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Q9EPW2 (KLF15_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 111. 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:
Krueppel-like factor 15
Alternative name(s):
Cardiovascular Krueppel-like factor
Gene names
Name:Klf15
Synonyms:Cklf
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length415 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional regulator that binds to the GA element of the CLCNKA promoter By similarity. Binds to the KCNIP2 promoter and regulates KCNIP2 circadian expression in the heart. Is a repressor of CTGF expression, involved in the control of cardiac fibrosis. Is also involved in the control of cardiac hypertrophy acting through the inhibition of MEF2A, GATA4 and MYOCD activity. Is a negative regulator of TP53 acetylation. Inhibits NF-kappa-B activation through repression of EP300-dependent RELA acetylation By similarity. Involved in podocyte differentiation. Ref.4 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11

Subunit structure

Interacts with MYOCD. Interacts with EP300 By similarity. Ref.7

Subcellular location

Nucleus.

Tissue specificity

Expressed in aortic smooth muscle cells. Ref.11

Induction

In the heart, up-regulated by the CLOCK/ARNTL heterodimer. In podocytes, up-regulated by retinoic acid. Ref.9 Ref.10

Disruption phenotype

KLF15 null mice are viable, but in response to pressure overload, they develop cardiac hypertrophy and fibrosis. Ref.4 Ref.6

Sequence similarities

Belongs to the Sp1 C2H2-type zinc-finger protein family.

Contains 3 C2H2-type zinc fingers.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionActivator
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcardiac muscle hypertrophy in response to stress

Inferred from mutant phenotype Ref.4. Source: UniProtKB

cellular response to peptide

Inferred from electronic annotation. Source: Ensembl

glial cell differentiation

Inferred from direct assay PubMed 19741146. Source: MGI

glomerular visceral epithelial cell differentiation

Inferred from mutant phenotype Ref.9. Source: UniProtKB

glucose transport

Inferred from direct assay Ref.1. Source: MGI

negative regulation of peptidyl-lysine acetylation

Inferred from mutant phenotype Ref.8. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.1. Source: MGI

regulation of gene expression

Inferred from mutant phenotype Ref.4. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleolus

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay Ref.1. Source: MGI

   Molecular_functionDNA binding

Inferred from direct assay Ref.1. Source: MGI

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.1. Source: MGI

sequence-specific DNA binding transcription factor activity

Inferred from direct assay Ref.1. Source: MGI

transcription regulatory region DNA binding

Inferred from direct assay Ref.10. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 415415Krueppel-like factor 15
PRO_0000047188

Regions

Zinc finger320 – 34425C2H2-type 1
Zinc finger350 – 37425C2H2-type 2
Zinc finger380 – 40223C2H2-type 3

Sequences

Sequence LengthMass (Da)Tools
Q9EPW2 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 127A7B80DB3E33CC

FASTA41544,253
        10         20         30         40         50         60 
MVDHLLPVDE TFSSPKCSVG YLGDRLASRQ PYHMLPSPIS EDDSDVSSPC SCASPDSQAF 

        70         80         90        100        110        120 
CSCYSAGPGP EAQGSILDFL LSRATLGSGG GSGGIGDSSG PVTWGSWRRA SVPVKEEHFC 

       130        140        150        160        170        180 
FPEFLSGDTD DVSRPFQPTL EEIEEFLEEN MEAEVKEAPE NGSRDLETCS QLSAGSHRSH 

       190        200        210        220        230        240 
LHPESAGRER CTPPPGGTSG GGAQSAGEGP AHDGPVPVLL QIQPVAVKQE AGTGPASPGQ 

       250        260        270        280        290        300 
APESVKVAQL LVNIQGQTFA LLPQVVPSSN LNLPSKFVRI APVPIAAKPI GSGSLGPGPA 

       310        320        330        340        350        360 
GLLVGQKFPK NPAAELLKMH KCTFPGCSKM YTKSSHLKAH LRRHTGEKPF ACTWPGCGWR 

       370        380        390        400        410 
FSRSDELSRH RRSHSGVKPY QCPVCEKKFA RSDHLSKHIK VHRFPRSSRA VRAIN 

« Hide

References

« Hide 'large scale' references
[1]"The Kruppel-like factor KLF15 regulates the insulin-sensitive glucose transporter GLUT4."
Gray S.J., Feinberg M.W., Hull S., Kuo C.T., Watanabe M., Sen-Banerjee S., DePina A., Haspel R., Jain M.K.
J. Biol. Chem. 277:34322-34328(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
[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: Mammary gland and Tongue.
[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: Liver.
[4]"Kruppel-like factor 15 is a regulator of cardiomyocyte hypertrophy."
Fisch S., Gray S., Heymans S., Haldar S.M., Wang B., Pfister O., Cui L., Kumar A., Lin Z., Sen-Banerjee S., Das H., Petersen C.A., Mende U., Burleigh B.A., Zhu Y., Pinto Y.M., Pinto Y., Liao R., Jain M.K.
Proc. Natl. Acad. Sci. U.S.A. 104:7074-7079(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS INHIBITOR OF CARDIAC HYPERTROPHY, FUNCTION AS REPRESSOR OF GATA4 AND MEF2A, DISRUPTION PHENOTYPE.
[5]Erratum
Fisch S., Gray S., Heymans S., Haldar S.M., Wang B., Pfister O., Cui L., Kumar A., Lin Z., Sen-Banerjee S., Das H., Petersen C.A., Mende U., Burleigh B.A., Zhu Y., Pinto Y.M., Pinto Y., Liao R., Jain M.K.
Proc. Natl. Acad. Sci. U.S.A. 104:13851-13851(2007)
[6]"The Kruppel-like factor KLF15 inhibits connective tissue growth factor (CTGF) expression in cardiac fibroblasts."
Wang B., Haldar S.M., Lu Y., Ibrahim O.A., Fisch S., Gray S., Leask A., Jain M.K.
J. Mol. Cell. Cardiol. 45:193-197(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS INHIBITOR OF CARDIAC FIBROSIS AND CTGF EXPRESSION, DISRUPTION PHENOTYPE.
[7]"Regulation of cardiac gene expression by KLF15, a repressor of myocardin activity."
Leenders J.J., Wijnen W.J., Hiller M., van der Made I., Lentink V., van Leeuwen R.E., Herias V., Pokharel S., Heymans S., de Windt L.J., Hoeydal M.A., Pinto Y.M., Creemers E.E.
J. Biol. Chem. 285:27449-27456(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS NEGATIVE REGULATOR OF MYOCD, INTERACTION WITH MYOCD.
[8]"Klf15 deficiency is a molecular link between heart failure and aortic aneurysm formation."
Haldar S.M., Lu Y., Jeyaraj D., Kawanami D., Cui Y., Eapen S.J., Hao C., Li Y., Doughman Y.Q., Watanabe M., Shimizu K., Kuivaniemi H., Sadoshima J., Margulies K.B., Cappola T.P., Jain M.K.
Sci. Transl. Med. 2:26ra26-26ra26(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS NEGATIVE REGULATOR OF TP53 ACETYLATION.
[9]"Kruppel-like factor 15 (KLF15) is a key regulator of podocyte differentiation."
Mallipattu S.K., Liu R., Zheng F., Narla G., Ma'ayan A., Dikman S., Jain M.K., Saleem M., D'Agati V., Klotman P., Chuang P.Y., He J.C.
J. Biol. Chem. 287:19122-19135(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PODOCYTE DIFFERENTIATION, INDUCTION.
[10]"Circadian rhythms govern cardiac repolarization and arrhythmogenesis."
Jeyaraj D., Haldar S.M., Wan X., McCauley M.D., Ripperger J.A., Hu K., Lu Y., Eapen B.L., Sharma N., Ficker E., Cutler M.J., Gulick J., Sanbe A., Robbins J., Demolombe S., Kondratov R.V., Shea S.A., Albrecht U. expand/collapse author list , Wehrens X.H., Rosenbaum D.S., Jain M.K.
Nature 483:96-99(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN KCNIP2 CIRCADIAN EXPRESSION, INDUCTION, BINDING TO THE KCNIP2 PROMOTER.
[11]"Kruppel-like factor 15 is critical for vascular inflammation."
Lu Y., Zhang L., Liao X., Sangwung P., Prosdocimo D.A., Zhou G., Votruba A.R., Brian L., Han Y.J., Gao H., Wang Y., Shimizu K., Weinert-Stein K., Khrestian M., Simon D.I., Freedman N.J., Jain M.K.
J. Clin. Invest. 123:4232-4241(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS INHIBITOR OF VASCULAR INFLAMMATION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF317225 mRNA. Translation: AAG38597.1.
AK009739 mRNA. Translation: BAB26470.1.
AK142618 mRNA. Translation: BAE25132.1.
BC013486 mRNA. Translation: AAH13486.1.
CCDSCCDS20360.1.
RefSeqNP_075673.1. NM_023184.3.
UniGeneMm.41389.

3D structure databases

ProteinModelPortalQ9EPW2.
SMRQ9EPW2. Positions 317-402.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ9EPW2.

Proteomic databases

PRIDEQ9EPW2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000032174; ENSMUSP00000032174; ENSMUSG00000030087.
ENSMUST00000113530; ENSMUSP00000109158; ENSMUSG00000030087.
GeneID66277.
KEGGmmu:66277.
UCSCuc009cxj.1. mouse.

Organism-specific databases

CTD28999.
MGIMGI:1929988. Klf15.

Phylogenomic databases

eggNOGCOG5048.
GeneTreeENSGT00750000117314.
HOGENOMHOG000294058.
HOVERGENHBG052266.
InParanoidQ9EPW2.
KOK09210.
OMATAGVRSY.
OrthoDBEOG7JMGF2.
PhylomeDBQ9EPW2.
TreeFamTF350556.

Gene expression databases

BgeeQ9EPW2.
CleanExMM_CKLF.
MM_KLF15.
GenevestigatorQ9EPW2.

Family and domain databases

Gene3D3.30.160.60. 3 hits.
InterProIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
SMARTSM00355. ZnF_C2H2. 3 hits.
[Graphical view]
PROSITEPS00028. ZINC_FINGER_C2H2_1. 3 hits.
PS50157. ZINC_FINGER_C2H2_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio321181.
PROQ9EPW2.
SOURCESearch...

Entry information

Entry nameKLF15_MOUSE
AccessionPrimary (citable) accession number: Q9EPW2
Secondary accession number(s): Q3UQB0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 111 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