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P50446 (K2C6A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Keratin, type II cytoskeletal 6A
Alternative name(s):
Cytokeratin-6A
Short name=CK-6A
Keratin-6-alpha
Short name=mK6-alpha
Keratin-6A
Short name=K6A
Gene names
Name:Krt6a
Synonyms:Ker2, Krt2-6, Krt2-6a, Krt6
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length553 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Subunit structure

Heterodimer of a type I and a type II keratin. KRT6 isomers associate with KRT16 and/or KRT17. Interacts with TCHP By similarity.

Tissue specificity

Predominates in the adult trunk skin, tongue, trachea/esophagus and eye. In adult skin, localization is restricted to hair follicles, where it is localized predominantly in the outer root sheath. Ref.2

Induction

With the exception of specific body sites, keratin-6 expression is induced under conditions of epithelial hyperproliferation such as wound healing, certain skin diseases, cancer, and by treatment of the skin with the phorbol ester PMA. Ref.2

Miscellaneous

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

Sequence similarities

Belongs to the intermediate filament family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 553553Keratin, type II cytoskeletal 6A
PRO_0000063736

Regions

Region1 – 151151Head
Region152 – 461310Rod
Region152 – 18736Coil 1A
Region188 – 20619Linker 1
Region207 – 29892Coil 1B
Region299 – 32224Linker 12
Region323 – 461139Coil 2
Region462 – 55392Tail

Sites

Site4031Stutter

Experimental info

Sequence conflict241P → L in AAA39395. Ref.1
Sequence conflict1211P → L in AAA39395. Ref.1
Sequence conflict1731L → M in AAA39395. Ref.1
Sequence conflict1801L → M in AAA39395. Ref.1
Sequence conflict1911G → D in AAA39395. Ref.1
Sequence conflict1991L → M in AAA39395. Ref.1
Sequence conflict224 – 2252LD → MN in AAA39395. Ref.1
Sequence conflict233 – 2408DTVEDYKS → ELVEELRN in AAA39395. Ref.1
Sequence conflict2511A → D in AAA39395. Ref.1
Sequence conflict3121D → V in AAA39395. Ref.1
Sequence conflict3181D → V in AAA39395. Ref.1
Sequence conflict330 – 3323YED → FEV in AAA39395. Ref.1
Sequence conflict3441W → L in AAA39395. Ref.1
Sequence conflict4321R → M in AAA39395. Ref.1
Sequence conflict4381Q → H in AAA39395. Ref.1
Sequence conflict4981L → M in AAA39395. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P50446 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: C4DF69569E738DAF

FASTA55359,335
        10         20         30         40         50         60 
MSTKTTIKSQ TSHRGYSASS ARVPGLNRSG FSSVSVCRSR GSGGSSAMCG GAGFGSRSLY 

        70         80         90        100        110        120 
GVGSSKRISI GGGSCGIGGG YGSRFGGSFG IGGGAGSGFG FGGGAGFGGG YGGAGFPVCP 

       130        140        150        160        170        180 
PGGIQEVTIN QSLLTPLNLQ IDPTIQRVRT EEREQIKTLN NKFASFIDKV RFLEQQNKVL 

       190        200        210        220        230        240 
DTKWALLQEQ GTKTVRQNLE PMFEQYISNL RRQLDSIIGE RGRLDSELRN MQDTVEDYKS 

       250        260        270        280        290        300 
KYEDEINKRT AAENEFVTLK KDVDAAYMNK VELQAKADSL TDDINFLRAL YEAELSQMQT 

       310        320        330        340        350        360 
HISDTSVVLS MDNNRSLDLD SIIAEVKAQY EDIAQRSRAE AESWYQTKYE ELQVTAGRHG 

       370        380        390        400        410        420 
DDLRNTKQEI AEINRMIQRL RSEIDHVKKQ CANLQAAIAD AEQRGEMALK DARGKLEGLE 

       430        440        450        460        470        480 
DALQKAKQDM ARLLKEYQEL MNVKLALDVE IATYRKLLEG EECRLNGEGV GPVNISVVQS 

       490        500        510        520        530        540 
TVSSGYGSAG GASSSLGLGG GSSYSYSSSH GLGGGFSAGS GRAIGGGLSS SGGLSSSTIK 

       550 
YTTTSSSKKS YRQ 

« Hide

References

« Hide 'large scale' references
[1]"The complete cDNA and deduced amino acid sequence of a type II mouse epidermal keratin of 60,000 Da: analysis of sequence differences between type I and type II keratins."
Steinert P.M., Parry D.A.D., Racoosin E.L., Idler W.W., Steven A.C., Trus B.L., Roop D.R.
Proc. Natl. Acad. Sci. U.S.A. 81:5709-5713(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Epidermis.
[2]"The two functional keratin 6 genes of mouse are differentially regulated and evolved independently from their human orthologs."
Takahashi K., Yan B., Yamanishi K., Imamura S., Coulombe P.A.
Genomics 53:170-183(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, INDUCTION.
Strain: 129/Sv.
Tissue: Skin.
[3]"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].
Tissue: Jaw and Limb.
[4]"Identification of a cloned sequence activated during multi-stage carcinogenesis in mouse skin."
Finch J., Andrews K., Krieg P., Furstenberger G., Slaga T., Ootsuyama A., Tanooka H., Bowden G.T.
Carcinogenesis 12:1519-1522(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 528-553.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K02108 mRNA. Translation: AAA39395.1.
AB012033 Genomic DNA. Translation: BAA34178.1.
BC080820 mRNA. Translation: AAH80820.1.
CCDSCCDS27860.1.
PIRI59009.
RefSeqNP_032502.3. NM_008476.3.
UniGeneMm.302399.

3D structure databases

ProteinModelPortalP50446.
SMRP50446. Positions 149-302, 318-460.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201035. 3 interactions.
IntActP50446. 2 interactions.
MINTMINT-1859525.
STRING10090.ENSMUSP00000023788.

PTM databases

PhosphoSiteP50446.

Proteomic databases

MaxQBP50446.
PaxDbP50446.
PRIDEP50446.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000023788; ENSMUSP00000023788; ENSMUSG00000058354.
GeneID16687.
KEGGmmu:16687.
UCSCuc007xtv.1. mouse.

Organism-specific databases

CTD3853.
MGIMGI:1100845. Krt6a.

Phylogenomic databases

eggNOGNOG315845.
GeneTreeENSGT00610000085801.
HOGENOMHOG000230976.
HOVERGENHBG013015.
InParanoidP50446.
KOK07605.
OMAMQDQVED.
OrthoDBEOG7FV3Q8.
PhylomeDBP50446.
TreeFamTF317854.

Gene expression databases

ArrayExpressP50446.
BgeeP50446.
CleanExMM_KRT6A.
GenevestigatorP50446.

Family and domain databases

InterProIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR003054. Keratin_II.
[Graphical view]
PANTHERPTHR23239. PTHR23239. 1 hit.
PfamPF00038. Filament. 1 hit.
[Graphical view]
PRINTSPR01276. TYPE2KERATIN.
PROSITEPS00226. IF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSKRT6A. mouse.
NextBio290437.
PROP50446.
SOURCESearch...

Entry information

Entry nameK2C6A_MOUSE
AccessionPrimary (citable) accession number: P50446
Secondary accession number(s): Q9Z332
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 111 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot