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P28574 (MAX_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein max
Alternative name(s):
Myc-associated factor X
Myc-binding novel HLH/LZ protein
Protein myn
Gene names
Name:Max
Synonyms:Myn
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length160 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Subunit structure

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. Ref.2

Subcellular location

Nucleus. Cell projectiondendrite By similarity.

Induction

By serum; in 3T3 fibroblasts.

Post-translational modification

Phosphorylated Probable.

Sequence similarities

Belongs to the MAX family.

Contains 1 bHLH (basic helix-loop-helix) domain.

Binary interactions

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms may be produced.
Isoform 1 (identifier: P28574-1)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 160159Protein max
PRO_0000127270

Regions

Domain23 – 7452bHLH
Region81 – 10222Leucine-zipper

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue21Phosphoserine By similarity
Modified residue111Phosphoserine By similarity
Modified residue1531N6-acetyllysine By similarity
Modified residue1541N6-acetyllysine By similarity

Secondary structure

..... 160
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: CBA5E1894E984F56

FASTA16018,197
        10         20         30         40         50         60 
MSDNDDIEVE SDEEQARFQS AADKRAHHNA LERKRRDHIK DSFHSLRDSV PSLQGEKASR 

        70         80         90        100        110        120 
AQILDKATEY IQYMRRKNDT HQQDIDDLKR QNALLEQQVR ALEKARSSAQ LQTNYPSSDN 

       130        140        150        160 
SLYTNAKGGT ISAFDGGSDS SSESEPEEPQ SRKKLRMEAS 

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M63903 mRNA. Translation: AAA39797.1.
CCDSCCDS36479.1. [P28574-1]
PIRA38488.
UniGeneMm.268548.
Mm.491131.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A93NMR-B74-102[»]
2A93NMR-B74-102[»]
3U5VX-ray1.70A22-36[»]
ProteinModelPortalP28574.
SMRP28574. Positions 23-102.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-116N.
IntActP28574. 23 interactions.
STRING10090.ENSMUSP00000106025.

PTM databases

PhosphoSiteP28574.

Proteomic databases

MaxQBP28574.
PaxDbP28574.
PRIDEP28574.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

MGIMGI:96921. Max.

Phylogenomic databases

eggNOGNOG239807.
HOGENOMHOG000293257.
HOVERGENHBG008542.
InParanoidP28574.
PhylomeDBP28574.

Gene expression databases

CleanExMM_MAX.
GenevestigatorP28574.

Family and domain databases

Gene3D4.10.280.10. 1 hit.
InterProIPR011598. bHLH_dom.
[Graphical view]
PfamPF00010. HLH. 1 hit.
[Graphical view]
SMARTSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMSSF47459. SSF47459. 1 hit.
PROSITEPS50888. BHLH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMAX. mouse.
EvolutionaryTraceP28574.
PROP28574.
SOURCESearch...

Entry information

Entry nameMAX_MOUSE
AccessionPrimary (citable) accession number: P28574
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: July 9, 2014
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot