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Q04695

- K1C17_HUMAN

UniProt

Q04695 - K1C17_HUMAN

Protein

Keratin, type I cytoskeletal 17

Gene

KRT17

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    May play a role in the formation and maintenance of various skin appendages, specifically in determining shape and orientation of hair. May be a marker of basal cell differentiation in complex epithelia and therefore indicative of a certain type of epithelial "stem cells". May act as an autoantigen in the immunopathogenesis of psoriasis, with certain peptide regions being a major target for autoreactive T-cells and hence causing their proliferation. Required for the correct growth of hair follicles, in particular for the persistence of the anagen (growth) state. Modulates the function of TNF-alpha in the specific context of hair cycling. Regulates protein synthesis and epithelial cell growth through binding to the adapter protein SFN and by stimulating Akt/mTOR pathway. Involved in tissue repair By similarity.By similarity

    GO - Molecular functioni

    1. MHC class II protein binding Source: UniProtKB
    2. MHC class II receptor activity Source: UniProtKB
    3. protein binding Source: IntAct
    4. structural constituent of cytoskeleton Source: ProtInc

    GO - Biological processi

    1. epidermis development Source: ProtInc
    2. intermediate filament organization Source: Ensembl
    3. keratinization Source: Ensembl
    4. morphogenesis of an epithelium Source: Ensembl
    5. positive regulation of cell growth Source: Ensembl
    6. positive regulation of hair follicle development Source: Ensembl
    7. positive regulation of translation Source: Ensembl
    8. signal transduction Source: UniProtKB

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Keratin, type I cytoskeletal 17
    Alternative name(s):
    39.1
    Cytokeratin-17
    Short name:
    CK-17
    Keratin-17
    Short name:
    K17
    Gene namesi
    Name:KRT17
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:6427. KRT17.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cell periphery Source: Ensembl
    2. cytoplasm Source: UniProtKB-SubCell
    3. extracellular vesicular exosome Source: UniProt
    4. intermediate filament Source: ProtInc

    Keywords - Cellular componenti

    Cytoplasm, Intermediate filament, Keratin

    Pathology & Biotechi

    Involvement in diseasei

    Pachyonychia congenita 2 (PC2) [MIM:167210]: An autosomal dominant ectodermal dysplasia characterized by hypertrophic nail dystrophy resulting in onchyogryposis (thickening and increase in curvature of the nail), palmoplantar keratoderma and hyperhidrosis, follicular hyperkeratosis, multiple epidermal cysts, absent/sparse eyebrow and body hair, and by the presence of natal teeth.11 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti88 – 881M → T in PC2 and SM. 2 Publications
    VAR_010512
    Natural varianti92 – 921N → D in PC2. 1 Publication
    VAR_003847
    Natural varianti92 – 921N → S in PC2. 2 Publications
    VAR_003849
    Natural varianti94 – 985Missing in PC2.
    VAR_017069
    Natural varianti94 – 941R → C in PC2 and SM. 1 Publication
    VAR_010513
    Natural varianti94 – 941R → P in PC2. 1 Publication
    VAR_017068
    Natural varianti95 – 951L → P in PC2. 1 Publication
    VAR_017071
    Natural varianti95 – 951L → Q in PC2. 1 Publication
    VAR_017070
    Natural varianti97 – 971Missing in PC2. 1 Publication
    VAR_017072
    Natural varianti98 – 981Y → D in PC2. 1 Publication
    VAR_003851
    Natural varianti99 – 991L → P in PC2. 1 Publication
    VAR_017073
    Natural varianti102 – 1021V → M in PC2. 2 Publications
    VAR_017074
    Natural varianti109 – 1091N → D in PC2. 2 Publications
    VAR_037083
    Steatocystoma multiplex (SM) [MIM:184500]: Disease characterized by round or oval cystic tumors widely distributed on the back, anterior trunk, arms, scrotum, and thighs.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti88 – 881M → T in PC2 and SM. 2 Publications
    VAR_010512
    Natural varianti92 – 921N → H in SM. 1 Publication
    VAR_003848
    Natural varianti94 – 941R → C in PC2 and SM. 1 Publication
    VAR_010513
    Natural varianti94 – 941R → H in SM. 1 Publication
    VAR_003850
    KRT16 and KRT17 are coexpressed only in pathological situations such as metaplasias and carcinomas of the uterine cervix and in psoriasis vulgaris.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi103 – 1031R → A: Down-regulates both proliferation of psoriatic T-cells and IFN-gamma production; suppresses keratinocyte growth when part of the altered peptide epitope S1. 1 Publication
    Mutagenesisi106 – 1061E → A: Down-regulates proliferation of psoriatic T-cells and IFN-gamma production when part of the altered peptide epitope S1. 1 Publication
    Mutagenesisi109 – 1091N → A: No significant effect on T-cell proliferation or IFN-gamma production when part of the altered peptide epitope S1. 1 Publication
    Mutagenesisi154 – 1541N → A: No significant effect on T-cell proliferation but reduces IFN-gamma production when part of the altered peptide epitope S2. 1 Publication
    Mutagenesisi155 – 1551I → A: No significant effect on T-cell proliferation but reduces IFN-gamma production when part of the altered peptide epitope S2. 1 Publication
    Mutagenesisi157 – 1571L → A: Down-regulates proliferation of psoriatic T-cells and IFN-gamma production when part of the altered peptide epitope S2. 1 Publication
    Mutagenesisi160 – 1601D → A: No significant effect on T-cell proliferation but reduces IFN-gamma production when part of the altered peptide epitope S4. 1 Publication
    Mutagenesisi333 – 3331N → A: No significant effect on T-cell proliferation but reduces IFN-gamma production when part of the altered peptide epitope S4. 1 Publication
    Mutagenesisi334 – 3341R → A: No significant effect on T-cell proliferation but can induce IFN-gamma production when part of the altered peptide epitope S2. 1 Publication
    Mutagenesisi336 – 3361C → A: No significant effect on T-cell proliferation but reduces IFN-gamma production when part of the altered peptide epitope S2. 1 Publication
    Mutagenesisi339 – 3391L → A: Down-regulates both proliferation of psoriatic T-cells and IFN-gamma production; suppresses keratinocyte growth when part of the altered peptide epitope S4. 1 Publication

