P35908 · K22E_HUMAN
- ProteinKeratin, type II cytoskeletal 2 epidermal
- GeneKRT2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids639 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Probably contributes to terminal cornification (PubMed:1380918).
Associated with keratinocyte activation, proliferation and keratinization (PubMed:12598329).
Required for maintenance of corneocytes and keratin filaments in suprabasal keratinocytes in the epidermis of the ear, potentially via moderation of expression and localization of keratins and their partner proteins (By similarity).
Plays a role in the establishment of the epidermal barrier on plantar skin (By similarity).
Associated with keratinocyte activation, proliferation and keratinization (PubMed:12598329).
Required for maintenance of corneocytes and keratin filaments in suprabasal keratinocytes in the epidermis of the ear, potentially via moderation of expression and localization of keratins and their partner proteins (By similarity).
Plays a role in the establishment of the epidermal barrier on plantar skin (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 | 429 | Stutter | ||||
Sequence: Q |
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 | cornified envelope | |
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | extracellular exosome | |
Cellular Component | extracellular space | |
Cellular Component | intermediate filament | |
Cellular Component | keratin filament | |
Cellular Component | membrane | |
Cellular Component | nucleus | |
Molecular Function | cytoskeletal protein binding | |
Molecular Function | structural constituent of cytoskeleton | |
Molecular Function | structural constituent of skin epidermis | |
Biological Process | epidermis development | |
Biological Process | intermediate filament organization | |
Biological Process | keratinization | |
Biological Process | keratinocyte activation | |
Biological Process | keratinocyte development | |
Biological Process | keratinocyte migration | |
Biological Process | keratinocyte proliferation | |
Biological Process | peptide cross-linking | |
Biological Process | positive regulation of epidermis development |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameKeratin, type II cytoskeletal 2 epidermal
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP35908
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Ichthyosis bullosa of Siemens (IBS)
- Note
- DescriptionA rare autosomal dominant skin disorder displaying a type of epidermolytic hyperkeratosis characterized by generalized erythema and extensive blistering from birth. Large, dark gray hyperkeratoses are observed in later weeks. The skin of IBS patients is unusually fragile and has a tendency to shed the outer layers of the epidermis, producing localized denuded areas (molting effect). IBS usually improves with age so that in most middle-aged patients the hyperkeratosis and keratotic lichenification is limited to the flexural folds of the major joints.
- See alsoMIM:146800
Natural variants in IBS
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_086330 | 178 | E>K | in IBS; uncertain significance; dbSNP:rs57728941 | |
VAR_003865 | 181 | Q>P | in IBS; dbSNP:rs57510142 | |
VAR_010514 | 182 | I>N | in IBS; dbSNP:rs61622714 | |
VAR_010515 | 186 | N>D | in IBS; dbSNP:rs137852631 | |
VAR_017829 | 186 | N>K | in IBS; dbSNP:rs137852632 | |
VAR_009185 | 186 | N>Y | in IBS; dbSNP:rs137852631 | |
VAR_031082 | 465 | E>D | in IBS | |
VAR_031083 | 465 | E>K | in IBS; dbSNP:rs758760389 | |
VAR_009186 | 476 | E>K | in IBS; dbSNP:rs56829062 | |
VAR_031084 | 476 | E>V | in IBS; dbSNP:rs60537449 | |
VAR_031085 | 477 | I>N | in IBS; dbSNP:rs2120939967 | |
