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P04264

- K2C1_HUMAN

UniProt

P04264 - K2C1_HUMAN

Protein

Keratin, type II cytoskeletal 1

Gene

KRT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 179 (01 Oct 2014)
      Sequence version 6 (26 May 2009)
      Previous versions | rss
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    Functioni

    May regulate the activity of kinases such as PKC and SRC via binding to integrin beta-1 (ITB1) and the receptor of activated protein kinase C (RACK1/GNB2L1). In complex with C1QBP is a high affinity receptor for kininogen-1/HMWK.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei433 – 4331Stutter

    GO - Molecular functioni

    1. carbohydrate binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. receptor activity Source: UniProtKB
    4. structural molecule activity Source: InterPro

    GO - Biological processi

    1. complement activation, lectin pathway Source: UniProtKB
    2. fibrinolysis Source: UniProtKB
    3. regulation of angiogenesis Source: UniProtKB
    4. response to oxidative stress Source: UniProtKB
    5. retina homeostasis Source: UniProt

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Keratin, type II cytoskeletal 1
    Alternative name(s):
    67 kDa cytokeratin
    Cytokeratin-1
    Short name:
    CK-1
    Hair alpha protein
    Keratin-1
    Short name:
    K1
    Type-II keratin Kb1
    Gene namesi
    Name:KRT1
    Synonyms:KRTA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:6412. KRT1.

    Subcellular locationi

    Cell membrane 1 Publication
    Note: Located on plasma membrane of neuroblastoma NMB7 cells.

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. cytoskeleton Source: ProtInc
    3. extracellular space Source: UniProt
    4. extracellular vesicular exosome Source: UniProt
    5. keratin filament Source: Ensembl
    6. membrane Source: UniProtKB
    7. nucleus Source: UniProt
    8. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Intermediate filament, Keratin, Membrane

    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.11 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti155 – 1551V → D in EHK. 1 Publication
    VAR_017820
    Natural varianti155 – 1551V → G in EHK. 1 Publication
    Corresponds to variant rs57959072 [ dbSNP | Ensembl ].
    VAR_003853
    Natural varianti161 – 1611L → P in EHK. 1 Publication
    Corresponds to variant rs57695159 [ dbSNP | Ensembl ].
    VAR_003854
    Natural varianti186 – 1861S → P in EHK. 1 Publication
    Corresponds to variant rs60022878 [ dbSNP | Ensembl ].
    VAR_003855
    Natural varianti188 – 1881N → K in EHK. 1 Publication
    Corresponds to variant rs59429455 [ dbSNP | Ensembl ].
    VAR_017821
    Natural varianti188 – 1881N → S in EHK. 2 Publications
    Corresponds to variant rs58928370 [ dbSNP | Ensembl ].
    VAR_003856
    Natural varianti188 – 1881N → T in EHK; severe. 1 Publication
    VAR_017822
    Natural varianti193 – 1931S → P in EHK. 1 Publication
    Corresponds to variant rs60937700 [ dbSNP | Ensembl ].
    VAR_003857
    Natural varianti214 – 2141L → P in EHK. 1 Publication
    Corresponds to variant rs61549035 [ dbSNP | Ensembl ].
    VAR_017823
    Natural varianti340 – 3401D → V in EHK. 1 Publication
    Corresponds to variant rs58062863 [ dbSNP | Ensembl ].
    VAR_017824
    Natural varianti479 – 4791I → T in AEI and EHK. 2 Publications
    Corresponds to variant rs57837128 [ dbSNP | Ensembl ].
    VAR_017826
    Natural varianti482 – 4821Y → C in EHK. 1 Publication
    Corresponds to variant rs58420087 [ dbSNP | Ensembl ].
    VAR_017827
    Natural varianti486 – 4861L → P in EHK. 1 Publication
    Corresponds to variant rs56914602 [ dbSNP | Ensembl ].
    VAR_017828
    Natural varianti490 – 4901E → Q in EHK. 1 Publication
    Corresponds to variant rs60279707 [ dbSNP | Ensembl ].
    VAR_003861
    Ichthyosis hystrix, Curth-Macklin type (IHCM) [MIM:146590]: A genodermatosis with severe verrucous hyperkeratosis. Affected individuals manifest congenital verrucous black scale on the scalp, neck, and limbs with truncal erythema, palmoplantar keratoderma and keratoses on the lips, ears, nipples and buttocks.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Keratoderma, palmoplantar, non-epidermolytic (NEPPK) [MIM:600962]: A dermatological disorder characterized by well-demarcated hyperkeratosis is present over the palms and soles. A red band is frequently present at the periphery of the keratosis. It is usually non-transgredient, with a sharp demarcation of the lesions at the wrists.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti74 – 741K → I in NEPPK. 1 Publication
    Corresponds to variant rs57977969 [ dbSNP | Ensembl ].
    VAR_017819
    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 varianti479 – 4791I → F in AEI. 2 Publications
    Corresponds to variant rs61218439 [ dbSNP | Ensembl ].
    VAR_017825
    Natural varianti479 – 4791I → T in AEI and EHK. 2 Publications
    Corresponds to variant rs57837128 [ dbSNP | Ensembl ].
    VAR_017826
    Keratoderma, palmoplantar, striate 3 (SPPK3) [MIM:607654]: A dermatological disorder characterized by thickening of the stratum corneum and epidermal layers on palms and soles. There is no involvement of non-palmoplantar skin, and both hair and nails are normal.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Disease mutation, Ichthyosis, Palmoplantar keratoderma

