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MLX_MOUSE
ID   MLX_MOUSE               Reviewed;         298 AA.
AC   O08609; Q9EQJ7; Q9EQJ8;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-2022, entry version 167.
DE   RecName: Full=Max-like protein X;
DE   AltName: Full=Max-like bHLHZip protein;
DE   AltName: Full=Protein BigMax;
DE   AltName: Full=Transcription factor-like protein 4;
GN   Name=Mlx; Synonyms=Tcfl4;
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] (ISOFORM GAMMA), AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/cJ; TISSUE=Intestine;
RX   PubMed=8973301; DOI=10.1016/s0378-1119(96)00376-9;
RA   Bjerknes M., Cheng H.;
RT   "TCFL4: a gene at 17q21.1 encoding a putative basic helix-loop-helix
RT   leucine-zipper transcription factor.";
RL   Gene 181:7-11(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RX   PubMed=10918583; DOI=10.1038/sj.onc.1203634;
RA   Meroni G., Cairo S., Merla G., Messali S., Brent R., Ballabio A.,
RA   Reymond A.;
RT   "Mlx, a new Max-like bHLHZip family member: the center stage of a novel
RT   transcription factors regulatory pathway?";
RL   Oncogene 19:3266-3277(2000).
RN   [3]
RP   FUNCTION, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Embryonic stem cell;
RX   PubMed=10593926; DOI=10.1074/jbc.274.51.36344;
RA   Billin A.N., Eilers A.L., Queva C., Ayer D.E.;
RT   "Mlx, a novel Max-like bHLHZip protein that interacts with the Max network
RT   of transcription factors.";
RL   J. Biol. Chem. 274:36344-36350(1999).
RN   [4]
RP   FUNCTION, AND INTERACTION WITH MLXIP.
RX   PubMed=11073985; DOI=10.1128/mcb.20.23.8845-8854.2000;
RA   Billin A.N., Eilers A.L., Coulter K.L., Logan J.S., Ayer D.E.;
RT   "MondoA, a novel basic helix-loop-helix-leucine zipper transcriptional
RT   activator that constitutes a positive branch of a max-like network.";
RL   Mol. Cell. Biol. 20:8845-8854(2000).
RN   [5]
RP   FUNCTION.
RX   PubMed=16644671; DOI=10.2337/db05-0822;
RA   Li M.V., Chang B., Imamura M., Poungvarin N., Chan L.;
RT   "Glucose-dependent transcriptional regulation by an evolutionarily
RT   conserved glucose-sensing module.";
RL   Diabetes 55:1179-1189(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 AND SER-48, 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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 AND SER-48, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Pancreas, Spleen, and
RC   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: Transcription regulator. Forms a sequence-specific DNA-
CC       binding protein complex with MAD1, MAD4, MNT, WBSCR14 and MLXIP which
CC       recognizes the core sequence 5'-CACGTG-3'. The TCFL4-MAD1, TCFL4-MAD4,
CC       TCFL4-WBSCR14 complexes are transcriptional repressors. Plays a role in
CC       transcriptional activation of glycolytic target genes. Involved in
CC       glucose-responsive gene regulation. {ECO:0000269|PubMed:10593926,
CC       ECO:0000269|PubMed:11073985, ECO:0000269|PubMed:16644671}.
CC   -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC       protein. Binds DNA as a heterodimer with MAD1, MAD4, MNT, WBSCR14 and
CC       MLXIP. Can also bind DNA as a homodimer.
CC   -!- SUBCELLULAR LOCATION: [Isoform Alpha]: Cytoplasm
CC       {ECO:0000250|UniProtKB:Q9UH92}. Note=Found predominantly in the
CC       cytoplasm. {ECO:0000250|UniProtKB:Q9UH92}.
CC   -!- SUBCELLULAR LOCATION: [Isoform Beta]: Cytoplasm
CC       {ECO:0000250|UniProtKB:Q9UH92}. Note=Found predominantly in the
CC       cytoplasm. {ECO:0000250|UniProtKB:Q9UH92}.
CC   -!- SUBCELLULAR LOCATION: [Isoform Gamma]: Nucleus
CC       {ECO:0000250|UniProtKB:Q9UH92}. Note=Found predominantly in the
CC       nucleus. {ECO:0000250|UniProtKB:Q9UH92}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=Gamma;
CC         IsoId=O08609-1; Sequence=Displayed;
CC       Name=Alpha;
CC         IsoId=O08609-2; Sequence=VSP_002139, VSP_002140;
CC       Name=Beta;
CC         IsoId=O08609-3; Sequence=VSP_002139;
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues examined: stomach,
CC       duodenum, jejunum, ileum, colon, liver, pancreas, salivary gland,
CC       kidney, spleen, lung, heart, skeletal muscle, brain, ovary and testis.
