Essential maintenance is planned to begin on Fri Jan 24 2025. The website may be temporarily unavailable. Please use our fallback: https://wwwdev.ebi.ac.uk/uniprot/front-end/fallback/ in case of any outage.

P04104 · K2C1_MOUSE

  • Protein
    Keratin, type II cytoskeletal 1
  • Gene
    Krt1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

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

Miscellaneous

There are two types of cytoskeletal and microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).

Features

Showing features for site.

163750100150200250300350400450500550600
TypeIDPosition(s)Description
Site452Stutter

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcollagen-containing extracellular matrix
Cellular Componentcornified envelope
Cellular Componentcytoplasm
Cellular Componentkeratin filament
Molecular Functioncarbohydrate binding
Molecular Functionprotein heterodimerization activity
Molecular Functionstructural constituent of skin epidermis
Biological Processcomplement activation, lectin pathway
Biological Processestablishment of skin barrier
Biological Processnegative regulation of inflammatory response
Biological Processpeptide cross-linking
Biological Processprotein heterotetramerization

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Keratin, type II cytoskeletal 1
  • Alternative names
    • 67 kDa cytokeratin
    • Cytokeratin-1 (CK-1)
    • Keratin-1 (K1)
    • Type-II keratin Kb1

Gene names

    • Name
      Krt1
    • Synonyms
      Krt2-1

Organism names

  • Taxonomic identifier
  • Strains
    • C57BL/6J
    • OF1
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    P04104
  • Secondary accessions
    • Q149E0
    • Q9D2K8

Proteomes

Organism-specific databases

Phenotypes & Variants

Involvement in disease

  • 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

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variant194in EHK

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 24 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_00000637101-637Keratin, type II cytoskeletal 1
Modified residue12Omega-N-methylarginine
Modified residue21Phosphoserine
Modified residue24Phosphoserine
Modified residue49Omega-N-methylarginine
Modified residue67Phosphoserine
Modified residue284N6,N6-dimethyllysine
Modified residue352Phosphoserine
Modified residue526Omega-N-methylarginine
Modified residue585Omega-N-methylarginine
Modified residue607Omega-N-methylarginine

Post-translational modification

Undergoes deimination of some arginine residues (citrullination).

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in the infundibular regions of the ear, the interfollicular epidermis of the back, in the interscale regions containing hair follicles in the tail, and in the soles of the footpads (at protein level).

Developmental stage

Expressed in the skin at birth.

Gene expression databases

Interaction

Subunit

Heterotetramer of two type I and two type II keratins (PubMed:11408584, PubMed:24940650).
Heterodimer with KRT10 (PubMed:24940650).
Two heterodimers of KRT1 and KRT10 form a heterotetramer (By similarity).
Forms a heterodimer with KRT14; the interaction is more abundant in the absence of KRT5 (PubMed:11408584).
Interacts with PLEC isoform 1C, when in a heterodimer with KRT10 (PubMed:24940650).
Interacts with ITGB1 in the presence of RACK1 and SRC, and with RACK1 (By similarity).
Interacts with C1QBP; the association represents a cell surface kininogen receptor (By similarity).
Interacts with EPPK1; interaction is dependent of higher-order structure of intermediate filament (By similarity).

Complex viewer

View interactors in UniProtKB
View CPX-5871 in Complex Portal

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, coiled coil, domain, compositional bias.

Type
IDPosition(s)Description
Region1-187Head
Coiled coil180-328
Region188-223Coil 1A
Domain188-501IF rod
Region224-243Linker 1
Region244-334Coil 1B
Region335-358Linker 12
Region359-497Coil 2
Coiled coil397-483
Region498-637Tail
Compositional bias505-528Polar residues
Region505-533Disordered
Region563-637Disordered
Compositional bias595-637Polar residues

Sequence similarities

Belongs to the intermediate filament family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    637
  • Mass (Da)
    65,606
  • Last updated
    2007-02-20 v4
  • MD5 Checksum
    492B3A2C5664155F5A154F3E759C1384
MSLQCSSRSLCRGGGGSRNFSSGSAGLVSFQRRSTSSSMRRSGGGGGGRFSGGGFCGSSGSGFGSKSLMNLGGGRSISKSVAGGGGSFCGGFGGGSYGGGGFGGGSYGGGGFGGGSFGGGGFGGSGFGGGLGGGGGFGSGGGFGGGRFGSMGPVCPPGGIQEVTINQSLLQPLNVEVDPQIQKVKSQEREQIKSLNDKFASFIDKVRFLEQQNQVLQTKWELLQQVDTTTRTQNLDPFFENYISILRRKVDSLKSDQSRMDSELKNMQDLVEEYRTKYEDEINKRTNAENEFVTIKKDVDSAYMTKVELQAKADALQQDIDFFSALYQMEMSQMQTQISETNVVLSMDNNRSLDLDGIISEVKAQYDSICQRSKAEAETFYQSKYEELQITAGKHGDSVRNTKMEISELNRMIQRLRSEIDGCKKQISQIQQNINDAEQRGEKALKDAQNKLNEIEDALSQCKEDLARLLRDFQELMNTKLALDMEIATYKKLLEGEEIRMSGECTPNVSVSVSTSHTSMSGSSSRGGGSGGGRYGGGGSYGGGSGGGSYGGSSGGGGSGGSYGGGSGGGSYGGGSGGGSSGSHRGGSGGGGGSSGGSYGGSSGGGRGGSSSGGGGVKSSGSSTVKFVSTSYSRGTK

Features

Showing features for sequence conflict, compositional bias.

Type
IDPosition(s)Description
Sequence conflict99in Ref. 1; AAD05191
Sequence conflict131in Ref. 1; AAD05191
Sequence conflict147in Ref. 3; BAB31776
Sequence conflict150-151in Ref. 1; AAD05191
Sequence conflict156-158in Ref. 1; AAD05191
Sequence conflict165in Ref. 1; AAD05191
Sequence conflict176in Ref. 1; AAD05191
Sequence conflict214in Ref. 1; AAD05191
Sequence conflict261in Ref. 1; AAD05191
Sequence conflict313in Ref. 1; AAD05191
Sequence conflict321in Ref. 1; AAD05191
Sequence conflict325in Ref. 1; AAD05191
Sequence conflict352-353in Ref. 1; AAD05191
Sequence conflict428in Ref. 3; BAB31776
Compositional bias505-528Polar residues
Sequence conflict572-580in Ref. 1; AAD05191
Compositional bias595-637Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M10937
EMBL· GenBank· DDBJ
AAD05191.1
EMBL· GenBank· DDBJ
mRNA
AK019521
EMBL· GenBank· DDBJ
BAB31776.1
EMBL· GenBank· DDBJ
mRNA
BC117842
EMBL· GenBank· DDBJ
AAI17843.1
EMBL· GenBank· DDBJ
mRNA
BC117843
EMBL· GenBank· DDBJ
AAI17844.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any 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. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help