P05783 (K1C18_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Keratin, type I cytoskeletal 18

Alternative name(s):
Cell proliferation-inducing gene 46 protein
Cytokeratin-18
Short name=CK-18
Keratin-18
Short name=K18

Gene names

Name:	KRT18
Synonyms:	CYK18
ORF Names:	PIG46

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	430 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the uptake of thrombin-antithrombin complexes by hepatic cells By similarity. When phosphorylated, plays a role in filament reorganization. Involved in the delivery of mutated CFTR to the plasma membrane. Together with KRT8, is involved in interleukin-6 (IL-6)-mediated barrier protection. Ref.11 Ref.13 Ref.15 Ref.16 Ref.22 Ref.25 Ref.26
Subunit structure	Heterotetramer of two type I and two type II keratins. KRT18 associates with KRT8. Interacts with the thrombin-antithrombin complex By similarity. Interacts with PNN, HCV core protein and mutated CFTR. Interacts with YWHAE, YWHAH and YWHAZ only when phosphorylated. Interacts with DNAJB6, TCHP and TRADD. Ref.14 Ref.16 Ref.17 Ref.18 Ref.19 Ref.22 Ref.23
Subcellular location	Cytoplasm › perinuclear region. Nucleus › nucleolus Ref.22 Ref.25 Ref.35.
Tissue specificity	Expressed in colon, placenta, liver and very weakly in exocervix. Increased expression observed in lymph nodes of breast carcinoma. Ref.1 Ref.7 Ref.8 Ref.26
Induction	By IL6/interleukin-6. Ref.26
Post-translational modification	Phosphorylation at Ser-34 increases during mitosis. Hyperphosphorylated at Ser-53 in diseased cirrhosis liver. Phosphorylation increases by IL-6. Ref.11 Ref.14 Ref.16 Ref.21 Ref.25 Ref.26 Proteolytically cleaved by caspases during epithelial cell apoptosis. Cleavage occurs at Asp-238 by either caspase-3, caspase-6 or caspase-7. Ref.15 O-GlcNAcylation increases solubility, and decreases stability by inducing proteasomal degradation.
Involvement in disease	Cirrhosis (CIRRH) [MIM:215600]: A liver disease characterized by severe panlobular liver-cell swelling with Mallory body formation, prominent pericellular fibrosis, and marked deposits of copper. Clinical features include abdomen swelling, jaundice and pulmonary hypertension. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.36 Ref.37
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	Cell cycle Host-virus interaction
Cellular component	Cytoplasm Intermediate filament Keratin Nucleus
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Coiled coil
PTM	Acetylation Glycoprotein Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	Golgi to plasma membrane CFTR protein transport Inferred from direct assay Ref.22. Source: UniProtKB anatomical structure morphogenesis Traceable author statement Ref.1. Source: ProtInc apoptotic process Inferred from electronic annotation. Source: Compara cell cycle Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of apoptotic process Inferred from direct assay Ref.19. Source: UniProtKB tumor necrosis factor-mediated signaling pathway Inferred from electronic annotation. Source: Compara virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	centriolar satellite Inferred from direct assay PubMed 18000879. Source: BHF-UCL keratin filament Inferred from direct assay Ref.25. Source: UniProtKB nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DNAJB6	O75190	6	EBI-297888,EBI-1053164
IKBKG	Q9Y6K9	3	EBI-297888,EBI-81279
KRT8	P05787	8	EBI-297888,EBI-297852
TRADD	Q15628	11	EBI-297888,EBI-359215

