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Krueppel-like factor 4 (Epithelial zinc finger protein EZF) (Gut-enriched krueppel-like factor)

 KLF4_MOUSE              Reviewed;         483 AA.
Q60793; P70421; Q3U2D6; Q3URS6; Q78K30; Q9R255;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
10-FEB-2009, sequence version 3.
22-NOV-2017, entry version 161.
RecName: Full=Krueppel-like factor 4;
AltName: Full=Epithelial zinc finger protein EZF;
AltName: Full=Gut-enriched krueppel-like factor;
Name=Klf4; Synonyms=Ezf, Gklf, Zie;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8702718; DOI=10.1074/jbc.271.33.20009;
Shields J.M., Christy R.J., Yang V.W.;
"Identification and characterization of a gene encoding a gut-enriched
Kruppel-like factor expressed during growth arrest.";
J. Biol. Chem. 271:20009-20017(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6 X DBA/2; TISSUE=Embryonic fibroblast;
PubMed=8940147; DOI=10.1074/jbc.271.49.31384;
Garrett-Sinha L.A., Eberspaecher H., Seldin M.F., de Crombrugghe B.;
"A gene for a novel zinc-finger protein expressed in differentiated
epithelial cells and transiently in certain mesenchymal cells.";
J. Biol. Chem. 271:31384-31390(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
STRAIN=129/SvJ;
PubMed=10556311; DOI=10.1093/nar/27.23.4562;
Mahatan C.S., Kaestner K.H., Geiman D.E., Yang V.W.;
"Characterization of the structure and regulation of the murine gene
encoding gut-enriched Kruppel-like factor (Kruppel-like factor 4).";
Nucleic Acids Res. 27:4562-4569(1999).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
STRAIN=C57BL/6J;
PubMed=12441126; DOI=10.1006/excr.2002.5633;
Chen Z.-Y., Shie J.-L., Tseng C.-C.;
"STAT1 is required for IFN-gamma-mediated gut-enriched Kruppel-like
factor expression.";
Exp. Cell Res. 281:19-27(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD;
TISSUE=Dendritic cell, Embryonic stem cell, and Mammary gland;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
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.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=10431239; DOI=10.1038/11926;
Segre J.A., Bauer C., Fuchs E.;
"Klf4 is a transcription factor required for establishing the barrier
function of the skin.";
Nat. Genet. 22:356-360(1999).
[10]
FUNCTION.
PubMed=15358627; DOI=10.1182/blood-2004-07-2681;
Li Y., McClintick J., Zhong L., Edenberg H.J., Yoder M.C., Chan R.J.;
"Murine embryonic stem cell differentiation is promoted by SOCS-3 and
inhibited by the zinc finger transcription factor Klf4.";
Blood 105:635-637(2005).
[11]
BIOTECHNOLOGY.
PubMed=16904174; DOI=10.1016/j.cell.2006.07.024;
Takahashi K., Yamanaka S.;
"Induction of pluripotent stem cells from mouse embryonic and adult
fibroblast cultures by defined factors.";
Cell 126:663-676(2006).
[12]
FUNCTION.
PubMed=16954384; DOI=10.1128/MCB.00468-06;
Nakatake Y., Fukui N., Iwamatsu Y., Masui S., Takahashi K., Yagi R.,
Yagi K., Miyazaki J., Matoba R., Ko M.S., Niwa H.;
"Klf4 cooperates with Oct3/4 and Sox2 to activate the Lefty1 core
promoter in embryonic stem cells.";
Mol. Cell. Biol. 26:7772-7782(2006).
[13]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17060454; DOI=10.1128/MCB.00846-06;
Swamynathan S.K., Katz J.P., Kaestner K.H., Ashery-Padan R.,
Crawford M.A., Piatigorsky J.;
"Conditional deletion of the mouse Klf4 gene results in corneal
epithelial fragility, stromal edema, and loss of conjunctival goblet
cells.";
Mol. Cell. Biol. 27:182-194(2007).
[14]
FUNCTION, INTERACTION WITH POU5F1/OCT4 AND SOX2, AND BIOTECHNOLOGY.
PubMed=19816951; DOI=10.1002/stem.231;
Wei Z., Yang Y., Zhang P., Andrianakos R., Hasegawa K., Lyu J.,
Chen X., Bai G., Liu C., Pera M., Lu W.;
"Klf4 interacts directly with Oct4 and Sox2 to promote
reprogramming.";
Stem Cells 27:2969-2978(2009).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, and Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[16]
FUNCTION.
PubMed=20071344; DOI=10.1074/jbc.M109.077958;
Zhang P., Andrianakos R., Yang Y., Liu C., Lu W.;
"Kruppel-like factor 4 (Klf4) prevents embryonic stem (ES) cell
differentiation by regulating Nanog gene expression.";
J. Biol. Chem. 285:9180-9189(2010).
[17]
INTERACTION WITH ZNF296, AND SUBCELLULAR LOCATION.
PubMed=24161396; DOI=10.1016/j.bbrc.2013.10.073;
Fujii Y., Kakegawa M., Koide H., Akagi T., Yokota T.;
"Zfp296 is a novel Klf4-interacting protein and functions as a
negative regulator.";
Biochem. Biophys. Res. Commun. 441:411-417(2013).
[18]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 395-483 IN COMPLEX WITH ZINC
IONS AND DNA.
Schuetz A., Zocher G., Carstanjen D., Heinemann U.;
"Crystal structure in complex with DNA.";
Submitted (APR-2010) to the PDB data bank.
-!- FUNCTION: Transcription factor; can act both as activator and as
repressor. Binds the 5'-CACCC-3' core sequence. Binds to the
promoter region of its own gene and can activate its own
transcription. Regulates the expression of key transcription
factors during embryonic development. Plays an important role in
maintaining embryonic stem cells, and in preventing their
differentiation. Required for establishing the barrier function of
the skin and for postnatal maturation and maintenance of the
ocular surface. Involved in the differentiation of epithelial
cells and may also function in skeletal and kidney development.
Contributes to the down-regulation of p53/TP53 transcription (By
similarity). {ECO:0000250, ECO:0000269|PubMed:10431239,
ECO:0000269|PubMed:10556311, ECO:0000269|PubMed:15358627,
ECO:0000269|PubMed:16954384, ECO:0000269|PubMed:17060454,
ECO:0000269|PubMed:19816951, ECO:0000269|PubMed:20071344}.
-!- SUBUNIT: Interacts with MUC1 (via the C-terminal domain) (By
similarity). Interacts with POU5F1/OCT4 and SOX2
(PubMed:19816951). Interacts with MEIS2 isoform MeisD and PBX1
isoform PBX1a (By similarity). Interacts with ZNF296
(PubMed:24161396). {ECO:0000250|UniProtKB:O43474,
ECO:0000269|PubMed:19816951, ECO:0000269|PubMed:24161396}.
-!- INTERACTION:
Q9Y297:BTRC (xeno); NbExp=3; IntAct=EBI-3043905, EBI-307461;
Q9UKB1:FBXW11 (xeno); NbExp=4; IntAct=EBI-3043905, EBI-355189;
P27361:MAPK3 (xeno); NbExp=2; IntAct=EBI-3043905, EBI-73995;
Q63844:Mapk3; NbExp=3; IntAct=EBI-3043905, EBI-397682;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10431239,
ECO:0000269|PubMed:24161396}.
-!- TISSUE SPECIFICITY: Highest expression in the colon. Lower levels
in testis, lung and small intestine.
-!- INDUCTION: By interferon-gamma in Stat1-dependent manner.
{ECO:0000269|PubMed:12441126}.
-!- DISRUPTION PHENOTYPE: Death shortly after birth due to loss of
epidermal barrier function resulting from perturbation of late-
stage epidermal differentiation structures including the cornified
envelope. When selectively deleted in the surface ectoderm-derived
structures of the eye, embryos develop normally and adults are
viable and fertile but mutants display down-regulation of Krt12
and Aqp5 and multiple ocular defects including corneal epithelial
fragility, stromal edema, defective lens and loss of conjunctival
goblet cells. {ECO:0000269|PubMed:10431239,
ECO:0000269|PubMed:17060454}.
-!- BIOTECHNOLOGY: POU5F1/OCT4, SOX2, MYC/c-Myc and KLF4 are the four
Yamanaka factors. When combined, these factors are sufficient to
reprogram differentiated cells to an embryonic-like state
designated iPS (induced pluripotent stem) cells. iPS cells exhibit
the morphology and growth properties of ES cells and express ES
cell marker genes. {ECO:0000269|PubMed:16904174,
ECO:0000269|PubMed:19816951}.
-!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC52939.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAH10301.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; U20344; AAC04892.1; -; mRNA.
EMBL; U70662; AAC52939.1; ALT_INIT; mRNA.
EMBL; AF117109; AAD17223.1; -; Genomic_DNA.
EMBL; AY071827; AAL60058.1; -; Genomic_DNA.
EMBL; AK141244; BAE24612.1; -; mRNA.
EMBL; AK144942; BAE26147.1; -; mRNA.
EMBL; AK155343; BAE33205.1; -; mRNA.
EMBL; AL732494; CAM20848.1; -; Genomic_DNA.
EMBL; CH466565; EDL02262.1; -; Genomic_DNA.
EMBL; BC010301; AAH10301.2; ALT_INIT; mRNA.
CCDS; CCDS18195.2; -.
RefSeq; NP_034767.2; NM_010637.3.
UniGene; Mm.4325; -.
PDB; 2WBS; X-ray; 1.70 A; A=395-483.
PDB; 2WBU; X-ray; 2.50 A; A=396-483.
PDB; 4M9E; X-ray; 1.85 A; A=396-483.
PDB; 5KE6; X-ray; 1.99 A; A=396-483.
PDB; 5KE7; X-ray; 2.06 A; A=396-483.
PDB; 5KE8; X-ray; 2.45 A; A=396-483.
PDB; 5KE9; X-ray; 2.34 A; A=396-483.
PDB; 5KEA; X-ray; 2.46 A; A=396-483.
PDB; 5KEB; X-ray; 2.45 A; A=396-483.
PDBsum; 2WBS; -.
PDBsum; 2WBU; -.
PDBsum; 4M9E; -.
PDBsum; 5KE6; -.
PDBsum; 5KE7; -.
PDBsum; 5KE8; -.
PDBsum; 5KE9; -.
PDBsum; 5KEA; -.
PDBsum; 5KEB; -.
ProteinModelPortal; Q60793; -.
SMR; Q60793; -.
BioGrid; 200966; 5.
DIP; DIP-59920N; -.
ELM; Q60793; -.
IntAct; Q60793; 12.
STRING; 10090.ENSMUSP00000103245; -.
iPTMnet; Q60793; -.
PhosphoSitePlus; Q60793; -.
MaxQB; Q60793; -.
PaxDb; Q60793; -.
PRIDE; Q60793; -.
Ensembl; ENSMUST00000107619; ENSMUSP00000103245; ENSMUSG00000003032.
GeneID; 16600; -.
KEGG; mmu:16600; -.
UCSC; uc008sxk.2; mouse.
CTD; 9314; -.
MGI; MGI:1342287; Klf4.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
GeneTree; ENSGT00760000118998; -.
HOGENOM; HOG000060173; -.
HOVERGEN; HBG006220; -.
InParanoid; Q60793; -.
KO; K17846; -.
OMA; STCSFSY; -.
OrthoDB; EOG091G1BN0; -.
PhylomeDB; Q60793; -.
TreeFam; TF350556; -.
Reactome; R-MMU-442533; Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.
EvolutionaryTrace; Q60793; -.
PRO; PR:Q60793; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000003032; -.
CleanEx; MM_KLF4; -.
ExpressionAtlas; Q60793; baseline and differential.
Genevisible; Q60793; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0000790; C:nuclear chromatin; ISO:MGI.
GO; GO:0005719; C:nuclear euchromatin; IDA:BHF-UCL.
GO; GO:0044798; C:nuclear transcription factor complex; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0008013; F:beta-catenin binding; IPI:BHF-UCL.
GO; GO:0001047; F:core promoter binding; IDA:BHF-UCL.
GO; GO:0000987; F:core promoter proximal region sequence-specific DNA binding; ISO:MGI.
GO; GO:0003677; F:DNA binding; ISS:MGI.
GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0035014; F:phosphatidylinositol 3-kinase regulator activity; IEA:Ensembl.
GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
GO; GO:0000975; F:regulatory region DNA binding; IDA:MGI.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; IPI:BHF-UCL.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
GO; GO:0001221; F:transcription cofactor binding; IEA:Ensembl.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:MGI.
GO; GO:0001010; F:transcription factor activity, sequence-specific DNA binding transcription factor recruiting; IDA:BHF-UCL.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:MGI.
GO; GO:0001190; F:transcriptional activator activity, RNA polymerase II transcription factor binding; ISO:MGI.
GO; GO:0060070; P:canonical Wnt signaling pathway; IMP:BHF-UCL.
GO; GO:0030154; P:cell differentiation; IMP:MGI.
GO; GO:0071409; P:cellular response to cycloheximide; IEA:Ensembl.
GO; GO:0071363; P:cellular response to growth factor stimulus; ISO:MGI.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0071499; P:cellular response to laminar fluid shear stress; ISO:MGI.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
GO; GO:1901653; P:cellular response to peptide; IEA:Ensembl.
GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl.
GO; GO:0009913; P:epidermal cell differentiation; IMP:MGI.
GO; GO:0048730; P:epidermis morphogenesis; IMP:MGI.
GO; GO:0045444; P:fat cell differentiation; IMP:BHF-UCL.
GO; GO:0030336; P:negative regulation of cell migration; IMP:CACAO.
GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; ISO:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:MGI.
GO; GO:2000342; P:negative regulation of chemokine (C-X-C motif) ligand 2 production; ISO:MGI.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
GO; GO:0034115; P:negative regulation of heterotypic cell-cell adhesion; ISO:MGI.
GO; GO:0045415; P:negative regulation of interleukin-8 biosynthetic process; ISO:MGI.
GO; GO:1904998; P:negative regulation of leukocyte adhesion to arterial endothelial cell; ISO:MGI.
GO; GO:0014740; P:negative regulation of muscle hyperplasia; IEA:Ensembl.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISO:MGI.
GO; GO:0014067; P:negative regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
GO; GO:0051898; P:negative regulation of protein kinase B signaling; IEA:Ensembl.
GO; GO:0060761; P:negative regulation of response to cytokine stimulus; ISO:MGI.
GO; GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IMP:MGI.
GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISO:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0032270; P:positive regulation of cellular protein metabolic process; ISO:MGI.
GO; GO:1904798; P:positive regulation of core promoter binding; IMP:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
GO; GO:0046985; P:positive regulation of hemoglobin biosynthetic process; ISO:MGI.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:MGI.
GO; GO:0051247; P:positive regulation of protein metabolic process; ISO:MGI.
GO; GO:0051973; P:positive regulation of telomerase activity; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0031077; P:post-embryonic camera-type eye development; IMP:MGI.
GO; GO:0035166; P:post-embryonic hemopoiesis; ISO:MGI.
GO; GO:0048679; P:regulation of axon regeneration; IMP:MGI.
GO; GO:0045595; P:regulation of cell differentiation; IDA:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; IGI:MGI.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0010033; P:response to organic substance; IDA:MGI.
GO; GO:0032526; P:response to retinoic acid; IDA:MGI.
GO; GO:0019827; P:stem cell population maintenance; IDA:UniProtKB.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0006351; P:transcription, DNA-templated; IMP:CACAO.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
SMART; SM00355; ZnF_C2H2; 3.
SUPFAM; SSF57667; SSF57667; 2.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
1: Evidence at protein level;
3D-structure; Activator; Complete proteome; DNA-binding;
Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Transcription; Transcription regulation;
Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 483 Krueppel-like factor 4.
/FTId=PRO_0000047168.
ZN_FING 400 424 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 430 454 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 460 482 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
REGION 386 483 Interaction with ZNF296.
{ECO:0000269|PubMed:24161396}.
REGION 443 474 Interaction with target DNA.
COMPBIAS 176 385 Pro-rich.
MOD_RES 251 251 Phosphoserine.
{ECO:0000250|UniProtKB:O43474}.
CROSSLNK 32 32 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:O43474}.
CONFLICT 162 162 S -> R (in Ref. 2; AAC52939).
{ECO:0000305}.
CONFLICT 185 185 A -> G (in Ref. 2; AAC52939).
{ECO:0000305}.
CONFLICT 302 302 H -> Q (in Ref. 5; BAE33205).
{ECO:0000305}.
CONFLICT 350 350 P -> A (in Ref. 2; AAC52939).
{ECO:0000305}.
TURN 405 407 {ECO:0000244|PDB:2WBS}.
STRAND 410 413 {ECO:0000244|PDB:2WBS}.
HELIX 414 421 {ECO:0000244|PDB:2WBS}.
TURN 435 437 {ECO:0000244|PDB:2WBS}.
STRAND 440 443 {ECO:0000244|PDB:2WBS}.
HELIX 444 455 {ECO:0000244|PDB:2WBS}.
STRAND 463 466 {ECO:0000244|PDB:2WBS}.
STRAND 468 471 {ECO:0000244|PDB:2WBS}.
HELIX 472 478 {ECO:0000244|PDB:2WBS}.
HELIX 479 482 {ECO:0000244|PDB:2WBS}.
SEQUENCE 483 AA; 51880 MW; 5D1B0BF7948C49B3 CRC64;
MRQPPGESDM AVSDALLPSF STFASGPAGR EKTLRPAGAP TNRWREELSH MKRLPPLPGR
PYDLAATVAT DLESGGAGAA CSSNNPALLA RRETEEFNDL LDLDFILSNS LTHQESVAAT
VTTSASASSS SSPASSGPAS APSTCSFSYP IRAGGDPGVA ASNTGGGLLY SRESAPPPTA
PFNLADINDV SPSGGFVAEL LRPELDPVYI PPQQPQPPGG GLMGKFVLKA SLTTPGSEYS
SPSVISVSKG SPDGSHPVVV APYSGGPPRM CPKIKQEAVP SCTVSRSLEA HLSAGPQLSN
GHRPNTHDFP LGRQLPTRTT PTLSPEELLN SRDCHPGLPL PPGFHPHPGP NYPPFLPDQM
QSQVPSLHYQ ELMPPGSCLP EEPKPKRGRR SWPRKRTATH TCDYAGCGKT YTKSSHLKAH
LRTHTGEKPY HCDWDGCGWK FARSDELTRH YRKHTGHRPF QCQKCDRAFS RSDHLALHMK
RHF


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