MLXPL_MOUSE
ID MLXPL_MOUSE Reviewed; 864 AA.
AC Q99MZ3; Q99MY9; Q99MZ0; Q99MZ1; Q99MZ2; Q9JLM5;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Carbohydrate-responsive element-binding protein;
DE Short=ChREBP;
DE AltName: Full=MLX interactor;
DE AltName: Full=MLX-interacting protein-like;
DE AltName: Full=Williams-Beuren syndrome chromosomal region 14 protein homolog;
GN Name=Mlxipl; Synonyms=Mio, Wbscr14;
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], CHARACTERIZATION, AND ALTERNATIVE SPLICING.
RX PubMed=11230181; DOI=10.1093/hmg/10.6.617;
RA Cairo S., Merla G., Urbinati F., Ballabio A., Reymond A.;
RT "WBSCR14, a gene mapping to the Williams-Beuren syndrome deleted region, is
RT a new member of the Mlx transcription factor network.";
RL Hum. Mol. Genet. 10:617-627(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10780788; DOI=10.1038/sj.ejhg.5200435;
RA de Luis O., Valero M.C., Perez Jurado L.A.;
RT "WBSCR14, a putative transcription factor gene deleted in Williams-Beuren
RT syndrome: complete characterisation of the human gene and the mouse
RT ortholog.";
RL Eur. J. Hum. Genet. 8:215-222(2000).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23 AND SER-25, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-25 AND THR-27, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-23; SER-25; SER-626
RP AND SER-643, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, and Testis;
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: Transcriptional repressor. Binds to the canonical and non-
CC canonical E box sequences 5'-CACGTG-3'.
CC -!- SUBUNIT: Binds DNA as a heterodimer with TCFL4/MLX.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=Zeta;
CC IsoId=Q99MZ3-1; Sequence=Displayed;
CC Name=2; Synonyms=Theta;
CC IsoId=Q99MZ3-2; Sequence=VSP_002174;
CC Name=3; Synonyms=Iota;
CC IsoId=Q99MZ3-3; Sequence=VSP_002177, VSP_002178;
CC Name=4; Synonyms=Kappa;
CC IsoId=Q99MZ3-4; Sequence=VSP_002179, VSP_002180;
CC Name=5; Synonyms=Eta;
CC IsoId=Q99MZ3-5; Sequence=VSP_002175, VSP_002176;
CC -!- TISSUE SPECIFICITY: Expressed in the ventricular and intermediate zones
CC of the developing spinal cord of 12.5 dpc embryos. In later embryos
CC expressed in a variety of tissues.
CC -!- PTM: Phosphorylation at Ser-566 by AMPK inactivates the DNA-binding
CC activity. {ECO:0000250}.
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DR EMBL; AF245475; AAK20940.1; -; mRNA.
DR EMBL; AF245476; AAK20941.1; -; mRNA.
DR EMBL; AF245477; AAK20942.1; -; mRNA.
DR EMBL; AF245478; AAK20943.1; -; mRNA.
DR EMBL; AF245479; AAK20944.1; -; mRNA.
DR EMBL; AF156604; AAF68175.1; -; mRNA.
DR CCDS; CCDS39316.1; -. [Q99MZ3-1]
DR RefSeq; NP_067430.2; NM_021455.4. [Q99MZ3-1]
DR PDB; 4GNT; X-ray; 2.41 A; B=117-137.
DR PDBsum; 4GNT; -.
DR AlphaFoldDB; Q99MZ3; -.
DR SMR; Q99MZ3; -.
DR BioGRID; 208443; 6.
DR STRING; 10090.ENSMUSP00000005507; -.
DR iPTMnet; Q99MZ3; -.
DR PhosphoSitePlus; Q99MZ3; -.
DR MaxQB; Q99MZ3; -.
DR PaxDb; Q99MZ3; -.
DR PeptideAtlas; Q99MZ3; -.