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 430	429	Keratin, type I cytoskeletal 18		PRO_0000063666
Regions
	Region	2 – 79	78	Head
	Region	70 – 373	304	Necessary for interaction with PNN
	Region	77 – 128	52	Interaction with TRADD
	Region	80 – 387	308	Rod
	Region	80 – 115	36	Coil 1A
	Region	116 – 132	17	Linker 1
	Region	133 – 224	92	Coil 1B
	Region	225 – 248	24	Linker 12
	Region	243 – 391	149	Interaction with DNAJB6
	Region	249 – 387	139	Coil 2
	Region	388 – 430	43	Tail
Sites
	Site	238 – 239	2	Cleavage; by caspase-3, caspase-6 or caspase-7
	Site	271	1	Stutter
	Site	331	1	Stutter
Amino acid modifications
	Modified residue	2	1	N-acetylserine
	Modified residue	7	1	Phosphoserine Ref.32
	Modified residue	8	1	Phosphothreonine By similarity
	Modified residue	10	1	Phosphoserine Ref.29
	Modified residue	11	1	Phosphothreonine By similarity
	Modified residue	15	1	Phosphoserine Ref.27 Ref.32
	Modified residue	18	1	Phosphoserine
	Modified residue	30	1	Phosphoserine By similarity
	Modified residue	31	1	Phosphoserine; alternate
	Modified residue	34	1	Phosphoserine; by CDK1 Ref.16 Ref.21 Ref.29 Ref.32
	Modified residue	36	1	Phosphotyrosine
	Modified residue	42	1	Phosphoserine Ref.29 Ref.32
	Modified residue	51	1	Phosphoserine; by MAPKAPK2 and MAPKAPK3 Probable
	Modified residue	53	1	Phosphoserine; by CAMK, PKC/PRKCE and AURKA Ref.11 Ref.21 Ref.25
	Modified residue	60	1	Phosphoserine Ref.28 Ref.29 Ref.32
	Modified residue	65	1	Phosphothreonine Ref.32
	Modified residue	100	1	Phosphoserine Ref.32
	Modified residue	131	1	N6-acetyllysine Ref.30
	Modified residue	177	1	Phosphoserine Ref.32
	Modified residue	302	1	Phosphothreonine Ref.29
	Modified residue	319	1	Phosphoserine Ref.32
	Modified residue	399	1	Phosphoserine Ref.29 Ref.32
	Modified residue	401	1	Phosphoserine By similarity
	Modified residue	404	1	Phosphothreonine Ref.32
	Modified residue	426	1	N6-acetyllysine Ref.30
	Glycosylation	30	1	O-linked (GlcNAc); alternate Ref.12 Ref.31		CAR_000175
	Glycosylation	31	1	O-linked (GlcNAc); alternate Ref.12 Ref.31		CAR_000193
	Glycosylation	49	1	O-linked (GlcNAc) Ref.12 Ref.31		CAR_000194
Natural variations
	Natural variant	103	1	T → A in CIRRH. Ref.37 Corresponds to variant rs61136606 [ dbSNP | Ensembl ].		VAR_023054
	Natural variant	128	1	H → L in CIRRH; interfers with the ability to form normal filaments. Ref.36 Ref.37 Corresponds to variant rs57758506 [ dbSNP | Ensembl ].		VAR_003852
	Natural variant	230	1	S → T. Ref.37		VAR_023055
	Natural variant	261	1	R → Q in CIRRH. Ref.37		VAR_023056
	Natural variant	340	1	G → R in CIRRH. Ref.37		VAR_023057
Experimental info
	Mutagenesis	2	1	S → A: No effect on phosphorylation; when associated with A-7 and A-10. Ref.11
	Mutagenesis	7	1	S → A: No effect on phosphorylation; when associated with A-2 and A-10. Ref.11
	Mutagenesis	10	1	S → A: No effect on phosphorylation; when associated with A-2 and A-7. Ref.11
	Mutagenesis	15	1	S → A: No effect on phosphorylation; when associated with A-18 and A-23. Abolishes phosphorylation; when associated with A-18; A-34; A-47; A-49; A-51 and A-53. Ref.11
	Mutagenesis	18	1	S → A: No effect on phosphorylation; when associated with A-15 and A-23. Abolishes phosphorylation; when associated with A-15; A-34; A-47; A-49; A-51 and A-53. Ref.11
	Mutagenesis	23	1	S → A: No effect on phosphorylation; when associated with A-15 and A-18. Ref.11
	Mutagenesis	30	1	S → A: No effect on phosphorylation; when associated with A-31 and A-34, or with A-31; A-44 and A-51. Abolishes glycosylation but does not affect binding to YWHAE and YWHAZ; when associated with A-31 and A-49. Ref.11 Ref.12
	Mutagenesis	31	1	S → A: No effect on phosphorylation; when associated with A-30 and A-34, or with A-30; A-44 and A-51. Abolishes glycosylation but does not affect binding to YWHAE and YWHAZ; when associated with A-30 and A-49. Ref.11 Ref.12
	Mutagenesis	34	1	S → A: No effect on phosphorylation; when associated with A-30 and A-31. Abolishes phosphorylation; when associated with A-15; A-18; A-47; A-49; A-51 and A-53. Abolishes binding to YWHAE and YWHAZ; and when associated with A-53. Ref.11 Ref.16
	Mutagenesis	34	1	S → D or E: Abolishes binding to YWHAE and YWHAZ. Ref.11 Ref.16
	Mutagenesis	42	1	S → A: No effect on phosphorylation; when associated with A-44. Ref.11
	Mutagenesis	44	1	S → A: No effect on phosphorylation; when associated with A-42, or with A-30; A-31 and A-51. Ref.11
	Mutagenesis	47	1	S → A: No effect on phosphorylation; when associated with A-49. Abolishes phosphorylation; when associated with A-49; A-51 and A-53, or with A-15; A-18; A-34; A-49; A-51 and A-53. Ref.11
	Mutagenesis	49	1	S → A: No effect on phosphorylation; when associated with A-47. Abolishes phosphorylation; when associated with A-47; A-51 and A-53, or with A-15; A-18; A-34; A-47; A-51 and A-53. Abolishes glycosylation but does not affect binding to YWHAE and YWHAZ; when associated with A-30 and A-31. Ref.11 Ref.12
	Mutagenesis	51	1	S → A: No effect on phosphorylation; when associated with A-30; A-31 and A-47. Abolishes phosphorylation; when associated with A-47; A-49 and A-53, or with A-15; A-18; A-34; A-47; A-49 and A-53. Ref.11
	Mutagenesis	53	1	S → A: Abolishes phosphorylation; when associated with A-47; A-49 and A-51, or with A-15; A-18; A-34; A-47; A-49 and A-51. Abolishes binding to YWHAE and YWHAZ; when associated with A-34. No effect on caspase cleavage during apoptosis. Ref.11 Ref.15 Ref.16
	Mutagenesis	90	1	R → C or H in transgenic mice, induces marked disruption of liver and pancreas keratin filament network. Increases phosphorylation and glycosylation. Ref.13
	Mutagenesis	238	1	D → E: Prevents cleavage by caspase-6 during apoptosis. Induces aggregates of keratin filaments in an altered organization. Ref.15
	Sequence conflict	168	1	Y → H in AAH00698. Ref.5
	Sequence conflict	202	1	E → Q in CAA31369. Ref.8
	Sequence conflict	208	1	E → G in BAD96813. Ref.3
	Sequence conflict	246	1	A → S in CAA31369. Ref.8
	Sequence conflict	309	1	D → R in CAA31369. Ref.8
	Sequence conflict	312	1	S → R in CAA31369. Ref.8

Sequences

	Sequence		Length	Mass (Da)
	P05783 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 1E5604C6BCC7A17A	FASTA	430	48,058
	10 20 30 40 50 60 MSFTTRSTFS TNYRSLGSVQ APSYGARPVS SAASVYAGAG GSGSRISVSR STSFRGGMGS 70 80 90 100 110 120 GGLATGIAGG LAGMGGIQNE KETMQSLNDR LASYLDRVRS LETENRRLES KIREHLEKKG 130 140 150 160 170 180 PQVRDWSHYF KIIEDLRAQI FANTVDNARI VLQIDNARLA ADDFRVKYET ELAMRQSVEN 190 200 210 220 230 240 DIHGLRKVID DTNITRLQLE TEIEALKEEL LFMKKNHEEE VKGLQAQIAS SGLTVEVDAP 250 260 270 280 290 300 KSQDLAKIMA DIRAQYDELA RKNREELDKY WSQQIEESTT VVTTQSAEVG AAETTLTELR 310 320 330 340 350 360 RTVQSLEIDL DSMRNLKASL ENSLREVEAR YALQMEQLNG ILLHLESELA QTRAEGQRQA 370 380 390 400 410 420 QEYEALLNIK VKLEAEIATY RRLLEDGEDF NLGDALDSSN SMQTIQKTTT RRIVDGKVVS 430 ETNDTKVLRH

