MNT_MOUSE
ID MNT_MOUSE Reviewed; 591 AA.
AC O08789; P97349; Q6GTJ3;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Max-binding protein MNT;
DE AltName: Full=Myc antagonist MNT;
DE AltName: Full=Protein ROX;
GN Name=Mnt; Synonyms=Rox;
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=Embryo;
RX PubMed=9000049; DOI=10.1101/gad.11.1.44;
RA Hurlin P.J., Queva C., Eisenman R.N.;
RT "Mnt, a novel Max-interacting protein is coexpressed with Myc in
RT proliferating cells and mediates repression at Myc binding sites.";
RL Genes Dev. 11:44-58(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RX PubMed=9184233; DOI=10.1093/emboj/16.10.2892;
RA Meroni G., Reymond A., Alcalay M., Borsani G., Tanigami A., Tonlorenzi R.,
RA Lo Nigro C., Messali S., Zollo M., Ledbetter D.H., Brent R., Ballabio A.,
RA Carrozzo R.;
RT "Rox, a novel bHLHZip protein expressed in quiescent cells that
RT heterodimerizes with Max, binds a non-canonical E box and acts as a
RT transcriptional repressor.";
RL EMBO J. 16:2892-2906(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Binds DNA as a heterodimer with MAX and represses
CC transcription. Binds to the canonical E box sequence 5'-CACGTG-3' and,
CC with higher affinity, to 5'-CACGCG-3'.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. Binds DNA as a homodimer or a heterodimer with MAX.
CC -!- SUBCELLULAR LOCATION: Nucleus.
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DR EMBL; U77356; AAB38687.1; -; mRNA.
DR EMBL; Y07609; CAA68878.1; -; mRNA.
DR EMBL; AL604066; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466596; EDL12780.1; -; Genomic_DNA.
DR EMBL; BC054534; AAH54534.1; -; mRNA.
DR CCDS; CCDS25037.1; -.
DR RefSeq; NP_034943.3; NM_010813.3.
DR AlphaFoldDB; O08789; -.
DR SMR; O08789; -.
DR BioGRID; 201461; 6.
DR IntAct; O08789; 1.
DR STRING; 10090.ENSMUSP00000000291; -.
DR iPTMnet; O08789; -.
DR PhosphoSitePlus; O08789; -.
DR EPD; O08789; -.
DR MaxQB; O08789; -.
DR PaxDb; O08789; -.
DR PeptideAtlas; O08789; -.
DR PRIDE; O08789; -.
DR ProteomicsDB; 295572; -.
DR Antibodypedia; 22924; 142 antibodies from 31 providers.
DR DNASU; 17428; -.
DR Ensembl; ENSMUST00000000291; ENSMUSP00000000291; ENSMUSG00000000282.
DR GeneID; 17428; -.
DR KEGG; mmu:17428; -.
DR UCSC; uc011xzb.1; mouse.
DR CTD; 4335; -.
DR MGI; MGI:109150; Mnt.
DR VEuPathDB; HostDB:ENSMUSG00000000282; -.
DR eggNOG; KOG2483; Eukaryota.
DR GeneTree; ENSGT00510000048287; -.
DR HOGENOM; CLU_020165_1_0_1; -.
DR InParanoid; O08789; -.
DR OMA; GPPKLNH; -.
DR OrthoDB; 445807at2759; -.
DR TreeFam; TF315654; -.
DR BioGRID-ORCS; 17428; 14 hits in 75 CRISPR screens.
DR ChiTaRS; Mnt; mouse.
DR PRO; PR:O08789; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; O08789; protein.
DR Bgee; ENSMUSG00000000282; Expressed in rostral migratory stream and 259 other tissues.
DR ExpressionAtlas; O08789; baseline and differential.
DR Genevisible; O08789; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IC:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IMP: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:0046983; F:protein dimerization activity; IEA:InterPro.
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:0090398; P:cellular senescence; IMP:MGI.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP: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 2: Evidence at transcript level;
KW Acetylation; DNA-binding; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q99583"
FT CHAIN 2..591
FT /note="Max-binding protein MNT"
FT /id="PRO_0000127282"
FT DOMAIN 222..273
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 17..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..301
FT /note="Leucine-zipper"
FT REGION 321..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..88
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..118
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..200
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..393
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..425
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q99583"
FT CONFLICT 379
FT /note="P -> T (in Ref. 1; AAB38687)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="A -> V (in Ref. 1; AAB38687)"
FT /evidence="ECO:0000305"
FT CONFLICT 402..403
FT /note="QQ -> EE (in Ref. 1; AAB38687)"
FT /evidence="ECO:0000305"
FT CONFLICT 414
FT /note="A -> G (in Ref. 1; AAB38687)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="A -> V (in Ref. 1; AAB38687)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="P -> A (in Ref. 1; AAB38687)"
FT /evidence="ECO:0000305"
FT CONFLICT 525
FT /note="A -> T (in Ref. 1; AAB38687)"
FT /evidence="ECO:0000305"
FT CONFLICT 558
FT /note="A -> G (in Ref. 1; AAB38687)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 591 AA; 63274 MW; 17C2B830381D2190 CRC64;
MSIETLLEAA RFLEWQAQQQ QRAREEQERL RLEREREREQ EQKRASNLAR LAHALPVEEP
RIEAPPLPLS PPAPPPAPPP PLATPAPLTV IPIPVVTNSP QSLPPPPPLP PAAQPLPLAP
RQPALVSTPG LSIKEPVTLP TRPQVPTPAP LLPDAKTTVA PTGSPKPLQP LPAPILTIAP
HPGVQPQLAP QQPPPPTLGT LKLAPAEEAK SSEQKKRPGG IGTREVHNKL EKNRRAHLKE
CFETLKRNIP NVDDKKTSNL SVLRTALRYI QSLKRKEKEY EHEMERLARE KIATQQRLAE
LKHELSQWMD VLEIDRVLRQ TGQPEDDQAS TSTASEGEDN VDEEMEGDRA GLGPPKLNHR
PQPELLKSAL PTPSTAPAPL PTHPHPHPHP VALSPAHLPV QQQQPPQQKT PLPAPPPPPA
TPTQTLVPAP AHLVATAGGG STVIAHTATT HASVIQTVNH VLQGPGGKHI AHIAPSAPSP
AVQLAPATPP IGHITVHPAT LNHVAHLGSQ LPLYPQPVAV SQPVAVSHIA HTLSHQQVNG
TAGLGPPATV MAKPAVGAQV VHHPQLVGQT VLNPVTMVTM PSFPVSTLKL A
