K1C19_HUMAN
ID K1C19_HUMAN Reviewed; 400 AA.
AC P08727; B2R874; Q5XG83; Q6NW33; Q7L5M9; Q96A53; Q96FV1; Q9BYF9; Q9P1Y4;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 4.
DT 03-AUG-2022, entry version 217.
DE RecName: Full=Keratin, type I cytoskeletal 19;
DE AltName: Full=Cytokeratin-19;
DE Short=CK-19;
DE AltName: Full=Keratin-19;
DE Short=K19;
GN Name=KRT19;
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 VARIANT GLY-60.
RC TISSUE=Placenta;
RX PubMed=2447559; DOI=10.1093/nar/15.23.10058;
RA Stasiak P.C., Lane E.B.;
RT "Sequence of cDNA coding for human keratin 19.";
RL Nucleic Acids Res. 15:10058-10058(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RX PubMed=2468493;
RA Bader B.L., Jahn L., Franke W.W.;
RT "Low level expression of cytokeratins 8, 18 and 19 in vascular smooth
RT muscle cells of human umbilical cord and in cultured cells derived
RT therefrom, with an analysis of the chromosomal locus containing the
RT cytokeratin 19 gene.";
RL Eur. J. Cell Biol. 47:300-319(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLY-60.
RX PubMed=2448790; DOI=10.1073/pnas.85.4.1114;
RA Eckert R.L.;
RT "Sequence of the human 40-kDa keratin reveals an unusual structure with
RT very high sequence identity to the corresponding bovine keratin.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:1114-1118(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP VARIANT GLY-60.
RC TISSUE=Placenta;
RX PubMed=2469734; DOI=10.1111/1523-1747.ep12721500;
RA Stasiak P.C., Purkis P.E., Leigh I.M., Lane E.B.;
RT "Keratin 19: predicted amino acid sequence and broad tissue distribution
RT suggest it evolved from keratinocyte keratins.";
RL J. Invest. Dermatol. 92:707-716(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLY-60.
RX PubMed=10623642; DOI=10.1006/bbrc.1999.1966;
RA Whittock N.V., Eady R.A.J., McGrath J.A.;
RT "Genomic organization and amplification of the human keratin 15 and 19
RT genes.";
RL Biochem. Biophys. Res. Commun. 267:462-465(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-60.
RC TISSUE=Placenta;
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 [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], AND VARIANT GLY-60.
RC TISSUE=Mammary gland, Pancreas, and Placenta;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
RC TISSUE=Peripheral blood leukocyte;
RX PubMed=11682035; DOI=10.1016/s0168-8278(01)00167-2;
RA Kagaya M., Kaneko S., Ohno H., Inamura K., Kobayashi K.;
RT "Cloning and characterization of the 5'-flanking region of human
RT cytokeratin 19 gene in human cholangiocarcinoma cell line.";
RL J. Hepatol. 35:504-511(2001).
RN [10]
RP PROTEIN SEQUENCE OF 25-31; 151-158 AND 227-237.
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 [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 145-352.
RC TISSUE=Lymph node;
RA Sato T., Weerasinghe A., Kuwano Y., Kaneko T., Ikeda T., Nagai T.,
RA Makino H., Sano M., Honma K., Nemoto K., Abo T., Shima Y.;
RT "Diversity of keratin 19 gene expressed in lymph nodes of breast cancer
RT patients -- strategy to clear the discrepancy between histological findings
RT and RT-PCR results in the detection of micrometastasis.";
RL Seibutsu Butsuri Kagaku 44:201-204(2000).
RN [12]
RP PHOSPHORYLATION AT SER-35, AND MUTAGENESIS OF SER-10 AND SER-35.
RX PubMed=10212274; DOI=10.1074/jbc.274.18.12861;
RA Zhou X., Liao J., Hu L., Feng L., Omary M.B.;
RT "Characterization of the major physiologic phosphorylation site of human
RT keratin 19 and its role in filament organization.";
RL J. Biol. Chem. 274:12861-12866(1999).
