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P28574

- MAX_MOUSE

UniProt

P28574 - MAX_MOUSE

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Protein

Protein max

Gene
Max, Myn
Organism
Mus musculus (Mouse)
Status
Reviewed - 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
  2. protein binding Source: IntAct

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. dendrite Source: UniProtKB-SubCell
  2. MLL1 complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Nucleus

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine By similarity
Modified residuei2 – 21Phosphoserine By similarity
Modified residuei11 – 111Phosphoserine By similarity
Modified residuei153 – 1531N6-acetyllysine By similarity
Modified residuei154 – 1541N6-acetyllysine By similarity

Post-translational modificationi

Phosphorylated Inferred.

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.1 Publication

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 – 367
Helixi74 – 10128

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP28574.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 7452bHLHAdd
BLAST

Region

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

Sequence similaritiesi

Belongs to the MAX family.

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

MSDNDDIEVE SDEEQARFQS AADKRAHHNA LERKRRDHIK DSFHSLRDSV    50
PSLQGEKASR AQILDKATEY IQYMRRKNDT HQQDIDDLKR QNALLEQQVR 100
ALEKARSSAQ LQTNYPSSDN SLYTNAKGGT ISAFDGGSDS SSESEPEEPQ 150
SRKKLRMEAS 160
Length:160
Mass (Da):18,197
Last modified:December 1, 1992 - v1
Checksum:iCBA5E1894E984F56
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
M63903 mRNA. Translation: AAA39797.1 .
PIRi A38488.
UniGenei Mm.268548.
Mm.491131.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A93 NMR - B 74-102 [» ]
2A93 NMR - B 74-102 [» ]
3U5V X-ray 1.70 A 22-36 [» ]
ProteinModelPortali P28574.
SMRi P28574. Positions 23-102.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-116N.
IntActi P28574. 23 interactions.
STRINGi 10090.ENSMUSP00000106025.

PTM databases

PhosphoSitei P28574.

Proteomic databases

MaxQBi P28574.
PaxDbi P28574.
PRIDEi P28574.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

MGIi MGI:96921. Max.

Phylogenomic databases

eggNOGi NOG239807.
HOGENOMi HOG000293257.
HOVERGENi HBG008542.
InParanoidi P28574.
PhylomeDBi P28574.

Miscellaneous databases

ChiTaRSi MAX. mouse.
EvolutionaryTracei P28574.
PROi P28574.
SOURCEi Search...

Gene expression databases

CleanExi MM_MAX.
Genevestigatori P28574.

Family and domain databases

Gene3Di 4.10.280.10. 1 hit.
InterProi IPR011598. bHLH_dom.
[Graphical view ]
Pfami PF00010. HLH. 1 hit.
[Graphical view ]
SMARTi SM00353. HLH. 1 hit.
[Graphical view ]
SUPFAMi SSF47459. SSF47459. 1 hit.
PROSITEi PS50888. BHLH. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 136 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

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