K1C20_HUMAN
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 03-AUG-2022, entry version 188.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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., Kasper M.,
RA Koch P.J., Franke W.W.;
RT "The human gene encoding cytokeratin 20 and its expression during fetal
RT 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., 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 [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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 11-28, FUNCTION, INTERACTION WITH KRT8, PHOSPHORYLATION
RP AT SER-13, PROTEOLYTIC CLEAVAGE AT ASP-228, AND MUTAGENESIS OF SER-13 AND
RP 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 goblet
RT 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 keratin
RT 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 novel
RT type I cytokeratin with unusual properties and expression 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 oral
RT 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., Omary M.B.;
RT "Keratin 20 helps maintain intermediate filament organization in intestinal
RT 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., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal 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., Davies H.,
RA Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J.,
RA Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M.,
RA Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L.,
RA Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J.,
RA Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A.,
RA Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K.,
RA Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.;
RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex gene
RT 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 role
CC in the secretion of mucin in the small intestine (By similarity).
CC {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 P35900; Q9NYB9: ABI2; NbExp=3; IntAct=EBI-742094, EBI-743598;
CC P35900; Q9Y2J4-4: AMOTL2; NbExp=3; IntAct=EBI-742094, EBI-10187270;
CC P35900; Q9BUW7: BBLN; NbExp=9; IntAct=EBI-742094, EBI-752084;
CC P35900; O75934: BCAS2; NbExp=3; IntAct=EBI-742094, EBI-1050106;
CC P35900; A0A1B0GWI1: CCDC196; NbExp=3; IntAct=EBI-742094, EBI-10181422;
CC P35900; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-742094, EBI-3867333;
CC P35900; P17661: DES; NbExp=3; IntAct=EBI-742094, EBI-1055572;
CC P35900; P42858: HTT; NbExp=9; IntAct=EBI-742094, EBI-466029;
CC P35900; A1A4E9: KRT13; NbExp=3; IntAct=EBI-742094, EBI-10171552;
CC P35900; P19012: KRT15; NbExp=5; IntAct=EBI-742094, EBI-739566;
CC P35900; Q2M2I5: KRT24; NbExp=3; IntAct=EBI-742094, EBI-2952736;
CC P35900; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-742094, EBI-3044087;
CC P35900; P12035: KRT3; NbExp=3; IntAct=EBI-742094, EBI-2430095;
CC P35900; Q15323: KRT31; NbExp=3; IntAct=EBI-742094, EBI-948001;
CC P35900; O76011: KRT34; NbExp=3; IntAct=EBI-742094, EBI-1047093;
CC P35900; Q6A162: KRT40; NbExp=3; IntAct=EBI-742094, EBI-10171697;
CC P35900; Q14CN4: KRT72; NbExp=3; IntAct=EBI-742094, EBI-1221280;
CC P35900; O95678: KRT75; NbExp=3; IntAct=EBI-742094, EBI-2949715;
CC P35900; Q01546: KRT76; NbExp=3; IntAct=EBI-742094, EBI-2952745;
CC P35900; Q6KB66: KRT80; NbExp=3; IntAct=EBI-742094, EBI-3046635;
CC P35900; Q6KB66-2: KRT80; NbExp=3; IntAct=EBI-742094, EBI-11999246;
CC P35900; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-742094, EBI-11959885;
CC P35900; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-742094, EBI-10172290;
CC P35900; P60410: KRTAP10-8; NbExp=6; IntAct=EBI-742094, EBI-10171774;
CC P35900; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-742094, EBI-10172052;
CC P35900; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-742094, EBI-11953334;
CC P35900; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-742094, EBI-945833;
CC P35900; P37198: NUP62; NbExp=7; IntAct=EBI-742094, EBI-347978;
CC P35900; O00459: PIK3R2; NbExp=3; IntAct=EBI-742094, EBI-346930;
CC P35900; Q96KQ4: PPP1R13B; NbExp=3; IntAct=EBI-742094, EBI-1105153;
CC P35900; P41219: PRPH; NbExp=6; IntAct=EBI-742094, EBI-752074;
CC P35900; O95295: SNAPIN; NbExp=3; IntAct=EBI-742094, EBI-296723;
CC P35900; Q9UBB9: TFIP11; NbExp=7; IntAct=EBI-742094, EBI-1105213;
CC P35900; P40222: TXLNA; NbExp=6; IntAct=EBI-742094, EBI-359793;
CC P35900; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-742094, EBI-739895;
CC P35900; P08670: VIM; NbExp=8; 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; specifically
CC at the tips of some rete ridges of the gingival mucosa, in the basal
CC layer of the palatal mucosa and in the taste buds of lingual mucosa.
CC {ECO:0000269|PubMed:10973561, ECO:0000269|PubMed:1696264}.
CC -!- DEVELOPMENTAL STAGE: First detected at embryonic week 8 in individual
CC 'converted' simple epithelial cells of the developing intestinal
CC mucosa. In later fetal stages, synthesis extends over most goblet cells
CC and a variable number of villus enterocytes. In the developing gastric
CC and intestinal mucosa, expressed in all enterocytes and goblet cells as
CC well as certain 'low-differentiated' columnar cells, whereas the
CC neuroendocrine and Paneth cells are negative.
CC {ECO:0000269|PubMed:8359595}.
CC -!- PTM: Hyperphosphorylation at Ser-13 occurs during the early stages of
CC apoptosis but becomes less prominent during the later stages.
CC Phosphorylation at Ser-13 also increases in response to stress brought
CC on by cell injury (By similarity). {ECO:0000250}.