VAR_009187 | 479 | T>P | in IBS; dbSNP:rs137852630 | |
VAR_010516 | 484 | L>P | in IBS; dbSNP:rs61726451 | |
VAR_003866 | 487 | E>D | in IBS; dbSNP:rs137852628 | |
VAR_003867 | 487 | E>K | in IBS; dbSNP:rs137852629 | |
VAR_031086 | 488 | E>K | in IBS; dbSNP:rs61726452 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_058293 | 101 | in dbSNP:rs2634041 | |||
Sequence: S → G | ||||||
Natural variant | VAR_086330 | 178 | in IBS; uncertain significance; dbSNP:rs57728941 | |||
Sequence: E → K | ||||||
Natural variant | VAR_003865 | 181 | in IBS; dbSNP:rs57510142 | |||
Sequence: Q → P | ||||||
Natural variant | VAR_010514 | 182 | in IBS; dbSNP:rs61622714 | |||
Sequence: I → N | ||||||
Natural variant | VAR_010515 | 186 | in IBS; dbSNP:rs137852631 | |||
Sequence: N → D | ||||||
Natural variant | VAR_017829 | 186 | in IBS; dbSNP:rs137852632 | |||
Sequence: N → K | ||||||
Natural variant | VAR_009185 | 186 | in IBS; dbSNP:rs137852631 | |||
Sequence: N → Y | ||||||
Natural variant | VAR_058294 | 219 | in dbSNP:rs638043 | |||
Sequence: G → D | ||||||
Natural variant | VAR_031082 | 465 | in IBS | |||
Sequence: E → D | ||||||
Natural variant | VAR_031083 | 465 | in IBS; dbSNP:rs758760389 | |||
Sequence: E → K | ||||||
Natural variant | VAR_009186 | 476 | in IBS; dbSNP:rs56829062 | |||
Sequence: E → K | ||||||
Natural variant | VAR_031084 | 476 | in IBS; dbSNP:rs60537449 | |||
Sequence: E → V | ||||||
Natural variant | VAR_031085 | 477 | in IBS; dbSNP:rs2120939967 | |||
Sequence: I → N | ||||||
Natural variant | VAR_009187 | 479 | in IBS; dbSNP:rs137852630 | |||
Sequence: T → P | ||||||
Natural variant | VAR_010516 | 484 | in IBS; dbSNP:rs61726451 | |||
Sequence: L → P | ||||||
Natural variant | VAR_003866 | 487 | in IBS; dbSNP:rs137852628 | |||
Sequence: E → D | ||||||
Natural variant | VAR_003867 | 487 | in IBS; dbSNP:rs137852629 | |||
Sequence: E → K | ||||||
Natural variant | VAR_031086 | 488 | in IBS; dbSNP:rs61726452 | |||
Sequence: E → K |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 820 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000063715 | 1-639 | Keratin, type II cytoskeletal 2 epidermal | |||
Sequence: MSCQISCKSRGRGGGGGGFRGFSSGSAVVSGGSRRSTSSFSCLSRHGGGGGGFGGGGFGSRSLVGLGGTKSISISVAGGGGGFGAAGGFGGRGGGFGGGSSFGGGSGFSGGGFGGGGFGGGRFGGFGGPGGVGGLGGPGGFGPGGYPGGIHEVSVNQSLLQPLNVKVDPEIQNVKAQEREQIKTLNNKFASFIDKVRFLEQQNQVLQTKWELLQQMNVGTRPINLEPIFQGYIDSLKRYLDGLTAERTSQNSELNNMQDLVEDYKKKYEDEINKRTAAENDFVTLKKDVDNAYMIKVELQSKVDLLNQEIEFLKVLYDAEISQIHQSVTDTNVILSMDNSRNLDLDSIIAEVKAQYEEIAQRSKEEAEALYHSKYEELQVTVGRHGDSLKEIKIEISELNRVIQRLQGEIAHVKKQCKNVQDAIADAEQRGEHALKDARNKLNDLEEALQQAKEDLARLLRDYQELMNVKLALDVEIATYRKLLEGEECRMSGDLSSNVTVSVTSSTISSNVASKAAFGGSGGRGSSSGGGYSSGSSSYGSGGRQSGSRGGSGGGGSISGGGYGSGGGSGGRYGSGGGSKGGSISGGGYGSGGGKHSSGGGSRGGSSSGGGYGSGGGGSSSVKGSSGEAFGSSVTFSFR | ||||||
Modified residue | 12 | Omega-N-methylarginine | ||||
Sequence: R | ||||||
Modified residue | 20 | Asymmetric dimethylarginine | ||||
Sequence: R | ||||||
Modified residue | 23 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 26 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 62 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in the upper spinous and granular suprabasal layers of normal adult epidermal tissues from most body sites including thigh, breast nipple, foot sole, penile shaft and axilla. Not present in foreskin, squamous metaplasias and carcinomas. Expression in hypertrophic and keloid scars begins in the deepest suprabasal layer. Weakly expressed in normal gingiva and tongue, however expression is induced in benign keratoses of lingual mucosa and in mild-to-moderate oral dysplasia with orthokeratinization.
