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P05787

- K2C8_HUMAN

UniProt

P05787 - K2C8_HUMAN

Protein

Keratin, type II cytoskeletal 8

Gene

KRT8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 180 (01 Oct 2014)
      Sequence version 7 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Together with KRT19, helps to link the contractile apparatus to dystrophin at the costameres of striated muscle.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei342 – 3421Stutter

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. scaffold protein binding Source: BHF-UCL
    3. structural molecule activity Source: InterPro

    GO - Biological processi

    1. cell differentiation involved in embryonic placenta development Source: Ensembl
    2. extrinsic apoptotic signaling pathway Source: Ensembl
    3. hepatocyte apoptotic process Source: Ensembl
    4. response to hydrostatic pressure Source: Ensembl
    5. response to other organism Source: Ensembl
    6. sarcomere organization Source: Ensembl
    7. tumor necrosis factor-mediated signaling pathway Source: Ensembl
    8. viral process Source: UniProtKB-KW

    Keywords - Biological processi

    Host-virus interaction

    Enzyme and pathway databases

    SignaLinkiP05787.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Keratin, type II cytoskeletal 8
    Alternative name(s):
    Cytokeratin-8
    Short name:
    CK-8
    Keratin-8
    Short name:
    K8
    Type-II keratin Kb8
    Gene namesi
    Name:KRT8
    Synonyms:CYK8
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:6446. KRT8.

    Subcellular locationi

    Cytoplasm 2 Publications. Nucleusnucleoplasm By similarity. Nucleus matrix By similarity

    GO - Cellular componenti

    1. costamere Source: Ensembl
    2. cytoplasm Source: UniProtKB
    3. dystrophin-associated glycoprotein complex Source: Ensembl
    4. extracellular vesicular exosome Source: UniProt
    5. intermediate filament Source: BHF-UCL
    6. keratin filament Source: Ensembl
    7. nuclear matrix Source: UniProtKB-SubCell
    8. nucleoplasm Source: UniProtKB-SubCell
    9. nucleus Source: UniProt
    10. sarcolemma Source: Ensembl
    11. Z disc Source: Ensembl

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti53 – 531G → V in CIRRH. 1 Publication
    Corresponds to variant rs61710484 [ dbSNP | Ensembl ].
    VAR_023058
    Natural varianti54 – 541Y → C in CIRRH. 1 Publication
    VAR_023059
    Natural varianti62 – 621G → C in CIRRH. 2 Publications
    Corresponds to variant rs11554495 [ dbSNP | Ensembl ].
    VAR_023060

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi72 – 721L → P: Increases phosphorylation. 1 Publication
    Mutagenesisi74 – 741S → A: Generates normal-appearing filaments, that remain stable after okadaic acid treatment. 1 Publication
    Mutagenesisi74 – 741S → D: Generates normal-appearing filaments, that are destabilized by okadaic acid. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi215600. phenotype.
    PharmGKBiPA30234.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 483483Keratin, type II cytoskeletal 8PRO_0000063740Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei9 – 91Phosphoserine; by PKC/PRKCE1 Publication
    Modified residuei13 – 131PhosphoserineBy similarity
    Modified residuei21 – 211Phosphoserine1 Publication
    Modified residuei24 – 241Phosphoserine; by PKC/PRKCE4 Publications
    Modified residuei27 – 271Phosphoserine1 Publication
    Modified residuei34 – 341Phosphoserine2 Publications
    Modified residuei36 – 361Phosphoserine1 Publication
    Modified residuei37 – 371Phosphoserine2 Publications
    Modified residuei43 – 431Phosphoserine2 Publications
    Modified residuei74 – 741Phosphoserine; by MAPK2 Publications
    Modified residuei101 – 1011N6-malonyllysine1 Publication
    Modified residuei117 – 1171N6-acetyllysine1 Publication
    Modified residuei207 – 2071N6-acetyllysine1 Publication
    Modified residuei253 – 2531Phosphoserine5 Publications
    Modified residuei258 – 2581Phosphoserine3 Publications
    Modified residuei295 – 2951N6-acetyllysine1 Publication
    Modified residuei325 – 3251N6-acetyllysine1 Publication
    Modified residuei330 – 3301Phosphoserine1 Publication
    Modified residuei347 – 3471N6-acetyllysine1 Publication
    Modified residuei400 – 4001Phosphoserine1 Publication
    Modified residuei410 – 4101Phosphoserine1 Publication
    Modified residuei417 – 4171PhosphoserineBy similarity
    Modified residuei424 – 4241PhosphoserineBy similarity
    Modified residuei432 – 4321Phosphoserine; by CaMK2 and MAPK2 Publications
    Modified residuei475 – 4751Phosphoserine2 Publications
    Modified residuei478 – 4781Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylation on serine residues is enhanced during EGF stimulation and mitosis. Ser-74 phosphorylation plays an important role in keratin filament reorganization.10 Publications
    O-glycosylated. O-GlcNAcylation at multiple sites increases solubility, and decreases stability by inducing proteasomal degradation.
    O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner.