References

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[1]	"Comparison of mouse and human keratin 18: a component of intermediate filaments expressed prior to implantation." Oshima R.G., Millan J.L., Cecena G. Differentiation 33:61-68(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Tissue: Placenta.
[2]	"Identification of a cell proliferation-inducing gene." Kim J.W. Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"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]. Tissue: Cervix, Colon, Pancreas, Placenta and Uterus.
[6]	"Cloning of the human keratin 18 gene and its expression in nonepithelial mouse cells." Kulesh D.A., Oshima R.G. Mol. Cell. Biol. 8:1540-1550(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-167.
[7]	"Cytokeratin expression in simple epithelia. III. Detection of mRNAs encoding human cytokeratins nos. 8 and 18 in normal and tumor cells by hybridization with cDNA sequences in vitro and in situ." Leube R.E., Bosch F.X., Romano V., Zimbelmann R., Hofler H., Franke W.W. Differentiation 33:69-85(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-430, TISSUE SPECIFICITY. Tissue: Vulva.
[8]	"Cytokeratin expression in simple epithelia. I. Identification of mRNA coding for human cytokeratin no. 18 by a cDNA clone." Romano V., Hatzfeld M., Magin T.M., Zimbelmann R., Franke W.W., Maier G., Ponstingl H. Differentiation 30:244-253(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 199-430, TISSUE SPECIFICITY. Tissue: Liver.
[9]	"A two-dimensional gel database of human colon carcinoma proteins." Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J. Electrophoresis 18:605-613(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE. Tissue: Colon carcinoma.
[10]	"Characterization and dynamics of O-linked glycosylation of human cytokeratin 8 and 18." Chou C.F., Smith A.J., Omary M.B. J. Biol. Chem. 267:3901-3906(1992) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION.
[11]	"Identification of the major physiologic phosphorylation site of human keratin 18: potential kinases and a role in filament reorganization." Ku N.O., Omary M.B. J. Cell Biol. 127:161-171(1994) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION AT SER-53, MUTAGENESIS OF SER-2; SER-7; SER-10; SER-15; SER-18; SER-23; SER-30; SER-31; SER-34; SER-42; SER-44; SER-47; SER-49; SER-51 AND SER-53.
[12]	"Identification and mutational analysis of the glycosylation sites of human keratin 18." Ku N.-O., Omary M.B. J. Biol. Chem. 270:11820-11827(1995) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT SER-30; SER-31 AND SER-49, MUTAGENESIS OF SER-30; SER-31 AND SER-49.
[13]	"Chronic hepatitis, hepatocyte fragility, and increased soluble phosphoglycokeratins in transgenic mice expressing a keratin 18 conserved arginine mutant." Ku N.O., Michie S., Oshima R.G., Omary M.B. J. Cell Biol. 131:1303-1314(1995) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ARG-90.
[14]	"14-3-3 proteins associate with phosphorylated simple epithelial keratins during cell cycle progression and act as a solubility cofactor." Liao J., Omary M.B. J. Cell Biol. 133:345-357(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION, INTERACTION WITH YWHAE; YWHAH AND YWHAZ.
[15]	"Caspase cleavage of keratin 18 and reorganization of intermediate filaments during epithelial cell apoptosis." Caulin C., Salvesen G.S., Oshima R.G. J. Cell Biol. 138:1379-1394(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CLEAVAGE BY CASPASES, MUTAGENESIS OF SER-53 AND ASP-238.
[16]	"Phosphorylation of human keratin 18 serine 33 regulates binding to 14-3-3 proteins." Ku N.O., Liao J., Omary M.B. EMBO J. 17:1892-1906(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH YWHAE AND YWHAZ, PHOSPHORYLATION AT SER-34, MUTAGENESIS OF SER-34 AND SER-53.
[17]	"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.
[18]	"Identification of Mrj, a DnaJ/Hsp40 family protein, as a keratin 8/18 filament regulatory protein." Izawa I., Nishizawa M., Ohtakara K., Ohtsuka K., Inada H., Inagaki M. J. Biol. Chem. 275:34521-34527(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DNAJB6.