Induction
Induced in keratinocytes by all-trans retinoic acid (ATRA), via increase in mRNA stability.
Developmental stage
Synthesized during maturation of epidermal keratinocytes and localized in the upper intermediate cells of fetal skin. Earliest expression is at 10 weeks in the developing embryo in the presumptive nail bed of developing digits, shifting to the proximal nail fold by 13.5 weeks. At 12.5 weeks, detected in scattered cells of the intermediate layer of trunk skin. At 19.3 weeks, regional expression patterns were observed in upper intermediate keratinocytes of cheek, trunk, dorsal and ventral knee, elbow and dorsal hand. Distal areas around the periumbilical region showed increased number of positive cells and by 15 weeks is expressed in small groups of cells in the fetal hair follicles.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Heterotetramer of two type I and two type II keratins. Associates with KRT10.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P35908 | KRT13 A1A4E9 | 3 | EBI-1247312, EBI-10171552 | |
BINARY | P35908 | KRT13 P13646 | 5 | EBI-1247312, EBI-1223876 | |
BINARY | P35908 | KRT15 P19012 | 7 | EBI-1247312, EBI-739566 | |
BINARY | P35908 | KRT16 P08779 | 3 | EBI-1247312, EBI-356410 | |
BINARY | P35908 | KRT19 P08727 | 10 | EBI-1247312, EBI-742756 | |
BINARY | P35908 | KRT25 Q7Z3Z0 | 5 | EBI-1247312, EBI-11980019 | |
BINARY | P35908 | KRT27 Q7Z3Y8 | 3 | EBI-1247312, EBI-3044087 | |
BINARY | P35908 | KRT31 Q15323 | 10 | EBI-1247312, EBI-948001 | |
BINARY | P35908 | KRT33B Q14525 | 3 | EBI-1247312, EBI-1049638 | |
BINARY | P35908 | KRT35 Q92764 | 3 | EBI-1247312, EBI-1058674 | |
BINARY | P35908 | KRT36 O76013-2 | 3 | EBI-1247312, EBI-11958506 | |
BINARY | P35908 | KRT38 O76015 | 11 | EBI-1247312, EBI-1047263 | |
BINARY | P35908 | KRT40 Q6A162 | 11 | EBI-1247312, EBI-10171697 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-177 | Head | ||||
Sequence: MSCQISCKSRGRGGGGGGFRGFSSGSAVVSGGSRRSTSSFSCLSRHGGGGGGFGGGGFGSRSLVGLGGTKSISISVAGGGGGFGAAGGFGGRGGGFGGGSSFGGGSGFSGGGFGGGGFGGGRFGGFGGPGGVGGLGGPGGFGPGGYPGGIHEVSVNQSLLQPLNVKVDPEIQNVKAQ | ||||||
Region | 178-213 | Coil 1A | ||||
Sequence: EREQIKTLNNKFASFIDKVRFLEQQNQVLQTKWELL | ||||||
Domain | 178-491 | IF rod | ||||