    Keywords - PTMi

    Acetylation, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP05787.
    PaxDbiP05787.
    PeptideAtlasiP05787.
    PRIDEiP05787.

    2D gel databases

    SWISS-2DPAGEP05787.

    PTM databases

    PhosphoSiteiP05787.
    UniCarbKBiP05787.

    Miscellaneous databases

    PMAP-CutDBP05787.

    Expressioni

    Tissue specificityi

    Observed in muscle fibers accumulating in the costameres of myoplasm at the sarcolemma membrane in structures that contain dystrophin and spectrin. Expressed in gingival mucosa and hard palate of the oral cavity.2 Publications

    Gene expression databases

    BgeeiP05787.
    GenevestigatoriP05787.

    Organism-specific databases

    HPAiCAB000131.
    CAB001696.
    HPA049866.

    Interactioni

    Subunit structurei

    Heterotetramer of two type I and two type II keratins. KRT8 associates with KRT18. Associates with KRT20. Interacts with HCV core protein and PNN. When associated with KRT19, interacts with DMD. Interacts with TCHP. Interacts with APEX1. Interacts with GPER1.8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CFTRP135697EBI-297852,EBI-349854
    GRB2P629933EBI-297852,EBI-401755
    IKBKGQ9Y6K92EBI-297852,EBI-81279
    KRT18P0578310EBI-297852,EBI-297888
    PKP1Q13835-23EBI-297852,EBI-9087684

    Protein-protein interaction databases

    BioGridi110054. 48 interactions.
    DIPiDIP-424N.
    IntActiP05787. 25 interactions.
    MINTiMINT-256526.

    Structurei

    3D structure databases

    ProteinModelPortaliP05787.
    SMRiP05787. Positions 88-239, 303-397.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 9090HeadAdd
    BLAST
    Regioni91 – 398308RodAdd
    BLAST
    Regioni91 – 12636Coil 1AAdd
    BLAST
    Regioni127 – 14317Linker 1Add
    BLAST
    Regioni144 – 23592Coil 1BAdd
    BLAST
    Regioni236 – 25924Linker 12Add
    BLAST
    Regioni260 – 398139Coil 2Add
    BLAST
    Regioni261 – 382122Necessary for interaction with PNNAdd
    BLAST
    Regioni399 – 48385TailAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi9 – 4941Ser-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the intermediate filament family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG146769.
    HOVERGENiHBG013015.
    InParanoidiP05787.
    KOiK07605.
    OMAiXRASLEA.
    OrthoDBiEOG7FV3Q8.
    PhylomeDBiP05787.
    TreeFamiTF317854.