RN [13]
RP INTERACTION WITH PNN.
RX PubMed=10809736; DOI=10.1074/jbc.275.20.14910;
RA Shi J., Sugrue S.P.;
RT "Dissection of protein linkage between keratins and pinin, a protein with
RT dual location at desmosome-intermediate filament complex and in the
RT nucleus.";
RL J. Biol. Chem. 275:14910-14915(2000).
RN [14]
RP INTERACTION WITH HEPATITIS C VIRUS CORE PROTEIN (MICROBIAL INFECTION).
RX PubMed=15846844; DOI=10.1002/pmic.200401093;
RA Kang S.-M., Shin M.-J., Kim J.-H., Oh J.-W.;
RT "Proteomic profiling of cellular proteins interacting with the hepatitis C
RT virus core protein.";
RL Proteomics 5:2227-2237(2005).
RN [15]
RP FUNCTION, INTERACTION WITH DMD, AND TISSUE SPECIFICITY.
RX PubMed=16000376; DOI=10.1091/mbc.e05-02-0112;
RA Stone M.R., O'Neill A., Catino D., Bloch R.J.;
RT "Specific interaction of the actin-binding domain of dystrophin with
RT intermediate filaments containing keratin 19.";
RL Mol. Biol. Cell 16:4280-4293(2005).
RN [16]
RP PHOSPHORYLATION AT TYR-391.
RX PubMed=21049038; DOI=10.1371/journal.pone.0013538;
RA Zhou Q., Snider N.T., Liao J., Li D.H., Hong A., Ku N.O., Cartwright C.A.,
RA Omary M.B.;
RT "Characterization of in vivo keratin 19 phosphorylation on tyrosine-391.";
RL PLoS ONE 5:E13538-E13538(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-22; THR-323; SER-395
RP AND SER-397, 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 [19]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-7; ARG-24; ARG-32; ARG-43 AND
RP ARG-51, AND IDENTIFICATION 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 [20]
RP VARIANT [LARGE SCALE ANALYSIS] GLY-60, 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).
CC -!- FUNCTION: Involved in the organization of myofibers. Together with
CC KRT8, helps to link the contractile apparatus to dystrophin at the
CC costameres of striated muscle. {ECO:0000269|PubMed:16000376}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC Interacts with PNN and the actin-binding domain of DMD. Interacts with
CC HCV core protein. {ECO:0000269|PubMed:10809736,
CC ECO:0000269|PubMed:16000376}.
CC -!- SUBUNIT: (Microbial infection) Interacts with hepatitis C virus/HCV
CC core protein. {ECO:0000269|PubMed:15846844}.
CC -!- INTERACTION:
CC P08727; Q9NYB9: ABI2; NbExp=3; IntAct=EBI-742756, EBI-743598;
CC P08727; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-742756, EBI-11096309;
CC P08727; A2BDD9: AMOT; NbExp=3; IntAct=EBI-742756, EBI-17286414;
CC P08727; Q9Y2J4-4: AMOTL2; NbExp=3; IntAct=EBI-742756, EBI-10187270;
CC P08727; P40617: ARL4A; NbExp=3; IntAct=EBI-742756, EBI-2875746;
CC P08727; Q9Y5Z0: BACE2; NbExp=3; IntAct=EBI-742756, EBI-11282723;
CC P08727; Q9BXY8: BEX2; NbExp=3; IntAct=EBI-742756, EBI-745073;
CC P08727; Q9NX04: C1orf109; NbExp=6; IntAct=EBI-742756, EBI-8643161;
CC P08727; Q9H257: CARD9; NbExp=4; IntAct=EBI-742756, EBI-751319;
CC P08727; Q8IYE0-2: CCDC146; NbExp=3; IntAct=EBI-742756, EBI-10247802;
CC P08727; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-742756, EBI-10175300;
CC P08727; Q8IYX8-2: CEP57L1; NbExp=3; IntAct=EBI-742756, EBI-10181988;
CC P08727; P28329-3: CHAT; NbExp=3; IntAct=EBI-742756, EBI-25837549;
CC P08727; Q9BT78: COPS4; NbExp=3; IntAct=EBI-742756, EBI-742413;
CC P08727; P09172: DBH; NbExp=3; IntAct=EBI-742756, EBI-8589586;
CC P08727; P11532: DMD; NbExp=2; IntAct=EBI-742756, EBI-295827;
CC P08727; O60573: EIF4E2; NbExp=3; IntAct=EBI-742756, EBI-398610;
CC P08727; Q9NRA8: EIF4ENIF1; NbExp=3; IntAct=EBI-742756, EBI-301024;
CC P08727; Q8IYI6: EXOC8; NbExp=4; IntAct=EBI-742756, EBI-742102;
CC P08727; Q9H5Z6: FAM124B; NbExp=3; IntAct=EBI-742756, EBI-741626;
CC P08727; P22607: FGFR3; NbExp=3; IntAct=EBI-742756, EBI-348399;
CC P08727; P14136: GFAP; NbExp=9; IntAct=EBI-742756, EBI-744302;
CC P08727; Q8IVS8: GLYCTK; NbExp=3; IntAct=EBI-742756, EBI-748515;
CC P08727; P06396: GSN; NbExp=3; IntAct=EBI-742756, EBI-351506;
CC P08727; Q96CS2: HAUS1; NbExp=3; IntAct=EBI-742756, EBI-2514791;
CC P08727; O14964: HGS; NbExp=4; IntAct=EBI-742756, EBI-740220;
CC P08727; P01112: HRAS; NbExp=3; IntAct=EBI-742756, EBI-350145;
CC P08727; O43464: HTRA2; NbExp=3; IntAct=EBI-742756, EBI-517086;
CC P08727; P42858: HTT; NbExp=6; IntAct=EBI-742756, EBI-466029;
CC P08727; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-742756, EBI-747204;
CC P08727; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-742756, EBI-1055254;
CC P08727; Q9BVG8: KIFC3; NbExp=3; IntAct=EBI-742756, EBI-2125614;
CC P08727; Q92876: KLK6; NbExp=3; IntAct=EBI-742756, EBI-2432309;
CC P08727; P04264: KRT1; NbExp=3; IntAct=EBI-742756, EBI-298429;
CC P08727; P35908: KRT2; NbExp=10; IntAct=EBI-742756, EBI-1247312;
CC P08727; P12035: KRT3; NbExp=3; IntAct=EBI-742756, EBI-2430095;
CC P08727; P19013: KRT4; NbExp=3; IntAct=EBI-742756, EBI-2371606;
CC P08727; P13647: KRT5; NbExp=3; IntAct=EBI-742756, EBI-702187;
CC P08727; P02538: KRT6A; NbExp=5; IntAct=EBI-742756, EBI-702198;
CC P08727; P04259: KRT6B; NbExp=4; IntAct=EBI-742756, EBI-740907;
CC P08727; P48668: KRT6C; NbExp=3; IntAct=EBI-742756, EBI-2564105;
CC P08727; Q3SY84: KRT71; NbExp=3; IntAct=EBI-742756, EBI-2952676;
CC P08727; Q14CN4: KRT72; NbExp=3; IntAct=EBI-742756, EBI-1221280;
CC P08727; Q7RTS7: KRT74; NbExp=3; IntAct=EBI-742756, EBI-968660;
CC P08727; O95678: KRT75; NbExp=3; IntAct=EBI-742756, EBI-2949715;
CC P08727; Q7Z794: KRT77; NbExp=3; IntAct=EBI-742756, EBI-3045529;
CC P08727; Q8N1N4: KRT78; NbExp=3; IntAct=EBI-742756, EBI-1056564;
CC P08727; Q5XKE5: KRT79; NbExp=3; IntAct=EBI-742756, EBI-2514135;
CC P08727; P05787: KRT8; NbExp=3; IntAct=EBI-742756, EBI-297852;
CC P08727; Q6KB66-2: KRT80; NbExp=5; IntAct=EBI-742756, EBI-11999246;
