95678: KRT75; NbExp=3; IntAct=EBI-1223876, EBI-2949715;
CC P13646; P07196: NEFL; NbExp=3; IntAct=EBI-1223876, EBI-475646;
CC P13646; P25786: PSMA1; NbExp=3; IntAct=EBI-1223876, EBI-359352;
CC P13646; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-1223876, EBI-742688;
CC P13646; Q8N3L3: TXLNB; NbExp=3; IntAct=EBI-1223876, EBI-6116822;
CC P13646; A0A0S2Z5X4: ZNF688; NbExp=3; IntAct=EBI-1223876, EBI-16429014;
CC P13646; PRO_0000449633 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-1223876, EBI-25492395;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=A;
CC IsoId=P13646-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P13646-2; Sequence=VSP_016376, VSP_016377;
CC Name=3;
CC IsoId=P13646-3; Sequence=VSP_038433;
CC -!- TISSUE SPECIFICITY: Expressed in some epidermal sweat gland ducts (at
CC protein level) and in exocervix, esophagus and placenta.
CC {ECO:0000269|PubMed:2483837}.
CC -!- PTM: O-glycosylated; glycans consist of single N-acetylglucosamine
CC residues. {ECO:0000269|PubMed:2474541}.
CC -!- DISEASE: White sponge nevus 2 (WSN2) [MIM:615785]: A rare disorder
CC characterized by the presence of soft, white, and spongy plaques in the
CC oral mucosa. The characteristic histopathologic features are epithelial
CC thickening, parakeratosis, and vacuolization of the suprabasal layer of
CC oral epithelial keratinocytes. Less frequently the mucous membranes of
CC the nose, esophagus, genitalia and rectum are involved.
CC {ECO:0000269|PubMed:10561721, ECO:0000269|PubMed:11379896,
CC ECO:0000269|PubMed:14600690, ECO:0000269|PubMed:18616775,
CC ECO:0000269|PubMed:25606422, ECO:0000269|PubMed:29476668,
CC ECO:0000269|PubMed:7493031}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: There are two types of cytoskeletal and microfibrillar
CC keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
CC -!- WEB RESOURCE: Name=Human Intermediate Filament Mutation Database;
CC URL="http://www.interfil.org";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Keratin-13 entry;
CC URL="https://en.wikipedia.org/wiki/Keratin_13";
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DR EMBL; X14640; CAA32786.1; -; mRNA.
DR EMBL; X52426; CAA36673.1; -; mRNA.
DR EMBL; AF049259; AAC35754.1; -; Genomic_DNA.
DR EMBL; AK092276; BAC03847.1; -; mRNA.
DR EMBL; AK223051; BAD96771.1; -; mRNA.
DR EMBL; AK223077; BAD96797.1; -; mRNA.
DR EMBL; AC019349; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002661; AAH02661.3; -; mRNA.
DR EMBL; BC077718; AAH77718.2; -; mRNA.
DR CCDS; CCDS11396.1; -. [P13646-1]
DR CCDS; CCDS11397.1; -. [P13646-3]
DR PIR; A37343; A37343.
DR PIR; S06088; KRHU3.
DR RefSeq; NP_002265.2; NM_002274.3. [P13646-3]
DR RefSeq; NP_705694.2; NM_153490.2. [P13646-1]
DR AlphaFoldDB; P13646; -.
DR SMR; P13646; -.
DR BioGRID; 110058; 90.
DR IntAct; P13646; 51.
DR MINT; P13646; -.
DR STRING; 9606.ENSP00000246635; -.
DR GlyConnect; 311; 1 O-Linked glycan.
DR GlyGen; P13646; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P13646; -.
DR PhosphoSitePlus; P13646; -.
DR SwissPalm; P13646; -.
DR BioMuta; KRT13; -.
DR DMDM; 269849755; -.
DR jPOST; P13646; -.
DR MassIVE; P13646; -.
DR PaxDb; P13646; -.
DR PeptideAtlas; P13646; -.
DR PRIDE; P13646; -.
