MAX_MOUSE
ID MAX_MOUSE Reviewed; 160 AA.
AC P28574; B2RS19; Q8C4Y1;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2018, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Protein max {ECO:0000250|UniProtKB:P61244};
DE AltName: Full=Myc-associated factor X {ECO:0000250|UniProtKB:P61244};
DE AltName: Full=Myc-binding novel HLH/LZ protein;
DE AltName: Full=Protein myn;
GN Name=Max {ECO:0000312|MGI:MGI:96921}; Synonyms=Myn;
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 1).
RX PubMed=1840505; DOI=10.1016/0092-8674(91)90457-a;
RA Prendergast G.C., Lawe D., Ziff E.B.;
RT "Association of Myn, the murine homolog of max, with c-Myc stimulates
RT methylation-sensitive DNA binding and ras cotransformation.";
RL Cell 65:395-407(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC37914.1};
RC TISSUE=Cerebellum {ECO:0000312|EMBL:BAC37914.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
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 MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain {ECO:0000312|EMBL:AAI38672.1};
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 [5]
RP INTERACTION WITH SPAG9.
RX PubMed=12391307; DOI=10.1073/pnas.232310199;
RA Lee C.M., Onesime D., Reddy C.D., Dhanasekaran N., Reddy E.P.;
RT "JLP: a scaffolding protein that tethers JNK/p38MAPK signaling modules and
RT transcription factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14189-14194(2002).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
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).
RN [7]
RP STRUCTURE BY NMR OF 70-102 IN COMPLEX WITH MYC.
RX PubMed=9680483; DOI=10.1006/jmbi.1998.1914;
RA Lavigne P., Crump M.P., Gagne S.M., Hodges R.S., Kay C.M., Sykes B.D.;
RT "Insights into the mechanism of heterodimerization from the 1H-NMR solution
RT structure of the c-Myc-Max heterodimeric leucine zipper.";
RL J. Mol. Biol. 281:165-181(1998).
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. CpG methylation
CC of the recognition site greatly inhibits DNA binding, suggesting that
CC DNA methylation may regulate the MYC:MAX complex in vivo. May repress
CC transcription via the recruitment of a chromatin remodeling complex
CC containing H3 'Lys-9' histone methyltransferase activity. Represses MYC
CC transcriptional activity from E-box elements (By similarity).
CC {ECO:0000250|UniProtKB:P61244}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. Binds DNA as a heterodimer with MYC or MAD. Part of the
CC E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3,
CC BAT8, EUHMTASE1, RING1, RNF2, MBLR, L3MBTL2 and YAF2. Component of some
CC MLL1/MLL complex, at least composed of the core components KMT2A/MLL1,
CC ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative
CC components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1,
CC MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B,
CC SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts with SPAG9.
CC The heterodimer MYC:MAX interacts with ABI1; the interaction may
CC enhance MYC:MAX transcriptional activity. {ECO:0000269|PubMed:12391307,
CC ECO:0000269|PubMed:9680483}.
CC -!- INTERACTION:
CC P28574; Q9QWV9: Ccnt1; NbExp=2; IntAct=EBI-1183003, EBI-2655009;
CC P28574; Q99J95: Cdk9; NbExp=2; IntAct=EBI-1183003, EBI-2654963;
CC P28574; P01108: Myc; NbExp=7; IntAct=EBI-1183003, EBI-1183114;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cell projection, dendrite {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P28574-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P28574-2; Sequence=VSP_059578;
CC -!- INDUCTION: By serum; in 3T3 fibroblasts.
CC -!- PTM: Phosphorylated. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MAX family. {ECO:0000305}.
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DR EMBL; M63903; AAA39797.1; -; mRNA.
DR EMBL; AK080431; BAC37914.1; -; mRNA.
DR EMBL; AC124556; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC138671; AAI38672.1; -; mRNA.
DR EMBL; BC138672; AAI38673.1; -; mRNA.
DR EMBL; BC145369; AAI45370.1; -; mRNA.
DR CCDS; CCDS36479.1; -. [P28574-1]
DR CCDS; CCDS49094.1; -. [P28574-2]
DR PIR; A38488; A38488.
DR RefSeq; NP_001139648.1; NM_001146176.1. [P28574-2]
DR RefSeq; NP_032584.2; NM_008558.2. [P28574-1]
DR PDB; 1A93; NMR; -; B=74-102.
DR PDB; 2A93; NMR; -; B=74-102.
DR PDB; 3U5V; X-ray; 1.70 A; A=22-36.
DR PDBsum; 1A93; -.
DR PDBsum; 2A93; -.
DR PDBsum; 3U5V; -.
DR AlphaFoldDB; P28574; -.
DR SMR; P28574; -.
DR ComplexPortal; CPX-105; Transcriptional repressor Mad-Max complex.
DR ComplexPortal; CPX-97; Transcriptional activator Myc-Max complex.
DR CORUM; P28574; -.
DR DIP; DIP-116N; -.
DR IntAct; P28574; 79.
DR MINT; P28574; -.
DR STRING; 10090.ENSMUSP00000106025; -.
DR iPTMnet; P28574; -.
DR PhosphoSitePlus; P28574; -.
DR EPD; P28574; -.
DR jPOST; P28574; -.
DR MaxQB; P28574; -.
DR PaxDb; P28574; -.
DR PeptideAtlas; P28574; -.
DR PRIDE; P28574; -.
DR ProteomicsDB; 293415; -. [P28574-1]
DR ProteomicsDB; 328864; -.
DR ProteomicsDB; 340525; -.
DR Antibodypedia; 159; 570 antibodies from 39 providers.
DR DNASU; 17187; -.
DR Ensembl; ENSMUST00000082136; ENSMUSP00000080778; ENSMUSG00000059436. [P28574-2]
DR Ensembl; ENSMUST00000110395; ENSMUSP00000106025; ENSMUSG00000059436. [P28574-1]
DR GeneID; 17187; -.
DR KEGG; mmu:17187; -.
DR UCSC; uc007nyw.2; mouse.
DR UCSC; uc007nyx.2; mouse.
DR CTD; 4149; -.
DR MGI; MGI:96921; Max.
DR VEuPathDB; HostDB:ENSMUSG00000059436; -.
DR eggNOG; KOG2483; Eukaryota.
DR GeneTree; ENSGT00530000064011; -.
DR HOGENOM; CLU_109424_1_0_1; -.
DR InParanoid; P28574; -.
DR OMA; QIQTNYS; -.
DR OrthoDB; 1545748at2759; -.
DR PhylomeDB; P28574; -.
DR TreeFam; TF318841; -.
DR Reactome; R-MMU-8953750; Transcriptional Regulation by E2F6.
DR BioGRID-ORCS; 17187; 23 hits in 74 CRISPR screens.
DR ChiTaRS; Max; mouse.
DR EvolutionaryTrace; P28574; -.
DR PRO; PR:P28574; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; P28574; protein.
DR Bgee; ENSMUSG00000059436; Expressed in granulocyte and 215 other tissues.
DR ExpressionAtlas; P28574; baseline and differential.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0070443; C:Mad-Max complex; ISO:MGI.
DR GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR GO; GO:0071943; C:Myc-Max complex; IPI:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0016605; C:PML body; ISO:MGI.
DR GO; GO:0032993; C:protein-DNA complex; ISO:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0070888; F:E-box binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0071375; P:cellular response to peptide hormone stimulus; IEA:Ensembl.
DR GO; GO:0009267; P:cellular response to starvation; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:ComplexPortal.
DR GO; GO:0065003; P:protein-containing complex assembly; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IGI:MGI.
DR GO; GO:0048678; P:response to axon injury; IEA:Ensembl.
DR GO; GO:0032868; P:response to insulin; IEA:Ensembl.
DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR Gene3D; 4.10.280.10; -; 1.
DR IDEAL; IID50243; -.
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 3D-structure; Acetylation; Activator; Alternative splicing;
KW Cell projection; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P61244"
FT CHAIN 2..160
FT /note="Protein max"
FT /id="PRO_0000127270"
FT DOMAIN 23..74
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..102
FT /note="Leucine-zipper"
FT REGION 104..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P61244"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61244"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61244"
FT MOD_RES 66
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P61244"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61244"
FT MOD_RES 153
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P61244"
FT MOD_RES 154
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P61244"
FT VAR_SEQ 13..21
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_059578"
FT CONFLICT 16
FT /note="P -> A (in Ref. 1; AAA39797)"
FT CONFLICT 79
FT /note="H -> D (in Ref. 1; AAA39797)"
FT HELIX 30..36
FT /evidence="ECO:0007829|PDB:3U5V"
FT HELIX 74..101
FT /evidence="ECO:0007829|PDB:1A93"
SQ SEQUENCE 160 AA; 18245 MW; 86D133137727A57A CRC64;
MSDNDDIEVE SDEEQPRFQS AADKRAHHNA LERKRRDHIK DSFHSLRDSV PSLQGEKASR
AQILDKATEY IQYMRRKNHT HQQDIDDLKR QNALLEQQVR ALEKARSSAQ LQTNYPSSDN
SLYTNAKGGT ISAFDGGSDS SSESEPEEPQ SRKKLRMEAS
