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P05783

- K1C18_HUMAN

UniProt

P05783 - K1C18_HUMAN

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Protein

Keratin, type I cytoskeletal 18

Gene

KRT18

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.By similarity7 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei238 – 2392Cleavage; by caspase-3, caspase-6 or caspase-7
Sitei271 – 2711Stutter
Sitei331 – 3311Stutter

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. scaffold protein binding Source: BHF-UCL
  3. structural molecule activity Source: InterPro

GO - Biological processi

  1. anatomical structure morphogenesis Source: ProtInc
  2. cell cycle Source: UniProtKB-KW
  3. extrinsic apoptotic signaling pathway Source: Ensembl
  4. Golgi to plasma membrane CFTR protein transport Source: UniProtKB
  5. hepatocyte apoptotic process Source: Ensembl
  6. intermediate filament cytoskeleton organization Source: UniProt
  7. negative regulation of apoptotic process Source: UniProtKB
  8. tumor necrosis factor-mediated signaling pathway Source: Ensembl
  9. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Host-virus interaction

Enzyme and pathway databases

SignaLinkiP05783.

Names & Taxonomyi

Protein namesi
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 namesi
Name:KRT18
Synonyms:CYK18
ORF Names:PIG46
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:6430. KRT18.

Subcellular locationi

GO - Cellular componenti

  1. cell periphery Source: Ensembl
  2. centriolar satellite Source: BHF-UCL
  3. cytoplasm Source: UniProtKB
  4. extracellular vesicular exosome Source: UniProt
  5. intermediate filament Source: BHF-UCL
  6. keratin filament Source: UniProtKB
  7. microtubule organizing center Source: BHF-UCL
  8. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Intermediate filament, Keratin, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti103 – 1031T → A in CIRRH. 1 Publication
Corresponds to variant rs61136606 [ dbSNP | Ensembl ].
VAR_023054
Natural varianti128 – 1281H → L in CIRRH; interfers with the ability to form normal filaments. 2 Publications
Corresponds to variant rs57758506 [ dbSNP | Ensembl ].
VAR_003852
Natural varianti261 – 2611R → Q in CIRRH. 1 Publication
VAR_023056
Natural varianti340 – 3401G → R in CIRRH. 1 Publication
VAR_023057

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2 – 21S → A: No effect on phosphorylation; when associated with A-7 and A-10. 1 Publication
Mutagenesisi7 – 71S → A: No effect on phosphorylation; when associated with A-2 and A-10. 1 Publication
Mutagenesisi10 – 101S → A: No effect on phosphorylation; when associated with A-2 and A-7. 1 Publication
Mutagenesisi15 – 151S → 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. 1 Publication
Mutagenesisi18 – 181S → 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. 1 Publication
Mutagenesisi23 – 231S → A: No effect on phosphorylation; when associated with A-15 and A-18. 1 Publication
Mutagenesisi30 – 301S → 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. 2 Publications
Mutagenesisi31 – 311S → 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. 2 Publications
Mutagenesisi34 – 341S → 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. 2 Publications
Mutagenesisi34 – 341S → D or E: Abolishes binding to YWHAE and YWHAZ. 2 Publications
Mutagenesisi42 – 421S → A: No effect on phosphorylation; when associated with A-44. 1 Publication
Mutagenesisi44 – 441S → A: No effect on phosphorylation; when associated with A-42, or with A-30; A-31 and A-51. 1 Publication
Mutagenesisi47 – 471S → 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. 1 Publication
Mutagenesisi49 – 491S → 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. 2 Publications
Mutagenesisi51 – 511S → 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. 1 Publication
Mutagenesisi53 – 531S → 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. 3 Publications
Mutagenesisi90 – 901R → C or H in transgenic mice, induces marked disruption of liver and pancreas keratin filament network. Increases phosphorylation and glycosylation. 1 Publication
Mutagenesisi238 – 2381D → E: Prevents cleavage by caspase-6 during apoptosis. Induces aggregates of keratin filaments in an altered organization. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi215600. phenotype.
PharmGKBiPA30217.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 430429Keratin, type I cytoskeletal 18PRO_0000063666Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei7 – 71Phosphoserine1 Publication
Modified residuei10 – 101Phosphoserine1 Publication
Modified residuei15 – 151Phosphoserine2 Publications
Modified residuei18 – 181PhosphoserineBy similarity
Modified residuei30 – 301Phosphoserine; alternateBy similarity
Glycosylationi30 – 301O-linked (GlcNAc); alternate2 PublicationsCAR_000175
Modified residuei31 – 311Phosphoserine; alternateBy similarity
Glycosylationi31 – 311O-linked (GlcNAc); alternate2 PublicationsCAR_000193
Modified residuei34 – 341Phosphoserine; by CDK14 Publications
Modified residuei36 – 361Phosphotyrosine
Modified residuei42 – 421Phosphoserine2 Publications
Glycosylationi49 – 491O-linked (GlcNAc)2 PublicationsCAR_000194
Modified residuei51 – 511Phosphoserine; by MAPKAPK2 and MAPKAPK3Curated
Modified residuei53 – 531Phosphoserine; by CAMK, PKC/PRKCE and AURKA3 Publications
Modified residuei60 – 601Phosphoserine3 Publications
Modified residuei65 – 651Phosphothreonine1 Publication
Modified residuei100 – 1001Phosphoserine1 Publication
Modified residuei131 – 1311N6-acetyllysine1 Publication
Modified residuei177 – 1771Phosphoserine1 Publication
Modified residuei302 – 3021Phosphothreonine1 Publication
Modified residuei319 – 3191Phosphoserine1 Publication
Modified residuei323 – 3231PhosphoserineBy similarity
Modified residuei399 – 3991Phosphoserine2 Publications
Modified residuei404 – 4041Phosphothreonine1 Publication
Modified residuei426 – 4261N6-acetyllysine1 Publication

Post-translational modificationi

Phosphorylation at Ser-34 increases during mitosis. Hyperphosphorylated at Ser-53 in diseased cirrhosis liver. Phosphorylation increases by IL-6.10 Publications
Proteolytically cleaved by caspases during epithelial cell apoptosis. Cleavage occurs at Asp-238 by either caspase-3, caspase-6 or caspase-7.1 Publication
O-GlcNAcylation increases solubility, and decreases stability by inducing proteasomal degradation.

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP05783.
PaxDbiP05783.
PRIDEiP05783.

2D gel databases

SWISS-2DPAGEP05783.

PTM databases

PhosphoSiteiP05783.
UniCarbKBiP05783.

Miscellaneous databases

PMAP-CutDBP05783.

Expressioni

Tissue specificityi

Expressed in colon, placenta, liver and very weakly in exocervix. Increased expression observed in lymph nodes of breast carcinoma.4 Publications

Inductioni

By IL6/interleukin-6.1 Publication

Gene expression databases

BgeeiP05783.
CleanExiHS_KRT18.
ExpressionAtlasiP05783. baseline and differential.
GenevestigatoriP05783.

Organism-specific databases

HPAiCAB000008.
CAB000030.
HPA001605.

Interactioni

Subunit structurei

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.By similarity7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DNAJB6O751906EBI-297888,EBI-1053164
IKBKGQ9Y6K93EBI-297888,EBI-81279
KRT8P0578710EBI-297888,EBI-297852
PKP1Q13835-24EBI-297888,EBI-9087684
TRADDQ1562811EBI-297888,EBI-359215

Protein-protein interaction databases

BioGridi110073. 81 interactions.
DIPiDIP-633N.
IntActiP05783. 51 interactions.
MINTiMINT-215967.
STRINGi9606.ENSP00000373487.

Structurei

3D structure databases

ProteinModelPortaliP05783.
SMRiP05783. Positions 129-228, 297-385.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 7978HeadAdd
BLAST
Regioni70 – 373304Necessary for interaction with PNNAdd
BLAST
Regioni77 – 12852Interaction with TRADDAdd
BLAST
Regioni80 – 387308RodAdd
BLAST
Regioni80 – 11536Coil 1AAdd
BLAST
Regioni116 – 13217Linker 1Add
BLAST
Regioni133 – 22492Coil 1BAdd
BLAST
Regioni225 – 24824Linker 12Add
BLAST
Regioni243 – 391149Interaction with DNAJB6Add
BLAST
Regioni249 – 387139Coil 2Add
BLAST
Regioni388 – 43043TailAdd
BLAST

