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Protein max (Myc-associated factor X) (Myc-binding novel HLH/LZ protein) (Protein myn)

 MAX_MOUSE               Reviewed;         160 AA.
P28574; B2RS19; Q8C4Y1;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
23-MAY-2018, sequence version 2.
18-JUL-2018, entry version 166.
RecName: Full=Protein max {ECO:0000250|UniProtKB:P61244};
AltName: Full=Myc-associated factor X {ECO:0000250|UniProtKB:P61244};
AltName: Full=Myc-binding novel HLH/LZ protein;
AltName: Full=Protein myn;
Name=Max {ECO:0000312|MGI:MGI:96921}; Synonyms=Myn;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1840505; DOI=10.1016/0092-8674(91)90457-A;
Prendergast G.C., Lawe D., Ziff E.B.;
"Association of Myn, the murine homolog of max, with c-Myc stimulates
methylation-sensitive DNA binding and ras cotransformation.";
Cell 65:395-407(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC37914.1};
TISSUE=Cerebellum {ECO:0000312|EMBL:BAC37914.1};
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain {ECO:0000312|EMBL:AAI38672.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
INTERACTION WITH SPAG9.
PubMed=12391307; DOI=10.1073/pnas.232310199;
Lee C.M., Onesime D., Reddy C.D., Dhanasekaran N., Reddy E.P.;
"JLP: a scaffolding protein that tethers JNK/p38MAPK signaling modules
and transcription factors.";
Proc. Natl. Acad. Sci. U.S.A. 99:14189-14194(2002).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
STRUCTURE BY NMR OF 70-102 IN COMPLEX WITH MYC.
PubMed=9680483; DOI=10.1006/jmbi.1998.1914;
Lavigne P., Crump M.P., Gagne S.M., Hodges R.S., Kay C.M., Sykes B.D.;
"Insights into the mechanism of heterodimerization from the 1H-NMR
solution structure of the c-Myc-Max heterodimeric leucine zipper.";
J. Mol. Biol. 281:165-181(1998).
-!- FUNCTION: Transcription regulator. Forms a sequence-specific DNA-
binding protein complex with MYC or MAD which recognizes the core
sequence 5'-CAC[GA]TG-3'. The MYC:MAX complex is a transcriptional
activator, whereas the MAD:MAX complex is a repressor. CpG
methylation of the recognition site greatly inhibits DNA binding,
suggesting that DNA methylation may regulate the MYC:MAX complex
in vivo. May repress transcription via the recruitment of a
chromatin remodeling complex containing H3 'Lys-9' histone
methyltransferase activity. Represses MYC transcriptional activity
from E-box elements (By similarity).
{ECO:0000250|UniProtKB:P61244}.
-!- SUBUNIT: Efficient DNA binding requires dimerization with another
bHLH protein. Binds DNA as a heterodimer with MYC or MAD. Part of
the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX,
TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2, MBLR, L3MBTL2 and YAF2.
Component of some MLL1/MLL complex, at least composed of the core
components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well
as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C,
KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31,
RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7,
TAF9 and TEX10. Interacts with SPAG9. The heterodimer MYC:MAX
interacts with ABI1; the interaction may enhance MYC:MAX
transcriptional activity. {ECO:0000269|PubMed:12391307,
ECO:0000269|PubMed:9680483}.
-!- INTERACTION:
Q9QWV9:Ccnt1; NbExp=2; IntAct=EBI-1183003, EBI-2655009;
Q99J95:Cdk9; NbExp=2; IntAct=EBI-1183003, EBI-2654963;
P01108:Myc; NbExp=6; IntAct=EBI-1183003, EBI-1183114;
-!- SUBCELLULAR LOCATION: Nucleus. Cell projection, dendrite
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P28574-1; Sequence=Displayed;
Name=2;
IsoId=P28574-2; Sequence=VSP_059578;
-!- INDUCTION: By serum; in 3T3 fibroblasts.
-!- PTM: Phosphorylated. {ECO:0000305}.
-!- SIMILARITY: Belongs to the MAX family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M63903; AAA39797.1; -; mRNA.
EMBL; AK080431; BAC37914.1; -; mRNA.
EMBL; AC124556; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC138671; AAI38672.1; -; mRNA.
EMBL; BC138672; AAI38673.1; -; mRNA.
EMBL; BC145369; AAI45370.1; -; mRNA.
CCDS; CCDS36479.1; -. [P28574-1]
CCDS; CCDS49094.1; -. [P28574-2]
PIR; A38488; A38488.
RefSeq; NP_001139648.1; NM_001146176.1. [P28574-2]
RefSeq; NP_032584.2; NM_008558.2. [P28574-1]
UniGene; Mm.268548; -.
UniGene; Mm.491131; -.
PDB; 1A93; NMR; -; B=74-102.
PDB; 2A93; NMR; -; B=74-102.
PDB; 3U5V; X-ray; 1.70 A; A=22-36.
PDBsum; 1A93; -.
PDBsum; 2A93; -.
PDBsum; 3U5V; -.
ProteinModelPortal; P28574; -.
SMR; P28574; -.
ComplexPortal; CPX-105; Transcriptional repressor Mad-Max complex.
ComplexPortal; CPX-97; Transcriptional repressor Myc-Max complex.
CORUM; P28574; -.
DIP; DIP-116N; -.
IntAct; P28574; 23.
MINT; P28574; -.
STRING; 10090.ENSMUSP00000106025; -.
iPTMnet; P28574; -.
PhosphoSitePlus; P28574; -.
EPD; P28574; -.
MaxQB; P28574; -.
PaxDb; P28574; -.
PeptideAtlas; P28574; -.
PRIDE; P28574; -.
Ensembl; ENSMUST00000082136; ENSMUSP00000080778; ENSMUSG00000059436. [P28574-2]
Ensembl; ENSMUST00000110395; ENSMUSP00000106025; ENSMUSG00000059436. [P28574-1]
GeneID; 17187; -.
KEGG; mmu:17187; -.
UCSC; uc007nyw.2; mouse.
UCSC; uc007nyx.2; mouse.
CTD; 4149; -.
MGI; MGI:96921; Max.
eggNOG; KOG2483; Eukaryota.
eggNOG; ENOG4111V1C; LUCA.
GeneTree; ENSGT00530000064011; -.
HOGENOM; HOG000293257; -.
HOVERGEN; HBG008542; -.
InParanoid; P28574; -.
KO; K04453; -.
OMA; RHTSTAN; -.
OrthoDB; EOG091G1312; -.
PhylomeDB; P28574; -.
TreeFam; TF318841; -.
Reactome; R-MMU-8953750; Transcriptional Regulation by E2F6.
ChiTaRS; Max; mouse.
EvolutionaryTrace; P28574; -.
PRO; PR:P28574; -.
Proteomes; UP000000589; Chromosome 12.
Bgee; ENSMUSG00000059436; -.
CleanEx; MM_MAX; -.
ExpressionAtlas; P28574; baseline and differential.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0030425; C:dendrite; ISO:MGI.
GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0016605; C:PML body; ISO:MGI.
GO; GO:0032993; C:protein-DNA complex; ISO:MGI.
GO; GO:0090575; C:RNA polymerase II transcription factor complex; ISO:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0003700; F:DNA binding transcription factor activity; ISO:MGI.
GO; GO:0070888; F:E-box binding; ISO:MGI.
GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
GO; GO:0000983; F:transcription factor activity, RNA polymerase II core promoter sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II proximal promoter sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
GO; GO:0065003; P:protein-containing complex assembly; ISO:MGI.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IGI:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00083; HLH; 1.
Gene3D; 4.10.280.10; -; 1.
InterPro; IPR011598; bHLH_dom.
InterPro; IPR036638; HLH_DNA-bd_sf.
InterPro; IPR037933; MAX.
PANTHER; PTHR10328; PTHR10328; 1.
Pfam; PF00010; HLH; 1.
SMART; SM00353; HLH; 1.
SUPFAM; SSF47459; SSF47459; 1.
PROSITE; PS50888; BHLH; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing;
Cell projection; Complete proteome; DNA-binding; Nucleus;
Phosphoprotein; Reference proteome; Repressor; Transcription;
Transcription regulation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P61244}.
CHAIN 2 160 Protein max.
/FTId=PRO_0000127270.
DOMAIN 23 74 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
REGION 81 102 Leucine-zipper.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:P61244}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000250|UniProtKB:P61244}.
MOD_RES 11 11 Phosphoserine.
{ECO:0000250|UniProtKB:P61244}.
MOD_RES 66 66 N6-acetyllysine.
{ECO:0000250|UniProtKB:P61244}.
MOD_RES 107 107 Phosphoserine.
{ECO:0000250|UniProtKB:P61244}.
MOD_RES 153 153 N6-acetyllysine.
{ECO:0000250|UniProtKB:P61244}.
MOD_RES 154 154 N6-acetyllysine.
{ECO:0000250|UniProtKB:P61244}.
VAR_SEQ 13 21 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_059578.
CONFLICT 16 16 P -> A (in Ref. 1; AAA39797).
CONFLICT 79 79 H -> D (in Ref. 1; AAA39797).
HELIX 30 36 {ECO:0000244|PDB:3U5V}.
HELIX 74 101 {ECO:0000244|PDB:1A93}.
SEQUENCE 160 AA; 18245 MW; 86D133137727A57A CRC64;
MSDNDDIEVE SDEEQPRFQS AADKRAHHNA LERKRRDHIK DSFHSLRDSV PSLQGEKASR
AQILDKATEY IQYMRRKNHT HQQDIDDLKR QNALLEQQVR ALEKARSSAQ LQTNYPSSDN
SLYTNAKGGT ISAFDGGSDS SSESEPEEPQ SRKKLRMEAS


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