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Q04695

- K1C17_HUMAN

UniProt

Q04695 - K1C17_HUMAN

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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

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.3 Publications

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
Complete GO annotation...

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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.11 Publications
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.3 Publications
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.

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.

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.

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

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

« Hide

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.

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 301R → Q in AL353997. 1 Publication
Sequence conflicti30 – 301R → Q in AC022596. 1 Publication
Sequence conflicti42 – 421L → P in AL353997. 1 Publication
Sequence conflicti42 – 421L → P in AC022596. 1 Publication
Sequence conflicti51 – 566Missing in BAC04534. 1 Publication
Sequence conflicti51 – 511T → A in AL353997. 1 Publication
Sequence conflicti51 – 511T → A in AC022596. 1 Publication
Sequence conflicti72 – 721S → SS in AL353997. 1 Publication
Sequence conflicti73 – 742FG → SFE in AC022596. 1 Publication
Sequence conflicti74 – 741G → E in AL353997. 1 Publication
Sequence conflicti81 – 811A → V in AL353997. 1 Publication
Sequence conflicti81 – 811A → V in AC022596. 1 Publication
Sequence conflicti94 – 10815Missing in AAH72018. 1 PublicationAdd
BLAST
Sequence conflicti137 – 1371T → I in AL353997. 1 Publication
Sequence conflicti137 – 1371T → I in AC022596. 1 Publication
Sequence conflicti145 – 1473ILT → VGPA in AL353997. 1 Publication
Sequence conflicti158 – 1581Q → H in AC022596. 1 Publication
Sequence conflicti159 – 1591I → N in AL353997. 1 Publication
Sequence conflicti163 – 1631R → H in AL353997. 1 Publication
Sequence conflicti163 – 1631R → H in AC022596. 1 Publication
Sequence conflicti167 – 1671D → A in AL353997. 1 Publication
Sequence conflicti167 – 1671D → A in AC022596. 1 Publication
Sequence conflicti180 – 1801R → C in AL353997. 1 Publication
Sequence conflicti180 – 1801R → C in AC022596. 1 Publication
Sequence conflicti190 – 1912LR → PC in AL353997. 1 Publication
Sequence conflicti190 – 1912LR → PC in AC022596. 1 Publication
Sequence conflicti204 – 2041L → P in AL353997. 1 Publication
Sequence conflicti207 – 2071Q → H in AL353997. 1 Publication
Sequence conflicti207 – 2071Q → H in AC022596. 1 Publication
Sequence conflicti225 – 2251Missing in AL353997. 1 Publication
Sequence conflicti225 – 2251Missing in AC022596. 1 Publication
Sequence conflicti229 – 2291L → P in AL353997. 1 Publication
Sequence conflicti229 – 2291L → P in AC022596. 1 Publication
Sequence conflicti242 – 2421D → G in AL353997. 1 Publication
Sequence conflicti242 – 2421D → G in AC022596. 1 Publication
Sequence conflicti258 – 2581D → E in AL353997. 1 Publication
Sequence conflicti258 – 2581D → E in AC022596. 1 Publication
Sequence conflicti305 – 3051R → C in AL353997. 1 Publication
Sequence conflicti305 – 3051R → C in AC022596. 1 Publication
Sequence conflicti337 – 3371V → M in AL353997. 1 Publication
Sequence conflicti337 – 3371V → M in AC022596. 1 Publication
Sequence conflicti352 – 3521Q → R in AL353997. 1 Publication
Sequence conflicti352 – 3521Q → R in AC022596. 1 Publication
Sequence conflicti357 – 3571R → L in AL353997. 1 Publication
Sequence conflicti357 – 3571R → L in AC022596. 1 Publication
Sequence conflicti373 – 3753VKT → MKM in AL353997. 1 Publication
Sequence conflicti373 – 3753VKT → MKM in AC022596. 1 Publication
Sequence conflicti379 – 3791Q → L in AL353997. 1 Publication
Sequence conflicti379 – 3791Q → L in AC022596. 1 Publication
Sequence conflicti382 – 3821A → T in AL353997. 1 Publication
Sequence conflicti382 – 3821A → T in AC022596. 1 Publication
Sequence conflicti385 – 3851R → H in AL353997. 1 Publication
Sequence conflicti385 – 3851R → H in AC022596. 1 Publication
Sequence conflicti395 – 40410LTQYKKEPVT → FRMSESSPVS in AC022596. 1 Publication
Sequence conflicti406 – 4061R → C in AL353997. 1 Publication
Sequence conflicti409 – 4091R → P in AL353997. 1 Publication
Sequence conflicti428 – 4281H → R in AL353997. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 151 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

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