    Organism-specific databases

    MIMi113800. phenotype.
    146590. phenotype.
    600962. phenotype.
    607602. phenotype.
    607654. phenotype.
    Orphaneti281139. Annular epidermolytic ichthyosis.
    312. Epidermolytic ichthyosis.
    2199. Epidermolytic palmoplantar keratoderma.
    79503. Ichthyosis hystrix of Curth-Macklin.
    50942. Keratosis palmoplantaris striata.
    PharmGKBiPA30199.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 644643Keratin, type II cytoskeletal 1PRO_0000063709Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei21 – 211Phosphoserine2 Publications
    Modified residuei66 – 661Phosphoserine2 Publications
    Modified residuei82 – 821Omega-N-methylarginine1 Publication
    Modified residuei276 – 2761N6,N6-dimethyllysine1 Publication
    Modified residuei344 – 3441Phosphoserine1 Publication

    Post-translational modificationi

    Undergoes deimination of some arginine residues (citrullination).2 Publications

    Keywords - PTMi

    Citrullination, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiP04264.
    PaxDbiP04264.
    PRIDEiP04264.
    ProMEXiP04264.

    2D gel databases

    REPRODUCTION-2DPAGEP04264.
    SWISS-2DPAGEP04264.

    PTM databases

    PhosphoSiteiP04264.

    Expressioni

    Tissue specificityi

    The source of this protein is neonatal foreskin. The 67-kDa type II keratins are expressed in terminally differentiating epidermis.

    Gene expression databases

    ArrayExpressiP04264.
    BgeeiP04264.
    CleanExiHS_KRT1.
    GenevestigatoriP04264.

    Organism-specific databases

    HPAiCAB002153.
    HPA017917.

    Interactioni

    Subunit structurei

    Heterotetramer of two type I and two type II keratins. Keratin-1 is generally associated with keratin-10. Interacts with ITGB1 in the presence of GNB2L1 and SRC, and with GNB2L1. Interacts with C1QBP; the association represents a cell surface kininogen receptor.2 Publications

    Protein-protein interaction databases

    BioGridi110046. 63 interactions.
    IntActiP04264. 19 interactions.
    MINTiMINT-4990403.
    STRINGi9606.ENSP00000252244.