    Keywords - Diseasei

    Disease mutation, Ectodermal dysplasia, Palmoplantar keratoderma

    Organism-specific databases

    MIMi167210. phenotype.
    184500. phenotype.
    Orphaneti2309. Pachyonychia congenita.
    841. Sebocystomatosis.
    PharmGKBiPA30214.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 432432Keratin, type I cytoskeletal 17PRO_0000063664Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei13 – 131Phosphoserine1 Publication
    Modified residuei32 – 321Phosphoserine3 Publications
    Modified residuei39 – 391Phosphoserine1 Publication
    Modified residuei44 – 441Phosphoserine; by RPS6KA11 Publication

    Post-translational modificationi

    Phosphorylation at Ser-44 occurs in a growth- and stress-dependent fashion in skin keratinocytes, it has no effect on filament organization.4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ04695.
    PaxDbiQ04695.
    PRIDEiQ04695.

    2D gel databases

    SWISS-2DPAGEQ04695.

    PTM databases

    PhosphoSiteiQ04695.

    Miscellaneous databases

    PMAP-CutDBQ04695.

    Expressioni

    Tissue specificityi

    Expressed in the outer root sheath and medulla region of hair follicle specifically from eyebrow and beard, digital pulp, nail matrix and nail bed epithelium, mucosal stratified squamous epithelia and in basal cells of oral epithelium, palmoplantar epidermis and sweat and mammary glands. Also expressed in myoepithelium of prostate, basal layer of urinary bladder, cambial cells of sebaceous gland and in exocervix (at protein level).4 Publications

    Inductioni

    Induced in damaged or stressed epidermis. Induced by the cytokines interferon-gamma (IFN-gamma), tumor necrosis factor alpha (TNF-alpha) and transforming growth factor-alpha (TGF-alpha), and by the potent NF-kappa B inhibitor compounds Bay 11-7082 and Bay 11-7085. Down-regulated by the drug Imatinib.4 Publications

    Gene expression databases

    BgeeiQ04695.
    GenevestigatoriQ04695.

    Organism-specific databases

    HPAiCAB000029.
    HPA000452.
    HPA000453.

    Interactioni

    Subunit structurei

    Heterodimer of a type I and a type II keratin. KRT17 associates with KRT6 isomers. Interacts with TRADD and SFN By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CCDC85BQ158342EBI-297873,EBI-739674

    Protein-protein interaction databases

    BioGridi110070. 32 interactions.
    DIPiDIP-33093N.
    IntActiQ04695. 13 interactions.
    MINTiMINT-256746.