CC P08727; Q14533: KRT81; NbExp=3; IntAct=EBI-742756, EBI-739648;
CC P08727; P78385: KRT83; NbExp=3; IntAct=EBI-742756, EBI-10221390;
CC P08727; P78386: KRT85; NbExp=3; IntAct=EBI-742756, EBI-1049371;
CC P08727; O43790: KRT86; NbExp=3; IntAct=EBI-742756, EBI-9996498;
CC P08727; Q96BZ8: LENG1; NbExp=3; IntAct=EBI-742756, EBI-726510;
CC P08727; Q8TCE9: LGALS14; NbExp=3; IntAct=EBI-742756, EBI-10274069;
CC P08727; P07196: NEFL; NbExp=3; IntAct=EBI-742756, EBI-475646;
CC P08727; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-742756, EBI-10271199;
CC P08727; Q9Y5F1: PCDHB12; NbExp=3; IntAct=EBI-742756, EBI-12012016;
CC P08727; Q16512: PKN1; NbExp=3; IntAct=EBI-742756, EBI-602382;
CC P08727; Q9UGP5-2: POLL; NbExp=3; IntAct=EBI-742756, EBI-10320765;
CC P08727; O15160: POLR1C; NbExp=3; IntAct=EBI-742756, EBI-1055079;
CC P08727; Q6NYC8: PPP1R18; NbExp=3; IntAct=EBI-742756, EBI-2557469;
CC P08727; P05129: PRKCG; NbExp=3; IntAct=EBI-742756, EBI-949799;
CC P08727; P41219: PRPH; NbExp=6; IntAct=EBI-742756, EBI-752074;
CC P08727; P25786: PSMA1; NbExp=3; IntAct=EBI-742756, EBI-359352;
CC P08727; Q9P2K3-2: RCOR3; NbExp=3; IntAct=EBI-742756, EBI-1504830;
CC P08727; Q96ES7: SGF29; NbExp=5; IntAct=EBI-742756, EBI-743117;
CC P08727; Q969G3: SMARCE1; NbExp=3; IntAct=EBI-742756, EBI-455078;
CC P08727; O95295: SNAPIN; NbExp=3; IntAct=EBI-742756, EBI-296723;
CC P08727; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-742756, EBI-742688;
CC P08727; Q9P0N9: TBC1D7; NbExp=7; IntAct=EBI-742756, EBI-3258000;
CC P08727; Q9BT92: TCHP; NbExp=3; IntAct=EBI-742756, EBI-740781;
CC P08727; P0C1Z6-2: TFPT; NbExp=3; IntAct=EBI-742756, EBI-10178002;
CC P08727; P21980: TGM2; NbExp=2; IntAct=EBI-742756, EBI-727668;
CC P08727; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-742756, EBI-10180829;
CC P08727; O76024: WFS1; NbExp=3; IntAct=EBI-742756, EBI-720609;
CC -!- TISSUE SPECIFICITY: Expressed in a defined zone of basal keratinocytes
CC in the deep outer root sheath of hair follicles. Also observed in sweat
CC gland and mammary gland ductal and secretory cells, bile ducts,
CC gastrointestinal tract, bladder urothelium, oral epithelia, esophagus,
CC ectocervical epithelium (at protein level). Expressed in epidermal
CC basal cells, in nipple epidermis and a defined region of the hair
CC follicle. Also seen in a subset of vascular wall cells in both the
CC veins and artery of human umbilical cord, and in umbilical cord
CC vascular smooth muscle. Observed in muscle fibers accumulating in the
CC costameres of myoplasm at the sarcolemma in structures that contain
CC dystrophin and spectrin. {ECO:0000269|PubMed:16000376,
CC ECO:0000269|PubMed:2468493, ECO:0000269|PubMed:2469734}.
CC -!- DEVELOPMENTAL STAGE: Present in hair follicles at all stages of
CC development. {ECO:0000269|PubMed:2469734}.
