P04104 · K2C1_MOUSE
- ProteinKeratin, type II cytoskeletal 1
- GeneKrt1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids637 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Site | 452 | Stutter | |||
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | collagen-containing extracellular matrix | |
Cellular Component | cornified envelope | |
Cellular Component | cytoplasm | |
Cellular Component | keratin filament | |
Molecular Function | carbohydrate binding | |
Molecular Function | protein heterodimerization activity | |
Molecular Function | structural constituent of skin epidermis | |
Biological Process | complement activation, lectin pathway | |
Biological Process | establishment of skin barrier | |
Biological Process | negative regulation of inflammatory response | |
Biological Process | peptide cross-linking | |
Biological Process | protein heterotetramerization |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameKeratin, type II cytoskeletal 1
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP04104
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Involvement in disease
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Natural variant | 194 | in 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.
Keywords
- Disease
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000063710 | 1-637 | Keratin, type II cytoskeletal 1 | ||
Modified residue | 12 | Omega-N-methylarginine | |||
Modified residue | 21 | Phosphoserine | |||
Modified residue | 24 | Phosphoserine | |||
Modified residue | 49 | Omega-N-methylarginine | |||
Modified residue | 67 | Phosphoserine | |||
Modified residue | 284 | N6,N6-dimethyllysine | |||
Modified residue | 352 | Phosphoserine | |||
Modified residue | 526 | Omega-N-methylarginine | |||
Modified residue | 585 | Omega-N-methylarginine | |||
Modified residue | 607 | Omega-N-methylarginine | |||
Post-translational modification
Undergoes deimination of some arginine residues (citrullination).
Keywords
- PTM
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).
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
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, coiled coil, domain, compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-187 | Head | |||
Coiled coil | 180-328 | ||||
Region | 188-223 | Coil 1A | |||
Domain | 188-501 | IF rod | |||
Region | 224-243 | Linker 1 | |||
Region | 244-334 | Coil 1B | |||
Region | 335-358 | Linker 12 | |||
Region | 359-497 | Coil 2 | |||
Coiled coil | 397-483 | ||||
Region | 498-637 | Tail | |||
Compositional bias | 505-528 | Polar residues | |||
Region | 505-533 | Disordered | |||
Region | 563-637 | Disordered | |||
Compositional bias | 595-637 | Polar residues | |||
Sequence similarities
Belongs to the intermediate filament family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length637
- Mass (Da)65,606
- Last updated2007-02-20 v4
- MD5 Checksum492B3A2C5664155F5A154F3E759C1384
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Sequence conflict | 99 | in Ref. 1; AAD05191 | |||
Sequence conflict | 131 | in Ref. 1; AAD05191 | |||
Sequence conflict | 147 | in Ref. 3; BAB31776 | |||
Sequence conflict | 150-151 | in Ref. 1; AAD05191 | |||
Sequence conflict | 156-158 | in Ref. 1; AAD05191 | |||
Sequence conflict | 165 | in Ref. 1; AAD05191 | |||
Sequence conflict | 176 | in Ref. 1; AAD05191 | |||
Sequence conflict | 214 | in Ref. 1; AAD05191 | |||
Sequence conflict | 261 | in Ref. 1; AAD05191 | |||
Sequence conflict | 313 | in Ref. 1; AAD05191 | |||
Sequence conflict | 321 | in Ref. 1; AAD05191 | |||
Sequence conflict | 325 | in Ref. 1; AAD05191 | |||
Sequence conflict | 352-353 | in Ref. 1; AAD05191 | |||
Sequence conflict | 428 | in Ref. 3; BAB31776 | |||
Compositional bias | 505-528 | Polar residues | |||
Sequence conflict | 572-580 | in Ref. 1; AAD05191 | |||
Compositional bias | 595-637 | Polar residues | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |