ID K1C20_HUMAN Reviewed; 424 AA. AC P35900; B2R6W7; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 09-DEC-2015, entry version 147. DE RecName: Full=Keratin, type I cytoskeletal 20; DE AltName: Full=Cytokeratin-20; DE Short=CK-20; DE AltName: Full=Keratin-20; DE Short=K20; DE AltName: Full=Protein IT; GN Name=KRT20; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DEVELOPMENTAL STAGE. RC TISSUE=Intestine; RX PubMed=8359595; DOI=10.1111/j.1432-0436.1993.tb00648.x; RA Moll R., Zimbelmann R., Goldschmidt M.D., Keith M., Laufer J., RA Kasper M., Koch P.J., Franke W.W.; RT "The human gene encoding cytokeratin 20 and its expression during RT fetal development and in gastrointestinal carcinomas."; RL Differentiation 53:75-93(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASN-129. RC TISSUE=Small intestine; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PROTEIN SEQUENCE OF 11-28, FUNCTION, INTERACTION WITH KRT8, RP PHOSPHORYLATION AT SER-13, CLEAVAGE AT ASP-228, AND MUTAGENESIS OF RP SER-13 AND SER-14. RX PubMed=16608857; DOI=10.1074/jbc.M512284200; RA Zhou Q., Cadrin M., Herrmann H., Chen C.-H., Chalkley R.J., RA Burlingame A.L., Omary M.B.; RT "Keratin 20 serine 13 phosphorylation is a stress and intestinal RT goblet cell marker."; RL J. Biol. Chem. 281:16453-16461(2006). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 86-424. RC TISSUE=Intestine; RX PubMed=7689500; DOI=10.1111/j.1432-0436.1993.tb00649.x; RA Calnek D., Quaroni A.; RT "Differential localization by in situ hybridization of distinct RT keratin mRNA species during intestinal epithelial cell development and RT differentiation."; RL Differentiation 53:95-104(1993). RN [6] RP IDENTIFICATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=1696264; DOI=10.1083/jcb.111.2.567; RA Moll R., Schiller D.L., Franke W.W.; RT "Identification of protein IT of the intestinal cytoskeleton as a RT novel type I cytokeratin with unusual properties and expression RT patterns."; RL J. Cell Biol. 111:567-580(1990). RN [7] RP INTERACTION WITH KRT8, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=10973561; DOI=10.1016/S0003-9969(00)00050-9; RA Barrett A.W., Cort E.M., Patel P., Berkovitz B.K.B.; RT "An immunohistological study of cytokeratin 20 in human and mammalian RT oral epithelium."; RL Arch. Oral Biol. 45:879-887(2000). RN [8] RP FUNCTION, AND MUTAGENESIS OF ARG-80. RX PubMed=12857878; DOI=10.1091/mbc.E03-02-0059; RA Zhou Q., Toivola D.M., Feng N., Greenberg H.B., Franke W.W., RA Omary M.B.; RT "Keratin 20 helps maintain intermediate filament organization in RT intestinal epithelia."; RL Mol. Biol. Cell 14:2959-2971(2003). RN [9] RP VARIANT [LARGE SCALE ANALYSIS] ARG-4. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., RA Vogelstein B., Kinzler K.W., Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal RT cancers."; RL Science 314:268-274(2006). RN [10] RP VARIANT CYS-214. RX PubMed=21248752; DOI=10.1038/nature09639; RA Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., RA Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A., RA Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., RA Jia M., Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., RA Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., RA Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A., RA Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C., RA Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R., RA Futreal P.A.; RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex RT gene PBRM1 in renal carcinoma."; RL Nature 469:539-542(2011). CC -!