    Family and domain databases

    InterProiIPR001664. IF.
    IPR018039. Intermediate_filament_CS.
    IPR003054. Keratin_II.
    IPR009053. Prefoldin.
    [Graphical view]
    PANTHERiPTHR23239. PTHR23239. 1 hit.
    PfamiPF00038. Filament. 1 hit.
    [Graphical view]
    PRINTSiPR01276. TYPE2KERATIN.
    SUPFAMiSSF46579. SSF46579. 1 hit.
    PROSITEiPS00226. IF. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P05787-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSIRVTQKSY KVSTSGPRAF SSRSYTSGPG SRISSSSFSR VGSSNFRGGL    50
    GGGYGGASGM GGITAVTVNQ SLLSPLVLEV DPNIQAVRTQ EKEQIKTLNN 100
    KFASFIDKVR FLEQQNKMLE TKWSLLQQQK TARSNMDNMF ESYINNLRRQ 150
    LETLGQEKLK LEAELGNMQG LVEDFKNKYE DEINKRTEME NEFVLIKKDV 200
    DEAYMNKVEL ESRLEGLTDE INFLRQLYEE EIRELQSQIS DTSVVLSMDN 250
    SRSLDMDSII AEVKAQYEDI ANRSRAEAES MYQIKYEELQ SLAGKHGDDL 300
    RRTKTEISEM NRNISRLQAE IEGLKGQRAS LEAAIADAEQ RGELAIKDAN 350
    AKLSELEAAL QRAKQDMARQ LREYQELMNV KLALDIEIAT YRKLLEGEES 400
    RLESGMQNMS IHTKTTSGYA GGLSSAYGGL TSPGLSYSLG SSFGSGAGSS 450
    SFSRTSSSRA VVVKKIETRD GKLVSESSDV LPK 483
    Length:483
    Mass (Da):53,704
    Last modified:January 23, 2007 - v7
    Checksum:iB0BC730B65929D37
    GO
    Isoform 2 (identifier: P05787-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MNGVSWSQDLQEGISAWFGPPASTPASTM

    Note: No experimental confirmation available.

    Show »
    Length:511
    Mass (Da):56,608
    Checksum:iDB55C0367CD6C37C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti56 – 561G → V in BAF83627. (PubMed:14702039)Curated
    Sequence conflicti77 – 771V → S in AAA35748. (PubMed:1692965)Curated
    Sequence conflicti201 – 2011D → DVD in CAA52882. (PubMed:1705144)Curated
    Sequence conflicti232 – 2321I → L in CAA67203. (PubMed:2434381)Curated
    Sequence conflicti257 – 2571D → E in AAA35748. (PubMed:1692965)Curated
    Sequence conflicti310 – 3101M → I in CAA31376. (PubMed:2434381)Curated
    Sequence conflicti324 – 3241L → F in BAD96661. 1 PublicationCurated
    Sequence conflicti384 – 3841L → M in CAA67203. (PubMed:2434381)Curated
    Sequence conflicti387 – 3871E → D in AAA35748. (PubMed:1692965)Curated
    Sequence conflicti401 – 4011R → P in AAA35748. (PubMed:1692965)Curated
    Sequence conflicti430 – 4334LTSP → SQA in AAA35763. (PubMed:1691124)Curated
    Sequence conflicti431 – 4311T → A in CAA67203. (PubMed:2434381)Curated
    Sequence conflicti432 – 4321S → D in AAA35748. (PubMed:1692965)Curated
    Sequence conflicti432 – 4321S → D in CAA67203. (PubMed:2434381)Curated
    Sequence conflicti432 – 4321S → D in CAA31376. (PubMed:2434381)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti53 – 531G → V in CIRRH. 1 Publication
    Corresponds to variant rs61710484 [ dbSNP | Ensembl ].
    VAR_023058
    Natural varianti54 – 541Y → C in CIRRH. 1 Publication
    VAR_023059
    Natural varianti62 – 621G → C in CIRRH. 2 Publications
    Corresponds to variant rs11554495 [ dbSNP | Ensembl ].
    VAR_023060
    Natural varianti63 – 631I → V.1 Publication
    Corresponds to variant rs59536457 [ dbSNP | Ensembl ].
    VAR_023061
    Natural varianti401 – 4011R → W.
    Corresponds to variant rs2277330 [ dbSNP | Ensembl ].
    VAR_049805
    Natural varianti417 – 4171S → G.2 Publications
    Corresponds to variant rs1065591 [ dbSNP | Ensembl ].
    VAR_069106
    Natural varianti429 – 4291G → D.1 Publication
    Corresponds to variant rs1065648 [ dbSNP | Ensembl ].
    VAR_069107

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MNGVSWSQDLQEGISAWFGP PASTPASTM in isoform 2. 1 PublicationVSP_046000