DR ProteomicsDB; 52951; -. [P13646-1]
DR ProteomicsDB; 52952; -. [P13646-2]
DR ProteomicsDB; 52953; -. [P13646-3]
DR Antibodypedia; 3599; 605 antibodies from 43 providers.
DR DNASU; 3860; -.
DR Ensembl; ENST00000246635.8; ENSP00000246635.3; ENSG00000171401.15. [P13646-1]
DR Ensembl; ENST00000336861.7; ENSP00000336604.3; ENSG00000171401.15. [P13646-3]
DR GeneID; 3860; -.
DR KEGG; hsa:3860; -.
DR MANE-Select; ENST00000246635.8; ENSP00000246635.3; NM_153490.3; NP_705694.3.
DR UCSC; uc002hwu.2; human. [P13646-1]
DR CTD; 3860; -.
DR DisGeNET; 3860; -.
DR GeneCards; KRT13; -.
DR HGNC; HGNC:6415; KRT13.
DR HPA; ENSG00000171401; Tissue enhanced (esophagus, vagina).
DR MalaCards; KRT13; -.
DR MIM; 148065; gene.
DR MIM; 615785; phenotype.
DR neXtProt; NX_P13646; -.
DR OpenTargets; ENSG00000171401; -.
DR Orphanet; 171723; White sponge nevus.
DR PharmGKB; PA30202; -.
DR VEuPathDB; HostDB:ENSG00000171401; -.
DR eggNOG; ENOG502QTM6; Eukaryota.
DR GeneTree; ENSGT00950000183311; -.
DR HOGENOM; CLU_012560_8_1_1; -.
DR InParanoid; P13646; -.
DR OMA; DAKMTGF; -.
DR OrthoDB; 856254at2759; -.
DR PhylomeDB; P13646; -.
DR TreeFam; TF332742; -.
DR PathwayCommons; P13646; -.
DR Reactome; R-HSA-6805567; Keratinization.
DR Reactome; R-HSA-6809371; Formation of the cornified envelope.
DR SignaLink; P13646; -.
DR BioGRID-ORCS; 3860; 12 hits in 1069 CRISPR screens.
DR ChiTaRS; KRT13; human.
DR GeneWiki; Keratin_13; -.
DR GenomeRNAi; 3860; -.
DR Pharos; P13646; Tbio.
DR PRO; PR:P13646; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P13646; protein.
DR Bgee; ENSG00000171401; Expressed in lower esophagus mucosa and 112 other tissues.
DR ExpressionAtlas; P13646; baseline and differential.
DR Genevisible; P13646; HS.
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:0045111; C:intermediate filament cytoskeleton; IDA:UniProtKB.
DR GO; GO:0045095; C:keratin filament; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0007010; P:cytoskeleton organization; IDA:UniProtKB.
DR GO; GO:0030855; P:epithelial cell differentiation; IBA:GO_Central.
DR GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
DR GO; GO:0043555; P:regulation of translation in response to stress; ISS: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 Alternative splicing; Coiled coil; Direct protein sequencing;
KW Disease variant; Glycoprotein; Intermediate filament; Keratin; Methylation;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..458
FT /note="Keratin, type I cytoskeletal 13"
FT /id="PRO_0000063647"
FT DOMAIN 104..416
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..103
FT /note="Head"
FT REGION 104..139
FT /note="Coil 1A"
FT REGION 140..158
FT /note="Linker 1"
FT REGION 159..250
FT /note="Coil 1B"
FT REGION 251..273
FT /note="Linker 12"
FT REGION 274..412
FT /note="Coil 2"
FT REGION 413..458
FT /note="Tail"
FT REGION 420..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 27
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 35