    Structurei

    3D structure databases

    ProteinModelPortaliP04264.
    SMRiP04264. Positions 180-319, 346-488.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 179178HeadAdd
    BLAST
    Regioni180 – 489310RodAdd
    BLAST
    Regioni180 – 21536Coil 1AAdd
    BLAST
    Regioni216 – 23419Linker 1Add
    BLAST
    Regioni235 – 32692Coil 1BAdd
    BLAST
    Regioni327 – 35024Linker 12Add
    BLAST
    Regioni351 – 489139Coil 2Add
    BLAST
    Regioni490 – 644155TailAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi2 – 151150Gly/Phe/Ser-richAdd
    BLAST
    Compositional biasi502 – 641140Gly/Ser-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the intermediate filament family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG146769.
    HOGENOMiHOG000230976.
    HOVERGENiHBG013015.
    InParanoidiP04264.
    KOiK07605.
    OMAiTHISETN.
    OrthoDBiEOG7FV3Q8.
    PhylomeDBiP04264.
    TreeFamiTF317854.

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P04264-1 [UniParc]FASTAAdd to Basket

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    MSRQFSSRSG YRSGGGFSSG SAGIINYQRR TTSSSTRRSG GGGGRFSSCG    50
    GGGGSFGAGG GFGSRSLVNL GGSKSISISV ARGGGRGSGF GGGYGGGGFG 100
    GGGFGGGGFG GGGIGGGGFG GFGSGGGGFG GGGFGGGGYG GGYGPVCPPG 150
    GIQEVTINQS LLQPLNVEID PEIQKVKSRE REQIKSLNNQ FASFIDKVRF 200
    LEQQNQVLQT KWELLQQVDT STRTHNLEPY FESFINNLRR RVDQLKSDQS 250
    RLDSELKNMQ DMVEDYRNKY EDEINKRTNA ENEFVTIKKD VDGAYMTKVD 300
    LQAKLDNLQQ EIDFLTALYQ AELSQMQTQI SETNVILSMD NNRSLDLDSI 350
    IAEVKAQYED IAQKSKAEAE SLYQSKYEEL QITAGRHGDS VRNSKIEISE 400
    LNRVIQRLRS EIDNVKKQIS NLQQSISDAE QRGENALKDA KNKLNDLEDA 450
    LQQAKEDLAR LLRDYQELMN TKLALDLEIA TYRTLLEGEE SRMSGECAPN 500
    VSVSVSTSHT TISGGGSRGG GGGGYGSGGS SYGSGGGSYG SGGGGGGGRG 550
    SYGSGGSSYG SGGGSYGSGG GGGGHGSYGS GSSSGGYRGG SGGGGGGSSG 600
    GRGSGGGSSG GSIGGRGSSS GGVKSSGGSS SVKFVSTTYS GVTR 644
    Length:644
    Mass (Da):66,039
    Last modified:May 26, 2009 - v6
    Checksum:iCE5DDE97388F5017
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti201 – 2011L → M in AAA36153. (PubMed:2581964)Curated
    Sequence conflicti206 – 2061Q → K in AAA36153. (PubMed:2581964)Curated
    Sequence conflicti238 – 2381L → S in AAA36153. (PubMed:2581964)Curated
    Sequence conflicti344 – 3452SL → QF in AAA36153. (PubMed:2581964)Curated
    Sequence conflicti403 – 4031R → H in BAG36698. (PubMed:14702039)Curated
    Sequence conflicti404 – 4041V → M in AAA36153. (PubMed:2581964)Curated
    Sequence conflicti447 – 4471L → M in AAA36153. (PubMed:2581964)Curated
    Sequence conflicti463 – 4631R → C in AAA36153. (PubMed:2581964)Curated
    Sequence conflicti466 – 4661Q → H in AAA36153. (PubMed:2581964)Curated
    Sequence conflicti504 – 5041S → T in AAA36153. (PubMed:2581964)Curated
    Sequence conflicti511 – 5122TI → SM in AAA36153. (PubMed:2581964)Curated
    Sequence conflicti564 – 5641G → S in AAA36153. (PubMed:2581964)Curated
    Sequence conflicti613 – 6131I → S in AAA36153. (PubMed:2581964)Curated
    Sequence conflicti638 – 6381T → S in AAA36153. (PubMed:2581964)Curated

    Polymorphismi

    There are two size variants of KRT1, termed allele 1A and allele 1B with allelic frequencies of 0.61 and 0.39. Allele 1B lacks 7 residues compared to allele 1A.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti74 – 741K → I in NEPPK. 1 Publication
    Corresponds to variant rs57977969 [ dbSNP | Ensembl ].
    VAR_017819
    Natural varianti155 – 1551V → D in EHK. 1 Publication
    VAR_017820
    Natural varianti155 – 1551V → G in EHK. 1 Publication
    Corresponds to variant rs57959072 [ dbSNP | Ensembl ].
    VAR_003853
    Natural varianti161 – 1611L → P in EHK. 1 Publication
    Corresponds to variant rs57695159 [ dbSNP | Ensembl ].
    VAR_003854
    Natural varianti176 – 19722Missing in palmoplantar keratoderma; and mild ichthyosis largely limited to the flexural areas.
    VAR_038627Add
    BLAST
    Natural varianti186 – 1861S → P in EHK. 1 Publication
    Corresponds to variant rs60022878 [ dbSNP | Ensembl ].
    VAR_003855
    Natural varianti188 – 1881N → K in EHK. 1 Publication
    Corresponds to variant rs59429455 [ dbSNP | Ensembl ].
    VAR_017821
    Natural varianti188 – 1881N → S in EHK. 2 Publications
    Corresponds to variant rs58928370 [ dbSNP | Ensembl ].
    VAR_003856
    Natural varianti188 – 1881N → T in EHK; severe. 1 Publication
    VAR_017822
    Natural varianti193 – 1931S → P in EHK. 1 Publication
    Corresponds to variant rs60937700 [ dbSNP | Ensembl ].
    VAR_003857
    Natural varianti214 – 2141L → P in EHK. 1 Publication
    Corresponds to variant rs61549035 [ dbSNP | Ensembl ].
    VAR_017823
    Natural varianti312 – 3121I → V.
    VAR_003858
    Natural varianti330 – 3301I → T.
    VAR_003859
    Natural varianti340 – 3401D → V in EHK. 1 Publication
    Corresponds to variant rs58062863 [ dbSNP | Ensembl ].
    VAR_017824
    Natural varianti358 – 3581Y → N.2 Publications
    Corresponds to variant rs1050872 [ dbSNP | Ensembl ].
    VAR_003860
    Natural varianti454 – 4541A → S.
    Corresponds to variant rs17678945 [ dbSNP | Ensembl ].
    VAR_038628
    Natural varianti459 – 4668Missing in palmoplantar keratoderma; and mild ichthyosis largely limited to the flexural areas.
    VAR_038629
    Natural varianti479 – 4791I → F in AEI. 2 Publications
    Corresponds to variant rs61218439 [ dbSNP | Ensembl ].
    VAR_017825
    Natural varianti479 – 4791I → T in AEI and EHK. 2 Publications
    Corresponds to variant rs57837128 [ dbSNP | Ensembl ].
    VAR_017826
    Natural varianti482 – 4821Y → C in EHK. 1 Publication
    Corresponds to variant rs58420087 [ dbSNP | Ensembl ].
    VAR_017827
    Natural varianti486 – 4861L → P in EHK. 1 Publication
    Corresponds to variant rs56914602 [ dbSNP | Ensembl ].
    VAR_017828
    Natural varianti490 – 4901E → Q in EHK. 1 Publication
    Corresponds to variant rs60279707 [ dbSNP | Ensembl ].
    VAR_003861
    Natural varianti537 – 5371G → C.1 Publication
    VAR_003862
    Natural varianti560 – 5667Missing in allele 1B. 1 Publication
    VAR_003864
    Natural varianti633 – 6331K → R.5 Publications
    Corresponds to variant rs14024 [ dbSNP | Ensembl ].
    VAR_003863

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M98776 Genomic DNA. Translation: AAB47721.1.
    AF237621 Genomic DNA. Translation: AAF60327.1.
    AF304164 Genomic DNA. Translation: AAG41947.1.
    AK313986 mRNA. Translation: BAG36698.1.
    AC055716 Genomic DNA. No translation available.
    BC063697 mRNA. Translation: AAH63697.1.
    M10938 mRNA. Translation: AAA36153.1.
    CCDSiCCDS8836.1.
    PIRiA22940. KRHU2.
    RefSeqiNP_006112.3. NM_006121.3.
    UniGeneiHs.80828.