- FUNCTION: Plays a significant role in maintaining keratin filament CC organization in intestinal epithelia. When phosphorylated, plays a CC role in the secretion of mucin in the small intestine (By CC similarity). {ECO:0000250, ECO:0000269|PubMed:12857878, CC ECO:0000269|PubMed:16608857}. CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins. CC Associates with KRT8. CC -!- INTERACTION: CC Q9Y2J4-4:AMOTL2; NbExp=3; IntAct=EBI-742094, EBI-10187270; CC Q9BUW7:C9orf16; NbExp=6; IntAct=EBI-742094, EBI-752084; CC A1A4E9:KRT13; NbExp=3; IntAct=EBI-742094, EBI-10171552; CC P19012:KRT15; NbExp=4; IntAct=EBI-742094, EBI-739566; CC Q6A162:KRT40; NbExp=3; IntAct=EBI-742094, EBI-10171697; CC Q6KB66:KRT80; NbExp=3; IntAct=EBI-742094, EBI-3046635; CC P60409:KRTAP10-7; NbExp=3; IntAct=EBI-742094, EBI-10172290; CC P60410:KRTAP10-8; NbExp=3; IntAct=EBI-742094, EBI-10171774; CC P60411:KRTAP10-9; NbExp=3; IntAct=EBI-742094, EBI-10172052; CC Q7Z3S9:NOTCH2NL; NbExp=3; IntAct=EBI-742094, EBI-945833; CC P37198:NUP62; NbExp=3; IntAct=EBI-742094, EBI-347978; CC O00459:PIK3R2; NbExp=3; IntAct=EBI-742094, EBI-346930; CC Q9UBB9:TFIP11; NbExp=4; IntAct=EBI-742094, EBI-1105213; CC P40222:TXLNA; NbExp=3; IntAct=EBI-742094, EBI-359793; CC Q8N6Y0:USHBP1; NbExp=3; IntAct=EBI-742094, EBI-739895; CC P08670:VIM; NbExp=4; IntAct=EBI-742094, EBI-353844; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10973561, CC ECO:0000269|PubMed:1696264}. CC -!- TISSUE SPECIFICITY: Expressed predominantly in the intestinal CC epithelium. Expressed in luminal cells of colonic mucosa. Also CC expressed in the Merkel cells of keratinized oral mucosa; CC specifically at the tips of some rete ridges of the gingival CC mucosa, in the basal layer of the palatal mucosa and in the taste CC buds of lingual mucosa. {ECO:0000269|PubMed:10973561, CC ECO:0000269|PubMed:1696264}. CC -!- DEVELOPMENTAL STAGE: First detected at embryonic week 8 in CC individual 'converted' simple epithelial cells of the developing CC intestinal mucosa. In later fetal stages, synthesis extends over CC most goblet cells and a variable number of villus enterocytes. In CC the developing gastric and intestinal mucosa, expressed in all CC enterocytes and goblet cells as well as certain 'low- CC differentiated' columnar cells, whereas the neuroendocrine and CC Paneth cells are negative. {ECO:0000269|PubMed:8359595}. CC -!- PTM: Hyperphosphorylation at Ser-13 occurs during the early stages CC of apoptosis but becomes less prominent during the later stages. CC Phosphorylation at Ser-13 also increases in response to stress CC brought on by cell injury (By similarity). {ECO:0000250}. CC -!- PTM: Proteolytically cleaved by caspases during apoptosis. CC Cleavage occurs at Asp-228. {ECO:0000269|PubMed:16608857}. CC -!- MISCELLANEOUS: There are two types of cytoskeletal and CC microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to CC basic; 56-70 kDa). CC -!- SIMILARITY: Belongs to the intermediate filament family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X73501; CAA51913.1; -; Genomic_DNA. DR EMBL; AK312744; BAG35614.1; -; mRNA. DR EMBL; BC031559; AAH31559.1; -; mRNA. DR EMBL; X73502; CAA51914.1; -; mRNA. DR CCDS; CCDS11379.1; -. DR PIR; S37780; S37780. DR RefSeq; NP_061883.1; NM_019010.2. DR UniGene; Hs.84905; -. DR ProteinModelPortal; P35900; -. DR SMR; P35900; 287-376. DR BioGrid; 119979; 28. DR IntAct; P35900; 27. DR MINT; MINT-1445560; -. DR STRING; 9606.ENSP00000167588; -. DR PhosphoSite; P35900; -. DR BioMuta; KRT20; -. DR DMDM; 547750; -. DR MaxQB; P35900; -. DR PaxDb; P35900; -. DR PRIDE; P35900; -. DR DNASU; 54474; -. DR