[19]	"Keratin attenuates tumor necrosis factor-induced cytotoxicity through association with TRADD." Inada H., Izawa I., Nishizawa M., Fujita E., Kiyono T., Takahashi T., Momoi T., Inagaki M. J. Cell Biol. 155:415-426(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TRADD.
[20]	"Conformational changes in the rod domain of human keratin 8 following heterotypic association with keratin 18 and its implication for filament stability." Waseem A., Karsten U., Leigh I.M., Purkis P., Waseem N.H., Lane E.B. Biochemistry 43:1283-1295(2004) [PubMed] [Europe PMC] [Abstract] Cited for: ASSOCIATION WITH KRT8.
[21]	"Keratin 8 and 18 hyperphosphorylation is a marker of progression of human liver disease." Toivola D.M., Ku N.O., Resurreccion E.Z., Nelson D.R., Wright T.L., Omary M.B. Hepatology 40:459-466(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-34 AND SER-53.
[22]	"Global proteomic approach unmasks involvement of keratins 8 and 18 in the delivery of cystic fibrosis transmembrane conductance regulator (CFTR)/deltaF508-CFTR to the plasma membrane." Davezac N., Tondelier D., Lipecka J., Fanen P., Demaugre F., Debski J., Dadlez M., Schrattenholz A., Cahill M.A., Edelman A. Proteomics 4:3833-3844(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH MUTATED CFTR, SUBCELLULAR LOCATION.
[23]	"Identification of trichoplein, a novel keratin filament-binding protein." Nishizawa M., Izawa I., Inoko A., Hayashi Y., Nagata K., Yokoyama T., Usukura J., Inagaki M. J. Cell Sci. 118:1081-1090(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TCHP.
[24]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[25]	"Rescue of DeltaF508-CFTR (cystic fibrosis transmembrane conductance regulator) by curcumin: involvement of the keratin 18 network." Lipecka J., Norez C., Bensalem N., Baudouin-Legros M., Planelles G., Becq F., Edelman A., Davezac N. J. Pharmacol. Exp. Ther. 317:500-505(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-53.
[26]	"Interleukin-6 induces keratin expression in intestinal epithelial cells: potential role of keratin-8 in interleukin-6-induced barrier function alterations." Wang L., Srinivasan S., Theiss A.L., Merlin D., Sitaraman S.V. J. Biol. Chem. 282:8219-8227(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION, INDUCTION.
[27]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[28]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[29]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-34; SER-42; SER-60; THR-302 AND SER-399, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[30]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-131 AND LYS-426, MASS SPECTROMETRY.
[31]	"O-GlcNAcylation determines the solubility, filament organization, and stability of keratins 8 and 18." Srikanth B., Vaidya M.M., Kalraiya R.D. J. Biol. Chem. 285:34062-34071(2010) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT SER-30; SER-31 AND SER-49.
[32]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-15; SER-34; SER-42; SER-60; THR-65; SER-100; SER-177; SER-319; SER-399 AND THR-404, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[33]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[34]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[35]	"Systematic analysis of protein pools, isoforms, and modifications affecting turnover and subcellular localization." Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I. Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[36]	"Mutation of human keratin 18 in association with cryptogenic cirrhosis." Ku N.-O., Wright T.L., Terrault N.A., Gish R., Omary M.B. J. Clin. Invest. 99:19-23(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CIRRH LEU-128.
[37]	"Keratin 8 and 18 mutations are risk factors for developing liver disease of multiple etiologies." Ku N.-O., Darling J.M., Krams S.M., Esquivel C.O., Keeffe E.B., Sibley R.K., Lee Y.M., Wright T.L., Omary M.B. Proc. Natl. Acad. Sci. U.S.A. 100:6063-6068(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CIRRH ALA-103; LEU-128; GLN-261 AND ARG-340, VARIANT THR-230.
+	Additional computationally mapped references.

