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

 KLF4_HUMAN              Reviewed;         513 AA.
O43474; B2R8S4; B3KT79; L0R3I6; L0R4N5; P78338; Q5T3J8; Q5T3J9;
Q8N717; Q9UNP3;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
10-FEB-2009, sequence version 3.
23-MAY-2018, entry version 176.
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;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=9422764; DOI=10.1074/jbc.273.2.1026;
Yet S.-F., McA'Nulty M.M., Folta S.C., Yen H.-W., Yoshizumi M.,
Hsieh C.-M., Layne M.D., Chin M.T., Wang H., Perrella M.A., Jain M.K.,
Lee M.-E.;
"Human EZF, a Kruppel-like zinc finger protein, is expressed in
vascular endothelial cells and contains transcriptional activation and
repression domains.";
J. Biol. Chem. 273:1026-1031(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=10392904;
Foster K.W., Ren S., Louro I.D., Lobo-Ruppert S.M., McKie-Bell P.,
Grizzle W., Hayes M.R., Broker T.R., Chow L.T., Ruppert J.M.;
"Oncogene expression cloning by retroviral transduction of adenovirus
E1A-immortalized rat kidney RK3E cells: transformation of a host with
epithelial features by c-MYC and the zinc finger protein GKLF.";
Cell Growth Differ. 10:423-434(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 5), AND ALTERNATIVE
SPLICING.
PubMed=23134681; DOI=10.1096/fj.12-220319;
Camacho-Vanegas O., Till J., Miranda-Lorenzo I., Ozturk B.,
Camacho S.C., Martignetti J.A.;
"Shaking the family tree: Identification of novel and biologically
active alternatively spliced isoforms across the KLF family of
transcription factors.";
FASEB J. 27:432-436(2013).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANTS SER-315 AND
PHE-321.
TISSUE=Placenta;
Garrett-Sinha L.A., de Crombrugghe B.;
Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=Substantia nigra, and Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Cervix, and Lung;
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).
[10]
INTERACTION WITH MUC1, AND FUNCTION.
PubMed=17308127; DOI=10.1158/0008-5472.CAN-06-3063;
Wei X., Xu H., Kufe D.;
"Human mucin 1 oncoprotein represses transcription of the p53 tumor
suppressor gene.";
Cancer Res. 67:1853-1858(2007).
[11]
BIOTECHNOLOGY.
PubMed=18035408; DOI=10.1016/j.cell.2007.11.019;
Takahashi K., Tanabe K., Ohnuki M., Narita M., Ichisaka T., Tomoda K.,
Yamanaka S.;
"Induction of pluripotent stem cells from adult human fibroblasts by
defined factors.";
Cell 131:861-872(2007).
[12]
DOMAIN.
PubMed=17467953; DOI=10.1016/j.ygeno.2007.02.003;
Piskacek S., Gregor M., Nemethova M., Grabner M., Kovarik P.,
Piskacek M.;
"Nine-amino-acid transactivation domain: establishment and prediction
utilities.";
Genomics 89:756-768(2007).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-32, AND IDENTIFICATION BY
MASS SPECTROMETRY.
TISSUE=Liver;
PubMed=18655026; DOI=10.1002/pmic.200700887;
Tan F., Lu L., Cai Y., Wang J., Xie Y., Wang L., Gong Y., Xu B.-E.,
Wu J., Luo Y., Qiang B., Yuan J., Sun X., Peng X.;
"Proteomic analysis of ubiquitinated proteins in normal hepatocyte
cell line Chang liver cells.";
Proteomics 8:2885-2896(2008).
[15]
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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
INTERACTION WITH PBX1 AND MEIS2.
PubMed=21746878; DOI=10.1128/MCB.01456-10;
Bjerke G.A., Hyman-Walsh C., Wotton D.;
"Cooperative transcriptional activation by Klf4, Meis2, and Pbx1.";
Mol. Cell. Biol. 31:3723-3733(2011).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- 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.
{ECO:0000269|PubMed:17308127, ECO:0000269|PubMed:20071344}.
-!- SUBUNIT: Interacts with POU5F1/OCT4 and SOX2 (By similarity).
Interacts with MUC1 (via the C-terminal domain) (PubMed:17308127).
Interacts with MEIS2 isoform 4 and PBX1 isoform PBX1a
(PubMed:21746878). Interacts with ZNF296 (By similarity).
{ECO:0000250|UniProtKB:Q60793, ECO:0000269|PubMed:17308127,
ECO:0000269|PubMed:21746878}.
-!- INTERACTION:
Q13363:CTBP1; NbExp=4; IntAct=EBI-7232405, EBI-908846;
O95983:MBD3; NbExp=3; IntAct=EBI-7232405, EBI-1783068;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=O43474-3; Sequence=Displayed;
Name=2;
IsoId=O43474-1; Sequence=VSP_036399;
Name=3;
IsoId=O43474-4; Sequence=VSP_040569, VSP_036399;
Note=No experimental confirmation available.;
Name=4; Synonyms=1a;
IsoId=O43474-5; Sequence=VSP_047470, VSP_047473;
Name=5;
IsoId=O43474-6; Sequence=VSP_047471, VSP_047472;
-!- DOMAIN: the 9aaTAD motif is a transactivation domain present in a
large number of yeast and animal transcription factors.
{ECO:0000269|PubMed:17467953}.
-!- 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:18035408}.
-!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB48399.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAC03462.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAD42165.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAH29923.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAH30811.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=ABG25917.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=BAG36271.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=EAW59020.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=EAW59021.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/KLF4ID44316ch9q31.html";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/klf4/";
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EMBL; AF022184; AAC03462.1; ALT_INIT; mRNA.
EMBL; AF105036; AAD42165.1; ALT_INIT; mRNA.
EMBL; HF546201; CCO02787.1; -; mRNA.
EMBL; HF546202; CCO02788.1; -; mRNA.
EMBL; U70663; AAB48399.1; ALT_INIT; mRNA.
EMBL; AK095134; BAG52991.1; -; mRNA.
EMBL; AK313489; BAG36271.1; ALT_INIT; mRNA.
EMBL; DQ658241; ABG25917.1; ALT_SEQ; Genomic_DNA.
EMBL; AL360218; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471105; EAW59020.1; ALT_SEQ; Genomic_DNA.
EMBL; CH471105; EAW59021.1; ALT_SEQ; Genomic_DNA.
EMBL; BC029923; AAH29923.1; ALT_INIT; mRNA.
EMBL; BC030811; AAH30811.1; ALT_INIT; mRNA.
CCDS; CCDS6770.2; -. [O43474-1]
RefSeq; NP_001300981.1; NM_001314052.1. [O43474-3]
RefSeq; NP_004226.3; NM_004235.5. [O43474-1]
UniGene; Hs.376206; -.
ProteinModelPortal; O43474; -.
SMR; O43474; -.
BioGrid; 114726; 32.
DIP; DIP-57667N; -.
IntAct; O43474; 15.
MINT; O43474; -.
iPTMnet; O43474; -.
PhosphoSitePlus; O43474; -.
BioMuta; KLF4; -.
MaxQB; O43474; -.
PeptideAtlas; O43474; -.
PRIDE; O43474; -.
DNASU; 9314; -.
Ensembl; ENST00000374672; ENSP00000363804; ENSG00000136826. [O43474-1]
GeneID; 9314; -.
KEGG; hsa:9314; -.
UCSC; uc004bdg.4; human. [O43474-3]
CTD; 9314; -.
DisGeNET; 9314; -.
EuPathDB; HostDB:ENSG00000136826.14; -.
GeneCards; KLF4; -.
HGNC; HGNC:6348; KLF4.
HPA; HPA002926; -.
MIM; 602253; gene.
neXtProt; NX_O43474; -.
OpenTargets; ENSG00000136826; -.
PharmGKB; PA30138; -.
GeneTree; ENSGT00760000118998; -.
HOVERGEN; HBG006220; -.
InParanoid; O43474; -.
KO; K17846; -.
OMA; STCSFSY; -.
OrthoDB; EOG091G1BN0; -.
PhylomeDB; O43474; -.
TreeFam; TF350556; -.
Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
Reactome; R-HSA-422085; Synthesis, secretion, and deacylation of Ghrelin.
Reactome; R-HSA-452723; Transcriptional regulation of pluripotent stem cells.
SignaLink; O43474; -.
SIGNOR; O43474; -.
ChiTaRS; KLF4; human.
GeneWiki; KLF4; -.
GenomeRNAi; 9314; -.
PRO; PR:O43474; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000136826; -.
CleanEx; HS_KLF4; -.
ExpressionAtlas; O43474; baseline and differential.
Genevisible; O43474; HS.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0005719; C:nuclear euchromatin; IEA:Ensembl.
GO; GO:0044798; C:nuclear transcription factor complex; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0008013; F:beta-catenin binding; IEA:Ensembl.
GO; GO:0003700; F:DNA binding transcription factor activity; TAS:ProtInc.
GO; GO:0035014; F:phosphatidylinositol 3-kinase regulator activity; IEA:Ensembl.
GO; GO:1990841; F:promoter-specific chromatin binding; IDA:UniProtKB.
GO; GO:0000987; F:proximal promoter sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; IPI:BHF-UCL.
GO; GO:0001010; F:transcription factor activity, sequence-specific DNA binding transcription factor recruiting; ISS:BHF-UCL.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISS:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IMP:BHF-UCL.
GO; GO:0001190; F:transcriptional activator activity, RNA polymerase II transcription factor binding; IDA:BHF-UCL.
GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
GO; GO:0071409; P:cellular response to cycloheximide; IEA:Ensembl.
GO; GO:0071363; P:cellular response to growth factor stimulus; IDA:BHF-UCL.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0071499; P:cellular response to laminar fluid shear stress; IMP:BHF-UCL.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
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; IEA:Ensembl.
GO; GO:0048730; P:epidermis morphogenesis; IEA:Ensembl.
GO; GO:0045444; P:fat cell differentiation; ISS:BHF-UCL.
GO; GO:0007500; P:mesodermal cell fate determination; TAS:ProtInc.
GO; GO:0016525; P:negative regulation of angiogenesis; IDA:BHF-UCL.
GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; IDA:BHF-UCL.
GO; GO:0008285; P:negative regulation of cell proliferation; TAS:ProtInc.
GO; GO:2000342; P:negative regulation of chemokine (C-X-C motif) ligand 2 production; IDA:BHF-UCL.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:BHF-UCL.
GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IDA:BHF-UCL.
GO; GO:0010629; P:negative regulation of gene expression; IGI:BHF-UCL.
GO; GO:0034115; P:negative regulation of heterotypic cell-cell adhesion; IDA:BHF-UCL.
GO; GO:0050728; P:negative regulation of inflammatory response; TAS:BHF-UCL.
GO; GO:0045415; P:negative regulation of interleukin-8 biosynthetic process; IDA:BHF-UCL.
GO; GO:1904998; P:negative regulation of leukocyte adhesion to arterial endothelial cell; IGI:BHF-UCL.
GO; GO:0014740; P:negative regulation of muscle hyperplasia; IEA:Ensembl.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:BHF-UCL.
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; IDA:BHF-UCL.
GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0032270; P:positive regulation of cellular protein metabolic process; IMP:BHF-UCL.
GO; GO:1904798; P:positive regulation of core promoter binding; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; IGI:BHF-UCL.
GO; GO:0046985; P:positive regulation of hemoglobin biosynthetic process; IMP:BHF-UCL.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IMP:BHF-UCL.
GO; GO:0051247; P:positive regulation of protein metabolic process; IGI:BHF-UCL.
GO; GO:1903672; P:positive regulation of sprouting angiogenesis; IGI:BHF-UCL.
GO; GO:0051973; P:positive regulation of telomerase activity; IDA:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL.
GO; GO:0031077; P:post-embryonic camera-type eye development; IEA:Ensembl.
GO; GO:0035166; P:post-embryonic hemopoiesis; IMP:BHF-UCL.
GO; GO:0061614; P:pri-miRNA transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:0048679; P:regulation of axon regeneration; IEA:Ensembl.
GO; GO:0045595; P:regulation of cell differentiation; ISS:UniProtKB.
GO; GO:0035019; P:somatic stem cell population maintenance; TAS:Reactome.
GO; GO:0019827; P:stem cell population maintenance; ISS:UniProtKB.
GO; GO:0006366; P:transcription by RNA polymerase II; ISS:BHF-UCL.
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;
Activator; Alternative splicing; Complete proteome; DNA-binding;
Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Transcription; Transcription regulation;
Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 513 Krueppel-like factor 4.
/FTId=PRO_0000047167.
ZN_FING 430 454 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 460 484 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 490 512 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
REGION 416 513 Interaction with ZNF296.
{ECO:0000250|UniProtKB:Q60793}.
REGION 473 504 Interaction with target DNA.
{ECO:0000250}.
MOTIF 101 109 9aaTAD.
COMPBIAS 125 149 Ser-rich.
COMPBIAS 179 415 Pro-rich.
MOD_RES 254 254 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
CROSSLNK 32 32 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:18655026}.
VAR_SEQ 1 50 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_040569.
VAR_SEQ 43 118 RWREELSHMKRLPPVLPGRPYDLAAATVATDLESGGAGAAC
GGSNLAPLPRRETEEFNDLLDLDFILSNSLTHPPE -> SS
CHPVPACQRSPSQRGEDDRGPGKGPPPTLVITRAAAKPTQR
VPISRHTCEPTQVRNLTTVTGTAVDGNSPAQMN (in
isoform 4).
{ECO:0000303|PubMed:23134681}.
/FTId=VSP_047470.
VAR_SEQ 43 63 RWREELSHMKRLPPVLPGRPY -> VRNLTTVTGTAVDGNS
PAQMN (in isoform 5).
{ECO:0000303|PubMed:23134681}.
/FTId=VSP_047471.
VAR_SEQ 64 513 Missing (in isoform 5).
{ECO:0000303|PubMed:23134681}.
/FTId=VSP_047472.
VAR_SEQ 119 513 Missing (in isoform 4).
{ECO:0000303|PubMed:23134681}.
/FTId=VSP_047473.
VAR_SEQ 367 400 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:10392904,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9422764,
ECO:0000303|Ref.4}.
/FTId=VSP_036399.
VARIANT 315 315 T -> S (in dbSNP:rs1059913).
{ECO:0000269|Ref.4}.
/FTId=VAR_059888.
VARIANT 321 321 L -> F (in dbSNP:rs1059914).
{ECO:0000269|Ref.4}.
/FTId=VAR_059889.
CONFLICT 60 61 GR -> AG (in Ref. 1; AAC03462).
{ECO:0000305}.
CONFLICT 77 77 G -> A (in Ref. 1; AAC03462).
{ECO:0000305}.
CONFLICT 251 251 S -> T (in Ref. 1; AAC03462).
{ECO:0000305}.
CONFLICT 304 304 D -> N (in Ref. 4; AAB48399).
{ECO:0000305}.
CONFLICT 329 329 D -> E (in Ref. 4; AAB48399).
{ECO:0000305}.
SEQUENCE 513 AA; 54671 MW; 3B6113A3EF333935 CRC64;
MRQPPGESDM AVSDALLPSF STFASGPAGR EKTLRQAGAP NNRWREELSH MKRLPPVLPG
RPYDLAAATV ATDLESGGAG AACGGSNLAP LPRRETEEFN DLLDLDFILS NSLTHPPESV
AATVSSSASA SSSSSPSSSG PASAPSTCSF TYPIRAGNDP GVAPGGTGGG LLYGRESAPP
PTAPFNLADI NDVSPSGGFV AELLRPELDP VYIPPQQPQP PGGGLMGKFV LKASLSAPGS
EYGSPSVISV SKGSPDGSHP VVVAPYNGGP PRTCPKIKQE AVSSCTHLGA GPPLSNGHRP
AAHDFPLGRQ LPSRTTPTLG LEEVLSSRDC HPALPLPPGF HPHPGPNYPS FLPDQMQPQV
PPLHYQGQSR GFVARAGEPC VCWPHFGTHG MMLTPPSSPL ELMPPGSCMP EEPKPKRGRR
SWPRKRTATH TCDYAGCGKT YTKSSHLKAH LRTHTGEKPY HCDWDGCGWK FARSDELTRH
YRKHTGHRPF QCQKCDRAFS RSDHLALHMK RHF


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