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Q3TTY5 (K22E_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 79. 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 2 epidermal
Alternative name(s):
Cytokeratin-2e
Short name=CK-2e
Epithelial keratin-2e
Keratin-2 epidermis
Keratin-2e
Short name=K2e
Type-II keratin Kb2
Gene names
Name:Krt2
Synonyms:K2e, Krt2-17, Krt2a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length707 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probably contributes to terminal cornification. Associated with keratinocyte activation, proliferation and keratinization By similarity. UniProtKB P35908

Subunit structure

Heterotetramer of two type I and two type II keratins. Associates with KRT10. Ref.6

Tissue specificity

Expressed mainly in the middle spinous and granular cells of the epidermis of adult tail, nipple and footsole skin. Also found in ear. Ref.1 Ref.2 Ref.7

Developmental stage

Induction occurs during the first 2 weeks after birth, being first observed in the epidermis of tail then the footpad and later in the ear. Ref.1

Involvement in disease

Defects in Krt2 are a cause of ichthyosis bullosa of siemens (IBS). IBS is a rare autosomal dominant disorder displaying a type of epidermolytic hyperkeratosis characterized by extensive blistering from birth. Hyperkeratoses and shedding of the outer layers of the epidermis (molting) are observed in later weeks. Ref.8

Miscellaneous

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

Sequence similarities

Belongs to the intermediate filament family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 707707Keratin, type II cytoskeletal 2 epidermal
PRO_0000283763

Regions

Region1 – 198198Head
Region199 – 508310Rod
Region199 – 23436Coil 1A
Region235 – 25319Linker 1
Region254 – 34592Coil 1B
Region346 – 36924Linker 12
Region370 – 508139Coil 2
Region509 – 707199Tail
Compositional bias12 – 701690Gly-rich

Sites

Site4501Stutter

Amino acid modifications

Modified residue641Phosphoserine By similarity UniProtKB P48668

Natural variations

Natural variant5001T → P in IBS. Ref.8

Experimental info

Sequence conflict238 – 2469DVGSRTTNL → ACRQPHHKP in CAA52788. Ref.2
Sequence conflict3611N → T in CAA52788. Ref.2
Sequence conflict4391K → I in CAA52788. Ref.2
Sequence conflict4511R → H in CAA52788. Ref.2
Sequence conflict5331V → M in CAA52788. Ref.2
Sequence conflict5621Missing in AAI20486. Ref.4
Sequence conflict5641T → S in CAA52788. Ref.2
Sequence conflict6251G → GG in AAI20486. Ref.4
Sequence conflict6411V → A in CAA52788. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q3TTY5 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: 464D375DCBA90EF4

FASTA70770,923
        10         20         30         40         50         60 
MSCQISCRSR RGGGGGGGGG FRGFSSGSAV VSGGSRRSNT SFSCISRHGG GRGGSGGGGF 

        70         80         90        100        110        120 
GSQSLVGLGG YKSISSSVAG NSGGYGGSSF GGSSGFGGGR GFGGGQGFGG SGGFGGGSGF 

       130        140        150        160        170        180 
GGGQGFGGGS RFGGGSGFGG GGFGGGSFGG GRFGGGPGGF GGPGGFPGGG IHEVSVNQSL 

       190        200        210        220        230        240 
LQPLDVKVDP EIQNVKSQER EQIKTLNNKF ASFIDKVRFL EQQNQVLRTK WELLQQLDVG 

       250        260        270        280        290        300 
SRTTNLDPIF QAYIGMLKKQ VDRLSAERTS QESELNNMQD LVEDFKKKYE DEINKRTSAE 

       310        320        330        340        350        360 
NDFVTIKKDV DSCYMDKTEL QARLDILAQE VNFLRTLYDA ELSQLQQDVT DTNVILSMDN 

       370        380        390        400        410        420 
NRNLDLDSII AEVQNQYEMI AHKSKAESEE LYHSKYEELQ VTAVKHGDSL KEIKMEISEL 

       430        440        450        460        470        480 
NRTIQRLQGE ISHVKKQCKG VQDSIADAEQ RGEHAIKDAR GKLTDLEEAL QQCREDLARL 

       490        500        510        520        530        540 
LRDYQELMNT KLSLDVEIAT YRKLLEGEEC RMSGDFSDNV SVSITSSTIS SSVASKTGFG 

       550        560        570        580        590        600 
SGGQSSGGRG SYGGRGGGGG GGSTYGSGGR SSGSRGSGSG SGGGGYSSGG GSRGGSGGGY 

       610        620        630        640        650        660 
GSGGGSRGGS GGGYGSGGGS GSGGGYSSGG GSRGGSGGGG VSSGGGSRGG SSSGGGSRGG 

       670        680        690        700 
SSSGGGGYSS GGGSRGGSSS GGAGSSSEKG GSGSGEGCGS GVTFSFR 

« Hide

References

« Hide 'large scale' references
[1]"An unusual type-II 70-kilodalton keratin protein of mouse epidermis exhibiting postnatal body-site specificity and sensitivity to hyperproliferation."
Rentrop M., Nischt R., Knapp B., Schweizer J., Winter H.
Differentiation 34:189-200(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Strain: NMRI.
Tissue: Foot sole tissue.
[2]"The large type II 70-kDa keratin of mouse epidermis is the ortholog of human keratin K2e."
Herzog F., Winter H., Schweizer J.
J. Invest. Dermatol. 102:165-170(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Strain: NMRI.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Skin.
[4]"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: Brain.
[5]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 23-36; 210-216; 288-296 AND 483-491, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
[6]"Out of balance: consequences of a partial keratin 10 knockout."
Reichelt J., Bauer C., Porter R., Lane E., Magin V.
J. Cell Sci. 110:2175-2186(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KRT10.
[7]"Keratin 2e: a marker for murine nipple epidermis."
Mahler B., Gocken T., Brojan M., Childress S., Spandau D.F., Foley J.
Cells Tissues Organs 176:169-177(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[8]"Genetics of dark skin in mice."
Fitch K.R., McGowan K.A., van Raamsdonk C.D., Fuchs H., Lee D., Puech A., Herault Y., Threadgill D.W., Hrabe de Angelis M., Barsh G.S.
Genes Dev. 17:214-228(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT IBS PRO-500.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X74784 mRNA. Translation: CAA52788.1.
AK132476 mRNA. Translation: BAE21186.1.
AK161078 mRNA. Translation: BAE36187.1.
AK161098 mRNA. Translation: BAE36194.1.
BC120485 mRNA. Translation: AAI20486.1.
CCDSCCDS37220.1.
RefSeqNP_034798.2. NM_010668.2.
UniGeneMm.358616.

3D structure databases

ProteinModelPortalQ3TTY5.
SMRQ3TTY5. Positions 199-338, 365-507.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201033. 7 interactions.
IntActQ3TTY5. 1 interaction.
MINTMINT-1867051.
STRING10090.ENSMUSP00000023712.

PTM databases

PhosphoSiteQ3TTY5.

Proteomic databases

MaxQBQ3TTY5.
PaxDbQ3TTY5.
PRIDEQ3TTY5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000023712; ENSMUSP00000023712; ENSMUSG00000064201.
GeneID16681.
KEGGmmu:16681.
UCSCuc007xub.1. mouse.

Organism-specific databases

CTD3849.
MGIMGI:96699. Krt2.

Phylogenomic databases

eggNOGNOG146769.
GeneTreeENSGT00730000110687.
HOVERGENHBG013015.
InParanoidQ3TTY5.
KOK07605.
OMATNLDPIF.
OrthoDBEOG7FV3Q8.
TreeFamTF317854.

Gene expression databases

BgeeQ3TTY5.
CleanExMM_KRT2.
GenevestigatorQ3TTY5.

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

NextBio290429.
PROQ3TTY5.
SOURCESearch...

Entry information

Entry nameK22E_MOUSE
AccessionPrimary (citable) accession number: Q3TTY5
Secondary accession number(s): Q0VBW1, Q61869
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: October 11, 2005
Last modified: July 9, 2014
This is version 79 of the entry and version 1 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