    Genome annotation databases

    EnsembliENST00000252244; ENSP00000252244; ENSG00000167768.
    GeneIDi3848.
    KEGGihsa:3848.
    UCSCiuc001sau.1. human.

    Polymorphism databases

    DMDMi238054406.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Human Intermediate Filament Mutation Database
    Wikipedia

    Keratin-1 entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M98776 Genomic DNA. Translation: AAB47721.1 .
    AF237621 Genomic DNA. Translation: AAF60327.1 .
    AF304164 Genomic DNA. Translation: AAG41947.1 .
    AK313986 mRNA. Translation: BAG36698.1 .
    AC055716 Genomic DNA. No translation available.
    BC063697 mRNA. Translation: AAH63697.1 .
    M10938 mRNA. Translation: AAA36153.1 .
    CCDSi CCDS8836.1.
    PIRi A22940. KRHU2.
    RefSeqi NP_006112.3. NM_006121.3.
    UniGenei Hs.80828.

    3D structure databases

    ProteinModelPortali P04264.
    SMRi P04264. Positions 180-319, 346-488.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110046. 63 interactions.
    IntActi P04264. 19 interactions.
    MINTi MINT-4990403.
    STRINGi 9606.ENSP00000252244.

    PTM databases

    PhosphoSitei P04264.

    Polymorphism databases

    DMDMi 238054406.

    2D gel databases

    REPRODUCTION-2DPAGE P04264.
    SWISS-2DPAGE P04264.

    Proteomic databases

    MaxQBi P04264.
    PaxDbi P04264.
    PRIDEi P04264.
    ProMEXi P04264.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000252244 ; ENSP00000252244 ; ENSG00000167768 .
    GeneIDi 3848.
    KEGGi hsa:3848.
    UCSCi uc001sau.1. human.

    Organism-specific databases

    CTDi 3848.
    GeneCardsi GC12M053069.
    H-InvDB HIX0036813.
    HGNCi HGNC:6412. KRT1.
    HPAi CAB002153.
    HPA017917.
    MIMi 113800. phenotype.
    139350. gene.
    146590. phenotype.
    600962. phenotype.
    607602. phenotype.
    607654. phenotype.
    neXtProti NX_P04264.
    Orphaneti 281139. Annular epidermolytic ichthyosis.
    312. Epidermolytic ichthyosis.
    2199. Epidermolytic palmoplantar keratoderma.
    79503. Ichthyosis hystrix of Curth-Macklin.
    50942. Keratosis palmoplantaris striata.
    PharmGKBi PA30199.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG146769.
    HOGENOMi HOG000230976.
    HOVERGENi HBG013015.
    InParanoidi P04264.
    KOi K07605.
    OMAi THISETN.
    OrthoDBi EOG7FV3Q8.
    PhylomeDBi P04264.
    TreeFami TF317854.

    Miscellaneous databases

    GeneWikii Keratin_1.
    GenomeRNAii 3848.
    NextBioi 15141.
    PROi P04264.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P04264.
    Bgeei P04264.
    CleanExi HS_KRT1.
    Genevestigatori P04264.

