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P08727 (K1C19_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Keratin, type I cytoskeletal 19
Alternative name(s):
Cytokeratin-19
Short name=CK-19
Keratin-19
Short name=K19
Gene names
Name:KRT19
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length400 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (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. Ref.14

Subunit structure

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. Ref.13 Ref.14

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. Ref.2 Ref.4 Ref.14

Developmental stage

Present in hair follicles at all stages of development. Ref.4

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).

Sequence similarities

Belongs to the intermediate filament family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DMDP115322EBI-742756,EBI-295827

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 400400Keratin, type I cytoskeletal 19
PRO_0000063671

Regions

Region1 – 7979Head
Region80 – 387308Rod
Region80 – 11536Coil 1A
Region116 – 13318Linker 1
Region134 – 22592Coil 1B
Region226 – 24823Linker 12
Region244 – 390147Necessary for interaction with PNN
Region249 – 387139Coil 2
Region388 – 40013Rod-like helical tail

Sites

Site2671Stutter
Site3271Stutter

Amino acid modifications

Modified residue351Phosphoserine Ref.12
Modified residue3911Phosphotyrosine Ref.15

Natural variations

Natural variant601A → G. Ref.1 Ref.3 Ref.4 Ref.5 Ref.6 Ref.8 Ref.17
Corresponds to variant rs4602 [ dbSNP | Ensembl ].
VAR_014629

Experimental info

Mutagenesis101S → A: No effect on phosphorylation; no functional effect. Ref.12
Mutagenesis351S → A: Abolishes phosphorylation; induces perinuclear collapse or short cytoplasmic filaments. Ref.12
Sequence conflict3501G → A in CAA68556. Ref.1
Sequence conflict3501G → A in AAF27048. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P08727 [UniParc].

Last modified November 2, 2010. Version 4.
Checksum: C559BBBACCE32DCB

FASTA40044,106
        10         20         30         40         50         60 
MTSYSYRQSS ATSSFGGLGG GSVRFGPGVA FRAPSIHGGS GGRGVSVSSA RFVSSSSSGA 

        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 

« Hide

References

« Hide 'large scale' references
[1]"Sequence of cDNA coding for human keratin 19."
Stasiak P.C., Lane E.B.
Nucleic Acids Res. 15:10058-10058(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLY-60.
Tissue: Placenta.
[2]"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."
Bader B.L., Jahn L., Franke W.W.
Eur. J. Cell Biol. 47:300-319(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY.
[3]"Sequence of the human 40-kDa keratin reveals an unusual structure with very high sequence identity to the corresponding bovine keratin."
Eckert R.L.
Proc. Natl. Acad. Sci. U.S.A. 85:1114-1118(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLY-60.
[4]"Keratin 19: predicted amino acid sequence and broad tissue distribution suggest it evolved from keratinocyte keratins."
Stasiak P.C., Purkis P.E., Leigh I.M., Lane E.B.
J. Invest. Dermatol. 92:707-716(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, VARIANT GLY-60.
Tissue: Placenta.
[5]"Genomic organization and amplification of the human keratin 15 and 19 genes."
Whittock N.V., Eady R.A.J., McGrath J.A.
Biochem. Biophys. Res. Commun. 267:462-465(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLY-60.
[6]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLY-60.
Tissue: Placenta.
[7]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLY-60.
Tissue: Mammary gland, Pancreas and Placenta.
[9]"Cloning and characterization of the 5'-flanking region of human cytokeratin 19 gene in human cholangiocarcinoma cell line."
Kagaya M., Kaneko S., Ohno H., Inamura K., Kobayashi K.
J. Hepatol. 35:504-511(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
Tissue: Peripheral blood leukocyte.
[10]"Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-31; 151-158 AND 227-237.
Tissue: Keratinocyte.
[11]"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 micrometastasis."
Sato T., Weerasinghe A., Kuwano Y., Kaneko T., Ikeda T., Nagai T., Makino H., Sano M., Honma K., Nemoto K., Abo T., Shima Y.
Seibutsu Butsuri Kagaku 44:201-204(2000)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 145-352.
Tissue: Lymph node.
[12]"Characterization of the major physiologic phosphorylation site of human keratin 19 and its role in filament organization."
Zhou X., Liao J., Hu L., Feng L., Omary M.B.
J. Biol. Chem. 274:12861-12866(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-35, MUTAGENESIS OF SER-10 AND SER-35.
[13]"Dissection of protein linkage between keratins and pinin, a protein with dual location at desmosome-intermediate filament complex and in the nucleus."
Shi J., Sugrue S.P.
J. Biol. Chem. 275:14910-14915(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PNN.
[14]"Specific interaction of the actin-binding domain of dystrophin with intermediate filaments containing keratin 19."
Stone M.R., O'Neill A., Catino D., Bloch R.J.
Mol. Biol. Cell 16:4280-4293(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH DMD, TISSUE SPECIFICITY.
[15]"Characterization of in vivo keratin 19 phosphorylation on tyrosine-391."
Zhou Q., Snider N.T., Liao J., Li D.H., Hong A., Ku N.O., Cartwright C.A., Omary M.B.
PLoS ONE 5:E13538-E13538(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-391.
[16]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] GLY-60, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03607 Genomic DNA. Translation: AAA36044.1.
Y00503 mRNA. Translation: CAA68556.1.
AF202321 Genomic DNA. Translation: AAF27048.1.
AK313261 mRNA. Translation: BAG36071.1.
AC019349 Genomic DNA. No translation available.
BC002539 mRNA. Translation: AAH02539.3.
BC007628 mRNA. Translation: AAH07628.1.
BC010409 mRNA. Translation: AAH10409.3.
BC067744 mRNA. Translation: AAH67744.2.
BC084574 mRNA. Translation: AAH84574.2.
AB045973 Genomic DNA. Translation: BAB40770.1.
AB041267 mRNA. Translation: BAA94607.1.
PIRKRHU9. A31370.
RefSeqNP_002267.2. NM_002276.4.
UniGeneHs.654568.

