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Center for Computational Systems Medicine
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Protein Summary

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AS Summary

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Protein Functional Features

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Gene Isoform Structures and Expression Levels

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Protein Structures

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pLDDT Score Distribution

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Ramachandran Plot of Protein Structures

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Potential Active Site Information

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Protein Structure and Feature Comparision

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Protein-Protein Interaction

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Related Drugs

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Related Diseases

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Clinically Important Variants

Protein:MAX

Protein Summary

check button Gene summary
Gene name: MAX
ASpdb.0 ID: 4149
Gene
Gene symbol

MAX

Gene ID

4149

Gene nameMYC associated factor X
SynonymsPDMCS|bHLHd4
Cytomap

14q23.3

Type of geneprotein-coding
Descriptionprotein maxclass D basic helix-loop-helix protein 4
Modification date20240403
UniProtAcc

P61244


check button Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez
PartnerGeneGO IDGO termPubMed ID
GeneMAX

GO:0000122

negative regulation of transcription by RNA polymerase II

8521822|10723141

GeneMAX

GO:0000785

chromatin

12837246

GeneMAX

GO:0000977

RNA polymerase II transcription regulatory region sequence-specific DNA binding

8425219|8521822

GeneMAX

GO:0000981

DNA-binding transcription factor activity, RNA polymerase II-specific

8425218

GeneMAX

GO:0001227

DNA-binding transcription repressor activity, RNA polymerase II-specific

8521822

GeneMAX

GO:0001227

DNA-binding transcription repressor activity, RNA polymerase II-specific

26070438

GeneMAX

GO:0003677

DNA binding

9399572

GeneMAX

GO:0005634

nucleus

10723141|15358760

GeneMAX

GO:0006357

regulation of transcription by RNA polymerase II

8425218

GeneMAX

GO:0032993

protein-DNA complex

9399572

GeneMAX

GO:0045893

positive regulation of DNA-templated transcription

8425218

GeneMAX

GO:0071339

MLL1 complex

15960975

GeneMAX

GO:0090575

RNA polymerase II transcription regulator complex

8425219|8521822

GeneMAX

GO:1990837

sequence-specific double-stranded DNA binding

28473536



AS Summary

check button Information of the canonical protein with experimentally identified structure from PDB (2023).
UniProt AccFile namePDB IDMethodResolutionChainStartEnd
P61244-1P61244-1_1hlo_A.pdb1HLOX-ray2.8A492

check button ASpdb's canonical and alternatively spliced isoform information.
accession_idgene_namecanonical_idalternative_idcanonical_lengthalternative_lengthcanonical_startcanonical_endtypeoriginalSEQvariationSEQalternative_startalternative_end
P61244MAXP61244-1P61244-21601511321Deletionnonenone1212
P61244MAXP61244-1P61244-316010399160SubstitutionVRALEKARSSAQLQTNYPSSDNSLYTNAKGSTISAFDGGSDSSSESEPEEPQSRKKLRMEASGESES99103
P61244MAXP61244-1P61244-416013499160SubstitutionVRALEKARSSAQLQTNYPSSDNSLYTNAKGSTISAFDGGSDSSSESEPEEPQSRKKLRMEASGEHPSSWGSWPCCAPARSGFGTWACRVRASHGVCAQ99134
P61244MAXP61244-1P61244-51609658160SubstitutionASRAQILDKATEYIQYMRRKNHTHQQDIDDLKRQNALLEQQVRALEKARSSAQLQTNYPSSDNSLYTNAKGSTISAFDGGSDSSSESEPEEPQSRKKLRMEASLYFLFWKLCTPVLHRQSLMQKCHTFISSYQVHKKKECKI5896
P61244MAXP61244-1P61244-61608358160SubstitutionASRAQILDKATEYIQYMRRKNHTHQQDIDDLKRQNALLEQQVRALEKARSSAQLQTNYPSSDNSLYTNAKGSTISAFDGGSDSSSESEPEEPQSRKKLRMEASGTKMKLTLPPVFPYEHLPFPTVFCHG5883

