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P05783

- K1C18_HUMAN

UniProt

P05783 - K1C18_HUMAN

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
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    • History
      Entry version 169 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    3. scaffold protein binding Source: BHF-UCL
    4. 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

    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. centriolar satellite Source: BHF-UCL
    2. cytoplasm Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt
    4. intermediate filament Source: BHF-UCL
    5. keratin filament Source: UniProtKB
    6. microtubule organizing center Source: BHF-UCL
    7. nucleolus Source: UniProtKB-SubCell
    8. perinuclear region of cytoplasm Source: UniProtKB-SubCell

    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); alternate3 PublicationsCAR_000175
    Modified residuei31 – 311Phosphoserine; alternateBy similarity
    Glycosylationi31 – 311O-linked (GlcNAc); alternate3 PublicationsCAR_000193
    Modified residuei34 – 341Phosphoserine; by CDK14 Publications
    Modified residuei36 – 361Phosphotyrosine
    Modified residuei42 – 421Phosphoserine2 Publications
    Glycosylationi49 – 491O-linked (GlcNAc)3 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.
    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.
    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.

    P05783-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSFTTRSTFS TNYRSLGSVQ APSYGARPVS SAASVYAGAG GSGSRISVSR    50
    STSFRGGMGS GGLATGIAGG LAGMGGIQNE KETMQSLNDR LASYLDRVRS 100
    LETENRRLES KIREHLEKKG PQVRDWSHYF KIIEDLRAQI FANTVDNARI 150
    VLQIDNARLA ADDFRVKYET ELAMRQSVEN DIHGLRKVID DTNITRLQLE 200
    TEIEALKEEL LFMKKNHEEE VKGLQAQIAS SGLTVEVDAP KSQDLAKIMA 250
    DIRAQYDELA RKNREELDKY WSQQIEESTT VVTTQSAEVG AAETTLTELR 300
    RTVQSLEIDL DSMRNLKASL ENSLREVEAR YALQMEQLNG ILLHLESELA 350
    QTRAEGQRQA QEYEALLNIK VKLEAEIATY RRLLEDGEDF NLGDALDSSN 400
    SMQTIQKTTT RRIVDGKVVS ETNDTKVLRH 430
    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.
    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.
    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

    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 1, 2014
    This is version 169 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

    Dasty 3