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34482 Genomic DNA. Translation: AAA35763.1.
    M34225 mRNA. Translation: AAA35748.1.
    X74929 mRNA. Translation: CAA52882.1.
    X74981 Genomic DNA. Translation: CAA52916.1.
    U76549 mRNA. Translation: AAB18966.1.
    AK290938 mRNA. Translation: BAF83627.1.
    AK310257 mRNA. No translation available.
    AK315826 mRNA. Translation: BAF98717.1.
    AK222941 mRNA. Translation: BAD96661.1.
    AC107016 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW96653.1.
    BC000654 mRNA. Translation: AAH00654.3.
    BC063513 mRNA. Translation: AAH63513.2.
    BC073760 mRNA. Translation: AAH73760.1.
    BC075839 mRNA. Translation: AAH75839.1.
    M26512 mRNA. Translation: AAA51542.1.
    X12882 mRNA. Translation: CAA31376.1.
    X98614 mRNA. Translation: CAA67203.1.
    CCDSiCCDS58234.1. [P05787-2]
    CCDS8841.1. [P05787-1]
    PIRiA34720.
    RefSeqiNP_001243222.1. NM_001256293.1. [P05787-1]
    NP_002264.1. NM_002273.3. [P05787-1]
    UniGeneiHs.533782.
    Hs.708445.

    Genome annotation databases

    EnsembliENST00000293308; ENSP00000293308; ENSG00000170421. [P05787-1]
    ENST00000546897; ENSP00000447402; ENSG00000170421. [P05787-1]
    ENST00000552150; ENSP00000449404; ENSG00000170421. [P05787-2]
    ENST00000552551; ENSP00000447566; ENSG00000170421. [P05787-1]
    GeneIDi3856.
    KEGGihsa:3856.
    UCSCiuc001sbd.2. human. [P05787-1]

    Polymorphism databases

    DMDMi90110027.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Human Intermediate Filament Mutation Database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34482 Genomic DNA. Translation: AAA35763.1 .
    M34225 mRNA. Translation: AAA35748.1 .
    X74929 mRNA. Translation: CAA52882.1 .
    X74981 Genomic DNA. Translation: CAA52916.1 .
    U76549 mRNA. Translation: AAB18966.1 .
    AK290938 mRNA. Translation: BAF83627.1 .
    AK310257 mRNA. No translation available.
    AK315826 mRNA. Translation: BAF98717.1 .
    AK222941 mRNA. Translation: BAD96661.1 .
    AC107016 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW96653.1 .
    BC000654 mRNA. Translation: AAH00654.3 .
    BC063513 mRNA. Translation: AAH63513.2 .
    BC073760 mRNA. Translation: AAH73760.1 .
    BC075839 mRNA. Translation: AAH75839.1 .
    M26512 mRNA. Translation: AAA51542.1 .
    X12882 mRNA. Translation: CAA31376.1 .
    X98614 mRNA. Translation: CAA67203.1 .
    CCDSi CCDS58234.1. [P05787-2 ]
    CCDS8841.1. [P05787-1 ]
    PIRi A34720.
    RefSeqi NP_001243222.1. NM_001256293.1. [P05787-1 ]
    NP_002264.1. NM_002273.3. [P05787-1 ]
    UniGenei Hs.533782.
    Hs.708445.

    3D structure databases

    ProteinModelPortali P05787.
    SMRi P05787. Positions 88-239, 303-397.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110054. 48 interactions.
    DIPi DIP-424N.
    IntActi P05787. 25 interactions.
    MINTi MINT-256526.

    Chemistry

    DrugBanki DB00009. Alteplase.
    DB00029. Anistreplase.
    DB00015. Reteplase.
    DB00031. Tenecteplase.

    PTM databases

    PhosphoSitei P05787.
    UniCarbKBi P05787.

    Polymorphism databases

    DMDMi 90110027.

    2D gel databases

    SWISS-2DPAGE P05787.

    Proteomic databases

    MaxQBi P05787.
    PaxDbi P05787.
    PeptideAtlasi P05787.
    PRIDEi P05787.