Web resources

Human Intermediate Filament Mutation Database

Cross-references

Sequence databases
EMBL GenBank DDBJ	X12881 mRNA. Translation: CAA31375.1. AY762101 mRNA. Translation: AAX07828.1. BT019412 mRNA. Translation: AAV38219.1. AK223093 mRNA. Translation: BAD96813.1. BC000180 mRNA. Translation: AAH00180.1. BC000698 mRNA. Translation: AAH00698.1. BC004253 mRNA. Translation: AAH04253.1. BC008636 mRNA. Translation: AAH08636.1. BC020982 mRNA. Translation: AAH20982.1. BC072017 mRNA. Translation: AAH72017.1. AF179904 Genomic DNA. Translation: AAA59461.1. X12883 mRNA. Translation: CAA31377.1. X12876 mRNA. Translation: CAA31369.1.
IPI	IPI00554788.
PIR	S05481.
RefSeq	NP_000215.1. NM_000224.2. NP_954657.1. NM_199187.1.
UniGene	Hs.406013.
3D structure databases
ProteinModelPortal	P05783.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-633N.
IntAct	P05783. 43 interactions.
MINT	MINT-215967.
STRING	9606.ENSP00000373487.
PTM databases
GlycoSuiteDB	P05783.
PhosphoSite	P05783.
Polymorphism databases
DMDM	125083.
2D gel databases
SWISS-2DPAGE	P05783.
Proteomic databases
PaxDb	P05783.
PRIDE	P05783.
Protocols and materials databases
DNASU	3875.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000388835; ENSP00000373487; ENSG00000111057. ENST00000388837; ENSP00000373489; ENSG00000111057.
GeneID	3875.
KEGG	hsa:3875.
UCSC	uc001sbe.3. human.
Organism-specific databases
CTD	3875.
GeneCards	GC12P053343.
H-InvDB	HIX0040371.
HGNC	HGNC:6430. KRT18.
HPA	CAB000008. CAB000030. HPA001605.
MIM	148070. gene. 215600. phenotype.
neXtProt	NX_P05783.
PharmGKB	PA30217.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG150427.
HOGENOM	HOG000230975.
HOVERGEN	HBG013015.
InParanoid	P05783.
KO	K07604.
OMA	KKNHEEA.
OrthoDB	EOG4RV2S1.
Enzyme and pathway databases
Pathway_Interaction_DB	caspase_pathway. Caspase cascade in apoptosis.
SignaLink	P05783.
Gene expression databases
ArrayExpress	P05783.
Bgee	P05783.
CleanEx	HS_KRT18.
Genevestigator	P05783.
GermOnline	ENSG00000111057. Homo sapiens.
Family and domain databases
InterPro	IPR016044. F. IPR001664. IF. IPR018039. Intermediate_filament_CS. IPR002957. Keratin_I. [Graphical view]
PANTHER	PTHR23239. PTHR23239. 1 hit.
Pfam	PF00038. Filament. 1 hit. [Graphical view]
PRINTS	PR01248. TYPE1KERATIN.
PROSITE	PS00226. IF. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	KRT18. human.
GenomeRNAi	3875.
NextBio	15217.
PMAP-CutDB	P05783.
SOURCE	Search...

Entry information

Entry name

K1C18_HUMAN

Accession

Primary (citable) accession number: P05783
Secondary accession number(s): Q53G38, Q5U0N8, Q9BW26

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 155 of the entry and version 2 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.