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UniProtKB/Swiss-Prot entry P08727


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name K1C19_HUMAN
Primary accession number P08727
Secondary accession numbers B2R874 Q5XG83 Q6NW33 Q7L5M9 Q96A53 Q96FV1 Q9BYF9 Q9P1Y4
Integrated into Swiss-Prot on August 1, 1988
Sequence was last modified on March 7, 2006 (Sequence version 3)
Annotations were last modified on    May 5, 2009 (Entry version 106)
Name and origin of the protein
Protein name Keratin, type I cytoskeletal 19
Synonyms Cytokeratin-19
CK-19
Keratin-19
K19
Gene name
Name: KRT19
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
DOI=10.1093/nar/15.23.10058; PubMed=2447559 [NCBI, ExPASy, EBI, Israel, Japan]
Stasiak P.C., Lane E.B.;
"Sequence of cDNA coding for human keratin 19.";
Nucleic Acids Res. 15:10058-10058(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
PubMed=2468493 [NCBI, ExPASy, EBI, Israel, Japan]
Bader B.L., Jahn L., Franke W.W.;
"Low level expression of cytokeratins 8, 18 and 19 in vascular smooth muscle cells of human umbilical cord and in cultured cells derived therefrom, with an analysis of the chromosomal locus containing the cytokeratin 19 gene.";
Eur. J. Cell Biol. 47:300-319(1988).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1073/pnas.85.4.1114; PubMed=2448790 [NCBI, ExPASy, EBI, Israel, Japan]
Eckert R.L.;
"Sequence of the human 40-kDa keratin reveals an unusual structure with very high sequence identity to the corresponding bovine keratin.";
Proc. Natl. Acad. Sci. U.S.A. 85:1114-1118(1988).
[4]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
TISSUE=Placenta;
DOI=10.1111/1523-1747.ep12721500; PubMed=2469734 [NCBI, ExPASy, EBI, Israel, Japan]
Stasiak P.C., Purkis P.E., Leigh I.M., Lane E.B.;
"Keratin 19: predicted amino acid sequence and broad tissue distribution suggest it evolved from keratinocyte keratins.";
J. Invest. Dermatol. 92:707-716(1989).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1006/bbrc.1999.1966; PubMed=10623642 [NCBI, ExPASy, EBI, Israel, Japan]
Whittock N.V., Eady R.A.J., McGrath J.A.;
"Genomic organization and amplification of the human keratin 15 and 19 genes.";
Biochem. Biophys. Res. Commun. 267:462-465(2000).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-60.
TISSUE=Mammary gland, Pancreas, and Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
TISSUE=Peripheral blood leukocyte;
DOI=10.1016/S0168-8278(01)00167-2; PubMed=11682035 [NCBI, ExPASy, EBI, Israel, Japan]
Kagaya M., Kaneko S., Ohno H., Inamura K., Kobayashi K.;
"Cloning and characterization of the 5'-flanking region of human cytokeratin 19 gene in human cholangiocarcinoma cell line.";
J. Hepatol. 35:504-511(2001).
[9]
PROTEIN SEQUENCE OF 25-31; 151-158 AND 227-237.
TISSUE=Keratinocyte;
DOI=10.1002/elps.11501301199; PubMed=1286667 [NCBI, ExPASy, EBI, Israel, Japan]
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.;
"Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes.";
Electrophoresis 13:960-969(1992).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 145-352.
TISSUE=Lymph node;
Sato T., Weerasinghe A., Kuwano Y., Kaneko T., Ikeda T., Nagai T., Makino H., Sano M., Honma K., Nemoto K., Abo T., Shima Y.;
"Diversity of keratin 19 gene expressed in lymph nodes of breast cancer patients -- strategy to clear the discrepancy between histological findings and RT-PCR results in the detection of micrometastsis.";
Seibutsu Butsuri Kagaku 44:201-204(2000).
[11]
PHOSPHORYLATION AT SER-35, AND MUTAGENESIS OF SER-10 AND SER-35.
DOI=10.1074/jbc.274.18.12861; PubMed=10212274 [NCBI, ExPASy, EBI, Israel, Japan]
Zhou X., Liao J., Hu L., Feng L., Omary M.B.;
"Characterization of the major physiologic phosphorylation site of human keratin 19 and its role in filament organization.";
J. Biol. Chem. 274:12861-12866(1999).
[12]
INTERACTION WITH PNN.
DOI=10.1074/jbc.275.20.14910; PubMed=10809736 [NCBI, ExPASy, EBI, Israel, Japan]
Shi J., Sugrue S.P.;
