KLF13_MOUSE
ID KLF13_MOUSE Reviewed; 289 AA.
AC Q9JJZ6; Q9ESX3; Q9JHF8;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2001, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Krueppel-like factor 13;
DE AltName: Full=Basic transcription element-binding protein 3;
DE Short=BTE-binding protein 3;
DE AltName: Full=Erythroid transcription factor FKLF-2;
DE AltName: Full=RANTES factor of late activated T-lymphocytes 1;
DE Short=RFLAT-1;
DE AltName: Full=Transcription factor BTEB3;
GN Name=Klf13; Synonyms=Bteb3, Fklf2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=10642511; DOI=10.1042/bj3450529;
RA Martin K.M., Cooper W.N., Metcalfe J.C., Kemp P.R.;
RT "Mouse BTEB3, a new member of the basic transcription element binding
RT protein (BTEB) family, activates expression from GC-rich minimal promoter
RT regions.";
RL Biochem. J. 345:529-533(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=B6D2F2; TISSUE=Yolk;
RX PubMed=10828046;
RA Asano H., Li X.S., Stamatoyannopoulos G.;
RT "FKLF-2: a novel Kruppel-like transcriptional factor that activates globin
RT and other erythroid lineage genes.";
RL Blood 95:3578-3584(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fetal liver;
RX PubMed=11087666; DOI=10.1006/geno.2000.6362;
RA Scohy S., Gabant P., Van Reeth T., Hertveldt V., Dreze P.-L.,
RA Van Vooren P., Riviere M., Szpirer J., Szpirer C.;
RT "Identification of KLF13 and KLF14 (SP6), novel members of the SP/XKLF
RT transcription factor family.";
RL Genomics 70:93-101(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RA Song A., Thamatrakoln K., Krensky A.M.;
RT "Identification of Mus musculus cDNA for RANTES factor of late activated T
RT lymphocytes-1.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280; SER-284 AND SER-288, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Transcription factor that activates expression from GC-rich
CC minimal promoter regions, including genes in the cells of the erythroid
CC lineage.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; AJ245644; CAB75887.1; -; mRNA.
DR EMBL; AF251796; AAF73964.1; -; mRNA.
DR EMBL; AJ275987; CAC06697.1; -; mRNA.
DR EMBL; AF252285; AAF65826.1; -; mRNA.
DR CCDS; CCDS21331.1; -.
DR RefSeq; NP_067341.2; NM_021366.3.
DR AlphaFoldDB; Q9JJZ6; -.
DR SMR; Q9JJZ6; -.
DR BioGRID; 206125; 3.
DR IntAct; Q9JJZ6; 1.
DR MINT; Q9JJZ6; -.
DR STRING; 10090.ENSMUSP00000067680; -.
DR iPTMnet; Q9JJZ6; -.
DR PhosphoSitePlus; Q9JJZ6; -.
DR EPD; Q9JJZ6; -.
DR jPOST; Q9JJZ6; -.
DR MaxQB; Q9JJZ6; -.
DR PaxDb; Q9JJZ6; -.
DR PeptideAtlas; Q9JJZ6; -.
DR PRIDE; Q9JJZ6; -.
DR ProteomicsDB; 264767; -.
DR Antibodypedia; 9456; 185 antibodies from 32 providers.
DR DNASU; 50794; -.
DR Ensembl; ENSMUST00000063694; ENSMUSP00000067680; ENSMUSG00000052040.
DR GeneID; 50794; -.
DR KEGG; mmu:50794; -.
DR UCSC; uc009hfn.2; mouse.
DR CTD; 51621; -.
DR MGI; MGI:1354948; Klf13.
DR VEuPathDB; HostDB:ENSMUSG00000052040; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161911; -.
DR HOGENOM; CLU_002678_33_2_1; -.
DR InParanoid; Q9JJZ6; -.
DR OMA; NQHVPNS; -.
DR OrthoDB; 1308225at2759; -.
DR PhylomeDB; Q9JJZ6; -.
DR TreeFam; TF351003; -.
DR BioGRID-ORCS; 50794; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Klf13; mouse.
DR PRO; PR:Q9JJZ6; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9JJZ6; protein.
DR Bgee; ENSMUSG00000052040; Expressed in rostral migratory stream and 267 other tissues.
DR ExpressionAtlas; Q9JJZ6; baseline and differential.
DR Genevisible; Q9JJZ6; MM.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:BHF-UCL.
DR GO; GO:0045647; P:negative regulation of erythrocyte differentiation; IMP:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; ISS:MGI.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..289
FT /note="Krueppel-like factor 13"
FT /id="PRO_0000047185"
FT ZN_FING 168..192
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 198..222
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 228..250
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 23..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..126
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Y9"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Y9"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 13..30
FT /note="ECLVSMSSRAVVHEPREG -> SASCPCQPRSRARAAGR (in Ref. 3;
FT CAC06697)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="E -> R (in Ref. 1; CAB75887)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="P -> L (in Ref. 1; CAB75887)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 289 AA; 31136 MW; E248EF12890DA090 CRC64;
MAAAAYVDHF AAECLVSMSS RAVVHEPREG PEPRPEGAAA AAPTLPRVDE RRDGKDSASL
FVVARILADL NQQAPAPAPA ERREGAAARK ARTPCRLPPA PPAPPPGPEP ASPGQAGAPA
APPSPAWSEP EAALEQEPGP AGSGEPGLRQ RGRRGRSRAD LESPQRKHKC HYAGCEKVYG
KSSHLKAHLR THTGERPFAC SWQECNKKFA RSDELARHYR THTGEKKFSC PICEKRFMRS
DHLTKHARRH ANFHPGMLQR RGGGSRTGSL SDYSRSDASS PTISPASSP
