P08727 (K1C19_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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.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.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Intermediate filament Keratin
Coding sequence diversity	Polymorphism
Domain	Coiled coil
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell differentiation involved in embryonic placenta development Inferred from electronic annotation. Source: Compara response to estrogen stimulus Inferred from expression pattern PubMed 10037815. Source: UniProtKB sarcomere organization Inferred from direct assay Ref.14. Source: UniProtKB virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Z disc Inferred from electronic annotation. Source: Compara cell periphery Inferred from direct assay PubMed 19185580. Source: MGI costamere Inferred from direct assay Ref.14. Source: UniProtKB dystrophin-associated glycoprotein complex Inferred from electronic annotation. Source: Compara intermediate filament Traceable author statement Ref.3. Source: ProtInc sarcolemma Inferred from electronic annotation. Source: Compara
Molecular_function	structural constituent of cytoskeleton Traceable author statement Ref.3. Source: ProtInc structural constituent of muscle Inferred from direct assay Ref.14. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DMD	P11532	2	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.12
	Modified residue	55	1	Phosphoserine By similarity
	Modified residue	58	1	Phosphoserine By similarity
	Modified residue	391	1	Phosphotyrosine Ref.15
Natural variations
	Natural variant	60	1	A → G. Ref.1 Ref.3 Ref.4 Ref.5 Ref.6 Ref.8 Ref.16 Corresponds to variant rs4602 [ dbSNP | Ensembl ].		VAR_014629
Experimental info
	Mutagenesis	10	1	S → A: No effect on phosphorylation; no functional effect. Ref.12
	Mutagenesis	35	1	S → A: Abolishes phosphorylation; induces perinuclear collapse or short cytoplasmic filaments. Ref.12
	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 [UniParc]. Last modified November 2, 2010. Version 4. Checksum: C559BBBACCE32DCB	FASTA	400	44,106
	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

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] [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. , 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. , 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]	"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, 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. 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.
IPI	IPI00479145.
PIR	KRHU9. A31370.
RefSeq	NP_002267.2. NM_002276.4.
UniGene	Hs.654568.
3D structure databases
ProteinModelPortal	P08727.
SMR	P08727. Positions 78-228, 244-386.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-35655N.
IntAct	P08727. 18 interactions.
MINT	MINT-1438883.
PTM databases
PhosphoSite	P08727.
Polymorphism databases
DMDM	311033484.
2D gel databases
SWISS-2DPAGE	P08727.
Proteomic databases
PaxDb	P08727.
PeptideAtlas	P08727.
PRIDE	P08727.
Protocols and materials databases
DNASU	3880.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000361566; ENSP00000355124; ENSG00000171345.
GeneID	3880.
KEGG	hsa:3880.
UCSC	uc002hxd.4. human.
Organism-specific databases
CTD	3880.
GeneCards	GC17M039679.
HGNC	HGNC:6436. KRT19.
HPA	CAB000031. HPA002465.
MIM	148020. gene.
neXtProt	NX_P08727.
PharmGKB	PA30225.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG148784.
HOVERGEN	HBG013015.
InParanoid	P08727.
KO	K07604.
OMA	TEQLQIS.
OrthoDB	EOG4RR6HT.
Enzyme and pathway databases
Pathway_Interaction_DB	p38alphabetadownstreampathway. Signaling mediated by p38-alpha and p38-beta.
Gene expression databases
ArrayExpress	P08727.
Bgee	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. PTHR23239. 1 hit.
Pfam	PF00038. Filament. 1 hit. [Graphical view]
PRINTS	PR01248. TYPE1KERATIN.
SUPFAM	SSF46579. Prefoldin. 1 hit.
PROSITE	PS00226. IF. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	KRT19. human.
GenomeRNAi	3880.
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:	November 2, 2010
Last modified:	May 1, 2013
This is version 143 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.