"Dissection of protein linkage between keratins and pinin, a protein with dual location at desmosome-intermediate filament complex and in the nucleus.";
J. Biol. Chem. 275:14910-14915(2000).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35 AND SER-46, AND MASS SPECTROMETRY.
DOI=10.1021/pr050048h; PubMed=16083285 [NCBI, ExPASy, EBI, Israel, Japan]
Kim J.-E., Tannenbaum S.R., White F.M.;
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
J. Proteome Res. 4:1339-1346(2005).
[14]
FUNCTION, INTERACTION WITH DMD, AND TISSUE SPECIFICITY.
DOI=10.1091/mbc.E05-02-0112; PubMed=16000376 [NCBI, ExPASy, EBI, Israel, Japan]
Stone M.R., O'Neill A., Catino D., Bloch R.J.;
"Specific interaction of the actin-binding domain of dystrophin with intermediate filaments containing keratin 19.";
Mol. Biol. Cell 16:4280-4293(2005).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-130, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[17]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
Comments
  • FUNCTION: Involved in the organization of myofibers. Together with KRT8, helps to link the contractile apparatus to dystrophin at the costameres of striated muscle.
  • SUBUNIT: Heterotetramer of two type I and two type II keratins. Interacts with PNN and the actin-binding domain of DMD. Interacts with HCV core protein.
  • INTERACTION:
    P11532:DMD; NbExp=1; IntAct=EBI-742756, EBI-295827;
  • TISSUE SPECIFICITY: Expressed in a defined zone of basal keratinocytes in the deep outer root sheath of hair follicles. Also observed in sweat gland and mammary gland ductal and secretory cells, bile ducts, gastrointestinal tract, bladder urothelium, oral epithelia, esophagus, ectocervical epithelium (at protein level). Expressed in epidermal basal cells, in nipple epidermis and a defined region of the hair follicle. Also seen in a subset of vascular wall cells in both the veins and artery of human umbilical cord, and in umbilical cord vascular smooth muscle. Observed in muscle fibers accumulating in the costameres of myoplasm at the sarcolemma in structures that contain dystrophin and spectrin.
  • DEVELOPMENTAL STAGE: Present in hair follicles at all stages of development.
  • DOMAIN: This keratin differs from all other IF proteins in lacking the C-terminal tail domain.
  • MISCELLANEOUS: There are two types of cytoskeletal and microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).
  • SIMILARITY: Belongs to the intermediate filament family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
J03607; AAA36044.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y00503; CAA68556.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF202321; AAF27048.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK313261; BAG36071.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002539; AAH02539.3; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC007628; AAH07628.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC010409; AAH10409.3; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC067744; AAH67744.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC084574; AAH84574.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB045973; BAB40770.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB041267; BAA94607.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00479145; -.
PIR A31370; KRHU9.
RefSeq NP_002267.2; -.
UniGene Hs.654568
3D structure databases
HSSP P08670; 1GK7. [HSSP ENTRY / PDB]
ModBase P08727.
Protein-protein interaction databases
IntAct P08727; 14.
PTM databases
PhosphoSite P08727; -.
Enzyme and pathway databases
Pathway_Interaction_DB p38alphabetadownstreampathway; Signaling mediated by p38-alpha and p38-beta.
2D gel databases
SWISS-2DPAGE P08727; -.
Aarhus/Ghent-2DPAGE 8216; IEF.
Organism-specific databases
GeneCards GC17M036933; -.
H-InvDB HIX0013813; -.
HGNC HGNC:6436; KRT19.
GenAtlas KRT19.
HPA CAB000031; -.
HPA002465; -.
MIM 148020; gene. [NCBI / EBI]
PharmGKB PA30225; -.
Gene expression databases
ArrayExpress P08727; -.
GermOnline ENSG00000171345; Homo sapiens.
Ontologies
GO
GO:0043034; Cellular component: costamere (inferred from direct assay from UniProtKB).