    Structurei

    3D structure databases

    ProteinModelPortaliQ04695.
    SMRiQ04695. Positions 86-120, 134-232, 248-390.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 8383HeadAdd
    BLAST
    Regioni84 – 392309RodAdd
    BLAST
    Regioni84 – 12037Coil 1AAdd
    BLAST
    Regioni102 – 11615Peptide epitope S1; induces T-cell and keratinocyte proliferation and IFN-gamma productionAdd
    BLAST
    Regioni121 – 13818Linker 1Add
    BLAST
    Regioni139 – 23092Coil 1BAdd
    BLAST
    Regioni153 – 16715Peptide epitope S2; induces T-cell proliferation and IFN-gamma productionAdd
    BLAST
    Regioni231 – 25020Linker 12Add
    BLAST
    Regioni251 – 392142Coil 2Add
    BLAST
    Regioni332 – 34615Peptide epitope S4; induces T-cell and keratinocyte proliferation and IFN-gamma productionAdd
    BLAST
    Regioni393 – 43240TailAdd
    BLAST

    Sequence similaritiesi

    Belongs to the intermediate filament family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG148784.
    HOVERGENiHBG013015.
    InParanoidiQ04695.
    KOiK07604.
    OMAiGCYSFGS.
    OrthoDBiEOG7FV3Q8.
    PhylomeDBiQ04695.
    TreeFamiTF332742.

    Family and domain databases

    InterProiIPR001664. IF.
    IPR018039. Intermediate_filament_CS.
    IPR002957. Keratin_I.
    IPR009053. Prefoldin.
    [Graphical view]
    PANTHERiPTHR23239. PTHR23239. 1 hit.
    PfamiPF00038. Filament. 1 hit.
    [Graphical view]
    PRINTSiPR01248. TYPE1KERATIN.
    SUPFAMiSSF46579. SSF46579. 1 hit.
    PROSITEiPS00226. IF. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q04695-1 [UniParc]FASTAAdd to Basket

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    MTTSIRQFTS SSSIKGSSGL GGGSSRTSCR LSGGLGAGSC RLGSAGGLGS    50
    TLGGSSYSSC YSFGSGGGYG SSFGGVDGLL AGGEKATMQN LNDRLASYLD 100
    KVRALEEANT ELEVKIRDWY QRQAPGPARD YSQYYRTIEE LQNKILTATV 150
    DNANILLQID NARLAADDFR TKFETEQALR LSVEADINGL RRVLDELTLA 200
    RADLEMQIEN LKEELAYLKK NHEEEMNALR GQVGGEINVE MDAAPGVDLS 250
    RILNEMRDQY EKMAEKNRKD AEDWFFSKTE ELNREVATNS ELVQSGKSEI 300
    SELRRTMQAL EIELQSQLSM KASLEGNLAE TENRYCVQLS QIQGLIGSVE 350
    EQLAQLRCEM EQQNQEYKIL LDVKTRLEQE IATYRRLLEG EDAHLTQYKK 400
    EPVTTRQVRT IVEEVQDGKV ISSREQVHQT TR 432
    Length:432
    Mass (Da):48,106
    Last modified:January 23, 2007 - v2
    Checksum:i35B429243F47EB5C
    GO