check buttonMultiple sequence alignment of our canonical and alternatively spliced MAX

check button Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of MAX
UniProt-idENSGENSTENSP
P61244-1ENSG00000125952.21ENST00000358664.9ENSP00000351490.4
P61244-2ENSG00000125952.21ENST00000358402.8ENSP00000351175.4
P61244-3ENSG00000125952.21ENST00000394606.6ENSP00000378104.2
P61244-3ENSG00000125952.21ENST00000553928.5ENSP00000451907.1
P61244-3ENSG00000125952.21ENST00000556979.6ENSP00000452378.1
P61244-4ENSG00000125952.21ENST00000284165.10ENSP00000284165.6
P61244-5ENSG00000125952.21ENST00000246163.2ENSP00000246163.2
P61244-6ENSG00000125952.21ENST00000341653.6ENSP00000342482.2

UniProt-idNM IDNP ID
P61244-1NM_002382.4NP_002373.3
P61244-2NM_145112.2NP_660087.1
P61244-3NM_145113.2NP_660088.1
P61244-5NM_145114.2NP_660089.1
P61244-6NM_197957.3NP_932061.1

check buttonAmino acid sequences of our canonical and alternatively spliced MAX
accession_idProtein sequence
P61244-1MSDNDDIEVESDEEQPRFQSAADKRAHHNALERKRRDHIKDSFHSLRDSVPSLQGEKASRAQILDKATEYIQYMRRKNHTHQQDIDDLKR
P61244-2MSDNDDIEVESDADKRAHHNALERKRRDHIKDSFHSLRDSVPSLQGEKASRAQILDKATEYIQYMRRKNHTHQQDIDDLKRQNALLEQQV
P61244-3MSDNDDIEVESDEEQPRFQSAADKRAHHNALERKRRDHIKDSFHSLRDSVPSLQGEKASRAQILDKATEYIQYMRRKNHTHQQDIDDLKR
P61244-4MSDNDDIEVESDEEQPRFQSAADKRAHHNALERKRRDHIKDSFHSLRDSVPSLQGEKASRAQILDKATEYIQYMRRKNHTHQQDIDDLKR
P61244-5MSDNDDIEVESDEEQPRFQSAADKRAHHNALERKRRDHIKDSFHSLRDSVPSLQGEKLYFLFWKLCTPVLHRQSLMQKCHTFISSYQVHK
P61244-6

Protein Functional Features

check buttonMain function of this protein. (from UniProt)
MAX (go to UniProt):P61244

check buttonRetention analysis result of protein across 39 protein features of UniProt such as six molecule processing features, 13 region features, four site features, six amino acid modification features, two natural variation features, five experimental info features, and 3 secondary structure features. Here, because of limited space for viewing, we only show the protein feature retention information belong to the 13 regional features. All retention annotation result can be downloaded at

