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P04104

- K2C1_MOUSE

UniProt

P04104 - K2C1_MOUSE

Protein

Keratin, type II cytoskeletal 1

Gene

Krt1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 4 (20 Feb 2007)
      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). activated protein kinase C (RACK1/GNB2L1). In complex with C1QBP is a high affinity receptor for kininogen-1/HMWK By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei452 – 4521Stutter

    GO - Molecular functioni

    1. carbohydrate binding Source: Ensembl
    2. structural molecule activity Source: InterPro

    GO - Biological processi

    1. complement activation, lectin pathway Source: Ensembl
    2. establishment of skin barrier Source: MGI
    3. negative regulation of inflammatory response Source: MGI

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Keratin, type II cytoskeletal 1
    Alternative name(s):
    67 kDa cytokeratin
    Cytokeratin-1
    Short name:
    CK-1
    Keratin-1
    Short name:
    K1
    Type-II keratin Kb1
    Gene namesi
    Name:Krt1
    Synonyms:Krt2-1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 15

    Organism-specific databases

    MGIiMGI:96698. Krt1.

    Subcellular locationi

    Cell membrane By similarity

    GO - Cellular componenti

    1. keratin filament Source: MGI
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Intermediate filament, Keratin, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Defects in Krt1 are a cause of epidermolytic hyperkeratosis (EHK); also known as bullous congenital ichthyosiform erythroderma (BIE). EHK is a hereditary skin disorder characterized by intraepidermal blistering, a marked thickening of the stratum corneum, pigmentation of the skin and erosions at sites of trauma which are all present from birth.

    Keywords - Diseasei

    Disease mutation

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 637636Keratin, type II cytoskeletal 1PRO_0000063710Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei24 – 241PhosphoserineBy similarity
    Modified residuei67 – 671PhosphoserineBy similarity
    Modified residuei284 – 2841N6,N6-dimethyllysineBy similarity
    Modified residuei352 – 3521PhosphoserineBy similarity

    Post-translational modificationi

    Undergoes deimination of some arginine residues (citrullination).1 Publication

    Keywords - PTMi

    Citrullination, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiP04104.
    PaxDbiP04104.
    PRIDEiP04104.

    2D gel databases

    SWISS-2DPAGEP04104.

    PTM databases

    PhosphoSiteiP04104.

    Expressioni

    Gene expression databases

    BgeeiP04104.
    CleanExiMM_KRT1.
    GenevestigatoriP04104.

    Interactioni

    Subunit structurei

    Heterotetramer of two type I and two type II keratins. Keratin-1 is generally associated with keratin-10. Interacts with ITB1 in the presence of GNB2L1 and SRC, and with GNB2L1 Interacts with C1QBP; the association represents a cell surface kininogen receptor By similarity.By similarity

    Protein-protein interaction databases

    BioGridi201030. 11 interactions.
    IntActiP04104. 2 interactions.
    MINTiMINT-1865848.

    Structurei

    3D structure databases

    ProteinModelPortaliP04104.
    SMRiP04104. Positions 186-327, 354-496.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 187186HeadAdd
    BLAST
    Regioni188 – 497310RodAdd
    BLAST
    Regioni188 – 22336Coil 1AAdd
    BLAST
    Regioni224 – 24320Linker 1Add
    BLAST
    Regioni244 – 33491Coil 1BAdd
    BLAST
    Regioni335 – 35824Linker 12Add
    BLAST
    Regioni359 – 497139Coil 2Add
    BLAST
    Regioni498 – 637140TailAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili180 – 328149Sequence AnalysisAdd
    BLAST
    Coiled coili397 – 48387Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi13 – 159147Gly-richAdd
    BLAST
    Compositional biasi522 – 621100Gly-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the intermediate filament family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG146769.
    GeneTreeiENSGT00730000110687.
    HOGENOMiHOG000230976.
    HOVERGENiHBG013015.
    InParanoidiP04104.
    KOiK07605.
    OMAiTHISETN.
    OrthoDBiEOG7FV3Q8.
    PhylomeDBiP04104.
    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.