CC       {ECO:0000269|PubMed:8973301}.
CC   -!- DEVELOPMENTAL STAGE: Expression peaks between dpc 9.5 to 11.5, then
CC       decreases during later stages of organogenesis.
CC       {ECO:0000269|PubMed:10593926}.
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DR   EMBL; U43607; AAB51368.1; -; mRNA.
DR   EMBL; U43548; AAB51367.1; -; mRNA.
DR   EMBL; AF213670; AAG40149.1; -; mRNA.
DR   EMBL; AF213671; AAG40150.1; -; mRNA.
DR   EMBL; AF213672; AAG40151.1; -; mRNA.
DR   CCDS; CCDS25447.1; -. [O08609-1]
DR   CCDS; CCDS48935.1; -. [O08609-3]
DR   CCDS; CCDS48936.1; -. [O08609-2]
DR   RefSeq; NP_001152856.1; NM_001159384.1.
DR   RefSeq; NP_001152857.1; NM_001159385.1.
DR   RefSeq; NP_035680.3; NM_011550.3.
DR   AlphaFoldDB; O08609; -.
DR   BioGRID; 204019; 1.
DR   CORUM; O08609; -.
DR   STRING; 10090.ENSMUSP00000017945; -.
DR   iPTMnet; O08609; -.
DR   PhosphoSitePlus; O08609; -.
DR   EPD; O08609; -.
DR   MaxQB; O08609; -.
DR   PaxDb; O08609; -.
DR   PRIDE; O08609; -.
DR   ProteomicsDB; 290261; -. [O08609-1]
DR   ProteomicsDB; 290262; -. [O08609-2]
DR   ProteomicsDB; 290263; -. [O08609-3]
DR   DNASU; 21428; -.
DR   GeneID; 21428; -.
DR   KEGG; mmu:21428; -.
DR   CTD; 6945; -.
DR   MGI; MGI:108398; Mlx.
DR   eggNOG; KOG1319; Eukaryota.
DR   InParanoid; O08609; -.
DR   OrthoDB; 1234389at2759; -.
DR   PhylomeDB; O08609; -.
DR   Reactome; R-MMU-163765; ChREBP activates metabolic gene expression.
DR   BioGRID-ORCS; 21428; 3 hits in 75 CRISPR screens.
DR   ChiTaRS; Mlx; mouse.
DR   PRO; PR:O08609; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; O08609; protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; 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; ISO:MGI.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR   GO; GO:0006913; P:nucleocytoplasmic transport; IDA:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 4.10.280.10; -; 1.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   InterPro; IPR032647; Mlx.
DR   PANTHER; PTHR15741:SF25; PTHR15741:SF25; 1.
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   Activator; Alternative splicing; Cytoplasm; DNA-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..298
FT                   /note="Max-like protein X"
FT                   /id="PRO_0000127280"
FT   DOMAIN          129..187
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          98..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          194..214
FT                   /note="Leucine-zipper"
FT   COMPBIAS        98..112
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         7
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UH92"
FT   MOD_RES         45
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         48
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         74
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UH92"
FT   MOD_RES         77
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UH92"
FT   MOD_RES         98
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UH92"
FT   VAR_SEQ         15..68
FT                   /note="Missing (in isoform Alpha and isoform Beta)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_002139"
FT   VAR_SEQ         81..110
FT                   /note="Missing (in isoform Alpha)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_002140"
SQ   SEQUENCE   298 AA;  33339 MW;  A494D5A86292B71C CRC64;
     MTEPGASPED PWVKASFADA HAGEGRAGRA RARRGSGRRG APQLSPESPL LSGARGCRED
     SSHPACAKVE YAYSDNSLDP GLFVESTHKG SVVSRANSIG STSASSVPNT DDEDSDYQQE
     AYKESYKDRR RRAHTQAEQK RRDAIKRGYD DLQTIVPTCQ QQDFSIGSQK LSKAIVLQKT
     IDYIQFLHKE KKKQEEEVST LRKDVTALKI MKVNYEQIVK AHQDNPHEGE DQVSDQVKFN
     VFQGIMDSLF QSFNASISVA SFQELSACVF SWIEEHCEPQ TLREIVIGVL HQLKNQLY
 
 
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