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P28574

- MAX_MOUSE

UniProt

P28574 - MAX_MOUSE

Protein

Protein max

Gene

Max

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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

    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

    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 – 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.
    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

    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: October 1, 2014
    This is version 137 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