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Protein

Protein max

Gene

Max

Organism
Drosophila melanogaster (Fruit fly)
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.1 Publication

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • protein heterodimerization activity Source: FlyBase
  • transcription factor activity, sequence-specific DNA binding Source: UniProtKB

GO - Biological processi

  • negative regulation of transcription from RNA polymerase II promoter Source: FlyBase
  • regulation of transcription, DNA-templated Source: UniProtKB
  • 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-DME-69202. Cyclin E associated events during G1/S transition.
R-DME-69656. Cyclin A:Cdk2-associated events at S phase entry.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein max
Short name:
dMax
Alternative name(s):
Myc-associated factor X
Gene namesi
Name:Max
ORF Names:CG9648
OrganismiDrosophila melanogaster (Fruit fly)Imported
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0017578. Max.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 161161Protein maxPRO_0000127275Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei131 – 1311Phosphoserine1 Publication
Modified residuei137 – 1371Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP91664.
PRIDEiP91664.

PTM databases

iPTMnetiP91664.

Expressioni

Tissue specificityi

Embryo, especially in central nervous system.1 Publication

Developmental stagei

Highest expression in embryos.1 Publication

Gene expression databases

BgeeiP91664.
ExpressionAtlasiP91664. differential.
GenevisibleiP91664. DM.

Interactioni

Subunit structurei

Efficient DNA binding requires dimerization with another bHLH protein. Binds DNA as a heterodimer with MYC or MAD.1 Publication

GO - Molecular functioni

  • protein heterodimerization activity Source: FlyBase

Protein-protein interaction databases

BioGridi65371. 1 interaction.
DIPiDIP-60982N.
IntActiP91664. 3 interactions.
MINTiMINT-977153.
STRINGi7227.FBpp0074785.

Structurei

3D structure databases

ProteinModelPortaliP91664.
SMRiP91664. Positions 36-108.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 9052bHLHPROSITE-ProRule annotationAdd
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.
InParanoidiP91664.
KOiK04453.
OMAiRHTSTAN.
OrthoDBiEOG7XPZ7J.
PhylomeDBiP91664.

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.

P91664-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSMSDDDRDI DIESDEDGDS DTGLGSSRHT NTANFTQAEK RAHHNALERR
60 70 80 90 100
RRDHIKESFT NLREAVPTLK GEKASRAQIL KKTTECIQTM RRKISENQKD
110 120 130 140 150
IEEIKRQNNI IAKQIQALES SNGDQFSEFL SDEEVGSEEA DDEDLDQDFS
160
RRNKKMKTFH A
Length:161
Mass (Da):18,530
Last modified:May 1, 1997 - v1
Checksum:iA217A22A7B514C77
GO

Sequence cautioni

The sequence AAL28562.1 differs from that shown.Intron retention.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti91 – 911R → G in AAL90428 (PubMed:12537569).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U77369 mRNA. Translation: AAB39841.1.
AE014296 Genomic DNA. Translation: AAF49179.1.
AY061014 mRNA. Translation: AAL28562.1. Sequence problems.
AY089690 mRNA. Translation: AAL90428.1.
BT025211 mRNA. Translation: ABF17902.1.
RefSeqiNP_001246833.1. NM_001259904.2.
NP_001287114.1. NM_001300185.1.
NP_649097.1. NM_140840.4.
UniGeneiDm.3749.

Genome annotation databases

EnsemblMetazoaiFBtr0075018; FBpp0074785; FBgn0017578.
FBtr0310276; FBpp0301959; FBgn0017578.
FBtr0345391; FBpp0311541; FBgn0017578.
GeneIDi40095.
KEGGidme:Dmel_CG9648.
UCSCiCG9648-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U77369 mRNA. Translation: AAB39841.1.
AE014296 Genomic DNA. Translation: AAF49179.1.
AY061014 mRNA. Translation: AAL28562.1. Sequence problems.
AY089690 mRNA. Translation: AAL90428.1.
BT025211 mRNA. Translation: ABF17902.1.
RefSeqiNP_001246833.1. NM_001259904.2.
NP_001287114.1. NM_001300185.1.
NP_649097.1. NM_140840.4.
UniGeneiDm.3749.

3D structure databases

ProteinModelPortaliP91664.
SMRiP91664. Positions 36-108.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi65371. 1 interaction.
DIPiDIP-60982N.
IntActiP91664. 3 interactions.
MINTiMINT-977153.
STRINGi7227.FBpp0074785.

PTM databases

iPTMnetiP91664.

Proteomic databases

PaxDbiP91664.
PRIDEiP91664.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0075018; FBpp0074785; FBgn0017578.
FBtr0310276; FBpp0301959; FBgn0017578.
FBtr0345391; FBpp0311541; FBgn0017578.
GeneIDi40095.
KEGGidme:Dmel_CG9648.
UCSCiCG9648-RA. d. melanogaster.

Organism-specific databases

CTDi4149.
FlyBaseiFBgn0017578. Max.

Phylogenomic databases

eggNOGiKOG2483. Eukaryota.
ENOG4111V1C. LUCA.
GeneTreeiENSGT00530000064011.
InParanoidiP91664.
KOiK04453.
OMAiRHTSTAN.
OrthoDBiEOG7XPZ7J.
PhylomeDBiP91664.

Enzyme and pathway databases

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

Miscellaneous databases

GenomeRNAii40095.
PROiP91664.

Gene expression databases

BgeeiP91664.
ExpressionAtlasiP91664. differential.
GenevisibleiP91664. DM.

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. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: Oregon-R1 Publication.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley1 Publication.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley1 Publication.
    Tissue: Head1 Publication.
  5. Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C., Celniker S.E.
    Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
  6. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131 AND SER-137, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiMAX_DROME
AccessioniPrimary (citable) accession number: P91664
Secondary accession number(s): Q1LZ15, Q8SXE2, Q95S07
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: May 1, 1997
Last modified: July 6, 2016
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. 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.