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 29-MAY-2024, entry version 227. 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; Q9NX04: AIRIM; NbExp=6; IntAct=EBI-742756, EBI-8643161; 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; 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}. 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; 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; 270. DR DIP; DIP-35655N; -. DR IntAct; P08727; 101. DR MINT; P08727; -. DR STRING; 9606.ENSP00000355124; -. DR GlyGen; P08727; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; P08727; -. DR PhosphoSitePlus; P08727; -. DR SwissPalm; P08727; -. DR BioMuta; KRT19; -. DR DMDM; 311033484; -. DR CPTAC; CPTAC-1522; -. DR CPTAC; CPTAC-1523; -. DR EPD; P08727; -. DR jPOST; P08727; -. DR MassIVE; P08727; -. DR MaxQB; P08727; -. DR PaxDb; 9606-ENSP00000355124; -. DR PeptideAtlas; P08727; -. DR PRIDE; P08727; -. DR ProteomicsDB; 52162; -. DR ABCD; P08727; 1 sequenced antibody. DR Antibodypedia; 1224; 3767 antibodies from 57 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 AGR; HGNC:6436; -. DR CTD; 3880; -. DR DisGeNET; 3880; -. DR GeneCards; KRT19; -. DR HGNC; HGNC:6436; KRT19. DR HPA; ENSG00000171345; Tissue enhanced (esophagus, salivary gland). 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; YWATIND; -. DR OrthoDB; 4640531at2759; -. 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 1151 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 162 other cell types or tissues. DR ExpressionAtlas; P08727; baseline and differential. 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 Gene3D; 1.20.5.170; -; 1. DR Gene3D; 1.20.5.500; Single helix bin; 1. DR Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1. DR InterPro; IPR018039; IF_conserved. DR InterPro; IPR039008; IF_rod_dom. DR InterPro; IPR002957; Keratin_I. DR PANTHER; PTHR23239; INTERMEDIATE FILAMENT; 1. DR PANTHER; PTHR23239:SF14; KERATIN, TYPE I CYTOSKELETAL 19; 1. DR Pfam; PF00038; Filament; 1. DR PRINTS; PR01248; TYPE1KERATIN. DR SMART; SM01391; Filament; 1. DR SUPFAM; SSF64593; Intermediate filament protein, coiled coil region; 2. DR SUPFAM; SSF46579; Prefoldin; 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 //