DR PRIDE; Q99MZ3; -.
DR ProteomicsDB; 290086; -. [Q99MZ3-1]
DR ProteomicsDB; 290087; -. [Q99MZ3-2]
DR ProteomicsDB; 290088; -. [Q99MZ3-3]
DR ProteomicsDB; 290089; -. [Q99MZ3-4]
DR ProteomicsDB; 290090; -. [Q99MZ3-5]
DR Antibodypedia; 14346; 354 antibodies from 30 providers.
DR DNASU; 58805; -.
DR Ensembl; ENSMUST00000005507; ENSMUSP00000005507; ENSMUSG00000005373. [Q99MZ3-1]
DR Ensembl; ENSMUST00000128691; ENSMUSP00000121348; ENSMUSG00000005373. [Q99MZ3-4]
DR Ensembl; ENSMUST00000129008; ENSMUSP00000114933; ENSMUSG00000005373. [Q99MZ3-5]
DR Ensembl; ENSMUST00000153519; ENSMUSP00000122198; ENSMUSG00000005373. [Q99MZ3-3]
DR GeneID; 58805; -.
DR KEGG; mmu:58805; -.
DR UCSC; uc008zxt.2; mouse. [Q99MZ3-1]
DR CTD; 51085; -.
DR MGI; MGI:1927999; Mlxipl.
DR VEuPathDB; HostDB:ENSMUSG00000005373; -.
DR eggNOG; KOG3582; Eukaryota.
DR GeneTree; ENSGT00940000159210; -.
DR HOGENOM; CLU_007471_1_0_1; -.
DR InParanoid; Q99MZ3; -.
DR OMA; EYHTSSM; -.
DR OrthoDB; 388166at2759; -.
DR PhylomeDB; Q99MZ3; -.
DR TreeFam; TF324749; -.
DR Reactome; R-MMU-163358; PKA-mediated phosphorylation of key metabolic factors.
DR Reactome; R-MMU-163765; ChREBP activates metabolic gene expression.
DR BioGRID-ORCS; 58805; 5 hits in 75 CRISPR screens.
DR ChiTaRS; Mlxipl; mouse.
DR PRO; PR:Q99MZ3; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q99MZ3; protein.
DR Bgee; ENSMUSG00000005373; Expressed in crypt of Lieberkuhn of small intestine and 126 other tissues.
DR ExpressionAtlas; Q99MZ3; baseline and differential.
DR Genevisible; Q99MZ3; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0035538; F:carbohydrate response element binding; TAS:BHF-UCL.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IDA:BHF-UCL.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0071333; P:cellular response to glucose stimulus; ISO:MGI.
DR GO; GO:0097009; P:energy homeostasis; ISS:UniProtKB.
DR GO; GO:0055089; P:fatty acid homeostasis; ISS:UniProtKB.
DR GO; GO:0042593; P:glucose homeostasis; IMP:BHF-UCL.
DR GO; GO:0010255; P:glucose mediated signaling pathway; IDA:BHF-UCL.
DR GO; GO:0090324; P:negative regulation of oxidative phosphorylation; ISO:MGI.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:BHF-UCL.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IMP:BHF-UCL.
DR GO; GO:0045821; P:positive regulation of glycolytic process; IMP:BHF-UCL.
DR GO; GO:0046889; P:positive regulation of lipid biosynthetic process; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL.
DR GO; GO:0006110; P:regulation of glycolytic process; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0009749; P:response to glucose; ISO:MGI.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..864
FT /note="Carbohydrate-responsive element-binding protein"
FT /id="PRO_0000127505"
FT DOMAIN 661..715
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 15..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..736
FT /note="Leucine-zipper"
FT COMPBIAS 339..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..601
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:21183079"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:21183079"
FT MOD_RES 27
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18630941"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NP71"
FT MOD_RES 566
FT /note="Phosphoserine; by AMPK"
FT /evidence="ECO:0000250|UniProtKB:Q8VIP2"
FT MOD_RES 614
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NP71"
FT MOD_RES 626
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 643
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 58..79
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_002174"
FT VAR_SEQ 545..556
FT /note="AKPEQALEPPTM -> VVLIVLPVPSQA (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_002175"
FT VAR_SEQ 557..864
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_002176"
FT VAR_SEQ 699..744
FT /note="VSKATTLQKTAEYILMLQQERAAMQEEAQQLRDEIEELNAAINLCQ -> GL
FT PTQRPTLVALAGEQSNHASEDSGVHPDAAAGTGSYAGGGAAAAG (in isoform
FT 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_002177"
FT VAR_SEQ 699..714
FT /note="VSKATTLQKTAEYILM -> LPGLANTEAHIGGARR (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_002179"
FT VAR_SEQ 715..864
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_002180"
FT VAR_SEQ 745..864
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_002178"
FT CONFLICT 67
FT /note="D -> Y (in Ref. 2; AAF68175)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="K -> N (in Ref. 2; AAF68175)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="R -> I (in Ref. 2; AAF68175)"
FT /evidence="ECO:0000305"
FT CONFLICT 138..139
FT /note="RK -> TR (in Ref. 2; AAF68175)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="D -> H (in Ref. 2; AAF68175)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="E -> D (in Ref. 2; AAF68175)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="K -> V (in Ref. 2; AAF68175)"
FT /evidence="ECO:0000305"
FT CONFLICT 727..728
FT /note="QQ -> HE (in Ref. 2; AAF68175)"
FT /evidence="ECO:0000305"
FT HELIX 118..134
FT /evidence="ECO:0007829|PDB:4GNT"
SQ SEQUENCE 864 AA; 94875 MW; 7E6AFFB04C71B327 CRC64;
MARALADLSV NLQVPRVVPS PDSDSDTDLE DPSPRRSAGG LHRSQVIHSG HFMVSSPHSD
SLTRRRDQEG PVGLADFGPR SIDPTLTHLF ECLSLAYSGK LVSPKWKNFK GLKLLCRDKI
RLNNAIWRAW YIQYVQRRKS PVCGFVTPLQ GSEADEHRKP EAVILEGNYW KRRIEVVMRE
YHKWRIYYKK RLRKSSREGD FLAPKQVEGG WPPPERWCEQ LFSSVVPVLL GGSEEEPGGR
QLLDLDCFLS DISDTLFTMT QPSPSSLQLP PEDAYVGNAD MIQPDLTPLQ PSLDDFMEIS
DFFTNYRPPQ TPTSSNYIES PSFGPMADSL FSSGILAPEM PSPASSSSSS GMTPHSGNTR
LQARNSCSGP LDPNPFLSSE FLLPEDPKTK IPPAPGPTPL LPFPTPVKVH GLEPCTPSPF
PTMAPPPSLL PEESLLSARF PFTSAPPAPG VSTLPAPTTF VPTPQPGPGP VPFSVDHLPH
GYLEPVFGPH FTVPQGMQPR CKPSSPSPGG QKASPPTLAS ATASPTATAT ARDNNPCLTQ
LLRAAKPEQA LEPPTMPGTL LRPPESPQDT VSEIPRARAF FPPIPAPTPP RPPPGPATLA
PPRSLVVPKA ERLSPPASSG SERRLSGDLN SIQPSGALSV HLSPPQTVLS RGRVDNNKME
NRRITHISAE QKRRFNIKLG FDTLHGLVST LSAQPSLKVS KATTLQKTAE YILMLQQERA
AMQEEAQQLR DEIEELNAAI NLCQQQLPAT GVPITHQRFD QMRDMFDDYV RTRTLHNWKF
WVFSILIRPL FESFNGMVST ASLHSLRQTS LAWLEQYCSL PALRPTVLNS LRQLSTSTSI
LTDPSLVPEQ ATRAVTEGTL GRPL
