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Q9D312

- K1C20_MOUSE

UniProt

Q9D312 - K1C20_MOUSE

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Protein

Keratin, type I cytoskeletal 20

Gene

Krt20

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

Functioni

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.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei235 – 2362Cleavage; by caspasesBy similarity

GO - Molecular functioni

  1. structural molecule activity Source: InterPro

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. cellular response to stress Source: UniProtKB
  3. intermediate filament organization Source: UniProtKB
  4. regulation of protein secretion Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Names & Taxonomyi

Protein namesi
Recommended name:
Keratin, type I cytoskeletal 20
Alternative name(s):
Cytokeratin-20
Short name:
CK-20
Keratin-20
Short name:
K20
Gene namesi
Name:Krt20Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:1914059. Krt20.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: Ensembl
  2. intermediate filament Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Intermediate filament, Keratin

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 431431Keratin, type I cytoskeletal 20PRO_0000308358Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei13 – 131Phosphoserine; by MAPKAPK2, MAPKAPK3 and PKC2 Publications

Post-translational modificationi

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.By similarity2 Publications
Proteolytically cleaved by caspases during apoptosis. Cleavage occurs at Asp-235 (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9D312.
PaxDbiQ9D312.
PRIDEiQ9D312.

PTM databases

PhosphoSiteiQ9D312.

Expressioni

Tissue specificityi

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.2 Publications

Gene expression databases

BgeeiQ9D312.
CleanExiMM_KRT20.
GenevestigatoriQ9D312.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi211731. 1 interaction.
MINTiMINT-1866652.

Structurei

3D structure databases

ProteinModelPortaliQ9D312.
SMRiQ9D312. Positions 294-383.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 7676HeadSequence AnalysisAdd
BLAST
Regioni77 – 384308RodSequence AnalysisAdd
BLAST
Regioni77 – 11236Coil 1ASequence AnalysisAdd
BLAST
Regioni113 – 13018Linker 1Sequence AnalysisAdd
BLAST
Regioni131 – 22292Coil 1BSequence AnalysisAdd
BLAST
Regioni223 – 24523Linker 12Sequence AnalysisAdd
BLAST
Regioni246 – 384139Coil 2Sequence AnalysisAdd
BLAST
Regioni385 – 43147TailSequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi11 – 166Poly-SerSequence Analysis

Sequence similaritiesi

Belongs to the intermediate filament family.Sequence Analysis

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG149615.
GeneTreeiENSGT00760000119046.
HOGENOMiHOG000230975.
HOVERGENiHBG013015.
InParanoidiQ9D312.
KOiK07604.
OMAiQIKQWYE.
OrthoDBiEOG7FV3Q8.
PhylomeDBiQ9D312.
TreeFamiTF332742.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR002957. Keratin_I.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PfamiPF00038. Filament. 1 hit.
[Graphical view]
PRINTSiPR01248. TYPE1KERATIN.
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9D312-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDFSRQSFHR SLSSSSQGPA LSMSGSLYRK GTVQRLGAAP SVYGGAGGHG
60 70 80 90 100
TRISVSKAVM SYGGDLSNGS DLFGGNGKLA MQNLNDRLAN YLEKVRSLEQ
110 120 130 140 150
SNSRLEAQIK QWYETNAPST IRDYSSYYAQ IKELQNQVKD AQVQNAQCVL
160 170 180 190 200
RIDNAKLAAE DFRLKFETER GMRIAVEADL QGLSKVYDNL TLQKTDLEIQ
210 220 230 240 250
IEELNKDLAL LKKEHQEEVE VLRRQLGNNV NVEVDAAPGL NLGEIMNEMR
260 270 280 290 300
QRYEVLAQKN LQEAKEQFER QSQTLQQQVT VNTEELKGFE VQVTELRRTY
310 320 330 340 350
QNLEIELQSH LSMKESLERN LEDVKARYAS QLAAIQEMLS SLEAQLMQIR
360 370 380 390 400
SDTERQNQEH NILLDIKTRL EQEIATYRRL LEGEDIKTTE YQLSTLEMKD
410 420 430
IKKTRKIKTV VEEVVDGKVV SSEVKEIEES V
Length:431
Mass (Da):49,034
Last modified:June 1, 2001 - v1
Checksum:i5375E42A8BA0ACB3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti24 – 241S → N in AAH57172. (PubMed:15489334)Curated
Sequence conflicti151 – 1511R → Q in AAH57172. (PubMed:15489334)Curated
Sequence conflicti173 – 1731R → H in AAH57172. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF473907 mRNA. Translation: AAL82480.1.
AK018567 mRNA. Translation: BAB31280.1.
AL591165 Genomic DNA. Translation: CAM21365.1.
BC057172 mRNA. Translation: AAH57172.1.
CCDSiCCDS25381.1.
RefSeqiNP_075745.1. NM_023256.1.
UniGeneiMm.28042.

Genome annotation databases

EnsembliENSMUST00000017743; ENSMUSP00000017743; ENSMUSG00000035775.
GeneIDi66809.
KEGGimmu:66809.
UCSCiuc007liu.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF473907 mRNA. Translation: AAL82480.1 .
AK018567 mRNA. Translation: BAB31280.1 .
AL591165 Genomic DNA. Translation: CAM21365.1 .
BC057172 mRNA. Translation: AAH57172.1 .
CCDSi CCDS25381.1.
RefSeqi NP_075745.1. NM_023256.1.
UniGenei Mm.28042.

3D structure databases

ProteinModelPortali Q9D312.
SMRi Q9D312. Positions 294-383.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 211731. 1 interaction.
MINTi MINT-1866652.

PTM databases

PhosphoSitei Q9D312.

Proteomic databases

MaxQBi Q9D312.
PaxDbi Q9D312.
PRIDEi Q9D312.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000017743 ; ENSMUSP00000017743 ; ENSMUSG00000035775 .
GeneIDi 66809.
KEGGi mmu:66809.
UCSCi uc007liu.1. mouse.

Organism-specific databases

CTDi 54474.
MGIi MGI:1914059. Krt20.

Phylogenomic databases

eggNOGi NOG149615.
GeneTreei ENSGT00760000119046.
HOGENOMi HOG000230975.
HOVERGENi HBG013015.
InParanoidi Q9D312.
KOi K07604.
OMAi QIKQWYE.
OrthoDBi EOG7FV3Q8.
PhylomeDBi Q9D312.
TreeFami TF332742.

Miscellaneous databases

NextBioi 322699.
PROi Q9D312.
SOURCEi Search...

Gene expression databases

Bgeei Q9D312.
CleanExi MM_KRT20.
Genevestigatori Q9D312.

Family and domain databases

InterProi IPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR002957. Keratin_I.
[Graphical view ]
PANTHERi PTHR23239. PTHR23239. 1 hit.
Pfami PF00038. Filament. 1 hit.
[Graphical view ]
PRINTSi PR01248. TYPE1KERATIN.
PROSITEi PS00226. IF. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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/6JImported.
    Tissue: ColonImported.
  3. 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/NImported.
    Tissue: ColonImported.
  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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver1 Publication.
  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.

Entry informationi

Entry nameiK1C20_MOUSE
AccessioniPrimary (citable) accession number: Q9D312
Secondary accession number(s): Q6PG82
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: June 1, 2001
Last modified: October 29, 2014
This is version 94 of the entry and version 1 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; 40-55 kDa) and II (neutral to basic; 56-70 kDa).Curated

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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