    Sequence cautioni

    The sequence AAH72018.1 differs from that shown. Reason: Frameshift at position 109.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti30 – 301R → Q in AL353997. (PubMed:16625196)Curated
    Sequence conflicti30 – 301R → Q in AC022596. (PubMed:16625196)Curated
    Sequence conflicti42 – 421L → P in AL353997. (PubMed:16625196)Curated
    Sequence conflicti42 – 421L → P in AC022596. (PubMed:16625196)Curated
    Sequence conflicti51 – 566Missing in BAC04534. (PubMed:14702039)Curated
    Sequence conflicti51 – 511T → A in AL353997. (PubMed:16625196)Curated
    Sequence conflicti51 – 511T → A in AC022596. (PubMed:16625196)Curated
    Sequence conflicti72 – 721S → SS in AL353997. (PubMed:16625196)Curated
    Sequence conflicti73 – 742FG → SFE in AC022596. (PubMed:16625196)Curated
    Sequence conflicti74 – 741G → E in AL353997. (PubMed:16625196)Curated
    Sequence conflicti81 – 811A → V in AL353997. (PubMed:16625196)Curated
    Sequence conflicti81 – 811A → V in AC022596. (PubMed:16625196)Curated
    Sequence conflicti94 – 10815Missing in AAH72018. (PubMed:15489334)CuratedAdd
    BLAST
    Sequence conflicti137 – 1371T → I in AL353997. (PubMed:16625196)Curated
    Sequence conflicti137 – 1371T → I in AC022596. (PubMed:16625196)Curated
    Sequence conflicti145 – 1473ILT → VGPA in AL353997. (PubMed:16625196)Curated
    Sequence conflicti158 – 1581Q → H in AC022596. (PubMed:16625196)Curated
    Sequence conflicti159 – 1591I → N in AL353997. (PubMed:16625196)Curated
    Sequence conflicti163 – 1631R → H in AL353997. (PubMed:16625196)Curated
    Sequence conflicti163 – 1631R → H in AC022596. (PubMed:16625196)Curated
    Sequence conflicti167 – 1671D → A in AL353997. (PubMed:16625196)Curated
    Sequence conflicti167 – 1671D → A in AC022596. (PubMed:16625196)Curated
    Sequence conflicti180 – 1801R → C in AL353997. (PubMed:16625196)Curated
    Sequence conflicti180 – 1801R → C in AC022596. (PubMed:16625196)Curated
    Sequence conflicti190 – 1912LR → PC in AL353997. (PubMed:16625196)Curated
    Sequence conflicti190 – 1912LR → PC in AC022596. (PubMed:16625196)Curated
    Sequence conflicti204 – 2041L → P in AL353997. (PubMed:16625196)Curated
    Sequence conflicti207 – 2071Q → H in AL353997. (PubMed:16625196)Curated
    Sequence conflicti207 – 2071Q → H in AC022596. (PubMed:16625196)Curated
    Sequence conflicti225 – 2251Missing in AL353997. (PubMed:16625196)Curated
    Sequence conflicti225 – 2251Missing in AC022596. (PubMed:16625196)Curated
    Sequence conflicti229 – 2291L → P in AL353997. (PubMed:16625196)Curated
    Sequence conflicti229 – 2291L → P in AC022596. (PubMed:16625196)Curated
    Sequence conflicti242 – 2421D → G in AL353997. (PubMed:16625196)Curated
    Sequence conflicti242 – 2421D → G in AC022596. (PubMed:16625196)Curated
    Sequence conflicti258 – 2581D → E in AL353997. (PubMed:16625196)Curated
    Sequence conflicti258 – 2581D → E in AC022596. (PubMed:16625196)Curated
    Sequence conflicti305 – 3051R → C in AL353997. (PubMed:16625196)Curated
    Sequence conflicti305 – 3051R → C in AC022596. (PubMed:16625196)Curated
    Sequence conflicti337 – 3371V → M in AL353997. (PubMed:16625196)Curated
    Sequence conflicti337 – 3371V → M in AC022596. (PubMed:16625196)Curated
    Sequence conflicti352 – 3521Q → R in AL353997. (PubMed:16625196)Curated
    Sequence conflicti352 – 3521Q → R in AC022596. (PubMed:16625196)Curated
    Sequence conflicti357 – 3571R → L in AL353997. (PubMed:16625196)Curated
    Sequence conflicti357 – 3571R → L in AC022596. (PubMed:16625196)Curated
    Sequence conflicti373 – 3753VKT → MKM in AL353997. (PubMed:16625196)Curated
    Sequence conflicti373 – 3753VKT → MKM in AC022596. (PubMed:16625196)Curated
    Sequence conflicti379 – 3791Q → L in AL353997. (PubMed:16625196)Curated
    Sequence conflicti379 – 3791Q → L in AC022596. (PubMed:16625196)Curated
    Sequence conflicti382 – 3821A → T in AL353997. (PubMed:16625196)Curated
    Sequence conflicti382 – 3821A → T in AC022596. (PubMed:16625196)Curated
    Sequence conflicti385 – 3851R → H in AL353997. (PubMed:16625196)Curated
    Sequence conflicti385 – 3851R → H in AC022596. (PubMed:16625196)Curated
    Sequence conflicti395 – 40410LTQYKKEPVT → FRMSESSPVS in AC022596. (PubMed:16625196)Curated
    Sequence conflicti406 – 4061R → C in AL353997. (PubMed:16625196)Curated
    Sequence conflicti409 – 4091R → P in AL353997. (PubMed:16625196)Curated
    Sequence conflicti428 – 4281H → R in AL353997. (PubMed:16625196)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti88 – 881M → T in PC2 and SM. 2 Publications
    VAR_010512
    Natural varianti92 – 921N → D in PC2. 1 Publication
    VAR_003847
    Natural varianti92 – 921N → H in SM. 1 Publication
    VAR_003848
    Natural varianti92 – 921N → S in PC2. 2 Publications
    VAR_003849
    Natural varianti94 – 985Missing in PC2.
    VAR_017069
    Natural varianti94 – 941R → C in PC2 and SM. 1 Publication
    VAR_010513
    Natural varianti94 – 941R → H in SM. 1 Publication
    VAR_003850
    Natural varianti94 – 941R → P in PC2. 1 Publication
    VAR_017068
    Natural varianti95 – 951L → P in PC2. 1 Publication
    VAR_017071
    Natural varianti95 – 951L → Q in PC2. 1 Publication
    VAR_017070
    Natural varianti97 – 971Missing in PC2. 1 Publication
    VAR_017072
    Natural varianti98 – 981Y → D in PC2. 1 Publication
    VAR_003851
    Natural varianti99 – 991L → P in PC2. 1 Publication
    VAR_017073
    Natural varianti102 – 1021V → M in PC2. 2 Publications
    VAR_017074
    Natural varianti109 – 1091N → D in PC2. 2 Publications
    VAR_037083