3D structure databases

ProteinModelPortalP08727.
SMRP08727. Positions 78-228, 244-386.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110078. 34 interactions.
DIPDIP-35655N.
IntActP08727. 19 interactions.
MINTMINT-1438883.

PTM databases

PhosphoSiteP08727.

Polymorphism databases

DMDM311033484.

2D gel databases

SWISS-2DPAGEP08727.

Proteomic databases

PaxDbP08727.
PeptideAtlasP08727.
PRIDEP08727.

Protocols and materials databases

DNASU3880.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000361566; ENSP00000355124; ENSG00000171345.
GeneID3880.
KEGGhsa:3880.
UCSCuc002hxd.4. human.

Organism-specific databases

CTD3880.
GeneCardsGC17M039679.
HGNCHGNC:6436. KRT19.
HPACAB000031.
HPA002465.
MIM148020. gene.
neXtProtNX_P08727.
PharmGKBPA30225.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG148784.
HOVERGENHBG013015.
InParanoidP08727.
KOK07604.
OMATEQLQIS.
OrthoDBEOG7FV3Q8.
PhylomeDBP08727.
TreeFamTF332742.

Gene expression databases

BgeeP08727.
GenevestigatorP08727.

Family and domain databases

InterProIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR002957. Keratin_I.
IPR009053. Prefoldin.
[Graphical view]
PANTHERPTHR23239. PTHR23239. 1 hit.
PfamPF00038. Filament. 1 hit.
[Graphical view]
PRINTSPR01248. TYPE1KERATIN.
SUPFAMSSF46579. SSF46579. 1 hit.
PROSITEPS00226. IF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSKRT19. human.
GeneWikiKeratin_19.
GenomeRNAi3880.
NextBio15231.
PROP08727.
SOURCESearch...

Entry information

Entry nameK1C19_HUMAN
AccessionPrimary (citable) accession number: P08727
Secondary accession number(s): B2R874 expand/collapse secondary AC list , Q5XG83, Q6NW33, Q7L5M9, Q96A53, Q96FV1, Q9BYF9, Q9P1Y4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: November 2, 2010
Last modified: April 16, 2014
This is version 151 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM