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P91664 (MAX_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein max

Short name=dMax
Alternative name(s):
Myc-associated factor X
Gene names
Name:Max
ORF Names:CG9648
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length161 AA.
Sequence statusComplete.
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. Ref.1

Subunit structure

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

Subcellular location

Nucleus.

Tissue specificity

Embryo, especially in central nervous system. Ref.1

Developmental stage

Highest expression in embryos. Ref.1

Sequence similarities

Belongs to the MAX family.

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

Sequence caution

The sequence AAL28562.1 differs from that shown. Reason: Intron retention.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   LigandDNA-binding
   Molecular functionActivator
Repressor
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processtranscription, DNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentnucleus

Inferred by curator Ref.1. Source: UniProtKB

   Molecular functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

sequence-specific DNA binding transcription factor activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 161161Protein max
PRO_0000127275

Regions

Domain55 – 9137Helix-loop-helix motif
DNA binding40 – 5213Basic motif

Amino acid modifications

Modified residue1311Phosphoserine Ref.6
Modified residue1371Phosphoserine Ref.6

Experimental info

Sequence conflict911R → G in AAL90428. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P91664 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: A217A22A7B514C77

FASTA16118,530
        10         20         30         40         50         60 
MSMSDDDRDI DIESDEDGDS DTGLGSSRHT NTANFTQAEK RAHHNALERR RRDHIKESFT 

        70         80         90        100        110        120 
NLREAVPTLK GEKASRAQIL KKTTECIQTM RRKISENQKD IEEIKRQNNI IAKQIQALES 

       130        140        150        160 
SNGDQFSEFL SDEEVGSEEA DDEDLDQDFS RRNKKMKTFH A 

« Hide

References

« Hide 'large scale' references
[1]"Myc and Max homologs in Drosophila."
Gallant P., Shiio Y., Cheng P.F., Parkhurst S.M., Eisenman R.N.
Science 274:1523-1527(1996) [PubMed: 8929412] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Strain: Oregon-R.
[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. expand/collapse author list , 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: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[4]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Head.
[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: 18327897] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131 AND SER-137, MASS SPECTROMETRY.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_649097.1. NM_140840.2.
UniGeneDm.3749.

3D structure databases

ProteinModelPortalP91664.
SMRP91664. Positions 36-108.
ModBaseSearch...

Protein-protein interaction databases

IntActP91664. 2 interactions.
MINTMINT-977153.
STRINGP91664.

Proteomic databases

PRIDEP91664.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0075018; FBpp0074785; FBgn0017578.
FBtr0306012; FBpp0297154; FBgn0017578.
GeneID40095.
KEGGdme:Dmel_CG9648.
NMPDRfig|7227.3.peg.10518.
UCSCCG9648-RA. d. melanogaster.

Organism-specific databases

CTD4149.
FlyBaseFBgn0017578. Max.

Phylogenomic databases

eggNOGinNOG11219.
GeneTreeEMGT00050000010707.
InParanoidP91664.
OMATTECIQT.
OrthoDBEOG480GD4.
PhylomeDBP91664.

Gene expression databases

BgeeP91664.
GermOnlineCG9648. Drosophila melanogaster.

Family and domain databases

InterProIPR011598. HLH_DNA-bd.
[Graphical view]
Gene3DG3DSA:4.10.280.10. HLH_DNA_bd. 1 hit.
KOK04453.
PfamPF00010. HLH. 1 hit.
[Graphical view]
SMARTSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMSSF47459. HLH_basic. 1 hit.
PROSITEPS50888. HLH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio816971.

Entry information

Entry nameMAX_DROME
AccessionPrimary (citable) accession number: P91664
Secondary accession number(s): Q1LZ15, Q8SXE2, Q95S07
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: May 1, 1997
Last modified: January 25, 2012
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

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

SIMILARITY comments

Index of protein domains and families