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Protein

Carbohydrate-responsive element-binding protein

Gene

Mlxipl

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transcriptional repressor. Binds to the canonical and non-canonical E box sequences 5'-CACGTG-3' (By similarity).By similarity

GO - Molecular functioni

  • carbohydrate response element binding Source: BHF-UCL
  • DNA binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • sequence-specific DNA binding Source: RGD
  • transcription factor activity, sequence-specific DNA binding Source: RGD

GO - Biological processi

  • cellular response to glucose stimulus Source: BHF-UCL
  • energy reserve metabolic process Source: Reactome
  • fatty acid homeostasis Source: UniProtKB
  • regulation of energy homeostasis Source: UniProtKB
  • regulation of fatty acid biosynthetic process Source: Reactome
  • regulation of glycolytic process Source: RGD
  • regulation of transcription from RNA polymerase II promoter Source: RGD
  • response to glucose Source: RGD
  • transcription, DNA-templated Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-RNO-163680. AMPK inhibits chREBP transcriptional activation activity.
R-RNO-163767. PP2A-mediated dephosphorylation of key metabolic factors.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbohydrate-responsive element-binding protein
Short name:
ChREBP
Alternative name(s):
Class D basic helix-loop-helix protein 14
Short name:
bHLHd14
MLX interactor
MLX-interacting protein-like
WS basic-helix-loop-helix leucine zipper protein
Short name:
WS-bHLH
Williams-Beuren syndrome chromosomal region 14 protein
Gene namesi
Name:Mlxipl
Synonyms:Wbscr14
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620400. Mlxipl.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation

GO - Cellular componenti

  • cytoplasm Source: RGD
  • cytosol Source: BHF-UCL
  • nucleoplasm Source: Reactome
  • nucleus Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi568 – 5681S → A: Impaired DNA-binding and fatty acid sensitivity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 865865Carbohydrate-responsive element-binding proteinPRO_0000413065Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei20 – 201PhosphoserineBy similarity
Modified residuei23 – 231PhosphoserineCombined sources
Modified residuei25 – 251PhosphoserineCombined sources
Modified residuei27 – 271PhosphothreonineCombined sources
Modified residuei196 – 1961PhosphoserineBy similarity
Modified residuei568 – 5681Phosphoserine; by AMPK1 Publication
Modified residuei615 – 6151PhosphoserineCombined sources
Modified residuei627 – 6271PhosphoserineBy similarity
Modified residuei644 – 6441PhosphoserineBy similarity

Post-translational modificationi

Phosphorylation at Ser-568 by AMPK inactivates the DNA-binding activity.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ8VIP2.
PRIDEiQ8VIP2.

PTM databases

iPTMnetiQ8VIP2.
PhosphoSiteiQ8VIP2.

Interactioni

Subunit structurei

Binds DNA as a heterodimer with TCFL4/MLX.By similarity

GO - Molecular functioni

  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000066522.

Structurei

Secondary structure

1
865
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi118 – 13417Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5F74X-ray2.35B1-196[»]
ProteinModelPortaliQ8VIP2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini662 – 71655bHLHPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni716 – 73722Leucine-zipperAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi308 – 646339Pro-richAdd
BLAST
Compositional biasi345 – 3506Poly-Ser