    P04104-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSLQCSSRSL CRGGGGSRNF SSGSAGLVSF QRRSTSSSMR RSGGGGGGRF    50
    SGGGFCGSSG SGFGSKSLMN LGGGRSISKS VAGGGGSFCG GFGGGSYGGG 100
    GFGGGSYGGG GFGGGSFGGG GFGGSGFGGG LGGGGGFGSG GGFGGGRFGS 150
    MGPVCPPGGI QEVTINQSLL QPLNVEVDPQ IQKVKSQERE QIKSLNDKFA 200
    SFIDKVRFLE QQNQVLQTKW ELLQQVDTTT RTQNLDPFFE NYISILRRKV 250
    DSLKSDQSRM DSELKNMQDL VEEYRTKYED EINKRTNAEN EFVTIKKDVD 300
    SAYMTKVELQ AKADALQQDI DFFSALYQME MSQMQTQISE TNVVLSMDNN 350
    RSLDLDGIIS EVKAQYDSIC QRSKAEAETF YQSKYEELQI TAGKHGDSVR 400
    NTKMEISELN RMIQRLRSEI DGCKKQISQI QQNINDAEQR GEKALKDAQN 450
    KLNEIEDALS QCKEDLARLL RDFQELMNTK LALDMEIATY KKLLEGEEIR 500
    MSGECTPNVS VSVSTSHTSM SGSSSRGGGS GGGRYGGGGS YGGGSGGGSY 550
    GGSSGGGGSG GSYGGGSGGG SYGGGSGGGS SGSHRGGSGG GGGSSGGSYG 600
    GSSGGGRGGS SSGGGGVKSS GSSTVKFVST SYSRGTK 637
    Length:637
    Mass (Da):65,606
    Last modified:February 20, 2007 - v4
    Checksum:iD2016D15066FD0A5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti99 – 991G → R in AAD05191. (PubMed:2581964)Curated
    Sequence conflicti131 – 1311L → S in AAD05191. (PubMed:2581964)Curated
    Sequence conflicti147 – 1471R → T in BAB31776. (PubMed:16141072)Curated
    Sequence conflicti150 – 1512SM → GY in AAD05191. (PubMed:2581964)Curated
    Sequence conflicti156 – 1583PPG → SPS in AAD05191. (PubMed:2581964)Curated
    Sequence conflicti165 – 1651I → L in AAD05191. (PubMed:2581964)Curated
    Sequence conflicti176 – 1761E → K in AAD05191. (PubMed:2581964)Curated
    Sequence conflicti214 – 2141Q → K in AAD05191. (PubMed:2581964)Curated
    Sequence conflicti261 – 2611D → E in AAD05191. (PubMed:2581964)Curated
    Sequence conflicti313 – 3131A → R in AAD05191. (PubMed:2581964)Curated
    Sequence conflicti321 – 3211D → N in AAD05191. (PubMed:2581964)Curated
    Sequence conflicti325 – 3251A → T in AAD05191. (PubMed:2581964)Curated
    Sequence conflicti352 – 3532SL → QF in AAD05191. (PubMed:2581964)Curated
    Sequence conflicti428 – 4281S → Y in BAB31776. (PubMed:16141072)Curated
    Sequence conflicti572 – 5809Missing in AAD05191. (PubMed:2581964)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti194 – 1941S → P in EHK. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M10937 mRNA. Translation: AAD05191.1.
    AK019521 mRNA. Translation: BAB31776.1.
    BC117842 mRNA. Translation: AAI17843.1.
    BC117843 mRNA. Translation: AAI17844.1.
    CCDSiCCDS37221.1.
    PIRiA02951. KRMS2.
    RefSeqiNP_032499.2. NM_008473.2.
    UniGeneiMm.183137.

    Genome annotation databases

    EnsembliENSMUST00000023790; ENSMUSP00000023790; ENSMUSG00000046834.
    GeneIDi16678.
    KEGGimmu:16678.
    UCSCiuc007xuc.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M10937 mRNA. Translation: AAD05191.1 .
    AK019521 mRNA. Translation: BAB31776.1 .
    BC117842 mRNA. Translation: AAI17843.1 .
    BC117843 mRNA. Translation: AAI17844.1 .
    CCDSi CCDS37221.1.
    PIRi A02951. KRMS2.
    RefSeqi NP_032499.2. NM_008473.2.
    UniGenei Mm.183137.

    3D structure databases

    ProteinModelPortali P04104.
    SMRi P04104. Positions 186-327, 354-496.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201030. 11 interactions.
    IntActi P04104. 2 interactions.
    MINTi MINT-1865848.

    PTM databases

    PhosphoSitei P04104.

    2D gel databases

    SWISS-2DPAGE P04104.

    Proteomic databases

    MaxQBi P04104.
    PaxDbi P04104.
    PRIDEi P04104.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000023790 ; ENSMUSP00000023790 ; ENSMUSG00000046834 .
    GeneIDi 16678.
    KEGGi mmu:16678.
    UCSCi uc007xuc.1. mouse.

    Organism-specific databases

    CTDi 3848.
    MGIi MGI:96698. Krt1.

    Phylogenomic databases

    eggNOGi NOG146769.
    GeneTreei ENSGT00730000110687.
    HOGENOMi HOG000230976.
    HOVERGENi HBG013015.
    InParanoidi P04104.
    KOi K07605.
    OMAi THISETN.
    OrthoDBi EOG7FV3Q8.
    PhylomeDBi P04104.
    TreeFami TF317854.

    Miscellaneous databases

    ChiTaRSi KRT1. mouse.
    NextBioi 290417.
    PROi P04104.
    SOURCEi Search...

    Gene expression databases

    Bgeei P04104.
    CleanExi MM_KRT1.
    Genevestigatori P04104.

    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. "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: NUCLEOTIDE SEQUENCE [MRNA].
    2. Roop D.R.
      Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Head.
    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].
    5. Lubec G., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 199-205; 208-219 AND 286-296, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: OF1.
      Tissue: Hippocampus.
    6. "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.
    7. "A mouse keratin 1 mutation causes dark skin and epidermolytic hyperkeratosis."
      McGowan K.A., Aradhya S., Fuchs H., de Angelis M.H., Barsh G.S.
      J. Invest. Dermatol. 126:1013-1016(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EHK PRO-194.

    Entry informationi

    Entry nameiK2C1_MOUSE
    AccessioniPrimary (citable) accession number: P04104
    Secondary accession number(s): Q149E0, Q9D2K8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1986
    Last sequence update: February 20, 2007
    Last modified: October 1, 2014
    This is version 128 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3