Q9D312 (K1C20_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Keratin, type I cytoskeletal 20

Alternative name(s):
Cytokeratin-20
Short name=CK-20
Keratin-20
Short name=K20

Gene names

Name:

Krt20

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	431 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Intermediate filament Keratin
Domain	Coiled coil
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW cellular response to stress Inferred from direct assay Ref.6. Source: UniProtKB intermediate filament organization Inferred from mutant phenotype Ref.1. Source: UniProtKB regulation of protein secretion Inferred from direct assay Ref.6. Source: UniProtKB
Cellular_component	cytoplasm Inferred from electronic annotation. Source: Compara intermediate filament Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 431	431	Keratin, type I cytoskeletal 20		PRO_0000308358
Regions
	Region	1 – 76	76	Head
	Region	77 – 384	308	Rod
	Region	77 – 112	36	Coil 1A
	Region	113 – 130	18	Linker 1
	Region	131 – 222	92	Coil 1B
	Region	223 – 245	23	Linker 12
	Region	246 – 384	139	Coil 2
	Region	385 – 431	47	Tail
	Compositional bias	11 – 16	6	Poly-Ser
Sites
	Site	235 – 236	2	Cleavage; by caspases By similarity
Amino acid modifications
	Modified residue	13	1	Phosphoserine; by MAPKAPK2, MAPKAPK3 and PKC Ref.6 Ref.7 Ref.8
	Modified residue	14	1	Phosphoserine Ref.7
Experimental info
	Sequence conflict	24	1	S → N in AAH57172. Ref.4
	Sequence conflict	151	1	R → Q in AAH57172. Ref.4
	Sequence conflict	173	1	R → H in AAH57172. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q9D312 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 5375E42A8BA0ACB3	FASTA	431	49,034
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND SER-14, MASS SPECTROMETRY. 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.
IPI	IPI00135197.
RefSeq	NP_075745.1. NM_023256.1.
UniGene	Mm.28042.
3D structure databases
HSSP	HSSP built from PDB template 1GK7 based on UniProtKB P08670.
ProteinModelPortal	Q9D312.
SMR	Q9D312. Positions 294-383.
ModBase	Search...
PTM databases
PhosphoSite	Q9D312.
Proteomic databases
PaxDb	Q9D312.
PRIDE	Q9D312.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000017743; ENSMUSP00000017743; ENSMUSG00000035775.
GeneID	66809.
KEGG	mmu:66809.
UCSC	uc007liu.1. mouse.
Organism-specific databases
CTD	54474.
MGI	MGI:1914059. Krt20.
Phylogenomic databases
eggNOG	NOG149615.
GeneTree	ENSGT00560000077101.
HOGENOM	HOG000230975.
HOVERGEN	HBG013015.
InParanoid	Q9D312.
KO	K07604.
OMA	QIKQWYE.
OrthoDB	EOG4NKBVQ.
Gene expression databases
Bgee	Q9D312.
CleanEx	MM_KRT20.
Genevestigator	Q9D312.
Family and domain databases
InterPro	IPR016044. F. IPR001664. IF. IPR018039. Intermediate_filament_CS. IPR002957. Keratin_I. [Graphical view]
PANTHER	PTHR23239. PTHR23239. 1 hit.
Pfam	PF00038. Filament. 1 hit. [Graphical view]
PRINTS	PR01248. TYPE1KERATIN.
PROSITE	PS00226. IF. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	322699.
SOURCE	Search...

Entry information

Entry name

K1C20_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program