MAX_RAT
ID MAX_RAT Reviewed; 160 AA.
AC P52164;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Protein max {ECO:0000250|UniProtKB:P61244};
DE AltName: Full=Myc-associated factor X {ECO:0000250|UniProtKB:P61244};
GN Name=Max {ECO:0000312|RGD:621101};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
RC STRAIN=Wistar; TISSUE=Seminal vesicle;
RX PubMed=8268234; DOI=10.1016/0167-4781(93)90021-5;
RA Izawa M.;
RT "Molecular cloning and sequencing of rat Max cDNA: castration-induced
RT expression of the 2 kb transcript in male accessory sex organs of rats.";
RL Biochim. Biophys. Acta 1216:492-494(1993).
RN [2]
RP FUNCTION AS TRANSCRIPTION REGULATOR, INTERACTION WITH ABI1, AND SUBCELLULAR
RP LOCATION.
RX PubMed=17304222; DOI=10.1038/sj.emboj.7601569;
RA Proepper C., Johannsen S., Liebau S., Dahl J., Vaida B., Bockmann J.,
RA Kreutz M.R., Gundelfinger E.D., Boeckers T.M.;
RT "Abelson interacting protein 1 (Abi-1) is essential for dendrite
RT morphogenesis and synapse formation.";
RL EMBO J. 26:1397-1409(2007).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-11, PHOSPHORYLATION
RP [LARGE SCALE ANALYSIS] AT SER-2 AND SER-11 (ISOFORM SHORT), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. 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, ECO:0000269|PubMed:17304222}.
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.
CC {ECO:0000269|PubMed:17304222}.
CC -!- INTERACTION:
CC P52164; Q9QZM5: Abi1; NbExp=2; IntAct=EBI-1184963, EBI-920097;
CC P52164; P01106: MYC; Xeno; NbExp=4; IntAct=EBI-1184963, EBI-447544;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981,
CC ECO:0000269|PubMed:17304222}. Cell projection, dendrite
CC {ECO:0000269|PubMed:17304222}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P52164-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P52164-2; Sequence=VSP_002119;
CC -!- PTM: Phosphorylated. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MAX family. {ECO:0000305}.
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DR EMBL; D14447; BAA03337.1; -; mRNA.
DR EMBL; D14448; BAA03338.1; -; mRNA.
DR PIR; S39792; S39792.
DR RefSeq; NP_071546.1; NM_022210.1. [P52164-1]
DR RefSeq; XP_006240310.1; XM_006240248.3. [P52164-2]
DR AlphaFoldDB; P52164; -.
DR BMRB; P52164; -.
DR SMR; P52164; -.
DR IntAct; P52164; 3.
DR MINT; P52164; -.
DR STRING; 10116.ENSRNOP00000010954; -.
DR iPTMnet; P52164; -.
DR PhosphoSitePlus; P52164; -.
DR PaxDb; P52164; -.
DR PRIDE; P52164; -.
DR Ensembl; ENSRNOT00000106817; ENSRNOP00000086002; ENSRNOG00000008049. [P52164-1]
DR GeneID; 60661; -.
DR KEGG; rno:60661; -.
DR UCSC; RGD:621101; rat. [P52164-1]
DR CTD; 4149; -.
DR RGD; 621101; Max.
DR eggNOG; KOG2483; Eukaryota.
DR GeneTree; ENSGT00530000064011; -.
DR HOGENOM; CLU_2346156_0_0_1; -.
DR InParanoid; P52164; -.
DR OMA; FAAETCE; -.
DR OrthoDB; 1545748at2759; -.
DR PhylomeDB; P52164; -.
DR TreeFam; TF318841; -.
DR Reactome; R-RNO-8953750; Transcriptional Regulation by E2F6.
DR PRO; PR:P52164; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000008049; Expressed in jejunum and 19 other tissues.
DR ExpressionAtlas; P52164; baseline and differential.
DR Genevisible; P52164; RN.
DR GO; GO:0000785; C:chromatin; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0070443; C:Mad-Max complex; ISO:RGD.
DR GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR GO; GO:0071943; C:Myc-Max complex; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0016605; C:PML body; IDA:RGD.
DR GO; GO:0032993; C:protein-DNA complex; ISO:RGD.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:RGD.
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:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0071375; P:cellular response to peptide hormone stimulus; IEP:RGD.
DR GO; GO:0009267; P:cellular response to starvation; IEP:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0051402; P:neuron apoptotic process; IEP:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:RGD.
DR GO; GO:0048678; P:response to axon injury; IEP:RGD.
DR GO; GO:0032868; P:response to insulin; IEP:RGD.
DR GO; GO:0010243; P:response to organonitrogen compound; IEP:RGD.
DR GO; GO:0060041; P:retina development in camera-type eye; IEP:RGD.
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 Acetylation; Activator; Alternative splicing; Cell projection; DNA-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
KW 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_0000127271"
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 105..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 105..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:0007744|PubMed:22673903"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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 Short)"
FT /evidence="ECO:0000303|PubMed:8268234"
FT /id="VSP_002119"
FT MOD_RES P52164-2:2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES P52164-2:11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 160 AA; 18272 MW; 86CB1A137727A57A CRC64;
MSDNDDIEVE SDEEQPRFQS AADKRAHHNA LERKRRDHIK DSFHSLRDSV PSLQGEKASR
AQILDKATEY IQYMRRKNHT HQQDIDDLKR QNALLEQQVR ALEKARSSAQ LQTNYPSSDN
SLYTNAKGGT ISAFDGGSDS SSESEPEEPQ NRKKLRMEAS
