Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Protein max

Gene

Max

Organism
Rattus norvegicus (Rat)
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. May repress transcription via the recruitment of a chromatin remodeling complex containing H3 'Lys-9' histone methyltransferase activity.1 Publication

GO - Molecular functioni

  • protein complex binding Source: RGD
  • protein heterodimerization activity Source: RGD
  • protein homodimerization activity Source: RGD
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: Ensembl
  • sequence-specific DNA binding Source: RGD
  • transcription factor activity, RNA polymerase II core promoter sequence-specific Source: Ensembl
  • transcription factor activity, sequence-specific DNA binding Source: RGD

GO - Biological processi

  • cellular response to peptide hormone stimulus Source: RGD
  • cellular response to starvation Source: RGD
  • negative regulation of gene expression Source: RGD
  • neuron apoptotic process Source: RGD
  • protein complex assembly Source: RGD
  • regulation of transcription, DNA-templated Source: RGD
  • response to axon injury Source: RGD
  • response to insulin Source: RGD
  • response to organonitrogen compound Source: RGD
  • retina development in camera-type eye Source: RGD
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-RNO-69202. Cyclin E associated events during G1/S transition.
R-RNO-69656. Cyclin A:Cdk2-associated events at S phase entry.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein max
Alternative name(s):
Myc-associated factor X
Gene namesi
Name:Max
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 6

Organism-specific databases

RGDi621101. Max.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: RGD
  • dendrite Source: RGD
  • MLL1 complex Source: UniProtKB
  • nucleus Source: RGD
  • PML body Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 160159Protein maxPRO_0000127271Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei2 – 21PhosphoserineCombined sources
Modified residuei11 – 111PhosphoserineCombined sources
Modified residuei153 – 1531N6-acetyllysineBy similarity
Modified residuei154 – 1541N6-acetyllysineBy similarity
Isoform Short (identifier: P52164-2)
Modified residuei2 – 21PhosphoserineCombined sources
Modified residuei11 – 111PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated.Curated

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP52164.
PRIDEiP52164.

PTM databases

iPTMnetiP52164.
PhosphoSiteiP52164.

Expressioni

Gene expression databases

ExpressionAtlasiP52164. baseline and differential.
GenevisibleiP52164. RN.

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
Abi1Q9QZM52EBI-1184963,EBI-920097
MYCP011064EBI-1184963,EBI-447544From a different organism.

GO - Molecular functioni

  • protein complex binding Source: RGD
  • protein heterodimerization activity Source: RGD
  • protein homodimerization activity Source: RGD

Protein-protein interaction databases

IntActiP52164. 3 interactions.
MINTiMINT-4508738.
STRINGi10116.ENSRNOP00000010954.

Structurei

3D structure databases

ProteinModelPortaliP52164.
SMRiP52164. Positions 23-102.
ModBaseiSearch...
MobiDBiSearch...

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

eggNOGiKOG2483. Eukaryota.
ENOG4111V1C. LUCA.
GeneTreeiENSGT00530000064011.
HOGENOMiHOG000293257.
HOVERGENiHBG008542.
InParanoidiP52164.
KOiK04453.
OMAiRHTSTAN.
OrthoDBiEOG7XPZ7J.
PhylomeDBiP52164.
TreeFamiTF318841.

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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Long (identifier: P52164-1) [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 SDEEQPRFQS AADKRAHHNA LERKRRDHIK DSFHSLRDSV
60 70 80 90 100
PSLQGEKASR AQILDKATEY IQYMRRKNHT HQQDIDDLKR QNALLEQQVR
110 120 130 140 150
ALEKARSSAQ LQTNYPSSDN SLYTNAKGGT ISAFDGGSDS SSESEPEEPQ
160
NRKKLRMEAS
Length:160
Mass (Da):18,272
Last modified:October 1, 1996 - v1
Checksum:i86CB1A137727A57A
GO
Isoform Short (identifier: P52164-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     13-21: Missing.

Show »
Length:151
Mass (Da):17,199
Checksum:iA6B21FF5F39793EF
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei13 – 219Missing in isoform Short. 1 PublicationVSP_002119

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14447 mRNA. Translation: BAA03337.1.
D14448 mRNA. Translation: BAA03338.1.
PIRiS39792.
RefSeqiNP_071546.1. NM_022210.1. [P52164-1]
XP_006240310.1. XM_006240248.2. [P52164-2]
UniGeneiRn.4210.

Genome annotation databases

EnsembliENSRNOT00000041442; ENSRNOP00000040275; ENSRNOG00000008049. [P52164-2]
ENSRNOT00000083286; ENSRNOP00000072268; ENSRNOG00000008049. [P52164-1]
GeneIDi60661.
KEGGirno:60661.
UCSCiRGD:621101. rat. [P52164-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14447 mRNA. Translation: BAA03337.1.
D14448 mRNA. Translation: BAA03338.1.
PIRiS39792.
RefSeqiNP_071546.1. NM_022210.1. [P52164-1]
XP_006240310.1. XM_006240248.2. [P52164-2]
UniGeneiRn.4210.

3D structure databases

ProteinModelPortaliP52164.
SMRiP52164. Positions 23-102.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP52164. 3 interactions.
MINTiMINT-4508738.
STRINGi10116.ENSRNOP00000010954.

PTM databases

iPTMnetiP52164.
PhosphoSiteiP52164.

Proteomic databases

PaxDbiP52164.
PRIDEiP52164.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000041442; ENSRNOP00000040275; ENSRNOG00000008049. [P52164-2]
ENSRNOT00000083286; ENSRNOP00000072268; ENSRNOG00000008049. [P52164-1]
GeneIDi60661.
KEGGirno:60661.
UCSCiRGD:621101. rat. [P52164-1]

Organism-specific databases

CTDi4149.
RGDi621101. Max.

Phylogenomic databases

eggNOGiKOG2483. Eukaryota.
ENOG4111V1C. LUCA.
GeneTreeiENSGT00530000064011.
HOGENOMiHOG000293257.
HOVERGENiHBG008542.
InParanoidiP52164.
KOiK04453.
OMAiRHTSTAN.
OrthoDBiEOG7XPZ7J.
PhylomeDBiP52164.
TreeFamiTF318841.

Enzyme and pathway databases

ReactomeiR-RNO-69202. Cyclin E associated events during G1/S transition.
R-RNO-69656. Cyclin A:Cdk2-associated events at S phase entry.

Miscellaneous databases

PROiP52164.

Gene expression databases

ExpressionAtlasiP52164. baseline and differential.
GenevisibleiP52164. RN.

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

« Hide 'large scale' publications
  1. "Molecular cloning and sequencing of rat Max cDNA: castration-induced expression of the 2 kb transcript in male accessory sex organs of rats."
    Izawa M.
    Biochim. Biophys. Acta 1216:492-494(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
    Strain: Wistar.
    Tissue: Seminal vesicle.
  2. "Abelson interacting protein 1 (Abi-1) is essential for dendrite morphogenesis and synapse formation."
    Proepper C., Johannsen S., Liebau S., Dahl J., Vaida B., Bockmann J., Kreutz M.R., Gundelfinger E.D., Boeckers T.M.
    EMBO J. 26:1397-1409(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS TRANSCRIPTION REGULATOR, INTERACTION WITH ABI1, SUBCELLULAR LOCATION.
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-11, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-11 (ISOFORM SHORT), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMAX_RAT
AccessioniPrimary (citable) accession number: P52164
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 8, 2016
This is version 128 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.