CC -!- DOMAIN: This keratin differs from all other IF proteins in lacking the
CC C-terminal tail domain.
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; J03607; AAA36044.1; -; Genomic_DNA.
DR EMBL; Y00503; CAA68556.1; -; mRNA.
DR EMBL; AF202321; AAF27048.1; -; Genomic_DNA.
DR EMBL; AK313261; BAG36071.1; -; mRNA.
DR EMBL; AC019349; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002539; AAH02539.3; -; mRNA.
DR EMBL; BC007628; AAH07628.1; -; mRNA.
DR EMBL; BC010409; AAH10409.3; -; mRNA.
DR EMBL; BC067744; AAH67744.2; -; mRNA.
DR EMBL; BC084574; AAH84574.2; -; mRNA.
DR EMBL; AB045973; BAB40770.1; -; Genomic_DNA.
DR EMBL; AB041267; BAA94607.1; -; mRNA.
DR CCDS; CCDS11399.1; -.
DR PIR; A31370; KRHU9.
DR RefSeq; NP_002267.2; NM_002276.4.
DR AlphaFoldDB; P08727; -.
DR SMR; P08727; -.
DR BioGRID; 110078; 253.
DR DIP; DIP-35655N; -.
DR IntAct; P08727; 96.
DR MINT; P08727; -.
DR STRING; 9606.ENSP00000355124; -.
DR iPTMnet; P08727; -.
DR PhosphoSitePlus; P08727; -.
DR SwissPalm; P08727; -.
DR BioMuta; KRT19; -.
DR DMDM; 311033484; -.
DR SWISS-2DPAGE; P08727; -.
DR CPTAC; CPTAC-1522; -.
DR CPTAC; CPTAC-1523; -.
DR EPD; P08727; -.
DR jPOST; P08727; -.
DR MassIVE; P08727; -.
DR MaxQB; P08727; -.
DR PaxDb; P08727; -.
DR PeptideAtlas; P08727; -.
DR PRIDE; P08727; -.
DR ProteomicsDB; 52162; -.
DR ABCD; P08727; 1 sequenced antibody.
DR Antibodypedia; 1224; 3385 antibodies from 56 providers.
DR DNASU; 3880; -.
DR Ensembl; ENST00000361566.7; ENSP00000355124.3; ENSG00000171345.13.
DR GeneID; 3880; -.
DR KEGG; hsa:3880; -.
DR MANE-Select; ENST00000361566.7; ENSP00000355124.3; NM_002276.5; NP_002267.2.
DR UCSC; uc002hxd.5; human.
DR CTD; 3880; -.
DR DisGeNET; 3880; -.
DR GeneCards; KRT19; -.
DR HGNC; HGNC:6436; KRT19.
DR HPA; ENSG00000171345; Tissue enhanced (esophagus, intestine, salivary gland, urinary bladder).
DR MIM; 148020; gene.
DR neXtProt; NX_P08727; -.
DR OpenTargets; ENSG00000171345; -.
DR PharmGKB; PA30225; -.
DR VEuPathDB; HostDB:ENSG00000171345; -.
DR eggNOG; ENOG502QV0B; Eukaryota.
DR GeneTree; ENSGT00940000155258; -.
DR HOGENOM; CLU_012560_8_1_1; -.
DR InParanoid; P08727; -.
DR OMA; QEYLLLM; -.
DR OrthoDB; 798081at2759; -.
DR PhylomeDB; P08727; -.
DR TreeFam; TF332742; -.
DR PathwayCommons; P08727; -.
DR Reactome; R-HSA-6805567; Keratinization.
DR Reactome; R-HSA-6809371; Formation of the cornified envelope.
DR SignaLink; P08727; -.
DR SIGNOR; P08727; -.
DR BioGRID-ORCS; 3880; 10 hits in 1075 CRISPR screens.
DR ChiTaRS; KRT19; human.
DR GeneWiki; Keratin_19; -.
DR GenomeRNAi; 3880; -.
DR Pharos; P08727; Tbio.