Ensembl; ENST00000167588; ENSP00000167588; ENSG00000171431. DR Ensembl; ENST00000576098; ENSP00000460501; ENSG00000263057. DR GeneID; 54474; -. DR KEGG; hsa:54474; -. DR UCSC; uc002hvl.3; human. DR CTD; 54474; -. DR GeneCards; KRT20; -. DR HGNC; HGNC:20412; KRT20. DR HPA; CAB000032; -. DR HPA; HPA024309; -. DR HPA; HPA024684; -. DR HPA; HPA027236; -. DR MIM; 608218; gene. DR neXtProt; NX_P35900; -. DR PharmGKB; PA134938907; -. DR eggNOG; ENOG410IVBB; Eukaryota. DR eggNOG; ENOG410YGAC; LUCA. DR GeneTree; ENSGT00760000118808; -. DR HOGENOM; HOG000230975; -. DR HOVERGEN; HBG013015; -. DR InParanoid; P35900; -. DR KO; K07604; -. DR OMA; KYETERG; -. DR OrthoDB; EOG7FV3Q8; -. DR PhylomeDB; P35900; -. DR TreeFam; TF332742; -. DR GeneWiki; Keratin_20; -. DR GenomeRNAi; 54474; -. DR NextBio; 56776; -. DR PRO; PR:P35900; -. DR Proteomes; UP000005640; Chromosome 17. DR Bgee; P35900; -. DR CleanEx; HS_KRT20; -. DR Genevisible; P35900; HS. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005882; C:intermediate filament; NAS:UniProtKB. DR GO; GO:0005200; F:structural constituent of cytoskeleton; NAS:UniProtKB. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0033554; P:cellular response to stress; IEA:Ensembl. DR GO; GO:0045109; P:intermediate filament organization; IMP:UniProtKB. DR GO; GO:0050708; P:regulation of protein secretion; IEA:Ensembl. DR InterPro; IPR001664; IF. DR InterPro; IPR018039; Intermediate_filament_CS. DR InterPro; IPR002957; Keratin_I. DR PANTHER; PTHR23239; PTHR23239; 1. DR Pfam; PF00038; Filament; 1. DR PRINTS; PR01248; TYPE1KERATIN. DR PROSITE; PS00226; IF; 1. PE 1: Evidence at protein level; KW Apoptosis; Coiled coil; Complete proteome; Cytoplasm; KW Direct protein sequencing; Intermediate filament; Keratin; KW Phosphoprotein; Polymorphism; Reference proteome. FT CHAIN 1 424 Keratin, type I cytoskeletal 20. FT /FTId=PRO_0000063675. FT REGION 1 69 Head. FT REGION 70 377 Rod. FT REGION 70 105 Coil 1A. FT REGION 106 123 Linker 1. FT REGION 124 215 Coil 1B. FT REGION 216 238 Linker 12. FT REGION 239 377 Coil 2. FT REGION 378 424 Tail. FT SITE 228 229 Cleavage; by caspases. FT MOD_RES 13 13 Phosphoserine; by MAPKAPK2, MAPKAPK3 and FT PKC. {ECO:0000269|PubMed:16608857}. FT VARIANT 4 4 S -> R (in a colorectal cancer sample; FT somatic mutation). FT {ECO:0000269|PubMed:16959974}. FT /FTId=VAR_036367. FT VARIANT 129 129 S -> N (in dbSNP:rs7212483). FT {ECO:0000269|PubMed:14702039}. FT /FTId=VAR_024489. FT VARIANT 214 214 G -> C (found in a renal cell carcinoma FT sample; somatic mutation). FT {ECO:0000269|PubMed:21248752}. FT /FTId=VAR_064726. FT MUTAGEN 13 13 S->A: Promotes keratin filament FT disassembly. FT {ECO:0000269|PubMed:16608857}. FT MUTAGEN 14 14 S->A: No effect on keratin filament FT organization. FT {ECO:0000269|PubMed:16608857}. FT MUTAGEN 80 80 R->H: Leads to collapsed filaments. FT {ECO:0000269|PubMed:12857878}. FT CONFLICT 161 161 T -> S (in Ref. 5; CAA51914). FT {ECO:0000305}. FT CONFLICT 349 349 Q -> P (in Ref. 5; CAA51914). FT {ECO:0000305}. FT CONFLICT 398 398 R -> T (in Ref. 5; CAA51914). FT {ECO:0000305}. SQ SEQUENCE 424 AA; 48487 MW; A8EF5A518C73CCE5 CRC64; MDFSRRSFHR SLSSSLQAPV VSTVGMQRLG TTPSVYGGAG GRGIRISNSR HTVNYGSDLT GGGDLFVGNE KMAMQNLNDR LASYLEKVRT LEQSNSKLEV QIKQWYETNA PRAGRDYSAY YRQIEELRSQ IKDAQLQNAR CVLQIDNAKL AAEDFRLKYE TERGIRLTVE ADLQGLNKVF DDLTLHKTDL EIQIEELNKD LALLKKEHQE EVDGLHKHLG NTVNVEVDAA PGLNLGVIMN EMRQKYEVMA QKNLQEAKEQ FERQTAVLQQ QVTVNTEELK GTEVQLTELR RTSQSLEIEL QSHLSMKESL EHTLEETKAR YSSQLANLQS LLSSLEAQLM QIRSNMERQN NEYHILLDIK TRLEQEIATY RRLLEGEDVK TTEYQLSTLE ERDIKKTRKI KTVVQEVVDG KVVSSEVKEV EENI //