    Protocols and materials databases

    DNASUi 3856.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000293308 ; ENSP00000293308 ; ENSG00000170421 . [P05787-1 ]
    ENST00000546897 ; ENSP00000447402 ; ENSG00000170421 . [P05787-1 ]
    ENST00000552150 ; ENSP00000449404 ; ENSG00000170421 . [P05787-2 ]
    ENST00000552551 ; ENSP00000447566 ; ENSG00000170421 . [P05787-1 ]
    GeneIDi 3856.
    KEGGi hsa:3856.
    UCSCi uc001sbd.2. human. [P05787-1 ]

    Organism-specific databases

    CTDi 3856.
    GeneCardsi GC12M053290.
    H-InvDB HIX0026255.
    HIX0034365.
    HIX0168895.
    HGNCi HGNC:6446. KRT8.
    HPAi CAB000131.
    CAB001696.
    HPA049866.
    MIMi 148060. gene.
    215600. phenotype.
    neXtProti NX_P05787.
    PharmGKBi PA30234.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG146769.
    HOVERGENi HBG013015.
    InParanoidi P05787.
    KOi K07605.
    OMAi XRASLEA.
    OrthoDBi EOG7FV3Q8.
    PhylomeDBi P05787.
    TreeFami TF317854.

    Enzyme and pathway databases

    SignaLinki P05787.

    Miscellaneous databases

    GeneWikii Keratin_8.
    GenomeRNAii 3856.
    NextBioi 15173.
    PMAP-CutDB P05787.
    PROi P05787.
    SOURCEi Search...

    Gene expression databases

    Bgeei P05787.
    Genevestigatori P05787.