Sequence similaritiesi

Contains 1 bHLH (basic helix-loop-helix) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3582. Eukaryota.
ENOG410XTA5. LUCA.
HOVERGENiHBG073589.
InParanoidiQ8VIP2.
KOiK09113.
PhylomeDBiQ8VIP2.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
[Graphical view]
PfamiPF00010. HLH. 1 hit.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8VIP2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARALADLSV NLQVPRVVPS PDSDSDTDLE DPSPRRSAGG LHRSQVIHSG
60 70 80 90 100
HFMVSSPHSD SLTRRRDQEG PVGLADFGPR SIDPTLTRLF ECLSLAYSGK
110 120 130 140 150
LVSPKWKNFK GLKLLCRDKI RLNNAIWRAW YIQYVQRRKS PVCGFVTPLQ
160 170 180 190 200
GSEADEHRKP EAVVLEGNYW KRRIEVVMRE YHKWRIYYKK RLRKSSREGD
210 220 230 240 250
FLAPKQVEGG WPPPERWCEQ LFSSVVPVLL GGSEEEPGGR QLLDLDCFLS
260 270 280 290 300
DISDTLFTMT QPSPSSLQLP SEDAYVGNAD MIQPDLTPLQ PSLDDFMEIS
310 320 330 340 350
DFFTNYRPPQ TPTSSNFPEP PSFGPMADSL FSGGILGPEM PSPASASSSS
360 370 380 390 400
GMTPLSGNTR LQARNSCSGP LDPSTFPSSE FLLPEDPKTK MPPAPVPTPL
410 420 430 440 450
LPYPGPVKVH GLEPCTPSPF PTMAPPPALL SEEPLFSARF PFTTVPPAPG
460 470 480 490 500
VSTLPAPTTF VPTPQPGPGP GPVPFPVDHL PHGYLEPVFG PHFTVPQGVQ
510 520 530 540 550
PRCKPCSPPP GGRKASPPTL TSATASPTAT ATARDNNPCL TQLLRAAKPE
560 570 580 590 600
QVLEPSTVPS TLLRPPESPD AVPEIPRVRA FYPPIPAPTP PRPPPGPATL
610 620 630 640 650
APPRSLVVPK AERLSPPASS GSERRPSGDL NSIQPPGALS VHLSPPQTVL
660 670 680 690 700
SRGRVDNNKM ENRRITHISA EQKRRFNIKL GFDTLHGLVS TLSAQPSLKV
710 720 730 740 750
SKATTLQKTA EYILMLQQER AAMQEEAQQL RDEIEELNAA INLCQQQLPA
760 770 780 790 800
TGVPITHQRF DQMRDMFDDY VRTRTLHNWK FWVFSILIRP LFESFNGMVS
810 820 830 840 850
TASLHSLRQT SLAWLDQYCS LPALRPTVLN SLRQLSTSTS ILTDPSLVPE
860
QATRAVTEGP LGRPL
Length:865
Mass (Da):94,921
Last modified:March 1, 2002 - v1
Checksum:i5B818B081B83C641
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB074517 mRNA. Translation: BAB77523.1.
RefSeqiNP_598236.1. NM_133552.1.
UniGeneiRn.144656.

Genome annotation databases

GeneIDi171078.
KEGGirno:171078.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB074517 mRNA. Translation: BAB77523.1.
RefSeqiNP_598236.1. NM_133552.1.
UniGeneiRn.144656.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5F74X-ray2.35B1-196[»]
ProteinModelPortaliQ8VIP2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000066522.

PTM databases

iPTMnetiQ8VIP2.
PhosphoSiteiQ8VIP2.

Proteomic databases

PaxDbiQ8VIP2.
PRIDEiQ8VIP2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi171078.
KEGGirno:171078.

Organism-specific databases

CTDi51085.
RGDi620400. Mlxipl.

Phylogenomic databases

eggNOGiKOG3582. Eukaryota.
ENOG410XTA5. LUCA.
HOVERGENiHBG073589.
InParanoidiQ8VIP2.
KOiK09113.
PhylomeDBiQ8VIP2.

Enzyme and pathway databases

ReactomeiR-RNO-163680. AMPK inhibits chREBP transcriptional activation activity.
R-RNO-163767. PP2A-mediated dephosphorylation of key metabolic factors.

Miscellaneous databases

PROiQ8VIP2.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
[Graphical view]
PfamiPF00010. HLH. 1 hit.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mechanism for fatty acid 'sparing' effect on glucose-induced transcription: regulation of carbohydrate-responsive element-binding protein by AMP-activated protein kinase."
    Kawaguchi T., Osatomi K., Yamashita H., Kabashima T., Uyeda K.
    J. Biol. Chem. 277:3829-3835(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION AT SER-568, MUTAGENESIS OF SER-568.
  2. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-25; THR-27 AND SER-615, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMLXPL_RAT
AccessioniPrimary (citable) accession number: Q8VIP2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: March 1, 2002
Last modified: July 6, 2016
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.