download page

* Minus value of BPloci means that the break pointn is located before the CDS.
- Retained protein feature among the 13 regional features.
Accession_idSubsectionStartEndFuncitonal featureSplicing information
P61244Domain2374Note=BHLH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00981Type=Substitution;Start=58;End=160
P61244Domain2374Note=BHLH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00981Type=Substitution;Start=58;End=160
P61244Region140Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=13;End=21
P61244Region81102Note=Leucine-zipperType=Substitution;Start=99;End=160
P61244Region81102Note=Leucine-zipperType=Substitution;Start=99;End=160
P61244Region81102Note=Leucine-zipperType=Substitution;Start=58;End=160
P61244Region81102Note=Leucine-zipperType=Substitution;Start=58;End=160
P61244Region103160Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Substitution;Start=99;End=160
P61244Region103160Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Substitution;Start=99;End=160
P61244Region103160Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Substitution;Start=58;End=160
P61244Region103160Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Substitution;Start=58;End=160
P61244Motif152156Note=Nuclear localization signalType=Substitution;Start=99;End=160
P61244Motif152156Note=Nuclear localization signalType=Substitution;Start=99;End=160
P61244Motif152156Note=Nuclear localization signalType=Substitution;Start=58;End=160
P61244Motif152156Note=Nuclear localization signalType=Substitution;Start=58;End=160
P61244Compositional bias1340Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=13;End=21
P61244Compositional bias103144Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Substitution;Start=99;End=160
P61244Compositional bias103144Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Substitution;Start=99;End=160
P61244Compositional bias103144Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Substitution;Start=58;End=160
P61244Compositional bias103144Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Substitution;Start=58;End=160
P61244Compositional bias145160Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Substitution;Start=99;End=160
P61244Compositional bias145160Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Substitution;Start=99;End=160
P61244Compositional bias145160Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Substitution;Start=58;End=160
P61244Compositional bias145160Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Substitution;Start=58;End=160


Gene Isoform Structures and Expression Levels for MAX

check buttonGene structures of our canonical and alternative spliced genes of MAX
* Click on the image to open the UCSC genome browser with custom track showing this image in a new window.
gene isoform structure of MAX

check button Expression levels of gene isoforms across GTEx.
gtex expression

check button Expression levels of gene isoforms across TCGA.
tcga expression


Protein Structures

check button PDB and CIF files of the predicted protein structures
* Here we show the 3D structure of the proteins using Mol*. AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Model confidence is shown from the pLDDT values per residue. pLDDT corresponds to the model’s prediction of its score on the local Distance Difference Test. It is a measure of local accuracy (from AlphfaFold website). To color code individual residues, we transformed individual PDB files into CIF format.
3D view using mol* of P61244-1
3D view using mol* of P61244-2
3D view using mol* of P61244-3
3D view using mol* of P61244-4
3D view using mol* of P61244-5
3D view using mol* of P61244-6


pLDDT Score Distribution

check button pLDDT score distribution of the predicted protein structures from AlphaFold2
* AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100.
pLDDT distribution across the protein length of P61244-1
all structure
pLDDT distribution across the protein length of P61244-2
all structure
pLDDT distribution across the protein length of P61244-3
all structure
pLDDT distribution across the protein length of P61244-4
all structure
pLDDT distribution across the protein length of P61244-5
all structure
pLDDT distribution across the protein length of P61244-6
all structure


Ramachandran Plot of Protein Structures


check button Ramachandran plot of the torsional angles - phi (φ)and psi (ψ) - of the residues (amino acids) contained in this protein peptide.
Ramachandran plot of P61244-1
all structure
Ramachandran plot of P61244-2
all structure
Ramachandran plot of P61244-3
all structure
Ramachandran plot of P61244-4
all structure
Ramachandran plot of P61244-5
all structure
Ramachandran plot of P61244-6
all structure

Potential Active Site Information


check button The potential binding sites of these proteins were identified using SiteMap, a module of the Schrodinger suite.
UniProt-idSite scoreSizeD scoreVolumeExposureEnclosureContactPhobicPhilicBalanceDon/AccResidues
P61244-10.599200.54659.6820.6720.6250.80.5650.7650.7390.54540,43,44,47,57,58,60,63
P61244-20.603240.54659.3390.6920.6140.7840.6690.8690.7690.86531,34,35,38,48,49,51,54
P61244-30.532130.53835.6720.8540.4770.581.0090.2673.7840.65150,52,66,69,70,73
P61244-40.558130.54636.3580.80.5450.7911.1330.3673.0890.51551,52,66,69,70,73,76
P61244-50.998541.068110.7890.4650.7531.0383.3590.23114.5641.88540,43,44,46,47,53,55,58,59,61,62
P61244-60.44790.38437.730.8620.530.6150.2630.6630.3962.4544,47,53,56,58