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG150427.
GeneTreeiENSGT00760000119046.
HOGENOMiHOG000230975.
HOVERGENiHBG013015.
InParanoidiP05783.
KOiK07604.
OMAiRAKYEKM.
PhylomeDBiP05783.
TreeFamiTF332742.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR027695. Keratin-18.
IPR002957. Keratin_I.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PTHR23239:SF35. PTHR23239:SF35. 1 hit.
PfamiPF00038. Filament. 1 hit.
[Graphical view]
PRINTSiPR01248. TYPE1KERATIN.
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P05783 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSFTTRSTFS TNYRSLGSVQ APSYGARPVS SAASVYAGAG GSGSRISVSR
60 70 80 90 100
STSFRGGMGS GGLATGIAGG LAGMGGIQNE KETMQSLNDR LASYLDRVRS
110 120 130 140 150
LETENRRLES KIREHLEKKG PQVRDWSHYF KIIEDLRAQI FANTVDNARI
160 170 180 190 200
VLQIDNARLA ADDFRVKYET ELAMRQSVEN DIHGLRKVID DTNITRLQLE
210 220 230 240 250
TEIEALKEEL LFMKKNHEEE VKGLQAQIAS SGLTVEVDAP KSQDLAKIMA
260 270 280 290 300
DIRAQYDELA RKNREELDKY WSQQIEESTT VVTTQSAEVG AAETTLTELR
310 320 330 340 350
RTVQSLEIDL DSMRNLKASL ENSLREVEAR YALQMEQLNG ILLHLESELA
360 370 380 390 400
QTRAEGQRQA QEYEALLNIK VKLEAEIATY RRLLEDGEDF NLGDALDSSN
410 420 430
SMQTIQKTTT RRIVDGKVVS ETNDTKVLRH
Length:430
Mass (Da):48,058
Last modified:January 23, 2007 - v2
Checksum:i1E5604C6BCC7A17A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti168 – 1681Y → H in AAH00698. (PubMed:15489334)Curated
Sequence conflicti202 – 2021E → Q in CAA31369. (PubMed:2422083)Curated
Sequence conflicti208 – 2081E → G in BAD96813. 1 PublicationCurated
Sequence conflicti246 – 2461A → S in CAA31369. (PubMed:2422083)Curated
Sequence conflicti309 – 3091D → R in CAA31369. (PubMed:2422083)Curated
Sequence conflicti312 – 3121S → R in CAA31369. (PubMed:2422083)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti103 – 1031T → A in CIRRH. 1 Publication
Corresponds to variant rs61136606 [ dbSNP | Ensembl ].
VAR_023054
Natural varianti128 – 1281H → L in CIRRH; interfers with the ability to form normal filaments. 2 Publications
Corresponds to variant rs57758506 [ dbSNP | Ensembl ].
VAR_003852
Natural varianti230 – 2301S → T.1 Publication
Corresponds to variant rs58472472 [ dbSNP | Ensembl ].
VAR_023055
Natural varianti261 – 2611R → Q in CIRRH. 1 Publication
VAR_023056
Natural varianti340 – 3401G → R in CIRRH. 1 Publication
VAR_023057

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS31809.1.
PIRiS05481.
RefSeqiNP_000215.1. NM_000224.2.
NP_954657.1. NM_199187.1.
UniGeneiHs.406013.

Genome annotation databases

EnsembliENST00000388835; ENSP00000373487; ENSG00000111057.
ENST00000388837; ENSP00000373489; ENSG00000111057.
GeneIDi3875.
KEGGihsa:3875.
UCSCiuc001sbe.3. human.

Polymorphism databases

DMDMi125083.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Human Intermediate Filament Mutation Database

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS31809.1.
PIRi S05481.
RefSeqi NP_000215.1. NM_000224.2.
NP_954657.1. NM_199187.1.
UniGenei Hs.406013.

3D structure databases

ProteinModelPortali P05783.
SMRi P05783. Positions 129-228, 297-385.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110073. 81 interactions.
DIPi DIP-633N.
IntActi P05783. 51 interactions.
MINTi MINT-215967.
STRINGi 9606.ENSP00000373487.

PTM databases

PhosphoSitei P05783.
UniCarbKBi P05783.

Polymorphism databases

DMDMi 125083.

2D gel databases

SWISS-2DPAGE P05783.

Proteomic databases

MaxQBi P05783.
PaxDbi P05783.
PRIDEi P05783.

Protocols and materials databases

DNASUi 3875.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000388835 ; ENSP00000373487 ; ENSG00000111057 .
ENST00000388837 ; ENSP00000373489 ; ENSG00000111057 .
GeneIDi 3875.
KEGGi hsa:3875.
UCSCi uc001sbe.3. human.

Organism-specific databases

CTDi 3875.
GeneCardsi GC12P053343.
H-InvDB HIX0040371.
HGNCi HGNC:6430. KRT18.
HPAi CAB000008.
CAB000030.
HPA001605.
MIMi 148070. gene.
215600. phenotype.
neXtProti NX_P05783.
PharmGKBi PA30217.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG150427.
GeneTreei ENSGT00760000119046.
HOGENOMi HOG000230975.
HOVERGENi HBG013015.
InParanoidi P05783.
KOi K07604.
OMAi RAKYEKM.
PhylomeDBi P05783.
TreeFami TF332742.

Enzyme and pathway databases

SignaLinki P05783.

Miscellaneous databases

ChiTaRSi KRT18. human.
GeneWikii Keratin_18.
GenomeRNAii 3875.
NextBioi 15217.
PMAP-CutDB P05783.
PROi P05783.
SOURCEi Search...

Gene expression databases

Bgeei P05783.
CleanExi HS_KRT18.
ExpressionAtlasi P05783. baseline and differential.
Genevestigatori P05783.

Family and domain databases

InterProi IPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR027695. Keratin-18.
IPR002957. Keratin_I.
[Graphical view ]
PANTHERi PTHR23239. PTHR23239. 1 hit.
PTHR23239:SF35. PTHR23239:SF35. 1 hit.
Pfami PF00038. Filament. 1 hit.
[Graphical view ]
PRINTSi PR01248. TYPE1KERATIN.
PROSITEi PS00226. IF. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2.
  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. 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. 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. 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.

Entry informationi

Entry nameiK1C18_HUMAN
AccessioniPrimary (citable) accession number: P05783
Secondary accession number(s): Q53G38, Q5U0N8, Q9BW26
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 170 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Miscellaneous

There are two types of cytoskeletal and microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

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