Keratin, type I cytoskeletal 18 - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P05783 (K1C18_HUMAN)

Last modified July 7, 2009. Version 113. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

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

Gene names

Name:	KRT18
Synonyms:	CYK18
ORF Names:	PIG46

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

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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.

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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.
Subunit structure	Heterotetramer of two type I and two type II keratins. Keratin-18 associates with keratin-8. 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.
Subcellular location	Cytoplasm › perinuclear region. Ref.22 Ref.25
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.27
Induction	By IL-6. Ref.27
Post-translational modification	Phosphorylation at Ser-34 increases during mitosis. Hyperphosphorylated at Ser-53 in diseased cirrhosis liver. Phosphorylation increases by IL-6. Ref.25 Ref.27 Ref.11 Ref.14 Ref.16 Ref.21 Ref.24 Ref.26 Ref.28 Ref.29 Ref.30 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-glycosylated at multiple sites; glycans consist of single N-acetylglucosamine residues. Ref.10 Ref.12
Involvement in disease	Defects in KRT18 are a cause of cryptogenic cirrhosis [MIM:215600]. Ref.32 Ref.33
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.

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Ontologies

Keywords
Biological process	Cell cycle Host-virus interaction
Cellular component	Cytoplasm Intermediate filament Keratin
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Coiled coil
PTM	Acetylation Glycoprotein Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	Golgi to plasma membrane CFTR protein transport Ref.22 Inferred from direct assay. Source: UniProtKB anatomical structure morphogenesis Ref.1 Traceable author statement. Source: ProtInc cell cycle Inferred from electronic annotation. Source: UniProtKB-KW interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of apoptosis Ref.19 Inferred from direct assay. Source: UniProtKB
Cellular component	centriolar satellite Inferred from direct assay. Source: UniProtKB keratin filament Ref.25 Inferred from direct assay. Source: UniProtKB perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein binding Ref.18 Ref.19 Ref.23 Inferred from physical interaction. Source: UniProtKB structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
CLEC3B	P05452	1	EBI-297888,EBI-1047626
DNAJB6	O75190	3	EBI-297888,EBI-1053164
KRT8	P05787	2	EBI-297888,EBI-297852
MCC	P23508	1	EBI-297888,EBI-307531
PPM1B	O75688	1	EBI-297888,EBI-1047039
TRADD	Q15628	3	EBI-297888,EBI-359215

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed

Chain

2 – 430

429

Keratin, type I cytoskeletal 18

PRO_0000063666

Regions

Region

2 – 79

Head

Region

70 – 373

304

Necessary for interaction with PNN

Region

77 – 128

Interaction with TRADD

Region

80 – 387

308

Rod

Region

80 – 115

Coil 1A

Region

116 – 132

Linker 1

Region

133 – 224

Coil 1B

Region

225 – 248

Linker 12

Region

243 – 391

149

Interaction with DNAJB6

Region

249 – 387

139

Coil 2

Region

388 – 430

Tail

Sites

Site

238 – 239

Cleavage; by caspase-3, caspase-6 or caspase-7

Site

271

Stutter

Site

331

Stutter

Amino acid modifications

Modified residue

N-acetylserine

Modified residue

Phosphoserine Ref.24

Modified residue

Phosphothreonine By similarity

Modified residue

Phosphoserine Ref.30

Modified residue

Phosphothreonine By similarity

Modified residue

Phosphotyrosine Ref.26

Modified residue

Phosphoserine Ref.28

Modified residue

Phosphoserine Ref.28

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine; by CDC2 Ref.16 Ref.21 Ref.24 Ref.30

Modified residue

Phosphotyrosine By similarity

Modified residue

Phosphoserine Ref.29 Ref.30

Modified residue

Phosphoserine; by CAMK, PKC/PRKCE and STK6 Ref.25 Ref.11 Ref.21 Ref.28 Ref.30

Modified residue

Phosphoserine Ref.28 Ref.29 Ref.30

Modified residue

302

Phosphothreonine Ref.30

Modified residue

399

Phosphoserine Ref.29 Ref.30

Modified residue

401

Phosphoserine By similarity

Modified residue

404

Phosphothreonine By similarity

Glycosylation

O-linked (GlcNAc) Ref.12

CAR_000175

Glycosylation

O-linked (GlcNAc) Ref.12

CAR_000193

Glycosylation

O-linked (GlcNAc) Ref.12

CAR_000194

Natural variations

Natural variant

103

T → A in cryptogenic cirrhosis. Ref.33

VAR_023054

Natural variant

128

H → L in cryptogenic cirrhosis; interfers with the ability to form normal filaments. Ref.32 Ref.33

VAR_003852

Natural variant

230

S → T Ref.33

VAR_023055

Natural variant

261

R → Q in cryptogenic cirrhosis. Ref.33

VAR_023056

Natural variant

340

G → R in cryptogenic cirrhosis. Ref.33

VAR_023057

Experimental info

Mutagenesis

S → A: No effect on phosphorylation; when associated with A-7 and A-10. Ref.11

Mutagenesis

S → A: No effect on phosphorylation; when associated with A-2 and A-10. Ref.11

Mutagenesis

S → A: No effect on phosphorylation; when associated with A-2 and A-7. Ref.11

Mutagenesis

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

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

S → A: No effect on phosphorylation; when associated with A-15 and A-18. Ref.11

Mutagenesis

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

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

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

S → D or E: Abolishes binding to YWHAE and YWHAZ. Ref.11 Ref.16

Mutagenesis

S → A: No effect on phosphorylation; when associated with A-44. Ref.11

Mutagenesis

S → A: No effect on phosphorylation; when associated with A-42, or with A-30; A-31 and A-51. Ref.11

Mutagenesis

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

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

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

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.16 Ref.15

Mutagenesis

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

D → E: Prevents cleavage by caspase-6 during apoptosis. Induces aggregates of keratin filaments in an altered organization. Ref.15

Sequence conflict

168

Y → H in AAH00698. Ref.5

Sequence conflict

202

E → Q in CAA31369. Ref.8

Sequence conflict

208

E → G in BAD96813. Ref.3

Sequence conflict

246

A → S in CAA31369. Ref.8

Sequence conflict

309

D → R in CAA31369. Ref.8

Sequence conflict

312

S → R in CAA31369. Ref.8

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Sequences

Sequence

Length

Mass (Da)

Tools

P05783-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 1E5604C6BCC7A17A
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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

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2434380] [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: 15489334] [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: 2454392] [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: 2434381] [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: 2422083] [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: 9150948] [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: 1371281] [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: 7523419] [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: 7538124] [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: 8522591] [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: 8609167] [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: 9298992] [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: 9524113] [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: 10809736] [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: 10954706] [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: 11684708] [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: 14756564] [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: 15368451] [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: 15529338] [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: 15731013] [Abstract] Cited for: INTERACTION WITH TCHP.
[24]	"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-7 AND SER-34, MASS SPECTROMETRY.
[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: 16424149] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-53.
[26]	"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. Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-13, MASS SPECTROMETRY.
[27]	"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: 17213200] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION, INDUCTION.
[28]	"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: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-18; SER-53 AND SER-60, MASS SPECTROMETRY. Tissue: Epithelium.
[29]	"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-42; SER-60 AND SER-399, MASS SPECTROMETRY.
[30]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-34; SER-42; SER-53; SER-60; THR-302 AND SER-399, MASS SPECTROMETRY.
[31]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[32]	"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: 9011570] [Abstract] Cited for: VARIANT CRYPTOGENIC CIRRHOSIS LEU-128.
[33]	"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: 12724528] [Abstract] Cited for: VARIANTS CRYPTOGENIC CIRRHOSIS ALA-103; LEU-128; GLN-261 AND ARG-340, VARIANT THR-230.
+	Additional computationally mapped references.

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Web resources

Human Intermediate Filament Mutation Database

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Cross-references

Sequence databases
	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. NP_954657.1.
UniGene	Hs.406013
3D structure databases
HSSP	HSSP built from PDB template 1GK7 based on UniProtKB P08670.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:633N.
IntAct	P05783. 22 interactions.
PTM databases
GlycoSuiteDB	P05783.
PhosphoSite	P05783.
2-D gel databases
SWISS-2DPAGE	P05783.
PMMA-2DPAGE	P05783.
Siena-2DPAGE	P05783.
Proteomic databases
PRIDE	P05783.
Genome annotation databases
Ensembl	ENSG00000111057. Homo sapiens. [Contig view]
GeneID	3875.
KEGG	hsa:3875.
UCSC	uc001sbe.1. human.
Organism-specific databases
GeneCards	GC12P051632.
H-InvDB	HIX0010657. HIX0029655. HIX0030618. HIX0040371. HIX0056530. HIX0056886. HIX0058984.
HGNC	HGNC:6430. KRT18.
HPA	CAB000008. CAB000030. CAB000092. HPA001605.
MIM	148070. gene. 215600. phenotype.
PharmGKB	PA30217.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	P05783.
OMA	P05783. KGLQNQI.
Enzyme and pathway databases
Pathway_Interaction_DB	caspase_pathway. Caspase cascade in apoptosis.
Gene expression databases
CleanEx	HS_KRT18.
GermOnline	ENSG00000111057. Homo sapiens.
Family and domain databases
InterPro	IPR016044. F. IPR001664. IF. IPR018039. Intermediate_filament_CS. IPR002957. Keratin_I. [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	15217.
PMAP-CutDB	P05783.
SOURCE	Search...

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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:	July 7, 2009
This is version 113 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents