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Krueppel-like factor 2 (Lung krueppel-like factor)

 KLF2_HUMAN              Reviewed;         355 AA.
Q9Y5W3; Q6IPC4; Q9UJS5; Q9UKR6;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
23-JAN-2002, sequence version 2.
10-OCT-2018, entry version 156.
RecName: Full=Krueppel-like factor 2;
AltName: Full=Lung krueppel-like factor;
Name=KLF2; Synonyms=LKLF;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PRO-104.
TISSUE=Lung;
PubMed=10217429; DOI=10.1016/S0014-5793(99)00348-8;
Kozyrev S.V., Hansen L.L., Poltaraus A.B., Domninsky D.A.,
Kisselev L.L.;
"Structure of the human CpG-island-containing lung Kruppel-like factor
(LKLF) gene and its location in chromosome 19p13.11-13 locus.";
FEBS Lett. 448:149-152(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lung;
PubMed=10458913; DOI=10.1006/geno.1999.5888;
Wani M.A., Conkright M.D., Jeffries S., Hughes M.J., Lingrel J.B.;
"cDNA isolation, genomic structure, regulation, and chromosomal
localization of human lung kruppel-like factor.";
Genomics 60:78-86(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Hair follicle dermal papilla;
Lee H.J., Kim M.K., Kim Y.H., Seo J.M., Lee H.M., Chung H.J.,
Sohn M.Y., Hwang S.Y., Im S.U., Jung E.J., Kim J.C.;
"A catalogue of genes in the human dermal papilla cells as identified
by expressed sequence tags.";
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PRO-104 AND PRO-145.
SeattleSNPs variation discovery resource;
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-104.
TISSUE=Spleen;
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).
[6]
INTERACTION WITH WWP1.
PubMed=11375995; DOI=10.1074/jbc.M103670200;
Conkright M.D., Wani M.A., Lingrel J.B.;
"Lung Krueppel-like factor contains an autoinhibitory domain that
regulates its transcriptional activation by binding WWP1, an E3
ubiquitin ligase.";
J. Biol. Chem. 276:29299-29306(2001).
[7]
FUNCTION.
PubMed=21063504; DOI=10.1007/s12079-010-0095-x;
Lin Z., Natesan V., Shi H., Hamik A., Kawanami D., Hao C.,
Mahabaleshwar G.H., Wang W., Jin Z.G., Atkins G.B., Firth S.M.,
Rittie L., Perbal B., Jain M.K.;
"A novel role of CCN3 in regulating endothelial inflammation.";
J. Cell Commun. Signal. 4:141-153(2010).
-!- FUNCTION: Transcription factor that binds to the CACCC box in the
promoter of target genes such as HBB/beta globin or NOV and
activates their transcription. {ECO:0000269|PubMed:21063504}.
-!- SUBUNIT: Interacts with WWP1. {ECO:0000269|PubMed:11375995}.
-!- INTERACTION:
Q92831:KAT2B; NbExp=2; IntAct=EBI-9846663, EBI-477430;
Q9HCE7:SMURF1; NbExp=2; IntAct=EBI-9846663, EBI-976466;
Q9HCE7-2:SMURF1; NbExp=4; IntAct=EBI-9846663, EBI-9845742;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
-!- PTM: Ubiquitinated. Polyubiquitination involves WWP1 and leads to
proteasomal degradation of this protein (By similarity).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
family. {ECO:0000305}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/klf2/";
-----------------------------------------------------------------------
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EMBL; AF123344; AAD25076.1; -; Genomic_DNA.
EMBL; AF134053; AAD55891.1; -; mRNA.
EMBL; AF205849; AAF13295.1; -; mRNA.
EMBL; EF078888; ABK41959.1; -; Genomic_DNA.
EMBL; BC071983; AAH71983.1; -; mRNA.
CCDS; CCDS12343.1; -.
RefSeq; NP_057354.1; NM_016270.3.
UniGene; Hs.685136; -.
UniGene; Hs.744182; -.
ProteinModelPortal; Q9Y5W3; -.
SMR; Q9Y5W3; -.
BioGrid; 115645; 11.
DIP; DIP-41973N; -.
ELM; Q9Y5W3; -.
IntAct; Q9Y5W3; 2.
STRING; 9606.ENSP00000248071; -.
iPTMnet; Q9Y5W3; -.
PhosphoSitePlus; Q9Y5W3; -.
BioMuta; KLF2; -.
DMDM; 20141620; -.
MaxQB; Q9Y5W3; -.
PaxDb; Q9Y5W3; -.
PeptideAtlas; Q9Y5W3; -.
PRIDE; Q9Y5W3; -.
ProteomicsDB; 86516; -.
Ensembl; ENST00000248071; ENSP00000248071; ENSG00000127528.
GeneID; 10365; -.
KEGG; hsa:10365; -.
UCSC; uc002ndw.4; human.
CTD; 10365; -.
DisGeNET; 10365; -.
EuPathDB; HostDB:ENSG00000127528.5; -.
GeneCards; KLF2; -.
HGNC; HGNC:6347; KLF2.
HPA; HPA055964; -.
MIM; 602016; gene.
neXtProt; NX_Q9Y5W3; -.
OpenTargets; ENSG00000127528; -.
PharmGKB; PA30136; -.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
GeneTree; ENSGT00760000118998; -.
HOGENOM; HOG000060173; -.
HOVERGEN; HBG006220; -.
InParanoid; Q9Y5W3; -.
KO; K17845; -.
OMA; MSFEQPR; -.
OrthoDB; EOG091G1BN0; -.
PhylomeDB; Q9Y5W3; -.
TreeFam; TF350556; -.
SIGNOR; Q9Y5W3; -.
ChiTaRS; KLF2; human.
GeneWiki; KLF2; -.
GenomeRNAi; 10365; -.
PRO; PR:Q9Y5W3; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000127528; Expressed in 234 organ(s), highest expression level in urethra.
CleanEx; HS_KLF2; -.
ExpressionAtlas; Q9Y5W3; baseline and differential.
Genevisible; Q9Y5W3; HS.
GO; GO:0000790; C:nuclear chromatin; IMP:BHF-UCL.
GO; GO:0003677; F:DNA binding; IMP:BHF-UCL.
GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IMP:BHF-UCL.
GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl.
GO; GO:0071409; P:cellular response to cycloheximide; IEA:Ensembl.
GO; GO:0071498; P:cellular response to fluid shear stress; IMP:BHF-UCL.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
GO; GO:0071499; P:cellular response to laminar fluid shear stress; IMP:BHF-UCL.
GO; GO:1901653; P:cellular response to peptide; IEA:Ensembl.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
GO; GO:0097533; P:cellular stress response to acid chemical; IMP:BHF-UCL.
GO; GO:0043249; P:erythrocyte maturation; IEA:Ensembl.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
GO; GO:0032715; P:negative regulation of interleukin-6 production; IEA:Ensembl.
GO; GO:1903671; P:negative regulation of sprouting angiogenesis; IMP:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IDA:BHF-UCL.
GO; GO:0051247; P:positive regulation of protein metabolic process; IGI:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
GO; GO:0036003; P:positive regulation of transcription from RNA polymerase II promoter in response to stress; IMP:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0040029; P:regulation of gene expression, epigenetic; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0060509; P:type I pneumocyte differentiation; IEA:Ensembl.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
Pfam; PF00096; zf-C2H2; 3.
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; Complete proteome; DNA-binding; Metal-binding; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Transcription; Transcription regulation; Ubl conjugation; Zinc;
Zinc-finger.
CHAIN 1 355 Krueppel-like factor 2.
/FTId=PRO_0000047162.
ZN_FING 272 296 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 302 326 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 332 354 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
REGION 111 268 Interaction with WWP1. {ECO:0000250}.
COMPBIAS 62 71 Poly-Pro.
COMPBIAS 130 135 Poly-Gly.
COMPBIAS 167 171 Poly-Pro.
COMPBIAS 225 231 Poly-Ala.
MOD_RES 173 173 Phosphothreonine.
{ECO:0000250|UniProtKB:Q60843}.
MOD_RES 244 244 Phosphothreonine.
{ECO:0000250|UniProtKB:Q60843}.
VARIANT 104 104 L -> P (in dbSNP:rs3745318).
{ECO:0000269|PubMed:10217429,
ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.4}.
/FTId=VAR_038830.
VARIANT 145 145 R -> P (in dbSNP:rs45586032).
{ECO:0000269|Ref.4}.
/FTId=VAR_038831.
CONFLICT 43 43 S -> N (in Ref. 2; AAD55891).
{ECO:0000305}.
CONFLICT 175 175 P -> S (in Ref. 2; AAD55891).
{ECO:0000305}.
CONFLICT 184 184 L -> M (in Ref. 2; AAD55891).
{ECO:0000305}.
SEQUENCE 355 AA; 37420 MW; D5849C831D676AE1 CRC64;
MALSEPILPS FSTFASPCRE RGLQERWPRA EPESGGTDDD LNSVLDFILS MGLDGLGAEA
APEPPPPPPP PAFYYPEPGA PPPYSAPAGG LVSELLRPEL DAPLGPALHG RFLLAPPGRL
VKAEPPEADG GGGYGCAPGL TRGPRGLKRE GAPGPAASCM RGPGGRPPPP PDTPPLSPDG
PARLPAPGPR ASFPPPFGGP GFGAPGPGLH YAPPAPPAFG LFDDAAAAAA ALGLAPPAAR
GLLTPPASPL ELLEAKPKRG RRSWPRKRTA THTCSYAGCG KTYTKSSHLK AHLRTHTGEK
PYHCNWDGCG WKFARSDELT RHYRKHTGHR PFQCHLCDRA FSRSDHLALH MKRHM


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