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 27-MAR-2024, entry version 198. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; Mad-Max transcriptional repressor complex. DR ComplexPortal; CPX-97; Myc-Max transcriptional activator 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; 10090-ENSMUSP00000106025; -. DR PeptideAtlas; P28574; -. DR ProteomicsDB; 293415; -. [P28574-1] DR ProteomicsDB; 328864; -. DR ProteomicsDB; 340525; -. DR Pumba; P28574; -. DR Antibodypedia; 159; 607 antibodies from 39 providers. DR DNASU; 17187; -. DR Ensembl; ENSMUST00000082136.7; ENSMUSP00000080778.6; ENSMUSG00000059436.14. [P28574-2] DR Ensembl; ENSMUST00000110395.11; ENSMUSP00000106025.4; ENSMUSG00000059436.14. [P28574-1] DR GeneID; 17187; -. DR KEGG; mmu:17187; -. DR UCSC; uc007nyw.2; mouse. DR UCSC; uc007nyx.2; mouse. DR AGR; MGI:96921; -. 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; YMDAHEL; -. DR OrthoDB; 5398829at2759; -. DR PhylomeDB; P28574; -. DR TreeFam; TF318841; -. DR Reactome; R-MMU-8953750; Transcriptional Regulation by E2F6. DR BioGRID-ORCS; 17187; 23 hits in 80 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 219 other cell types or tissues. DR ExpressionAtlas; P28574; baseline and differential. DR GO; GO:0000785; C:chromatin; 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:ComplexPortal. 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:0046983; F:protein dimerization 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: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:0045893; P:positive regulation of DNA-templated transcription; IDA:ComplexPortal. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB. DR GO; GO:0065003; P:protein-containing complex assembly; ISO:MGI. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IGI:MGI. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:NTNU_SB. 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 CDD; cd11406; bHLHzip_Max; 1. DR Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1. DR IDEAL; IID50243; -. DR InterPro; IPR011598; bHLH_dom. DR InterPro; IPR036638; HLH_DNA-bd_sf. DR PANTHER; PTHR10328:SF3; PROTEIN MAX; 1. DR PANTHER; PTHR10328; PROTEIN MAX MYC-ASSOCIATED FACTOR X; 1. DR Pfam; PF00010; HLH; 1. DR SMART; SM00353; HLH; 1. DR SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 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 //