CC -!- PTM: Proteolytically cleaved by caspases during apoptosis. Cleavage
CC occurs at Asp-228. {ECO:0000269|PubMed:16608857}.
CC -!- MISCELLANEOUS: There are two types of cytoskeletal and microfibrillar
CC keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; 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 AlphaFoldDB; P35900; -.
DR SMR; P35900; -.
DR BioGRID; 119979; 50.
DR IntAct; P35900; 47.
DR MINT; P35900; -.
DR STRING; 9606.ENSP00000167588; -.
DR iPTMnet; P35900; -.
DR PhosphoSitePlus; P35900; -.
DR SwissPalm; P35900; -.
DR BioMuta; KRT20; -.
DR DMDM; 547750; -.
DR jPOST; P35900; -.
DR MassIVE; P35900; -.
DR PaxDb; P35900; -.
DR PeptideAtlas; P35900; -.
DR PRIDE; P35900; -.
DR ProteomicsDB; 55160; -.
DR Antibodypedia; 3502; 1407 antibodies from 50 providers.
DR DNASU; 54474; -.
DR Ensembl; ENST00000167588.4; ENSP00000167588.3; ENSG00000171431.4.
DR Ensembl; ENST00000576098.2; ENSP00000460501.2; ENSG00000263057.2.
DR GeneID; 54474; -.
DR KEGG; hsa:54474; -.
DR MANE-Select; ENST00000167588.4; ENSP00000167588.3; NM_019010.3; NP_061883.1.
DR UCSC; uc002hvl.4; human.
DR CTD; 54474; -.
DR DisGeNET; 54474; -.
DR GeneCards; KRT20; -.
DR HGNC; HGNC:20412; KRT20.
DR HPA; ENSG00000171431; Tissue enriched (intestine).
DR MIM; 608218; gene.
DR neXtProt; NX_P35900; -.
DR OpenTargets; ENSG00000171431; -.
DR PharmGKB; PA134938907; -.
DR VEuPathDB; HostDB:ENSG00000171431; -.
DR eggNOG; ENOG502QUY3; Eukaryota.
DR GeneTree; ENSGT00940000161855; -.
DR HOGENOM; CLU_012560_8_1_1; -.
DR InParanoid; P35900; -.
DR OMA; YSAYYKQ; -.
DR OrthoDB; 798081at2759; -.
DR PhylomeDB; P35900; -.
DR TreeFam; TF332742; -.
DR PathwayCommons; P35900; -.
DR Reactome; R-HSA-6805567; Keratinization.
DR Reactome; R-HSA-6809371; Formation of the cornified envelope.
DR SignaLink; P35900; -.
DR SIGNOR; P35900; -.
DR BioGRID-ORCS; 54474; 13 hits in 1068 CRISPR screens.
DR ChiTaRS; KRT20; human.
DR GeneWiki; Keratin_20; -.
DR GenomeRNAi; 54474; -.
DR Pharos; P35900; Tbio.
DR PRO; PR:P35900; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P35900; protein.
DR Bgee; ENSG00000171431; Expressed in mucosa of transverse colon and 76 other tissues.
DR Genevisible; P35900; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
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:0009267; P:cellular response to starvation; IEA:Ensembl.
DR GO; GO:0030855; P:epithelial cell differentiation; IBA:GO_Central.
DR GO; GO:0045109; P:intermediate filament organization; IMP:UniProtKB.
DR GO; GO:0050708; P:regulation of protein secretion; IEA:Ensembl.
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 Apoptosis; Coiled coil; Cytoplasm; Direct protein sequencing;
KW Intermediate filament; Keratin; Phosphoprotein; Reference proteome.
FT CHAIN 1..424
FT /note="Keratin, type I cytoskeletal 20"
FT /id="PRO_0000063675"
FT DOMAIN 70..381
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..69
FT /note="Head"
FT REGION 70..105
FT /note="Coil 1A"
FT REGION 106..123
FT /note="Linker 1"
FT REGION 124..215
FT /note="Coil 1B"
FT REGION 216..238
FT /note="Linker 12"
FT REGION 239..377
FT /note="Coil 2"
FT REGION 378..424
FT /note="Tail"
FT SITE 228..229
FT /note="Cleavage; by caspases"
FT /evidence="ECO:0000269|PubMed:16608857"
FT MOD_RES 13
FT /note="Phosphoserine; by MAPKAPK2, MAPKAPK3 and PKC"
FT /evidence="ECO:0000269|PubMed:16608857"
FT VARIANT 4
FT /note="S -> R (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036367"
FT VARIANT 129
FT /note="S -> N (in dbSNP:rs7212483)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_024489"
FT VARIANT 214
FT /note="G -> C (found in a renal cell carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:21248752"
FT /id="VAR_064726"
FT MUTAGEN 13
FT /note="S->A: Promotes keratin filament disassembly."
FT /evidence="ECO:0000269|PubMed:16608857"
FT MUTAGEN 14
FT /note="S->A: No effect on keratin filament organization."
FT /evidence="ECO:0000269|PubMed:16608857"
FT MUTAGEN 80
FT /note="R->H: Leads to collapsed filaments."
FT /evidence="ECO:0000269|PubMed:12857878"
FT CONFLICT 161
FT /note="T -> S (in Ref. 5; CAA51914)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="Q -> P (in Ref. 5; CAA51914)"
FT /evidence="ECO:0000305"
FT CONFLICT 398
FT /note="R -> T (in Ref. 5; CAA51914)"
FT /evidence="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
