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Protein

Keratin, type II cytoskeletal 6A

Gene

Krt6a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Epidermis-specific type I keratin involved in wound healing (PubMed:10866680). Involved in the activation of follicular keratinocytes after wounding, while it does not play a major role in keratinocyte proliferation or migration (PubMed:10866680). Participates in the regulation of epithelial migration by inhibiting the activity of SRC during wound repair (PubMed:22529101).2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei403 – 4031Stutter

GO - Molecular functioni

GO - Biological processi

  • intermediate filament organization Source: MGI
  • keratinization Source: MGI
  • morphogenesis of an epithelium Source: UniProtKB
  • Wnt signaling pathway Source: MGI
  • wound healing Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Krt6a
Synonyms:Ker2, Krt2-6, Krt2-6a, Krt6
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1100845. Krt6a.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Intermediate filament, Keratin

Pathology & Biotechi

Disruption phenotypei

Wound healing defects. Delay in reepithelialization from the hair follicle while the healing of full-thickness skin wounds is not impaired.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 553553Keratin, type II cytoskeletal 6APRO_0000063736Add
BLAST

Proteomic databases

MaxQBiP50446.
PaxDbiP50446.
PRIDEiP50446.

PTM databases

PhosphoSiteiP50446.

Expressioni

Tissue specificityi

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.2 Publications

Inductioni

With the exception of specific body sites, 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. Upon wounding, induced in the outer root sheath and the interfollicular epidermis including the basal cell layer (PubMed:10866680).3 Publications

Gene expression databases

BgeeiP50446.
CleanExiMM_KRT6A.
ExpressionAtlasiP50446. baseline and differential.
GenevisibleiP50446. MM.

Interactioni

Subunit structurei

Heterodimer of a type I and a type II keratin. KRT6 isomers associate with KRT16 and/or KRT17 (PubMed:8636216). Interacts with TCHP (By similarity).By similarity1 Publication

Protein-protein interaction databases

BioGridi201035. 3 interactions.
IntActiP50446. 2 interactions.
MINTiMINT-1859525.
STRINGi10090.ENSMUSP00000023788.

Structurei

3D structure databases

ProteinModelPortaliP50446.
SMRiP50446. Positions 149-302, 318-460.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 151151HeadAdd
BLAST
Regioni152 – 461310RodAdd
BLAST
Regioni152 – 18736Coil 1AAdd
BLAST
Regioni188 – 20619Linker 1Add
BLAST
Regioni207 – 29892Coil 1BAdd
BLAST
Regioni299 – 32224Linker 12Add
BLAST
Regioni323 – 461139Coil 2Add
BLAST
Regioni462 – 55392TailAdd
BLAST

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG315845.
GeneTreeiENSGT00760000118796.
HOGENOMiHOG000230976.
HOVERGENiHBG013015.
InParanoidiP50446.
KOiK07605.
OMAiMQDQVED.
OrthoDBiEOG7FV3Q8.
PhylomeDBiP50446.
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.

P50446-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTKTTIKSQ TSHRGYSASS ARVPGLNRSG FSSVSVCRSR GSGGSSAMCG
60 70 80 90 100
GAGFGSRSLY GVGSSKRISI GGGSCGIGGG YGSRFGGSFG IGGGAGSGFG
110 120 130 140 150
FGGGAGFGGG YGGAGFPVCP PGGIQEVTIN QSLLTPLNLQ IDPTIQRVRT
160 170 180 190 200
EEREQIKTLN NKFASFIDKV RFLEQQNKVL DTKWALLQEQ GTKTVRQNLE
210 220 230 240 250
PMFEQYISNL RRQLDSIIGE RGRLDSELRN MQDTVEDYKS KYEDEINKRT
260 270 280 290 300
AAENEFVTLK KDVDAAYMNK VELQAKADSL TDDINFLRAL YEAELSQMQT
310 320 330 340 350
HISDTSVVLS MDNNRSLDLD SIIAEVKAQY EDIAQRSRAE AESWYQTKYE
360 370 380 390 400
ELQVTAGRHG DDLRNTKQEI AEINRMIQRL RSEIDHVKKQ CANLQAAIAD
410 420 430 440 450
AEQRGEMALK DARGKLEGLE DALQKAKQDM ARLLKEYQEL MNVKLALDVE
460 470 480 490 500
IATYRKLLEG EECRLNGEGV GPVNISVVQS TVSSGYGSAG GASSSLGLGG
510 520 530 540 550
GSSYSYSSSH GLGGGFSAGS GRAIGGGLSS SGGLSSSTIK YTTTSSSKKS

YRQ
Length:553
Mass (Da):59,335
Last modified:January 23, 2007 - v3
Checksum:iC4DF69569E738DAF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti24 – 241P → L in AAA39395 (PubMed:6207530).Curated
Sequence conflicti121 – 1211P → L in AAA39395 (PubMed:6207530).Curated
Sequence conflicti173 – 1731L → M in AAA39395 (PubMed:6207530).Curated
Sequence conflicti180 – 1801L → M in AAA39395 (PubMed:6207530).Curated
Sequence conflicti191 – 1911G → D in AAA39395 (PubMed:6207530).Curated
Sequence conflicti199 – 1991L → M in AAA39395 (PubMed:6207530).Curated
Sequence conflicti224 – 2252LD → MN in AAA39395 (PubMed:6207530).Curated
Sequence conflicti233 – 2408DTVEDYKS → ELVEELRN in AAA39395 (PubMed:6207530).Curated
Sequence conflicti251 – 2511A → D in AAA39395 (PubMed:6207530).Curated
Sequence conflicti312 – 3121D → V in AAA39395 (PubMed:6207530).Curated
Sequence conflicti318 – 3181D → V in AAA39395 (PubMed:6207530).Curated
Sequence conflicti330 – 3323YED → FEV in AAA39395 (PubMed:6207530).Curated
Sequence conflicti344 – 3441W → L in AAA39395 (PubMed:6207530).Curated
Sequence conflicti432 – 4321R → M in AAA39395 (PubMed:6207530).Curated
Sequence conflicti438 – 4381Q → H in AAA39395 (PubMed:6207530).Curated
Sequence conflicti498 – 4981L → M in AAA39395 (PubMed:6207530).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02108 mRNA. Translation: AAA39395.1.
AB012033 Genomic DNA. Translation: BAA34178.1.
BC080820 mRNA. Translation: AAH80820.1.
CCDSiCCDS27860.1.
PIRiI59009.
RefSeqiNP_032502.3. NM_008476.3.
UniGeneiMm.302399.

Genome annotation databases

EnsembliENSMUST00000023788; ENSMUSP00000023788; ENSMUSG00000058354.
GeneIDi16687.
KEGGimmu:16687.
UCSCiuc007xtv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02108 mRNA. Translation: AAA39395.1.
AB012033 Genomic DNA. Translation: BAA34178.1.
BC080820 mRNA. Translation: AAH80820.1.
CCDSiCCDS27860.1.
PIRiI59009.
RefSeqiNP_032502.3. NM_008476.3.
UniGeneiMm.302399.

3D structure databases

ProteinModelPortaliP50446.
SMRiP50446. Positions 149-302, 318-460.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201035. 3 interactions.
IntActiP50446. 2 interactions.
MINTiMINT-1859525.
STRINGi10090.ENSMUSP00000023788.

PTM databases

PhosphoSiteiP50446.

Proteomic databases

MaxQBiP50446.
PaxDbiP50446.
PRIDEiP50446.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023788; ENSMUSP00000023788; ENSMUSG00000058354.
GeneIDi16687.
KEGGimmu:16687.
UCSCiuc007xtv.1. mouse.

Organism-specific databases

CTDi3853.
MGIiMGI:1100845. Krt6a.

Phylogenomic databases

eggNOGiNOG315845.
GeneTreeiENSGT00760000118796.
HOGENOMiHOG000230976.
HOVERGENiHBG013015.
InParanoidiP50446.
KOiK07605.
OMAiMQDQVED.
OrthoDBiEOG7FV3Q8.
PhylomeDBiP50446.
TreeFamiTF317854.

Miscellaneous databases

ChiTaRSiKrt6a. mouse.
NextBioi290437.
PROiP50446.
SOURCEiSearch...

Gene expression databases

BgeeiP50446.
CleanExiMM_KRT6A.
ExpressionAtlasiP50446. baseline and differential.
GenevisibleiP50446. MM.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
  5. "Onset of re-epithelialization after skin injury correlates with a reorganization of keratin filaments in wound edge keratinocytes: defining a potential role for keratin 16."
    Paladini R.D., Takahashi K., Bravo N.S., Coulombe P.A.
    J. Cell Biol. 132:381-397(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, INDUCTION.
  6. "Analysis of mouse keratin 6a regulatory sequences in transgenic mice reveals constitutive, tissue-specific expression by a keratin 6a minigene."
    Mahony D., Karunaratne S., Cam G., Rothnagel J.A.
    J. Invest. Dermatol. 115:795-804(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  7. "Delayed wound healing in keratin 6a knockout mice."
    Wojcik S.M., Bundman D.S., Roop D.R.
    Mol. Cell. Biol. 20:5248-5255(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, INDUCTION.
  8. "A wound-induced keratin inhibits Src activity during keratinocyte migration and tissue repair."
    Rotty J.D., Coulombe P.A.
    J. Cell Biol. 197:381-389(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiK2C6A_MOUSE
AccessioniPrimary (citable) accession number: P50446
Secondary accession number(s): Q9Z332
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 120 of the entry and version 3 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) and II (neutral to basic) (40-55 and 56-70 kDa, respectively).

Keywords - Technical termi

Complete proteome, 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.