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P05783 (K1C18_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 164. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length430 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Cytoplasmperinuclear region. Nucleusnucleolus 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.37 Ref.38

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 processCell cycle
Host-virus interaction
   Cellular componentCytoplasm
Intermediate filament
Keratin
Nucleus
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainCoiled coil
   PTMAcetylation
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processGolgi to plasma membrane CFTR protein transport

Inferred from direct assay Ref.22. Source: UniProtKB

anatomical structure morphogenesis

Traceable author statement Ref.1. Source: ProtInc

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

extrinsic apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

hepatocyte apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from direct assay Ref.19. Source: UniProtKB

tumor necrosis factor-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcentriolar satellite

Inferred from direct assay PubMed 18000879. Source: BHF-UCL

cytoplasm

Inferred from direct assay Ref.25. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708. Source: UniProt

intermediate filament

Inferred from direct assay PubMed 10852826. Source: BHF-UCL

keratin filament

Inferred from direct assay Ref.25. Source: UniProtKB

microtubule organizing center

Inferred from direct assay PubMed 18000879. Source: BHF-UCL

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionpoly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

scaffold protein binding

Inferred from physical interaction PubMed 10852826. Source: BHF-UCL

structural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 430429Keratin, type I cytoskeletal 18
PRO_0000063666

Regions

Region2 – 7978Head
Region70 – 373304Necessary for interaction with PNN
Region77 – 12852Interaction with TRADD
Region80 – 387308Rod
Region80 – 11536Coil 1A
Region116 – 13217Linker 1
Region133 – 22492Coil 1B
Region225 – 24824Linker 12
Region243 – 391149Interaction with DNAJB6
Region249 – 387139Coil 2
Region388 – 43043Tail

Sites

Site238 – 2392Cleavage; by caspase-3, caspase-6 or caspase-7
Site2711Stutter
Site3311Stutter

Amino acid modifications

Modified residue21N-acetylserine
Modified residue71Phosphoserine Ref.32
Modified residue101Phosphoserine Ref.29
Modified residue151Phosphoserine Ref.27 Ref.32
Modified residue181Phosphoserine
Modified residue301Phosphoserine; alternate By similarity
Modified residue311Phosphoserine; alternate
Modified residue341Phosphoserine; by CDK1 Ref.16 Ref.21 Ref.29 Ref.32
Modified residue361Phosphotyrosine
Modified residue421Phosphoserine Ref.29 Ref.32
Modified residue511Phosphoserine; by MAPKAPK2 and MAPKAPK3 Probable
Modified residue531Phosphoserine; by CAMK, PKC/PRKCE and AURKA Ref.11 Ref.21 Ref.25
Modified residue601Phosphoserine Ref.28 Ref.29 Ref.32
Modified residue651Phosphothreonine Ref.32
Modified residue1001Phosphoserine Ref.32
Modified residue1311N6-acetyllysine Ref.30
Modified residue1771Phosphoserine Ref.32
Modified residue3021Phosphothreonine Ref.29
Modified residue3191Phosphoserine Ref.32
Modified residue3231Phosphoserine By similarity
Modified residue3991Phosphoserine Ref.29 Ref.32
Modified residue4041Phosphothreonine Ref.32
Modified residue4261N6-acetyllysine Ref.30
Glycosylation301O-linked (GlcNAc); alternate Ref.12 Ref.31
CAR_000175
Glycosylation311O-linked (GlcNAc); alternate Ref.12 Ref.31
CAR_000193
Glycosylation491O-linked (GlcNAc) Ref.12 Ref.31
CAR_000194

Natural variations

Natural variant1031T → A in CIRRH. Ref.38
Corresponds to variant rs61136606 [ dbSNP | Ensembl ].
VAR_023054
Natural variant1281H → L in CIRRH; interfers with the ability to form normal filaments. Ref.37 Ref.38
Corresponds to variant rs57758506 [ dbSNP | Ensembl ].
VAR_003852
Natural variant2301S → T. Ref.38
Corresponds to variant rs58472472 [ dbSNP | Ensembl ].
VAR_023055
Natural variant2611R → Q in CIRRH. Ref.38
VAR_023056
Natural variant3401G → R in CIRRH. Ref.38
VAR_023057

Experimental info

Mutagenesis21S → A: No effect on phosphorylation; when associated with A-7 and A-10. Ref.11
Mutagenesis71S → A: No effect on phosphorylation; when associated with A-2 and A-10. Ref.11
Mutagenesis101S → A: No effect on phosphorylation; when associated with A-2 and A-7. Ref.11
Mutagenesis151S → 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
Mutagenesis181S → 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
Mutagenesis231S → A: No effect on phosphorylation; when associated with A-15 and A-18. Ref.11
Mutagenesis301S → 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
Mutagenesis311S → 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
Mutagenesis341S → 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
Mutagenesis341S → D or E: Abolishes binding to YWHAE and YWHAZ. Ref.11 Ref.16
Mutagenesis421S → A: No effect on phosphorylation; when associated with A-44. Ref.11
Mutagenesis441S → A: No effect on phosphorylation; when associated with A-42, or with A-30; A-31 and A-51. Ref.11
Mutagenesis471S → 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
Mutagenesis491S → 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
Mutagenesis511S → 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
Mutagenesis531S → 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
Mutagenesis901R → C or H in transgenic mice, induces marked disruption of liver and pancreas keratin filament network. Increases phosphorylation and glycosylation. Ref.13
Mutagenesis2381D → E: Prevents cleavage by caspase-6 during apoptosis. Induces aggregates of keratin filaments in an altered organization. Ref.15
Sequence conflict1681Y → H in AAH00698. Ref.5
Sequence conflict2021E → Q in CAA31369. Ref.8
Sequence conflict2081E → G in BAD96813. Ref.3
Sequence conflict2461A → S in CAA31369. Ref.8
Sequence conflict3091D → R in CAA31369. Ref.8
Sequence conflict3121S → R in CAA31369. Ref.8

Sequences

Sequence LengthMass (Da)Tools
P05783 [UniParc].

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

FASTA43048,058
        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' 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] [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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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]"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].
[37]"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.
[38]"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.

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.
PIRS05481.
RefSeqNP_000215.1. NM_000224.2.
NP_954657.1. NM_199187.1.
UniGeneHs.406013.

3D structure databases

ProteinModelPortalP05783.
SMRP05783. Positions 78-228, 243-385.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110073. 79 interactions.
DIPDIP-633N.
IntActP05783. 51 interactions.
MINTMINT-215967.
STRING9606.ENSP00000373487.

PTM databases

PhosphoSiteP05783.
UniCarbKBP05783.

Polymorphism databases

DMDM125083.

2D gel databases

SWISS-2DPAGEP05783.

Proteomic databases

PaxDbP05783.
PRIDEP05783.

Protocols and materials databases

DNASU3875.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000388835; ENSP00000373487; ENSG00000111057.
ENST00000388837; ENSP00000373489; ENSG00000111057.
GeneID3875.
KEGGhsa:3875.
UCSCuc001sbe.3. human.

Organism-specific databases

CTD3875.
GeneCardsGC12P053343.
H-InvDBHIX0040371.
HGNCHGNC:6430. KRT18.
HPACAB000008.
CAB000030.
HPA001605.
MIM148070. gene.
215600. phenotype.
neXtProtNX_P05783.
PharmGKBPA30217.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG150427.
HOGENOMHOG000230975.
HOVERGENHBG013015.
InParanoidP05783.
KOK07604.
OMARAKYEKM.
PhylomeDBP05783.
TreeFamTF332742.

Enzyme and pathway databases

SignaLinkP05783.

Gene expression databases

BgeeP05783.
CleanExHS_KRT18.
GenevestigatorP05783.

Family and domain databases

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

Other

ChiTaRSKRT18. human.
GeneWikiKeratin_18.
GenomeRNAi3875.
NextBio15217.
PMAP-CutDBP05783.
PROP05783.
SOURCESearch...

Entry information

Entry nameK1C18_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 164 of the entry and version 2 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 12

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