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 62..73
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_016376"
FT VAR_SEQ 351..458
FT /note="ETECRYALQLQQIQGLISSIEAQLSELRSEMECQNQEYKMLLDIKTRLEQEI
FT ATYRSLLEGQDAKMIGFPSSAGSVSPRSTSVTTTSSASVTTTSNASGRRTSDVRRP ->
FT DPGTHQQHRGPAERAPQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_016377"
FT VAR_SEQ 416..458
FT /note="MIGFPSSAGSVSPRSTSVTTTSSASVTTTSNASGRRTSDVRRP -> KRQPP
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:2483837"
FT /id="VSP_038433"
FT VARIANT 81
FT /note="F -> Y (in dbSNP:rs12150581)"
FT /id="VAR_059376"
FT VARIANT 108
FT /note="M -> T (in WSN2; dbSNP:rs60364670)"
FT /evidence="ECO:0000269|PubMed:10561721"
FT /id="VAR_016035"
FT VARIANT 111
FT /note="L -> P (in WSN2; dbSNP:rs59897026)"
FT /evidence="ECO:0000269|PubMed:14600690"
FT /id="VAR_023924"
FT VARIANT 112
FT /note="N -> S (in WSN2; dbSNP:rs59970018)"
FT /evidence="ECO:0000269|PubMed:11379896"
FT /id="VAR_016036"
FT VARIANT 114
FT /note="R -> C (in WSN2; unknown pathological significance;
FT dbSNP:rs545085703)"
FT /evidence="ECO:0000269|PubMed:25606422"
FT /id="VAR_086269"
FT VARIANT 114
FT /note="R -> H (in WSN2; unknown pathological significance;
FT dbSNP:rs267607388)"
FT /evidence="ECO:0000269|PubMed:18616775"
FT /id="VAR_086270"
FT VARIANT 115
FT /note="L -> P (in WSN2; dbSNP:rs60906702)"
FT /evidence="ECO:0000269|PubMed:10561721"
FT /id="VAR_016037"
FT VARIANT 118
FT /note="Y -> D (in WSN2)"
FT /evidence="ECO:0000269|PubMed:29476668"
FT /id="VAR_086271"
FT VARIANT 119
FT /note="L -> P (in WSN2; dbSNP:rs60440396)"
FT /evidence="ECO:0000269|PubMed:7493031"
FT /id="VAR_003836"
FT VARIANT 146
FT /note="A -> G (in dbSNP:rs760134)"
FT /id="VAR_024488"
FT VARIANT 187
FT /note="A -> V (in dbSNP:rs9891361)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:2475110,
FT ECO:0000269|PubMed:2477803, ECO:0000269|PubMed:2483837,
FT ECO:0000269|PubMed:9714826, ECO:0000269|Ref.6,
FT ECO:0007744|PubMed:21269460"
FT /id="VAR_060724"
FT VARIANT 298
FT /note="T -> A (in dbSNP:rs4796697)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:2475110,
FT ECO:0000269|PubMed:2477803, ECO:0000269|PubMed:2483837,
FT ECO:0000269|PubMed:9714826, ECO:0000269|Ref.6"
FT /id="VAR_059377"
FT CONFLICT 46
FT /note="G -> R (in Ref. 6; BAD96771/BAD96797)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="G -> D (in Ref. 1; CAA32786 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 458 AA; 49588 MW; A51AECFD6195ACB4 CRC64;
MSLRLQSSSA SYGGGFGGGS CQLGGGRGVS TCSTRFVSGG SAGGYGGGVS CGFGGGAGSG
FGGGYGGGLG GGYGGGLGGG FGGGFAGGFV DFGACDGGLL TGNEKITMQN LNDRLASYLE
KVRALEEANA DLEVKIRDWH LKQSPASPER DYSPYYKTIE ELRDKILTAT IENNRVILEI
DNARLAADDF RLKYENELAL RQSVEADING LRRVLDELTL SKTDLEMQIE SLNEELAYMK
KNHEEEMKEF SNQVVGQVNV EMDATPGIDL TRVLAEMREQ YEAMAERNRR DAEEWFHTKS
AELNKEVSTN TAMIQTSKTE ITELRRTLQG LEIELQSQLS MKAGLENTVA ETECRYALQL
QQIQGLISSI EAQLSELRSE MECQNQEYKM LLDIKTRLEQ EIATYRSLLE GQDAKMIGFP
SSAGSVSPRS TSVTTTSSAS VTTTSNASGR RTSDVRRP