DR PRO; PR:P08727; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P08727; protein.
DR Bgee; ENSG00000171345; Expressed in palpebral conjunctiva and 160 other tissues.
DR ExpressionAtlas; P08727; baseline and differential.
DR Genevisible; P08727; HS.
DR GO; GO:0016327; C:apicolateral plasma membrane; IEA:Ensembl.
DR GO; GO:0071944; C:cell periphery; IDA:MGI.
DR GO; GO:0043034; C:costamere; 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:0005882; C:intermediate filament; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IDA:CACAO.
DR GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
DR GO; GO:1990357; C:terminal web; IEA:Ensembl.
DR GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
DR GO; GO:0008307; F:structural constituent of muscle; IDA:UniProtKB.
DR GO; GO:0060706; P:cell differentiation involved in embryonic placenta development; IEA:Ensembl.
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:0007219; P:Notch signaling pathway; IEA:Ensembl.
DR GO; GO:0043627; P:response to estrogen; IEP:UniProtKB.
DR GO; GO:0045214; P:sarcomere organization; 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 Coiled coil; Direct protein sequencing; Host-virus interaction;
KW Intermediate filament; Keratin; Methylation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..400
FT /note="Keratin, type I cytoskeletal 19"
FT /id="PRO_0000063671"
FT DOMAIN 80..391
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..79
FT /note="Head"
FT REGION 80..115
FT /note="Coil 1A"
FT REGION 116..133
FT /note="Linker 1"
FT REGION 134..225
FT /note="Coil 1B"
FT REGION 226..248
FT /note="Linker 12"
FT REGION 244..390
FT /note="Necessary for interaction with PNN"
FT /evidence="ECO:0000269|PubMed:10809736"
FT REGION 249..387
FT /note="Coil 2"
FT REGION 388..400
FT /note="Rod-like helical tail"
FT SITE 267
FT /note="Stutter"
FT SITE 327
FT /note="Stutter"
FT MOD_RES 7
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 24
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 24
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 32
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10212274"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63279"
FT MOD_RES 43
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 51
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63279"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19001"
FT MOD_RES 323
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 391
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:21049038"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 397
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 60
FT /note="A -> G (in dbSNP:rs4602)"
FT /evidence="ECO:0000269|PubMed:10623642,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:2447559, ECO:0000269|PubMed:2448790,
FT ECO:0000269|PubMed:2469734, ECO:0007744|PubMed:21269460"
FT /id="VAR_014629"
FT MUTAGEN 10
FT /note="S->A: No effect on phosphorylation; no functional
FT effect."
FT /evidence="ECO:0000269|PubMed:10212274"
FT MUTAGEN 35
FT /note="S->A: Abolishes phosphorylation; induces perinuclear
FT collapse or short cytoplasmic filaments."
FT /evidence="ECO:0000269|PubMed:10212274"
FT CONFLICT 350
FT /note="G -> A (in Ref. 1; CAA68556 and 5; AAF27048)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 400 AA; 44106 MW; C559BBBACCE32DCB CRC64;
MTSYSYRQSS ATSSFGGLGG GSVRFGPGVA FRAPSIHGGS GGRGVSVSSA RFVSSSSSGA
YGGGYGGVLT ASDGLLAGNE KLTMQNLNDR LASYLDKVRA LEAANGELEV KIRDWYQKQG
PGPSRDYSHY YTTIQDLRDK ILGATIENSR IVLQIDNARL AADDFRTKFE TEQALRMSVE
ADINGLRRVL DELTLARTDL EMQIEGLKEE LAYLKKNHEE EISTLRGQVG GQVSVEVDSA
PGTDLAKILS DMRSQYEVMA EQNRKDAEAW FTSRTEELNR EVAGHTEQLQ MSRSEVTDLR
RTLQGLEIEL QSQLSMKAAL EDTLAETEAR FGAQLAHIQA LISGIEAQLG DVRADSERQN
QEYQRLMDIK SRLEQEIATY RSLLEGQEDH YNNLSASKVL
