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P13645

- K1C10_HUMAN

UniProt

P13645 - K1C10_HUMAN

Protein

Keratin, type I cytoskeletal 10

Gene

KRT10

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 6 (24 Nov 2009)
      Previous versions | rss
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    Functioni

    GO - Molecular functioni

    1. structural constituent of epidermis Source: UniProtKB

    GO - Biological processi

    1. cellular response to calcium ion Source: Ensembl
    2. keratinocyte differentiation Source: UniProtKB

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Keratin, type I cytoskeletal 10
    Alternative name(s):
    Cytokeratin-10
    Short name:
    CK-10
    Keratin-10
    Short name:
    K10
    Gene namesi
    Name:KRT10
    Synonyms:KPP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:6413. KRT10.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. extracellular space Source: UniProt
    3. extracellular vesicular exosome Source: UniProt
    4. intermediate filament Source: UniProtKB
    5. keratin filament Source: Ensembl
    6. membrane Source: UniProtKB
    7. nucleus Source: UniProt

    Keywords - Cellular componenti

    Intermediate filament, Keratin

    Pathology & Biotechi

    Involvement in diseasei

    Epidermolytic hyperkeratosis (EHK) [MIM:113800]: An autosomal dominant skin disorder characterized by widespread blistering and an ichthyotic erythroderma at birth that persist into adulthood. Histologically there is a diffuse epidermolytic degeneration in the lower spinous layer of the epidermis. Within a few weeks from birth, erythroderma and blister formation diminish and hyperkeratoses develop.8 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti150 – 1501M → R in EHK. 1 Publication
    Corresponds to variant rs58901407 [ dbSNP | Ensembl ].
    VAR_010506
    Natural varianti154 – 1541N → H in EHK. 1 Publication
    Corresponds to variant rs57784225 [ dbSNP | Ensembl ].
    VAR_003826
    Natural varianti156 – 1561R → C in EHK. 3 Publications
    VAR_003828
    Natural varianti156 – 1561R → H in EHK. 4 Publications
    Corresponds to variant rs58075662 [ dbSNP | Ensembl ].
    VAR_003827
    Natural varianti156 – 1561R → P in EHK. 1 Publication
    VAR_003829
    Natural varianti156 – 1561R → S in EHK. 1 Publication
    Corresponds to variant rs58852768 [ dbSNP | Ensembl ].
    VAR_003830
    Natural varianti160 – 1601Y → D in EHK; severe phenotype. 1 Publication
    Corresponds to variant rs58414354 [ dbSNP | Ensembl ].
    VAR_003831
    Natural varianti160 – 1601Y → N in EHK; severe phenotype. 1 Publication
    VAR_010508
    Natural varianti160 – 1601Y → S in EHK; severe phenotype. 1 Publication
    Corresponds to variant rs58735429 [ dbSNP | Ensembl ].
    VAR_010509
    Natural varianti161 – 1611L → S in EHK. 1 Publication
    Corresponds to variant rs60118264 [ dbSNP | Ensembl ].
    VAR_003832
    Natural varianti439 – 4391K → E in EHK; mild phenotype. 1 Publication
    Corresponds to variant rs61434181 [ dbSNP | Ensembl ].
    VAR_010510
    Natural varianti442 – 4421L → Q in EHK. 1 Publication
    Corresponds to variant rs58026994 [ dbSNP | Ensembl ].
    VAR_003833
    Ichthyosis annular epidermolytic (AEI) [MIM:607602]: A skin disorder resembling bullous congenital ichthyosiform erythroderma. Affected individuals present with bullous ichthyosis in early childhood and hyperkeratotic lichenified plaques in the flexural areas and extensor surfaces at later ages. The feature that distinguishes AEI from BCIE is dramatic episodes of flares of annular polycyclic plaques with scale, which coalesce to involve most of the body surface and can persist for several weeks or even months.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti422 – 4221R → E in AEI; requires 2 nucleotide substitutions. 1 Publication
    Corresponds to variant rs59075499 [ dbSNP | Ensembl ].
    VAR_033145
    Natural varianti446 – 4461I → T in AEI. 1 Publication
    VAR_010511
    Erythroderma, ichthyosiform, congenital reticular (CRIE) [MIM:609165]: A rare skin condition characterized by slowly enlarging islands of normal skin surrounded by erythematous ichthyotic patches in a reticulated pattern. The condition starts in infancy as a lamellar ichthyosis, with small islands of normal skin resembling confetti appearing in late childhood and at puberty. Histopathologic findings include band-like parakeratosis, psoriasiform acanthosis, and vacuolization of keratinocytes with binucleated cells in the upper epidermis, sometimes associated with amyloid deposition in the dermis. Ultrastructural abnormalities include perinuclear shells formed from a network of fine filaments in the upper epidermis.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Disease mutation, Ichthyosis