    Family and domain databases

    InterProi IPR001664. IF.
    IPR018039. Intermediate_filament_CS.
    IPR003054. Keratin_II.
    IPR009053. Prefoldin.
    [Graphical view ]
    PANTHERi PTHR23239. PTHR23239. 1 hit.
    Pfami PF00038. Filament. 1 hit.
    [Graphical view ]
    PRINTSi PR01276. TYPE2KERATIN.
    SUPFAMi SSF46579. SSF46579. 1 hit.
    PROSITEi PS00226. IF. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Organization and sequence of the human gene encoding cytokeratin 8."
      Krauss S., Franke W.W.
      Gene 86:241-249(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLY-417.
    2. "Cloning and sequence of cDNA for human placental cytokeratin 8. Regulation of the mRNA in trophoblastic cells by cAMP."
      Yamamoto R., Kao L.C., McKnight C.E., Strauss J.F. III
      Mol. Endocrinol. 4:370-374(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Embryonic simple epithelial keratins 8 and 18: chromosomal location emphasizes difference from other keratin pairs."
      Waseem A., Alexander C.M., Steel J.B., Lane E.B.
      New Biol. 2:464-478(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
      Tissue: Placenta.
    4. "Phosphorylation of human keratin 8 in vivo at conserved head domain serine 23 and at epidermal growth factor-stimulated tail domain serine 431."
      Ku N.-O., Omary M.B.
      J. Biol. Chem. 272:7556-7564(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION AT SER-24 AND SER-432.
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Testis.
    6. 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] (ISOFORM 1).
      Tissue: Kidney.
    7. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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] (ISOFORM 1), VARIANT CYS-62.
      Tissue: Colon, Liver, Lung and Placenta.
    10. "Posttranslational regulation of keratins: degradation of mouse and human keratins 18 and 8."
      Kulesh D.A., Cecena G., Darmon Y.M., Vasseur M., Oshima R.G.
      Mol. Cell. Biol. 9:1553-1565(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-231 (ISOFORM 1).
    11. "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 205-483 (ISOFORM 1), VARIANTS GLY-417 AND ASP-429.
    12. "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.
    13. "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.
    14. "PKC epsilon-related kinase associates with and phosphorylates cytokeratin 8 and 18."
      Omary M.B., Baxter G.T., Chou C.F., Riopel C.L., Lin W.Y., Strulovici B.
      J. Cell Biol. 117:583-593(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-9 AND SER-24.
    15. "An immunohistological study of cytokeratin 20 in human and mammalian oral epithelium."
      Barrett A.W., Cort E.M., Patel P., Berkovitz B.K.B.
      Arch. Oral Biol. 45:879-887(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KRT20, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    16. "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.
    17. "The intermediate filament protein keratin 8 is a novel cytoplasmic substrate for c-Jun N-terminal kinase."
      He T., Stepulak A., Holmstrom T.H., Omary M.B., Eriksson J.E.
      J. Biol. Chem. 277:10767-10774(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-74.
    18. "Keratin 8 phosphorylation by p38 kinase regulates cellular keratin filament reorganization: modulation by a keratin 1-like disease causing mutation."
      Ku N.O., Azhar S., Omary M.B.
      J. Biol. Chem. 277:10775-10782(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-74, MUTAGENESIS OF LEU-72 AND SER-74.
    19. "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.
    20. "Specific interaction of the actin-binding domain of dystrophin with intermediate filaments containing keratin 19."
      Stone M.R., O'Neill A., Catino D., Bloch R.J.
      Mol. Biol. Cell 16:4280-4293(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, TISSUE SPECIFICITY.
    21. "Proteomic profiling of cellular proteins interacting with the hepatitis C virus core protein."
      Kang S.-M., Shin M.-J., Kim J.-H., Oh J.-W.
      Proteomics 5:2227-2237(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HCV CORE PROTEIN.
    22. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253 AND SER-330, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    23. "Keratin 20 serine 13 phosphorylation is a stress and intestinal goblet cell marker."
      Zhou Q., Cadrin M., Herrmann H., Chen C.-H., Chalkley R.J., Burlingame A.L., Omary M.B.
      J. Biol. Chem. 281:16453-16461(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KRT20.
    24. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    25. "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-253 AND SER-258, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    26. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-24; SER-27; SER-34; SER-36; SER-37; SER-43; SER-253; SER-258; SER-400; SER-410; SER-432; SER-475 AND SER-478, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    27. "APE1/Ref-1 interacts with NPM1 within nucleoli and plays a role in the rRNA quality control process."
      Vascotto C., Fantini D., Romanello M., Cesaratto L., Deganuto M., Leonardi A., Radicella J.P., Kelley M.R., D'Ambrosio C., Scaloni A., Quadrifoglio F., Tell G.
      Mol. Cell. Biol. 29:1834-1854(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH APEX1, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
    28. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. "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-117; LYS-207; LYS-295; LYS-325 AND LYS-347, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. "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.
    31. "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-475 AND SER-478, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    32. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    33. Cited for: MALONYLATION AT LYS-101.
    34. "G protein-coupled estrogen receptor 1/G protein-coupled receptor 30 localizes in the plasma membrane and traffics intracellularly on cytokeratin intermediate filaments."
      Sanden C., Broselid S., Cornmark L., Andersson K., Daszkiewicz-Nilsson J., Martensson U.E., Olde B., Leeb-Lundberg L.M.
      Mol. Pharmacol. 79:400-410(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GPER1.
    35. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-34; SER-37; SER-43; SER-253 AND SER-258, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    36. "Characterization of O-GlcNAc cycling and proteomic identification of differentially O-GlcNAcylated proteins during G1/S transition."
      Drougat L., Olivier-Van Stichelen S., Mortuaire M., Foulquier F., Lacoste A.S., Michalski J.C., Lefebvre T., Vercoutter-Edouart A.S.
      Biochim. Biophys. Acta 1820:1839-1848(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION.
    37. "Keratin 8 and 18 mutations are risk factors for developing liver disease of multiple etiologies."
      Ku N.-O., Darling J.M., Krams S.M., Esquivel C.O., Keeffe E.B., Sibley R.K., Lee Y.M., Wright T.L., Omary M.B.
      Proc. Natl. Acad. Sci. U.S.A. 100:6063-6068(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CIRRH VAL-53; CYS-54 AND CYS-62, VARIANT VAL-63.

    Entry informationi

    Entry nameiK2C8_HUMAN
    AccessioniPrimary (citable) accession number: P05787
    Secondary accession number(s): A8K4H3
    , B0AZN5, F8VXB4, Q14099, Q14716, Q14717, Q53GJ0, Q6DHW5, Q6GMY0, Q6P4C7, Q96J60
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 180 of the entry and version 7 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