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z19574 Genomic DNA. Translation: CAA79626.1.
    X62571 mRNA. Translation: CAA44451.1.
    AK095342 mRNA. Translation: BAC04534.1.
    AC022596 Genomic DNA. No translation available.
    AL353997 Genomic DNA. No translation available.
    BC000159 mRNA. Translation: AAH00159.2.
    BC011901 mRNA. Translation: AAH11901.1.
    BC056421 mRNA. Translation: AAH56421.1.
    BC072018 mRNA. Translation: AAH72018.1. Frameshift.
    BC072019 mRNA. Translation: AAH72019.1.
    S78515 Genomic DNA. Translation: AAB34565.1.
    EF608068 mRNA. Translation: ABQ96595.1.
    EF608069 mRNA. Translation: ABQ96596.1.
    EF608070 mRNA. Translation: ABQ96597.1.
    EF608071 mRNA. Translation: ABQ96598.1.
    CCDSiCCDS11402.1.
    PIRiS30433.
    RefSeqiNP_000413.1. NM_000422.2.
    UniGeneiHs.2785.

    Genome annotation databases

    EnsembliENST00000311208; ENSP00000308452; ENSG00000128422.
    GeneIDi3872.
    KEGGihsa:3872.
    UCSCiuc002hxh.2. human.

    Polymorphism databases

    DMDMi547751.

    Cross-referencesi

    Web resourcesi

    Human Intermediate Filament Mutation Database
    Wikipedia

    Keratin-17 entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z19574 Genomic DNA. Translation: CAA79626.1 .
    X62571 mRNA. Translation: CAA44451.1 .
    AK095342 mRNA. Translation: BAC04534.1 .
    AC022596 Genomic DNA. No translation available.
    AL353997 Genomic DNA. No translation available.
    BC000159 mRNA. Translation: AAH00159.2 .
    BC011901 mRNA. Translation: AAH11901.1 .
    BC056421 mRNA. Translation: AAH56421.1 .
    BC072018 mRNA. Translation: AAH72018.1 . Frameshift.
    BC072019 mRNA. Translation: AAH72019.1 .
    S78515 Genomic DNA. Translation: AAB34565.1 .
    EF608068 mRNA. Translation: ABQ96595.1 .
    EF608069 mRNA. Translation: ABQ96596.1 .
    EF608070 mRNA. Translation: ABQ96597.1 .
    EF608071 mRNA. Translation: ABQ96598.1 .
    CCDSi CCDS11402.1.
    PIRi S30433.
    RefSeqi NP_000413.1. NM_000422.2.
    UniGenei Hs.2785.

    3D structure databases

    ProteinModelPortali Q04695.
    SMRi Q04695. Positions 86-120, 134-232, 248-390.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110070. 32 interactions.
    DIPi DIP-33093N.
    IntActi Q04695. 13 interactions.
    MINTi MINT-256746.