Sequence: EREQIKTLNNKFASFIDKVRFLEQQNQVLQTKWELLQQMNVGTRPINLEPIFQGYIDSLKRYLDGLTAERTSQNSELNNMQDLVEDYKKKYEDEINKRTAAENDFVTLKKDVDNAYMIKVELQSKVDLLNQEIEFLKVLYDAEISQIHQSVTDTNVILSMDNSRNLDLDSIIAEVKAQYEEIAQRSKEEAEALYHSKYEELQVTVGRHGDSLKEIKIEISELNRVIQRLQGEIAHVKKQCKNVQDAIADAEQRGEHALKDARNKLNDLEEALQQAKEDLARLLRDYQELMNVKLALDVEIATYRKLLEGEECRM | ||||||
Region | 214-232 | Linker 1 | ||||
Sequence: QQMNVGTRPINLEPIFQGY | ||||||
Region | 233-324 | Coil 1B | ||||
Sequence: IDSLKRYLDGLTAERTSQNSELNNMQDLVEDYKKKYEDEINKRTAAENDFVTLKKDVDNAYMIKVELQSKVDLLNQEIEFLKVLYDAEISQI | ||||||
Region | 325-348 | Linker 12 | ||||
Sequence: HQSVTDTNVILSMDNSRNLDLDSI | ||||||
Region | 349-487 | Coil 2 | ||||
Sequence: IAEVKAQYEEIAQRSKEEAEALYHSKYEELQVTVGRHGDSLKEIKIEISELNRVIQRLQGEIAHVKKQCKNVQDAIADAEQRGEHALKDARNKLNDLEEALQQAKEDLARLLRDYQELMNVKLALDVEIATYRKLLEGE | ||||||
Region | 488-639 | Tail | ||||
Sequence: ECRMSGDLSSNVTVSVTSSTISSNVASKAAFGGSGGRGSSSGGGYSSGSSSYGSGGRQSGSRGGSGGGGSISGGGYGSGGGSGGRYGSGGGSKGGSISGGGYGSGGGKHSSGGGSRGGSSSGGGYGSGGGGSSSVKGSSGEAFGSSVTFSFR | ||||||
Region | 514-559 | Disordered | ||||
Sequence: SKAAFGGSGGRGSSSGGGYSSGSSSYGSGGRQSGSRGGSGGGGSIS | ||||||
Compositional bias | 526-553 | Polar residues | ||||
Sequence: SSSGGGYSSGSSSYGSGGRQSGSRGGSG | ||||||
Region | 574-639 | Disordered | ||||
Sequence: GSGGGSKGGSISGGGYGSGGGKHSSGGGSRGGSSSGGGYGSGGGGSSSVKGSSGEAFGSSVTFSFR | ||||||
Compositional bias | 600-639 | Polar residues | ||||
Sequence: GGSRGGSSSGGGYGSGGGGSSSVKGSSGEAFGSSVTFSFR |
Sequence similarities
Belongs to the intermediate filament family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length639
- Mass (Da)65,433
- Last updated2009-06-16 v2
- ChecksumB80526BAF70078A7
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 108 | in Ref. 1; AAC83410 and 2; AAB81946 | ||||
Sequence: F → FGGGSGF | ||||||
Compositional bias | 526-553 | Polar residues | ||||
Sequence: SSSGGGYSSGSSSYGSGGRQSGSRGGSG | ||||||
Compositional bias | 600-639 | Polar residues | ||||
Sequence: GGSRGGSSSGGGYGSGGGGSSSVKGSSGEAFGSSVTFSFR |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M99061 EMBL· GenBank· DDBJ | AAC83410.1 EMBL· GenBank· DDBJ | mRNA | ||
AF019084 EMBL· GenBank· DDBJ | AAB81946.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC055715 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC055716 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC096294 EMBL· GenBank· DDBJ | AAH96294.1 EMBL· GenBank· DDBJ | mRNA | ||
BC099643 EMBL· GenBank· DDBJ | AAH99643.1 EMBL· GenBank· DDBJ | mRNA | ||
BC099644 EMBL· GenBank· DDBJ | AAH99644.1 EMBL· GenBank· DDBJ | mRNA |