    Family and domain databases

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

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASN-358 AND ARG-633.
    2. "Genomic organization and amplification of the human epidermal type II keratin genes K1 and K5."
      Whittock N.V., Eady R.A.J., McGrath J.A.
      Biochem. Biophys. Res. Commun. 274:149-152(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASN-358 AND ARG-633.
    3. "Novel splice site mutation in keratin 1 underlies mild epidermolytic palmoplantar keratoderma in three kindreds."
      Hatsell S.J., Eady R.A.J., Wennerstrand L., Dopping-Hepenstal P.J., Leigh I.M., Munro C., Kelsell D.P.
      J. Invest. Dermatol. 116:606-609(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INVOLVEMENT IN NEPPK, VARIANT ARG-633.
    4. "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.
    5. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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], VARIANT ARG-633.
      Tissue: Skin.
    7. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-8.
      Tissue: Platelet.
    8. Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 13-30; 66-82; 186-240; 258-276; 278-298; 344-355; 365-386; 396-403; 408-416; 418-432; 442-455 AND 461-588, METHYLATION AT ARG-82 AND LYS-276, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Ovarian carcinoma.
    9. "Amino acid sequences of mouse and human epidermal type II keratins of Mr 67,000 provide a systematic basis for the structural and functional diversity of the end domains of keratin intermediate filament subunits."
      Steinert P.M., Parry D.A.D., Idler W.W., Johnson L.D., Steven A.C., Roop D.R.
      J. Biol. Chem. 260:7142-7149(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] OF 152-644, VARIANTS CYS-537 AND ARG-633.
    10. Lubec G., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 377-386, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Fetal brain cortex.
    11. "Preferential deimination of keratin K1 and filaggrin during the terminal differentiation of human epidermis."
      Senshu T., Kan S., Ogawa H., Manabe M., Asaga H.
      Biochem. Biophys. Res. Commun. 225:712-719(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: CITRULLINATION.
    12. "Evidence for novel functions of the keratin tail emerging from a mutation causing ichthyosis hystrix."
      Sprecher E., Ishida-Yamamoto A., Becker O.M., Marekov L.N., Miller C.J., Steinert P.M., Neldner K., Richard G.
      J. Invest. Dermatol. 116:511-519(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN IHCM.
    13. "Sequential reorganization of cornified cell keratin filaments involving filaggrin-mediated compaction and keratin 1 deimination."
      Ishida-Yamamoto A., Senshu T., Eady R.A.J., Takahashi H., Shimizu H., Akiyama M., Iizuka H.
      J. Invest. Dermatol. 118:282-287(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: CITRULLINATION.
    14. "Frameshift mutation in the V2 domain of human keratin 1 results in striate palmoplantar keratoderma."
      Whittock N.V., Smith F.J., Wan H., Mallipeddi R., Griffiths W.A.D., Dopping-Hepenstal P.J., Ashton G.H.S., Eady R.A.J., McLean W.H.I., McGrath J.A.
      J. Invest. Dermatol. 118:838-844(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN SPPK3.
    15. "Interaction of integrin beta1 with cytokeratin 1 in neuroblastoma NMB7 cells."
      Chuang N.N., Huang C.C.
      Biochem. Soc. Trans. 35:1292-1294(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH GNB2L1 AND ITGB1, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    16. "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-66, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    18. "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-21; SER-66 AND SER-344, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Interaction of high-molecular-weight kininogen with endothelial cell binding proteins suPAR, gC1qR and cytokeratin 1 determined by surface plasmon resonance (BiaCore)."
      Pixley R.A., Espinola R.G., Ghebrehiwet B., Joseph K., Kao A., Bdeir K., Cines D.B., Colman R.W.
      Thromb. Haemost. 105:1053-1059(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH C1QBP.
    21. "A leucine-->proline mutation in the H1 subdomain of keratin 1 causes epidermolytic hyperkeratosis."
      Chipev C.C., Korge B.P., Markova N., Bale S.J., Digiovanna J.J., Compton J.G., Steinert P.M.
      Cell 70:821-828(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EHK PRO-161.
    22. "The two size alleles of human keratin 1 are due to a deletion in the glycine-rich carboxyl-terminal V2 subdomain."
      Korge B.P., Compton J.G., Steinert P.M., Mischke D.
      J. Invest. Dermatol. 99:697-702(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ALLELE 1B 560-GLY--TYR-566 DEL.
    23. "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: VARIANT EHK GLN-490.
    24. "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: VARIANT EHK CYS-482.
    25. "Mutations in the H1 and 1A domains in the keratin 1 gene in epidermolytic hyperkeratosis."
      Yang J.-M., Chipev C.C., Digiovanna J.J., Bale S.J., Marekov L.N., Steinert P.M., Compton J.G.
      J. Invest. Dermatol. 102:17-23(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS EHK GLY-155; SER-188 AND PRO-193.
    26. "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-186 AND SER-188.
    27. "A mutation in the V1 end domain of keratin 1 in non-epidermolytic palmar-plantar keratoderma."
      Kimonis V., DiGiovanna J.J., Yang J.-M., Doyle S.Z., Bale S.J., Compton J.G.
      J. Invest. Dermatol. 103:764-769(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT NEPPK ILE-74.
    28. "An atypical form of bullous congenital ichthyosiform erythroderma is caused by a mutation in the L12 linker region of keratin 1."
      Kremer H., Lavrijsen A.P., McLean W.H.I., Lane E.B., Melchers D., Ruiter D.J., Mariman E.C., Steijlen P.M.
      J. Invest. Dermatol. 111:1224-1226(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EHK VAL-340.
    29. "Cyclic ichthyosis with epidermolytic hyperkeratosis: a phenotype conferred by mutations in the 2B domain of keratin K1."
      Sybert V.P., Francis J.S., Corden L.D., Smith L.T., Weaver M., Stephens K., McLean W.H.I.
      Am. J. Hum. Genet. 64:732-738(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS AEI PHE-479 AND THR-479.
    30. "An asparagine to threonine substitution in the 1A domain of keratin 1: a novel mutation that causes epidermolytic hyperkeratosis."
      Arin M.J., Longley M.A., Kuster W., Huber M., Hohl D., Rothnagel J.A., Roop D.R.
      Exp. Dermatol. 8:124-127(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EHK THR-188.
    31. "Epidermolytic hyperkeratosis with polycyclic psoriasiform plaques resulting from a mutation in the keratin 1 gene."
      Michael E.J., Schneiderman P., Grossman M.E., Christiano A.M.
      Exp. Dermatol. 8:501-503(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT AEI PHE-479.
    32. "Epidermolytic hyperkeratosis in a Hispanic family resulting from a mutation in the keratin 1 gene."
      Cserhalmi-Friedman P.B., Squeo R., Gordon D., Garzon M., Schneiderman P., Grossman M.E., Christiano A.M.
      Clin. Exp. Dermatol. 25:241-243(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EHK PRO-214.
    33. "Identification of a novel mutation in keratin 1 in a family with epidermolytic hyperkeratosis."
      Arin M.J., Longley M.A., Epstein E.H. Jr., Rothnagel J.A., Roop D.R.
      Exp. Dermatol. 9:16-19(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EHK THR-479.
    34. "New mutations in keratin 1 that cause bullous congenital ichthyosiform erythroderma and keratin 2e that cause ichthyosis bullosa of Siemens."
      Whittock N.V., Ashton G.H.S., Griffiths W.A.D., Eady R.A.J., McGrath J.A.
      Br. J. Dermatol. 145:330-335(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EHK ASP-155.
    35. "Two cases of primarily palmoplantar keratoderma associated with novel mutations in keratin 1."
      Terron-Kwiatkowski A., Paller A.S., Compton J., Atherton D.J., McLean W.H., Irvine A.D.
      J. Invest. Dermatol. 119:966-971(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PALMOPLANTAR KERATODERMA VAL-176--LYS-197 DEL AND ALA-459--466-GLN DEL.
    36. "Two novel mutations in the keratin 1 gene in epidermolytic hyperkeratosis."
      Lee D.-Y., Ahn K.-S., Lee C.-H., Rho N.-K., Lee J.-H., Lee E.-S., Steinert P.M., Yang J.-M.
      J. Invest. Dermatol. 119:976-977(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS EHK LYS-188 AND PRO-486.

    Entry informationi

    Entry nameiK2C1_HUMAN
    AccessioniPrimary (citable) accession number: P04264
    Secondary accession number(s): B2RA01
    , Q14720, Q6GSJ0, Q9H298
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 20, 1987
    Last sequence update: May 26, 2009
    Last modified: October 1, 2014
    This is version 179 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3