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Protein

Protein max

Gene

Max

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. DNA binding Source: MGI

GO - Biological processi

  1. regulation of transcription, DNA-templated Source: MGI
  2. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein max
Alternative name(s):
Myc-associated factor X
Myc-binding novel HLH/LZ protein
Protein myn
Gene namesi
Name:Max
Synonyms:Myn
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:96921. Max.

Subcellular locationi

Nucleus. Cell projectiondendrite By similarity

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. dendrite Source: UniProtKB-SubCell
  3. MLL1 complex Source: UniProtKB
  4. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 160159Protein maxPRO_0000127270Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei2 – 21PhosphoserineBy similarity
Modified residuei11 – 111PhosphoserineBy similarity
Modified residuei153 – 1531N6-acetyllysineBy similarity
Modified residuei154 – 1541N6-acetyllysineBy similarity

Post-translational modificationi

Phosphorylated.Curated

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP28574.
PaxDbiP28574.
PRIDEiP28574.

PTM databases

PhosphoSiteiP28574.

Expressioni

Inductioni

By serum; in 3T3 fibroblasts.

Gene expression databases

CleanExiMM_MAX.
GenevestigatoriP28574.

Interactioni

Subunit structurei

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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Ccnt1Q9QWV92EBI-1183003,EBI-2655009
Cdk9Q99J952EBI-1183003,EBI-2654963
MycP011086EBI-1183003,EBI-1183114

Protein-protein interaction databases

DIPiDIP-116N.
IntActiP28574. 23 interactions.
STRINGi10090.ENSMUSP00000106025.

Structurei

Secondary structure

1
160
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi30 – 367Combined sources
Helixi74 – 10128Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A93NMR-B74-102[»]
2A93NMR-B74-102[»]
3U5VX-ray1.70A22-36[»]
ProteinModelPortaliP28574.
SMRiP28574. Positions 23-102.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28574.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 7452bHLHPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni81 – 10222Leucine-zipperAdd
BLAST

Sequence similaritiesi

Belongs to the MAX family.Curated
Contains 1 bHLH (basic helix-loop-helix) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG239807.
HOGENOMiHOG000293257.
HOVERGENiHBG008542.
InParanoidiP28574.
PhylomeDBiP28574.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
[Graphical view]
PfamiPF00010. HLH. 1 hit.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 1 isoform i produced by alternative splicing. Align

Note: A number of isoforms may be produced.

Isoform 1 (identifier: P28574-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSDNDDIEVE SDEEQARFQS AADKRAHHNA LERKRRDHIK DSFHSLRDSV
60 70 80 90 100
PSLQGEKASR AQILDKATEY IQYMRRKNDT HQQDIDDLKR QNALLEQQVR
110 120 130 140 150
ALEKARSSAQ LQTNYPSSDN SLYTNAKGGT ISAFDGGSDS SSESEPEEPQ
160
SRKKLRMEAS
Length:160
Mass (Da):18,197
Last modified:December 1, 1992 - v1
Checksum:iCBA5E1894E984F56
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63903 mRNA. Translation: AAA39797.1.
PIRiA38488.
UniGeneiMm.268548.
Mm.491131.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63903 mRNA. Translation: AAA39797.1.
PIRiA38488.
UniGeneiMm.268548.
Mm.491131.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A93NMR-B74-102[»]
2A93NMR-B74-102[»]
3U5VX-ray1.70A22-36[»]
ProteinModelPortaliP28574.
SMRiP28574. Positions 23-102.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-116N.
IntActiP28574. 23 interactions.
STRINGi10090.ENSMUSP00000106025.

PTM databases

PhosphoSiteiP28574.

Proteomic databases

MaxQBiP28574.
PaxDbiP28574.
PRIDEiP28574.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:96921. Max.

Phylogenomic databases

eggNOGiNOG239807.
HOGENOMiHOG000293257.
HOVERGENiHBG008542.
InParanoidiP28574.
PhylomeDBiP28574.

Miscellaneous databases

ChiTaRSiMax. mouse.
EvolutionaryTraceiP28574.
PROiP28574.
SOURCEiSearch...

Gene expression databases

CleanExiMM_MAX.
GenevestigatoriP28574.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
[Graphical view]
PfamiPF00010. HLH. 1 hit.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Association of Myn, the murine homolog of max, with c-Myc stimulates methylation-sensitive DNA binding and ras cotransformation."
    Prendergast G.C., Lawe D., Ziff E.B.
    Cell 65:395-407(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "JLP: a scaffolding protein that tethers JNK/p38MAPK signaling modules and transcription factors."
    Lee C.M., Onesime D., Reddy C.D., Dhanasekaran N., Reddy E.P.
    Proc. Natl. Acad. Sci. U.S.A. 99:14189-14194(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SPAG9.
  3. "Insights into the mechanism of heterodimerization from the 1H-NMR solution structure of the c-Myc-Max heterodimeric leucine zipper."
    Lavigne P., Crump M.P., Gagne S.M., Hodges R.S., Kay C.M., Sykes B.D.
    J. Mol. Biol. 281:165-181(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 70-102 IN COMPLEX WITH MYC.

Entry informationi

Entry nameiMAX_MOUSE
AccessioniPrimary (citable) accession number: P28574
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: February 4, 2015
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.