    Organism-specific databases

    MIMi113800. phenotype.
    607602. phenotype.
    609165. phenotype.
    Orphaneti281139. Annular epidermolytic ichthyosis.
    281190. Congenital reticular ichthyosiform erythroderma.
    312. Epidermolytic ichthyosis.
    PharmGKBiPA30200.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 584584Keratin, type I cytoskeletal 10PRO_0000063642Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei16 – 161Phosphoserine1 Publication
    Modified residuei42 – 421Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP13645.
    PaxDbiP13645.
    PeptideAtlasiP13645.
    PRIDEiP13645.
    ProMEXiP13645.

    2D gel databases

    REPRODUCTION-2DPAGEP13645.
    SWISS-2DPAGEP13645.

    PTM databases

    PhosphoSiteiP13645.

    Expressioni

    Tissue specificityi

    Seen in all suprabasal cell layers including stratum corneum.

    Gene expression databases

    BgeeiP13645.
    CleanExiHS_KRT10.
    GenevestigatoriP13645.

    Organism-specific databases

    HPAiCAB000132.
    HPA012014.

    Interactioni

    Subunit structurei

    Heterotetramer of two type I and two type II keratins. keratin-10 is generally associated with keratin-1.

    Protein-protein interaction databases

    BioGridi110056. 51 interactions.
    IntActiP13645. 19 interactions.
    MINTiMINT-1132575.
    STRINGi9606.ENSP00000269576.

    Structurei

    Secondary structure

    1
    584
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi479 – 4813
    Beta strandi483 – 4864
    Beta strandi500 – 5089

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3ASWX-ray2.60B473-487[»]
    4F1ZX-ray2.30Q499-512[»]
    ProteinModelPortaliP13645.
    SMRiP13645. Positions 145-287, 313-455.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 145145HeadAdd
    BLAST
    Regioni146 – 456311RodAdd
    BLAST
    Regioni146 – 18136Coil 1AAdd
    BLAST
    Regioni182 – 20221Linker 1Add
    BLAST
    Regioni203 – 29492Coil 1BAdd
    BLAST
    Regioni295 – 31723Linker 12Add
    BLAST
    Regioni318 – 456139Coil 2Add
    BLAST
    Regioni457 – 584128TailAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi17 – 575559Gly-richAdd
    BLAST
    Compositional biasi477 – 579103Ser-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the intermediate filament family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG147548.
    HOGENOMiHOG000230975.
    HOVERGENiHBG013015.
    InParanoidiP13645.
    KOiK07604.
    OMAiRYSSSKH.
    OrthoDBiEOG7FV3Q8.
    PhylomeDBiP13645.
    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.

    P13645-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSVRYSSSKH YSSSRSGGGG GGGGCGGGGG VSSLRISSSK GSLGGGFSSG    50
    GFSGGSFSRG SSGGGCFGGS SGGYGGLGGF GGGSFRGSYG SSSFGGSYGG 100
    IFGGGSFGGG SFGGGSFGGG GFGGGGFGGG FGGGFGGDGG LLSGNEKVTM 150
    QNLNDRLASY LDKVRALEES NYELEGKIKE WYEKHGNSHQ GEPRDYSKYY 200
    KTIDDLKNQI LNLTTDNANI LLQIDNARLA ADDFRLKYEN EVALRQSVEA 250
    DINGLRRVLD ELTLTKADLE MQIESLTEEL AYLKKNHEEE MKDLRNVSTG 300
    DVNVEMNAAP GVDLTQLLNN MRSQYEQLAE QNRKDAEAWF NEKSKELTTE 350
    IDNNIEQISS YKSEITELRR NVQALEIELQ SQLALKQSLE ASLAETEGRY 400
    CVQLSQIQAQ ISALEEQLQQ IRAETECQNT EYQQLLDIKI RLENEIQTYR 450
    SLLEGEGSSG GGGRGGGSFG GGYGGGSSGG GSSGGGHGGG HGGSSGGGYG 500
    GGSSGGGSSG GGYGGGSSSG GHGGSSSGGY GGGSSGGGGG GYGGGSSGGG 550
    SSSGGGYGGG SSSGGHKSSS SGSVGESSSK GPRY 584
    Length:584
    Mass (Da):58,827
    Last modified:November 24, 2009 - v6
    Checksum:i4941ECD2AE46D417
    GO

    Sequence cautioni

    The sequence AAA59468.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti9 – 113KHY → SKQF in AAA60544. (PubMed:2459124)Curated
    Sequence conflicti24 – 318Missing in AAA60544. (PubMed:2459124)Curated
    Sequence conflicti86 – 861R → H in CAA32649. (PubMed:2464696)Curated
    Sequence conflicti106 – 1061S → N in CAA32649. (PubMed:2464696)Curated
    Sequence conflicti181 – 1844WYEK → RYDQ in AAA60544. (PubMed:2459124)Curated
    Sequence conflicti189 – 1891H → R in AAA60544. (PubMed:2459124)Curated
    Sequence conflicti197 – 1971S → G in AAA59199. (PubMed:1378806)Curated
    Sequence conflicti266 – 2661K → Q in AAA60544. (PubMed:2459124)Curated
    Sequence conflicti279 – 2802EL → YV in AAA59468. (PubMed:2448602)Curated
    Sequence conflicti287 – 2871H → R in AAA60544. (PubMed:2459124)Curated
    Sequence conflicti293 – 2931D → H in AAA60544. (PubMed:2459124)Curated
    Sequence conflicti312 – 3121V → I in AAA59468. (PubMed:2448602)Curated
    Sequence conflicti323 – 3231S → N in AAA60544. (PubMed:2459124)Curated
    Sequence conflicti340 – 3401F → V in AAA59468. (PubMed:2448602)Curated
    Sequence conflicti374 – 3741A → R in AAA59468. (PubMed:2448602)Curated
    Sequence conflicti408 – 4081Q → H in CAA32649. (PubMed:2464696)Curated
    Sequence conflicti420 – 4201Q → E in AAA60544. (PubMed:2459124)Curated
    Sequence conflicti436 – 4361L → T in AAA60544. (PubMed:2459124)Curated
    Sequence conflicti451 – 4511S → G in AAA59199. (PubMed:1378806)Curated
    Sequence conflicti460 – 4612GG → RS in AAA59468. (PubMed:2448602)Curated
    Sequence conflicti477 – 4771S → T in AAA59468. (PubMed:2448602)Curated
    Sequence conflicti482 – 4821S → T in AAA59468. (PubMed:2448602)Curated
    Sequence conflicti487 – 4904Missing in AAA59199. (PubMed:1378806)Curated
    Sequence conflicti491 – 51626Missing in AAA60544. (PubMed:2459124)CuratedAdd
    BLAST
    Sequence conflicti503 – 5031S → T in AAA59468. (PubMed:2448602)Curated
    Sequence conflicti508 – 5081S → T in AAA59468. (PubMed:2448602)Curated
    Sequence conflicti513 – 5197YGGGSSS → LRGELH in AAA59468. (PubMed:2448602)Curated
    Sequence conflicti523 – 5275GGSSS → AHST in AAA59468. (PubMed:2448602)Curated
    Sequence conflicti524 – 5241G → GGSSSGGHGG in CAA32649. (PubMed:2464696)Curated
    Sequence conflicti534 – 5341S → N in AAA59468. (PubMed:2448602)Curated
    Sequence conflicti535 – 5351S → F in AAA60544. (PubMed:2459124)Curated
    Sequence conflicti542 – 5465YGGGS → LRGRH in AAA59468. (PubMed:2448602)Curated
    Sequence conflicti565 – 5651G → GGYGGGSSSGG in AAA60544. (PubMed:2459124)Curated

    Polymorphismi

    A number of alleles are known that mainly differ in the Gly-rich region (positions 490-560).