Protein Structure and Feature Comparision


check button Protein Structure Comparision Using Template Modeling Scores (TM-score).
all structure

check button Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Canonical validated structure (PDB)(green)
3D view using mol* of P61244-1_P61244-1_1hlo_A.pdb

check button Protein Structure Comparision Visualization with mol*. between Canonical validated structure (PDB)(orange) vs Alternative predicted structure (AF2)(green)
3D view using mol* of P61244-1_1hlo_A_P61244-2.pdb
3D view using mol* of P61244-1_1hlo_A_P61244-3.pdb
3D view using mol* of P61244-1_1hlo_A_P61244-4.pdb
3D view using mol* of P61244-1_1hlo_A_P61244-5.pdb
3D view using mol* of P61244-1_1hlo_A_P61244-6.pdb

check button Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green)
3D view using mol* of P61244-1_P61244-2.pdb
3D view using mol* of P61244-1_P61244-3.pdb
3D view using mol* of P61244-1_P61244-4.pdb
3D view using mol* of P61244-1_P61244-5.pdb
3D view using mol* of P61244-1_P61244-6.pdb

check button Protein Feature Comparison of the protein sequendary structures among the protiens.
./stats/secondary_structure/figure/P61244-1_vs_P61244-2.png
all structure<
./stats/secondary_structure/figure/P61244-1_vs_P61244-3.png
all structure<
./stats/secondary_structure/figure/P61244-1_vs_P61244-4.png
all structure<
./stats/secondary_structure/figure/P61244-1_vs_P61244-5.png
all structure<
./stats/secondary_structure/figure/P61244-1_vs_P61244-6.png
all structure<

check button Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens.
./stats/relative_asa/P61244-1_vs_P61244-2.png
all structure<
./stats/relative_asa/P61244-1_vs_P61244-3.png
all structure<
./stats/relative_asa/P61244-1_vs_P61244-4.png
all structure<
./stats/relative_asa/P61244-1_vs_P61244-5.png
all structure<
./stats/relative_asa/P61244-1_vs_P61244-6.png
all structure<


Protein-Protein Interaction


check button Interactors from UniProt.
Accession_idSubsectionStartEndFuncitonal featureSplicing information


check button Interactors from STRING.
Gene nameInteractors


Related Drugs to MAX


check button Drugs targeting this gene/protein.
(DrugBank)
UniProt accessionGene nameDrugBank IDDrug nameDrug groupActions

Related Diseases to MAX


check button Previous studies relating to the alternative splicing of MAX and disease information from the MeSH term (PubMed)
GenePMIDTitleAbstractMeSH IDMeSH term
MAX23707073EGFR mutation-induced alternative splicing of Max contributes to growth of glycolytic tumors in brain cancer.Alternative splicing contributes to diverse aspects of cancer pathogenesis including altered cellular metabolism, but the specificity of the process or its consequences are not well understood. We characterized genome-wide alternative splicing induced by the activating EGFRvIII mutation in glioblastoma (GBM). EGFRvIII upregulates the heterogeneous nuclear ribonucleoprotein (hnRNP) A1 splicing factor, promoting glycolytic gene expression and conferring significantly shorter survival in patients. HnRNPA1 promotes splicing of a transcript encoding the Myc-interacting partner Max, generating Delta Max, an enhancer of Myc-dependent transformation. Delta Max, but not full-length Max, rescues Myc-dependent glycolytic gene expression upon induced EGFRvIII loss, and correlates with hnRNPA1 expression and downstream Myc-dependent gene transcription in patients. Finally, Delta Max is shown to promote glioma cell proliferation in vitro and augment EGFRvIII expressing GBM growth in vivo. These results demonstrate an important role for alternative splicing in GBM and identify Delta Max as a mediator of Myc-dependent tumor cell metabolism.D005909Glioblastoma


Clinically important variants in MAX


check button (ClinVar, 04/20/2024)
accession_iduniprot_idgene_nameTypeVariantClinical_significance