MNT_HUMAN
ID MNT_HUMAN Reviewed; 582 AA.
AC Q99583; A8K6D1; D3DTI7; Q1ED38;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Max-binding protein MNT;
DE AltName: Full=Class D basic helix-loop-helix protein 3;
DE Short=bHLHd3;
DE AltName: Full=Myc antagonist MNT;
DE AltName: Full=Protein ROX;
GN Name=MNT; Synonyms=BHLHD3, ROX;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fetal brain;
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=9598315; DOI=10.1006/geno.1998.5241;
RA Nigro C.L., Venesio T., Reymond A., Meroni G., Alberici P., Cainarca S.,
RA Enrico F., Stack M., Ledbetter D.H., Liscia D.S., Ballabio A., Carrozzo R.;
RT "The human ROX gene: genomic structure and mutation analysis in human
RT breast tumors.";
RL Genomics 49:275-282(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
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).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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 -!- INTERACTION:
CC Q99583; O43639: NCK2; NbExp=3; IntAct=EBI-7959025, EBI-713635;
CC -!- SUBCELLULAR LOCATION: Nucleus.
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DR EMBL; X96401; CAA65265.1; -; mRNA.
DR EMBL; Y13440; CAA73851.1; -; Genomic_DNA.
DR EMBL; Y13441; CAA73851.1; JOINED; Genomic_DNA.
DR EMBL; Y13442; CAA73851.1; JOINED; Genomic_DNA.
DR EMBL; Y13443; CAA73851.1; JOINED; Genomic_DNA.
DR EMBL; Y13444; CAA73851.1; JOINED; Genomic_DNA.
DR EMBL; AK291596; BAF84285.1; -; mRNA.
DR EMBL; CH471108; EAW90541.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90542.1; -; Genomic_DNA.
DR EMBL; BC117563; AAI17564.1; -; mRNA.
DR CCDS; CCDS11018.1; -.
DR RefSeq; NP_064706.1; NM_020310.2.
DR AlphaFoldDB; Q99583; -.
DR SMR; Q99583; -.
DR BioGRID; 110478; 29.
DR ELM; Q99583; -.
DR IntAct; Q99583; 12.
DR MINT; Q99583; -.
DR STRING; 9606.ENSP00000174618; -.
DR GlyGen; Q99583; 2 sites, 2 O-linked glycans (2 sites).
DR iPTMnet; Q99583; -.
DR PhosphoSitePlus; Q99583; -.
DR BioMuta; MNT; -.
DR DMDM; 3914034; -.
DR EPD; Q99583; -.
DR jPOST; Q99583; -.
DR MassIVE; Q99583; -.
DR MaxQB; Q99583; -.
DR PaxDb; Q99583; -.
DR PeptideAtlas; Q99583; -.
DR PRIDE; Q99583; -.
DR ProteomicsDB; 78341; -.
DR Antibodypedia; 22924; 142 antibodies from 31 providers.
DR DNASU; 4335; -.
DR Ensembl; ENST00000174618.5; ENSP00000174618.4; ENSG00000070444.15.
DR GeneID; 4335; -.
DR KEGG; hsa:4335; -.
DR MANE-Select; ENST00000174618.5; ENSP00000174618.4; NM_020310.3; NP_064706.1.
DR UCSC; uc002fur.4; human.
DR CTD; 4335; -.
DR DisGeNET; 4335; -.
DR GeneCards; MNT; -.
DR HGNC; HGNC:7188; MNT.
DR HPA; ENSG00000070444; Low tissue specificity.
DR MIM; 603039; gene.
DR neXtProt; NX_Q99583; -.
DR OpenTargets; ENSG00000070444; -.
DR PharmGKB; PA30898; -.
DR VEuPathDB; HostDB:ENSG00000070444; -.
DR eggNOG; KOG2483; Eukaryota.
DR GeneTree; ENSGT00510000048287; -.
DR HOGENOM; CLU_020165_1_0_1; -.
DR InParanoid; Q99583; -.
DR OMA; GPPKLNH; -.
DR OrthoDB; 445807at2759; -.
DR PhylomeDB; Q99583; -.
DR TreeFam; TF315654; -.
DR PathwayCommons; Q99583; -.
DR SignaLink; Q99583; -.
DR SIGNOR; Q99583; -.
DR BioGRID-ORCS; 4335; 62 hits in 1103 CRISPR screens.
DR ChiTaRS; MNT; human.
DR GeneWiki; MNT_(gene); -.
DR GenomeRNAi; 4335; -.
DR Pharos; Q99583; Tbio.
DR PRO; PR:Q99583; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q99583; protein.
DR Bgee; ENSG00000070444; Expressed in cervix squamous epithelium and 205 other tissues.
DR ExpressionAtlas; Q99583; baseline and differential.
DR Genevisible; Q99583; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
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; IDA:NTNU_SB.
DR GO; GO:0090398; P:cellular senescence; IEA:Ensembl.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
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 Acetylation; DNA-binding; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..582
FT /note="Max-binding protein MNT"
FT /id="PRO_0000127281"
FT DOMAIN 220..271
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 18..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..299
FT /note="Leucine-zipper"
FT REGION 319..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..86
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..115
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..153
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..177
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..198
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..391
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..422
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT VARIANT 109
FT /note="A -> T (in dbSNP:rs7207965)"
FT /id="VAR_061258"
SQ SEQUENCE 582 AA; 62300 MW; 06AC320D79BF18A0 CRC64;
MSIETLLEAA RFLEWQAQQQ QRAREEQERL RLEQEREQEQ KKANSLARLA HTLPVEEPRM
EAPPLPLSPP APPPAPPPPL ATPAPLTVIP IPVVTNSPQP LPPPPPLPAA AQPLPLAPRQ
PALVGAPGLS IKEPAPLPSR PQVPTPAPLL PDSKATIPPN GSPKPLQPLP TPVLTIAPHP
GVQPQLAPQQ PPPPTLGTLK LAPAEEVKSS EQKKRPGGIG TREVHNKLEK NRRAHLKECF
ETLKRNIPNV DDKKTSNLSV LRTALRYIQS LKRKEKEYEH EMERLAREKI ATQQRLAELK
HELSQWMDVL EIDRVLRQTG QPEDDQASTS TASEGEDNID EDMEEDRAGL GPPKLSHRPQ
PELLKSTLPP PSTTPAPLPP HPHPHPHSVA LPPAHLPVQQ QQPQQKTPLP APPPPPAAPA
QTLVPAPAHL VATAGGGSTV IAHTATTHAS VIQTVNHVLQ GPGGKHIAHI APSAPSPAVQ
LAPATPPIGH ITVHPATLNH VAHLGSQLPL YPQPVAVSHI AHTLSHQQVN GTAGLGPPAT
VMAKPAVGAQ VVHHPQLVGQ TVLNPVTMVT MPSFPVSTLK LA
