Reviewed, UniProtKB/Swiss-Prot P08727 (K1C19_HUMAN)

Names and origin

Protein names

Recommended name:
    Keratin, type I cytoskeletal 19
Alternative name(s):
    Cytokeratin-19
      Short name=CK-19
    Keratin-19
      Short name=K19

Gene names

Name:

KRT19

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	400 AA.
Sequence status	Complete.
Protein existence	Evidence 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.14 Ref.12
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.14 Ref.2 Ref.4
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.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Intermediate filament Keratin
Coding sequence diversity	Polymorphism
Domain	Coiled coil
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW response to estrogen stimulus Inferred from expression pattern. Source: UniProtKB sarcomere organization Ref.14 Inferred from direct assay. Source: UniProtKB
Cellular component	costamere Ref.14 Inferred from direct assay. Source: UniProtKB intermediate filament Ref.3 Traceable author statement. Source: ProtInc
Molecular function	protein binding Ref.14 Inferred from physical interaction. Source: UniProtKB structural constituent of cytoskeleton Ref.3 Traceable author statement. Source: ProtInc structural constituent of muscle Ref.14 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DMD	P11532	1	EBI-742756,EBI-295827

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 400	400	Keratin, type I cytoskeletal 19		PRO_0000063671
Regions
	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
Sites
	Site	267	1	Stutter
	Site	327	1	Stutter
Amino acid modifications
	Modified residue	9	1	Phosphoserine By similarity
	Modified residue	13	1	Phosphoserine By similarity
	Modified residue	35	1	Phosphoserine Ref.11 Ref.13
	Modified residue	40	1	Phosphoserine Ref.16
	Modified residue	46	1	Phosphoserine Ref.13
	Modified residue	56	1	Phosphoserine By similarity
	Modified residue	58	1	Phosphoserine By similarity
	Modified residue	97	1	N6-acetyllysine Ref.18
	Modified residue	130	1	Phosphotyrosine Ref.15
Natural variations
	Natural variant	60	1	G → A: dbSNP rs4602. Ref.7		VAR_014629
Experimental info
	Mutagenesis	10	1	S → A: No effect on phosphorylation; no functional effect. Ref.11
	Mutagenesis	35	1	S → A: Abolishes phosphorylation; induces perinuclear collapse or short cytoplasmic filaments. Ref.11
	Sequence conflict	76 – 77	2	LA → H in CAA68556. Ref.1
	Sequence conflict	342	1	I → Y in CAA68556. Ref.1
	Sequence conflict	350	1	G → A in CAA68556. Ref.1
	Sequence conflict	350	1	G → A in AAF27048. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P08727-1 [UniParc]. Last modified March 7, 2006. Version 3. Checksum: 1EBF9E5EF460EAB5	FASTA	400	44,092
	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

References

	« Hide 'large scale' referencesShow '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: 2447559] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. 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: 2468493] [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: 2448790] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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: 2469734] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. 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: 10623642] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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. , 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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
[7]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-60. Tissue: Mammary gland, Pancreas and Placenta.
[8]	"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: 11682035] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9. Tissue: Peripheral blood leukocyte.
[9]	"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: 1286667] [Abstract] Cited for: PROTEIN SEQUENCE OF 25-31; 151-158 AND 227-237. Tissue: Keratinocyte.
[10]	"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." 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.
[11]	"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: 10212274] [Abstract] Cited for: PHOSPHORYLATION AT SER-35, MUTAGENESIS OF SER-10 AND SER-35.
[12]	"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: 10809736] [Abstract] Cited for: INTERACTION WITH PNN.
[13]	"Global phosphoproteome of HT-29 human colon adenocarcinoma cells." Kim J.-E., Tannenbaum S.R., White F.M. J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35 AND SER-46, MASS SPECTROMETRY.
[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: 16000376] [Abstract] Cited for: FUNCTION, INTERACTION WITH DMD, TISSUE SPECIFICITY.
[15]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." 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. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-130, MASS SPECTROMETRY.
[16]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40, MASS SPECTROMETRY.
[17]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[18]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-97, MASS SPECTROMETRY.
+	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. 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.
IPI	IPI00479145.
PIR	KRHU9. A31370.
RefSeq	NP_002267.2.
UniGene	Hs.654568
3D structure databases
SMR	P08727. Positions 78-114, 309-386.
ModBase	Search...
Protein-protein interaction databases
IntAct	P08727. 14 interactions.
STRING	P08727.
PTM databases
PhosphoSite	P08727.
2-D gel databases
SWISS-2DPAGE	P08727.
Aarhus/Ghent-2DPAGE	8216. IEF.
Proteomic databases
PeptideAtlas	P08727.
PRIDE	P08727.
Genome annotation databases
Ensembl	ENST00000361566; ENSP00000355124; ENSG00000171345; Homo sapiens. [Genome view]
GeneID	3880.
KEGG	hsa:3880.
Organism-specific databases
CTD	3880.
GeneCards	GC17M036933.
H-InvDB	HIX0013813.
HGNC	HGNC:6436. KRT19.
HPA	CAB000031. HPA002465.
MIM	148020. gene.
PharmGKB	PA30225.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG19339.
HOVERGEN	P08727.
InParanoid	P08727.
Enzyme and pathway databases
Pathway_Interaction_DB	p38alphabetadownstreampathway. Signaling mediated by p38-alpha and p38-beta.
Gene expression databases
ArrayExpress	P08727.
Genevestigator	P08727.
GermOnline	ENSG00000171345. Homo sapiens.
Family and domain databases
InterPro	IPR016044. F. IPR001664. IF. IPR018039. Intermediate_filament_CS. IPR002957. Keratin_I. IPR009053. Prefoldin. [Graphical view]
PANTHER	PTHR23239. IF. 1 hit.
Pfam	PF00038. Filament. 1 hit. [Graphical view]
PRINTS	PR01248. TYPE1KERATIN.
PROSITE	PS00226. IF. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	15231.
SOURCE	Search...

Entry information

Entry name

K1C19_HUMAN

Accession

Primary (citable) accession number: P08727
Secondary accession number(s): B2R874 , Q5XG83, Q6NW33, Q7L5M9, Q96A53, Q96FV1, Q9BYF9, Q9P1Y4

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	March 7, 2006
Last modified:	January 19, 2010
This is version 113 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.