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Q9D312 (K1C20_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 92. 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 I cytoskeletal 20
Alternative name(s):
Cytokeratin-20
Short name=CK-20
Keratin-20
Short name=K20
Gene names
Name:Krt20
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length431 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a significant role in maintaining keratin filament organization in intestinal epithelia. When phosphorylated, plays a role in the secretion of mucin in the small intestine. Ref.1 Ref.6

Subunit structure

Heterotetramer of two type I and two type II keratins. Associates with KRT8. Ref.1

Tissue specificity

Expressed at low levels in the more differentiated suprabasal regions of the small intestine, and at higher levels in the colon, mainly in the upper region and in scattered cells throughout the remaining epithelium. Also expressed in epithelial cells of bladder, ileum and stomach and at lower levels in pancreas and earskin. The phosphorylated form is nearly exclusively expressed in goblet cells of the small intestine and in the lumen-proximal cells of the colon (at protein level). Also expressed in jejunum and duodenum. Ref.1 Ref.6

Post-translational modification

Hyperphosphorylation at Ser-13 occurs during the early stages of apoptosis but becomes less prominent during the later stages By similarity. Phosphorylation at Ser-13 also increases in response to stress brought on by cell injury. Ref.6 UniProtKB P35900

Proteolytically cleaved by caspases during apoptosis. Cleavage occurs at Asp-235 By similarity. UniProtKB P35900

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 – 431431Keratin, type I cytoskeletal 20
PRO_0000308358

Regions

Region1 – 7676Head
Region77 – 384308Rod
Region77 – 11236Coil 1A
Region113 – 13018Linker 1
Region131 – 22292Coil 1B
Region223 – 24523Linker 12
Region246 – 384139Coil 2
Region385 – 43147Tail
Compositional bias11 – 166Poly-Ser

Sites

Site235 – 2362Cleavage; by caspases By similarity

Amino acid modifications

Modified residue131Phosphoserine; by MAPKAPK2, MAPKAPK3 and PKC Ref.6 Ref.7 Ref.8

Experimental info

Sequence conflict241S → N in AAH57172. Ref.4
Sequence conflict1511R → Q in AAH57172. Ref.4
Sequence conflict1731R → H in AAH57172. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9D312 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 5375E42A8BA0ACB3

FASTA43149,034
        10         20         30         40         50         60 
MDFSRQSFHR SLSSSSQGPA LSMSGSLYRK GTVQRLGAAP SVYGGAGGHG TRISVSKAVM 

        70         80         90        100        110        120 
SYGGDLSNGS DLFGGNGKLA MQNLNDRLAN YLEKVRSLEQ SNSRLEAQIK QWYETNAPST 

       130        140        150        160        170        180 
IRDYSSYYAQ IKELQNQVKD AQVQNAQCVL RIDNAKLAAE DFRLKFETER GMRIAVEADL 

       190        200        210        220        230        240 
QGLSKVYDNL TLQKTDLEIQ IEELNKDLAL LKKEHQEEVE VLRRQLGNNV NVEVDAAPGL 

       250        260        270        280        290        300 
NLGEIMNEMR QRYEVLAQKN LQEAKEQFER QSQTLQQQVT VNTEELKGFE VQVTELRRTY 

       310        320        330        340        350        360 
QNLEIELQSH LSMKESLERN LEDVKARYAS QLAAIQEMLS SLEAQLMQIR SDTERQNQEH 

       370        380        390        400        410        420 
NILLDIKTRL EQEIATYRRL LEGEDIKTTE YQLSTLEMKD IKKTRKIKTV VEEVVDGKVV 

       430 
SSEVKEIEES V 

« Hide

References

« Hide 'large scale' references
[1]"Keratin 20 helps maintain intermediate filament organization in intestinal epithelia."
Zhou Q., Toivola D.M., Feng N., Greenberg H.B., Franke W.W., Omary M.B.
Mol. Biol. Cell 14:2959-2971(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH KRT8, TISSUE SPECIFICITY.
[2]"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: Colon.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[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].
Strain: FVB/N.
Tissue: Colon.
[5]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 79-87 AND 370-378, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
[6]"Keratin 20 serine 13 phosphorylation is a stress and intestinal goblet cell marker."
Zhou Q., Cadrin M., Herrmann H., Chen C.-H., Chalkley R.J., Burlingame A.L., Omary M.B.
J. Biol. Chem. 281:16453-16461(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-13.
[7]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[8]"p38 MAP kinase and MAPKAP kinases MK2/3 cooperatively phosphorylate epithelial keratins."
Menon M.B., Schwermann J., Singh A.K., Franz-Wachtel M., Pabst O., Seidler U., Omary M.B., Kotlyarov A., Gaestel M.
J. Biol. Chem. 285:33242-33251(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-13 BY MAPKAPK2 AND MAPKAPK3.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF473907 mRNA. Translation: AAL82480.1.
AK018567 mRNA. Translation: BAB31280.1.
AL591165 Genomic DNA. Translation: CAM21365.1.
BC057172 mRNA. Translation: AAH57172.1.
CCDSCCDS25381.1.
RefSeqNP_075745.1. NM_023256.1.
UniGeneMm.28042.

3D structure databases

ProteinModelPortalQ9D312.
SMRQ9D312. Positions 294-383.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid211731. 1 interaction.
MINTMINT-1866652.

PTM databases

PhosphoSiteQ9D312.

Proteomic databases

MaxQBQ9D312.
PaxDbQ9D312.
PRIDEQ9D312.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000017743; ENSMUSP00000017743; ENSMUSG00000035775.
GeneID66809.
KEGGmmu:66809.
UCSCuc007liu.1. mouse.

Organism-specific databases

CTD54474.
MGIMGI:1914059. Krt20.

Phylogenomic databases

eggNOGNOG149615.
GeneTreeENSGT00750000117520.
HOGENOMHOG000230975.
HOVERGENHBG013015.
InParanoidQ9D312.
KOK07604.
OMAQIKQWYE.
OrthoDBEOG7FV3Q8.
PhylomeDBQ9D312.
TreeFamTF332742.

Gene expression databases

BgeeQ9D312.
CleanExMM_KRT20.
GenevestigatorQ9D312.

Family and domain databases

InterProIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR002957. Keratin_I.
[Graphical view]
PANTHERPTHR23239. PTHR23239. 1 hit.
PfamPF00038. Filament. 1 hit.
[Graphical view]
PRINTSPR01248. TYPE1KERATIN.
PROSITEPS00226. IF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio322699.
PROQ9D312.
SOURCESearch...

Entry information

Entry nameK1C20_MOUSE
AccessionPrimary (citable) accession number: Q9D312
Secondary accession number(s): Q6PG82
Entry history
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 92 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