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti101 – 1011I → S.2 Publications
    Corresponds to variant rs4261597 [ dbSNP | Ensembl ].
    VAR_058202
    Natural varianti126 – 1261G → S.1 Publication
    Corresponds to variant rs77919366 [ dbSNP | Ensembl ].
    VAR_010505
    Natural varianti150 – 1501M → R in EHK. 1 Publication
    Corresponds to variant rs58901407 [ dbSNP | Ensembl ].
    VAR_010506
    Natural varianti150 – 1501M → T in a patient with epidermal nevi hyperkeratotic type due to genetic mosaicism. 1 Publication
    VAR_010507
    Natural varianti154 – 1541N → H in EHK. 1 Publication
    Corresponds to variant rs57784225 [ dbSNP | Ensembl ].
    VAR_003826
    Natural varianti156 – 1561R → C in EHK. 3 Publications
    VAR_003828
    Natural varianti156 – 1561R → H in EHK. 4 Publications
    Corresponds to variant rs58075662 [ dbSNP | Ensembl ].
    VAR_003827
    Natural varianti156 – 1561R → P in EHK. 1 Publication
    VAR_003829
    Natural varianti156 – 1561R → S in EHK. 1 Publication
    Corresponds to variant rs58852768 [ dbSNP | Ensembl ].
    VAR_003830
    Natural varianti160 – 1601Y → D in EHK; severe phenotype. 1 Publication
    Corresponds to variant rs58414354 [ dbSNP | Ensembl ].
    VAR_003831
    Natural varianti160 – 1601Y → N in EHK; severe phenotype. 1 Publication
    VAR_010508
    Natural varianti160 – 1601Y → S in EHK; severe phenotype. 1 Publication
    Corresponds to variant rs58735429 [ dbSNP | Ensembl ].
    VAR_010509
    Natural varianti161 – 1611L → S in EHK. 1 Publication
    Corresponds to variant rs60118264 [ dbSNP | Ensembl ].
    VAR_003832
    Natural varianti422 – 4221R → E in AEI; requires 2 nucleotide substitutions. 1 Publication
    Corresponds to variant rs59075499 [ dbSNP | Ensembl ].
    VAR_033145
    Natural varianti439 – 4391K → E in EHK; mild phenotype. 1 Publication
    Corresponds to variant rs61434181 [ dbSNP | Ensembl ].
    VAR_010510
    Natural varianti442 – 4421L → Q in EHK. 1 Publication
    Corresponds to variant rs58026994 [ dbSNP | Ensembl ].
    VAR_003833
    Natural varianti446 – 4461I → T in AEI. 1 Publication
    VAR_010511
    Natural varianti487 – 4871H → Y.4 Publications
    Corresponds to variant rs17855579 [ dbSNP | Ensembl ].
    VAR_060723

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04029 mRNA. Translation: AAA60544.1.
    X14487 Genomic DNA. Translation: CAA32649.1.
    AC090283 mRNA. No translation available.
    BC034697 mRNA. Translation: AAH34697.1.
    M19156 mRNA. Translation: AAA59468.1. Different initiation.
    L20218 Genomic DNA. Translation: AAB59438.1.
    L20219 Genomic DNA. Translation: AAB59439.1.
    M77663 mRNA. Translation: AAA59199.1.
    CCDSiCCDS11377.1.
    PIRiA31994.
    S02158. KRHU0.
    RefSeqiNP_000412.3. NM_000421.3.
    UniGeneiHs.99936.

    Genome annotation databases

    EnsembliENST00000269576; ENSP00000269576; ENSG00000186395.
    GeneIDi3858.
    KEGGihsa:3858.
    UCSCiuc002hvi.3. human.

    Polymorphism databases

    DMDMi269849769.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Human Intermediate Filament Mutation Database
    Wikipedia

    Keratin-10 entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04029 mRNA. Translation: AAA60544.1 .
    X14487 Genomic DNA. Translation: CAA32649.1 .
    AC090283 mRNA. No translation available.
    BC034697 mRNA. Translation: AAH34697.1 .
    M19156 mRNA. Translation: AAA59468.1 . Different initiation.
    L20218 Genomic DNA. Translation: AAB59438.1 .
    L20219 Genomic DNA. Translation: AAB59439.1 .
    M77663 mRNA. Translation: AAA59199.1 .
    CCDSi CCDS11377.1.
    PIRi A31994.
    S02158. KRHU0.
    RefSeqi NP_000412.3. NM_000421.3.
    UniGenei Hs.99936.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3ASW X-ray 2.60 B 473-487 [» ]
    4F1Z X-ray 2.30 Q 499-512 [» ]
    ProteinModelPortali P13645.
    SMRi P13645. Positions 145-287, 313-455.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110056. 51 interactions.
    IntActi P13645. 19 interactions.
    MINTi MINT-1132575.
    STRINGi 9606.ENSP00000269576.

    PTM databases

    PhosphoSitei P13645.

    Polymorphism databases

    DMDMi 269849769.

    2D gel databases

    REPRODUCTION-2DPAGE P13645.
    SWISS-2DPAGE P13645.

    Proteomic databases

    MaxQBi P13645.
    PaxDbi P13645.
    PeptideAtlasi P13645.
    PRIDEi P13645.
    ProMEXi P13645.

    Protocols and materials databases

    DNASUi 3858.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000269576 ; ENSP00000269576 ; ENSG00000186395 .
    GeneIDi 3858.
    KEGGi hsa:3858.
    UCSCi uc002hvi.3. human.

    Organism-specific databases

    CTDi 3858.
    GeneCardsi GC17M038974.
    HGNCi HGNC:6413. KRT10.
    HPAi CAB000132.
    HPA012014.
    MIMi 113800. phenotype.
    148080. gene.
    607602. phenotype.
    609165. phenotype.
    neXtProti NX_P13645.
    Orphaneti 281139. Annular epidermolytic ichthyosis.
    281190. Congenital reticular ichthyosiform erythroderma.
    312. Epidermolytic ichthyosis.
    PharmGKBi PA30200.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG147548.
    HOGENOMi HOG000230975.
    HOVERGENi HBG013015.
    InParanoidi P13645.
    KOi K07604.
    OMAi RYSSSKH.
    OrthoDBi EOG7FV3Q8.
    PhylomeDBi P13645.
    TreeFami TF332742.

    Miscellaneous databases

    GeneWikii Keratin_10.
    GenomeRNAii 3858.
    NextBioi 15181.
    PROi P13645.
    SOURCEi Search...

    Gene expression databases

    Bgeei P13645.
    CleanExi HS_KRT10.
    Genevestigatori P13645.

    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. "The complete sequence of the human intermediate filament chain keratin 10. Subdomainal divisions and model for folding of end domain sequences."
      Zhou X.M., Idler W.W., Steven A.C., Roop D.R., Steinert P.M.
      J. Biol. Chem. 263:15584-15589(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS SER-101 AND TYR-487.
      Tissue: Foreskin.
    2. "Identification of an orthologous mammalian cytokeratin gene. High degree of intron sequence conservation during evolution of human cytokeratin 10."
      Rieger M., Franke W.W.
      J. Mol. Biol. 204:841-856(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT TYR-487.
    3. "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].
    4. "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], VARIANTS SER-101 AND TYR-487.
      Tissue: Skin.
    5. "Sequence of a cDNA encoding human keratin No 10 selected according to structural homologies of keratins and their tissue-specific expression."
      Darmon M.Y., Semat A., Darmon M.C., Vasseur M.
      Mol. Biol. Rep. 12:277-283(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 130-584, VARIANT TYR-487.
    6. "Prenatal diagnosis of epidermolytic hyperkeratosis by direct gene sequencing."
      Rothnagel J.A., Longley M.A., Holder R.A., Kuster W., Roop D.R.
      J. Invest. Dermatol. 102:13-16(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 147-161, VARIANTS EHK HIS-156 AND ASN-160.
    7. "Identification of mutational hot spots in the suprabasal keratin genes from patients with epidermolytic hyperkeratosis."
      Rothnagel J.J., Dominey A., Fisher M., Axtell S., Pittelkow M., Anton-Lamprecht I., Hohl D., Roop D.
      Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 147-161, VARIANT EHK CYS-156.
    8. "Exons I and VII of the gene (Ker10) encoding human keratin 10 undergo structural rearrangements within repeats."
      Tkachenko A.V., Buchman V.L., Bliskovsky V.V., Shvets Y.P., Kisselev L.L.
      Gene 116:245-251(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 197-584.
    9. "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
      Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
      Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 180-184 AND 568-580.
      Tissue: Keratinocyte.
    10. "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-16 AND SER-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Mitotic recombination in patients with ichthyosis causes reversion of dominant mutations in KRT10."
      Choate K.A., Lu Y., Zhou J., Choi M., Elias P.M., Farhi A., Nelson-Williams C., Crumrine D., Williams M.L., Nopper A.J., Bree A., Milstone L.M., Lifton R.P.
      Science 330:94-97(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN CRIE.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "The genetic basis of epidermolytic hyperkeratosis: a disorder of differentiation-specific epidermal keratin genes."
      Cheng J., Syder A.J., Yu Q.-C., Letai A., Paller A.S., Fuchs E.
      Cell 70:811-819(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EHK HIS-156.
    14. "Extensive size polymorphism of the human keratin 10 chain resides in the C-terminal V2 subdomain due to variable numbers and sizes of glycine loops."
      Korge B.P., Gan S.-Q., McBridge O.W., Mischke D., Steinert P.M.
      Proc. Natl. Acad. Sci. U.S.A. 89:910-914(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS.
    15. "Mutations in the rod domains of keratins 1 and 10 in epidermolytic hyperkeratosis."
      Rothnagel J.A., Dominey A.M., Dempsey L.D., Longley M.A., Greenhalgh D.A., Gagne T.A., Huber M., Frenk E., Hohl D., Roop D.R.
      Science 257:1128-1130(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS EHK HIS-156 AND SER-161.
    16. "Preferential sites in keratin 10 that are mutated in epidermolytic hyperkeratosis."
      Chipev C.C., Yang J.-M., Digiovanna J.J., Steinert P.M., Marekov L., Compton J.G., Bale S.J.
      Am. J. Hum. Genet. 54:179-190(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS EHK HIS-154; CYS-156; HIS-156; ASP-160 AND GLN-442.
    17. "Genetic mutations in the K1 and K10 genes of patients with epidermolytic hyperkeratosis. Correlation between location and disease severity."
      Syder A.J., Yu Q.-C., Paller A.S., Giudice G., Pearson R., Fuchs E.
      J. Clin. Invest. 93:1533-1542(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS EHK ARG-150; CYS-156 AND GLU-439, VARIANT SER-126.
    18. "Mutations in the rod 1A domain of keratins 1 and 10 in bullous congenital ichthyosiform erythroderma (BCIE)."
      McLean W.H.I., Eady R.A.J., Dopping-Hepenstal P.J.C., McMillan J.R., Leigh I.M., Navsaria H.A., Higgins C., Harper J.I., Paige D.G., Morley S.M.
      J. Invest. Dermatol. 102:24-30(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS EHK PRO-156 AND SER-156.
    19. Cited for: VARIANT THR-150.
    20. "A novel dinucleotide mutation in keratin 10 in the annular epidermolytic ichthyosis variant of bullous congenital ichthyosiform erythroderma."
      Joh G.-Y., Traupe H., Metze D., Nashan D., Huber M., Hohl D., Longley M.A., Rothnagel J.A., Roop D.R.
      J. Invest. Dermatol. 108:357-361(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT AEI GLU-422.
    21. "A novel helix termination mutation in keratin 10 in annular epidermolytic ichthyosis, a variant of bullous congenital ichthyosiform erythroderma."
      Suga Y., Duncan K.O., Heald P.W., Roop D.R.
      J. Invest. Dermatol. 111:1220-1223(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT AEI THR-446.
    22. Cited for: VARIANT EHK SER-160.

    Entry informationi

    Entry nameiK1C10_HUMAN
    AccessioniPrimary (citable) accession number: P13645
    Secondary accession number(s): Q14664, Q8N175
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: November 24, 2009
    Last modified: October 1, 2014
    This is version 156 of the entry and version 6 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

    3D-structure, Complete proteome, Direct protein sequencing, 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3