    PTM databases

    PhosphoSitei Q04695.

    Polymorphism databases

    DMDMi 547751.

    2D gel databases

    SWISS-2DPAGE Q04695.

    Proteomic databases

    MaxQBi Q04695.
    PaxDbi Q04695.
    PRIDEi Q04695.

    Protocols and materials databases

    DNASUi 3872.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000311208 ; ENSP00000308452 ; ENSG00000128422 .
    GeneIDi 3872.
    KEGGi hsa:3872.
    UCSCi uc002hxh.2. human.

    Organism-specific databases

    CTDi 3872.
    GeneCardsi GC17M039775.
    GeneReviewsi KRT17.
    H-InvDB HIX0059686.
    HGNCi HGNC:6427. KRT17.
    HPAi CAB000029.
    HPA000452.
    HPA000453.
    MIMi 148069. gene.
    167210. phenotype.
    184500. phenotype.
    neXtProti NX_Q04695.
    Orphaneti 2309. Pachyonychia congenita.
    841. Sebocystomatosis.
    PharmGKBi PA30214.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG148784.
    HOVERGENi HBG013015.
    InParanoidi Q04695.
    KOi K07604.
    OMAi GCYSFGS.
    OrthoDBi EOG7FV3Q8.
    PhylomeDBi Q04695.
    TreeFami TF332742.

    Miscellaneous databases

    GeneWikii Keratin_17.
    GenomeRNAii 3872.
    NextBioi 15209.
    PMAP-CutDB Q04695.
    PROi Q04695.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q04695.
    Genevestigatori Q04695.

    Family and domain databases

    InterProi IPR001664. IF.
    IPR018039. Intermediate_filament_CS.
    IPR002957. Keratin_I.
    IPR009053. Prefoldin.
    [Graphical view ]
    PANTHERi PTHR23239. PTHR23239. 1 hit.
    Pfami PF00038. Filament. 1 hit.
    [Graphical view ]
    PRINTSi PR01248. TYPE1KERATIN.
    SUPFAMi SSF46579. SSF46579. 1 hit.
    PROSITEi PS00226. IF. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of the human gene encoding cytokeratin 17 and its expression pattern."
      Troyanovsky S.M., Leube R.E., Franke W.W.
      Eur. J. Cell Biol. 59:127-137(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
    2. "Interferon-gamma regulates expression of a novel keratin class I gene."
      Flohr T., Buwitt U., Bonnekoh B., Decker T., Boettger E.C.
      Eur. J. Immunol. 22:975-979(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
    3. "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].
      Tissue: Tongue.
    4. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT PC2 ASP-109.
    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: Brain, Cervix and Muscle.
    6. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 85-101, VARIANT PC2 ASP-92.
    7. Shen Z., Chen L., Wang G., Liu Y.-F.
      Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 101-117; 152-168; 306-322 AND 331-347.
    8. "Patterns of expression of keratin 17 in human epithelia: dependency on cell position."
      Troyanovsky S.M., Guelstein V.I., Tchipysheva T.A., Krutovskikh V.A., Bannikov G.A.
      J. Cell Sci. 93:419-426(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    9. "Keratin expression in the normal nail unit: markers of regional differentiation."
      De Berker D., Wojnarowska F., Sviland L., Westgate G.E., Dawber R.P., Leigh I.M.
      Br. J. Dermatol. 142:89-96(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    10. "Keratin 17 expression in the hard epithelial context of the hair and nail, and its relevance for the pachyonychia congenita phenotype."
      McGowan K.M., Coulombe P.A.
      J. Invest. Dermatol. 114:1101-1107(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    11. "HLA DR B1*04, *07-restricted epitopes on Keratin 17 for autoreactive T cells in psoriasis."
      Shen Z., Wang G., Fan J.-Y., Li W., Liu Y.-F.
      J. Dermatol. Sci. 38:25-39(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.
    12. "Interferon-gamma-dependent in vitro model for the putative keratin 17 autoimmune loop in psoriasis: exploration of pharmaco- and gene-therapeutic effects."
      Bockelmann R., Horn T., Gollnick H., Bonnekoh B.
      Skin Pharmacol. Physiol. 18:42-54(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    13. "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.
    14. "Altered keratin 17 peptide ligands inhibit in vitro proliferation of keratinocytes and T cells isolated from patients with psoriasis."
      Shen Z., Chen L., Liu Y.-F., Gao T.-W., Wang G., Fan X.-L., Fan J.-Y., Fan P.-S., Li C.-Y., Liu B., Dang Y.-P., Li C.-X.
      J. Am. Acad. Dermatol. 54:992-1002(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION, MUTAGENESIS OF ARG-103; GLU-106; ASN-109; ASN-154; ILE-155; LEU-157; ASP-160; ASN-333; ARG-334; CYS-336 AND LEU-339.
    15. "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-32, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-32 AND SER-39, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "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-32, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Type I keratin 17 protein is phosphorylated on serine 44 by p90 ribosomal protein S6 kinase 1 (RSK1) in a growth- and stress-dependent fashion."
      Pan X., Kane L.A., Van Eyk J.E., Coulombe P.A.
      J. Biol. Chem. 286:42403-42413(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-44.
    20. "Missense mutations in keratin 17 cause either pachyonychia congenita type 2 or a phenotype resembling steatocystoma multiplex."
      Smith F.J.D., Corden L.D., Rugg E.L., Ratnavel R., Leigh I.M., Moss C., Tidman M.J., Hohl D., Huber M., Kunkeler L., Munro C.S., Lane E.B., McLean W.H.I.
      J. Invest. Dermatol. 108:220-223(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PC2 SER-92 AND ASP-98, VARIANTS SM HIS-92 AND HIS-94.
    21. "Keratin 17 mutations cause either steatocystoma multiplex or pachyonychia congenita type 2."
      Covello S.P., Smith F.J.D., Sillevis Smitt J.H., Paller A.S., Munro C.S., Jonkman M.F., Uitto J., McLean W.H.I.
      Br. J. Dermatol. 139:475-480(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PC2 SER-92 AND CYS-94, VARIANT SM CYS-94.
    22. "Mutation report: identification of a germline mutation in keratin 17 in a family with pachyonychia congenita type 2."
      Celebi J.T., Tanzi E.L., Yao Y.J., Michael E.J., Peacocke M.
      J. Invest. Dermatol. 113:848-850(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PC2 THR-88.
    23. Cited for: VARIANTS PC2 94-PRO--TYR-98 DEL; PRO-94 AND GLN-95.
    24. "Novel and recurrent mutations in the genes encoding keratins K6a, K16 and K17 in 13 cases of pachyonychia congenita."
      Terrinoni A., Smith F.J.D., Didona B., Canzona F., Paradisi M., Huber M., Hohl D., David A., Verloes A., Leigh I.M., Munro C.S., Melino G., McLean W.H.I.
      J. Invest. Dermatol. 117:1391-1396(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PC2 PRO-95; SER-97 DEL AND PRO-99.
    25. "A novel point mutation in the keratin 17 gene in a Japanese case of pachyonychia congenita type 2."
      Hashiguchi T., Yotsumoto S., Shimada H., Terasaki K., Setoyama M., Kobayashi K., Saheki T., Kanzaki T.
      J. Invest. Dermatol. 118:545-547(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PC2 MET-102.
    26. "A novel mutation in the second half of the keratin 17 1A domain in a large pedigree with delayed-onset pachyonychia congenita type 2."
      Xiao S.-X., Feng Y.-G., Ren X.-R., Tan S.-S., Li L., Wang J.-M., Shi Y.-Z.
      J. Invest. Dermatol. 122:892-895(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PC2 ASP-109.
    27. "Identification of a recurrent mutation in keratin 17 in a Japanese family with pachyonychia congenita type 2."
      Uchida T., Inaoki M., Makino E., Fujimoto W.
      J. Dermatol. Sci. 38:60-63(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PC2 MET-102.
    28. "Keratin 17 mutation in pachyonychia congenita type 2 patient with early onset steatocystoma multiplex and Hutchinson-like tooth deformity."
      Oh S.-W., Kim M.Y., Lee J.S., Kim S.-C.
      J. Dermatol. 33:161-164(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PC2 THR-88, VARIANT SM THR-88.

    Entry informationi

    Entry nameiK1C17_HUMAN
    AccessioniPrimary (citable) accession number: Q04695
    Secondary accession number(s): A5Z1M9
    , A5Z1N0, A5Z1N1, A5Z1N2, A6NDV6, A6NKQ2, Q6IP98, Q8N1P6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 152 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, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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