GO:0005882; Cellular component: intermediate filament (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0005200; Molecular function: structural constituent of cytoskeleton (traceable author statement from ProtInc).
GO:0008307; Molecular function: structural constituent of muscle (inferred from direct assay from UniProtKB).
GO:0044419; Biological process: interspecies interaction between organisms (inferred from electronic annotation from UniProtKB-KW).
GO:0043627; Biological process: response to estrogen stimulus (inferred from expression pattern from UniProtKB).
GO:0045214; Biological process: sarcomere organization (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR016044; F.
IPR001664; IF.
IPR018039; Intermediate_filament_CS.
IPR002957; Keratin_I.
Graphical view of domain structure.
PANTHER PTHR23239; IF; 1.
Pfam PF00038; Filament; 1.
Pfam graphical view of domain structure.
PRINTS PR01248; TYPE1KERATIN.
PROSITE PS00226; IF; 1.
Proteomic databases
PeptideAtlas P08727; -.
PRIDE P08727; -.
Genome annotation databases
Ensembl ENSG00000171345; Homo sapiens. [Contig view]
GeneID 3880; -.
KEGG hsa:3880; -.
Phylogenomic databases
HOVERGEN P08727; -.
Other
NextBio 15231; -.
SOURCE KRT19; Homo sapiens.
ProtoNet P08727.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Coiled coil; Direct protein sequencing; Host-virus interaction; Intermediate filament; Keratin; Phosphoprotein; Polymorphism.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   400  400     Keratin, type I cytoskeletal 19. PRO_0000063671
REGION   1    79  79     Head. 
REGION   80   387  308     Rod. 
REGION   80   115  36     Coil 1A. 
REGION   116   133  18     Linker 1. 
REGION   134   225  92     Coil 1B. 
REGION   226   248  23     Linker 12. 
REGION   244   390  147     Necessary for interaction with PNN. 
REGION   249   387  139     Coil 2. 
REGION   388   400  13     Rod-like helical tail. 
SITE   267   267  1     Stutter. 
SITE   327   327  1     Stutter. 
MOD_RES   9     9        Phosphoserine (By similarity). 
MOD_RES   13    13        Phosphoserine (By similarity). 
MOD_RES   35    35        Phosphoserine. 
MOD_RES   40    40        Phosphoserine. 
MOD_RES   46    46        Phosphoserine. 
MOD_RES   56    56        Phosphoserine (By similarity). 
MOD_RES   58    58        Phosphoserine (By similarity). 
MOD_RES   130   130        Phosphotyrosine. 
VARIANT   60    60  1     G -> A (in dbSNP:rs4602 [NCBI]). VAR_014629 
MUTAGEN   10    10        S->A: No effect on phosphorylation; no functional effect. 
MUTAGEN   35    35        S->A: Abolishes phosphorylation; induces perinuclear collapse or short cytoplasmic filaments. 
CONFLICT   76    77        LA -> H (in Ref. 1; CAA68556). 
CONFLICT   342   342        I -> Y (in Ref. 1; CAA68556). 
CONFLICT   350   350        G -> A (in Ref. 1; CAA68556 and 5; AAF27048). 
Sequence information
Length: 400 AA [This is the length of the unprocessed precursor] Molecular weight: 44092 Da [This is the MW of the unprocessed precursor] CRC64: 1EBF9E5EF460EAB5 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTSYSYRQSS ATSSFGGLGG GSVRFGPGVA FRAPSIHGGS GGRGVSVSSA RFVSSSSSGG 

        70         80         90        100        110        120 
YGGGYGGVLT ASDGLLAGNE KLTMQNLNDR LASYLDKVRA LEAANGELEV KIRDWYQKQG 

       130        140        150        160        170        180 
PGPSRDYSHY YTTIQDLRDK ILGATIENSR IVLQIDNARL AADDFRTKFE TEQALRMSVE 

       190        200        210        220        230        240 
ADINGLRRVL DELTLARTDL EMQIEGLKEE LAYLKKNHEE EISTLRGQVG GQVSVEVDSA 

       250        260        270        280        290        300 
PGTDLAKILS DMRSQYEVMA EQNRKDAEAW FTSRTEELNR EVAGHTEQLQ MSRSEVTDLR 

       310        320        330        340        350        360 
RTLQGLEIEL QSQLSMKAAL EDTLAETEAR FGAQLAHIQA LISGIEAQLG DVRADSERQN 

       370        380        390        400 
QEYQRLMDIK SRLEQEIATY RSLLEGQEDH YNNLSASKVL 

P08727 in FASTA format

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