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MAX_DROME
ID   MAX_DROME               Reviewed;         161 AA.
AC   P91664; Q1LZ15; Q8SXE2; Q95S07;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 161.
DE   RecName: Full=Protein max;
DE            Short=dMax;
DE   AltName: Full=Myc-associated factor X;
GN   Name=Max; ORFNames=CG9648;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227 {ECO:0000312|EMBL:AAL90428.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=Oregon-R {ECO:0000269|PubMed:8929412};
RX   PubMed=8929412; DOI=10.1126/science.274.5292.1523;
RA   Gallant P., Shiio Y., Cheng P.F., Parkhurst S.M., Eisenman R.N.;
RT   "Myc and Max homologs in Drosophila.";
RL   Science 274:1523-1527(1996).
RN   [2] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC   TISSUE=Head {ECO:0000269|PubMed:12537569};
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley;
RA   Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C.,
RA   Celniker S.E.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131 AND SER-137, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18327897; DOI=10.1021/pr700696a;
RA   Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT   "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL   J. Proteome Res. 7:1675-1682(2008).
CC   -!- FUNCTION: Transcription regulator. Forms a sequence-specific DNA-
CC       binding protein complex with MYC or MAD which recognizes the core
CC       sequence 5'-CAC[GA]TG-3'. The MYC-MAX complex is a transcriptional
CC       activator, whereas the MAD-MAX complex is a repressor.
CC       {ECO:0000269|PubMed:8929412}.
CC   -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC       protein. Binds DNA as a heterodimer with MYC or MAD.
CC       {ECO:0000269|PubMed:8929412}.
CC   -!- INTERACTION:
CC       P91664; Q9W4S7: Myc; NbExp=3; IntAct=EBI-193577, EBI-120162;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Embryo, especially in central nervous system.
CC       {ECO:0000269|PubMed:8929412}.
CC   -!- DEVELOPMENTAL STAGE: Highest expression in embryos.
CC       {ECO:0000269|PubMed:8929412}.
CC   -!- SIMILARITY: Belongs to the MAX family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL28562.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR   EMBL; U77369; AAB39841.1; -; mRNA.
DR   EMBL; AE014296; AAF49179.1; -; Genomic_DNA.
DR   EMBL; AY061014; AAL28562.1; ALT_SEQ; mRNA.
DR   EMBL; AY089690; AAL90428.1; -; mRNA.
DR   EMBL; BT025211; ABF17902.1; -; mRNA.
DR   RefSeq; NP_001246833.1; NM_001259904.2.
DR   RefSeq; NP_001287114.1; NM_001300185.1.
DR   RefSeq; NP_649097.1; NM_140840.4.
DR   AlphaFoldDB; P91664; -.
DR   SMR; P91664; -.
DR   BioGRID; 65371; 8.
DR   DIP; DIP-60982N; -.
DR   IntAct; P91664; 8.
DR   STRING; 7227.FBpp0074785; -.
DR   iPTMnet; P91664; -.
DR   PaxDb; P91664; -.
DR   DNASU; 40095; -.
DR   EnsemblMetazoa; FBtr0075018; FBpp0074785; FBgn0017578.
DR   EnsemblMetazoa; FBtr0310276; FBpp0301959; FBgn0017578.
DR   EnsemblMetazoa; FBtr0345391; FBpp0311541; FBgn0017578.
DR   GeneID; 40095; -.
DR   KEGG; dme:Dmel_CG9648; -.
DR   UCSC; CG9648-RA; d. melanogaster.
DR   CTD; 4149; -.
DR   FlyBase; FBgn0017578; Max.
DR   VEuPathDB; VectorBase:FBgn0017578; -.
DR   eggNOG; KOG2483; Eukaryota.
DR   GeneTree; ENSGT00530000064011; -.
DR   HOGENOM; CLU_109424_0_0_1; -.
DR   InParanoid; P91664; -.
DR   OMA; FAAETCE; -.
DR   OrthoDB; 1545748at2759; -.
DR   PhylomeDB; P91664; -.
DR   Reactome; R-DME-8953750; Transcriptional Regulation by E2F6.
DR   SignaLink; P91664; -.
DR   BioGRID-ORCS; 40095; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 40095; -.
DR   PRO; PR:P91664; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0017578; Expressed in saliva-secreting gland and 42 other tissues.
DR   ExpressionAtlas; P91664; baseline and differential.
DR   Genevisible; P91664; DM.
DR   GO; GO:0071339; C:MLL1 complex; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IC:UniProtKB.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IBA:GO_Central.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:FlyBase.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IEA:InterPro.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   Gene3D; 4.10.280.10; -; 1.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   InterPro; IPR037933; MAX-like.
DR   PANTHER; PTHR10328; PTHR10328; 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; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..161
FT                   /note="Protein max"
FT                   /id="PRO_0000127275"
FT   DOMAIN          39..90
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          122..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..59
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..145
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         131
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         137
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   CONFLICT        91
FT                   /note="R -> G (in Ref. 4; AAL90428)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   161 AA;  18530 MW;  A217A22A7B514C77 CRC64;
     MSMSDDDRDI DIESDEDGDS DTGLGSSRHT NTANFTQAEK RAHHNALERR RRDHIKESFT
     NLREAVPTLK GEKASRAQIL KKTTECIQTM RRKISENQKD IEEIKRQNNI IAKQIQALES
     SNGDQFSEFL SDEEVGSEEA DDEDLDQDFS RRNKKMKTFH A
 
 
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