Protein:MAX |
Protein Summary |
Gene summary |
| Gene name: MAX | ASpdb.0 ID: 4149 | Gene | Gene symbol | MAX | Gene ID | 4149 |
| Gene name | MYC associated factor X |
| Synonyms | PDMCS|bHLHd4 |
| Cytomap | 14q23.3 |
| Type of gene | protein-coding |
| Description | protein maxclass D basic helix-loop-helix protein 4 |
| Modification date | 20240403 |
| UniProtAcc | P61244 |
Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
| Partner | Gene | GO ID | GO term | PubMed ID |
| Gene | MAX | GO:0000122 | negative regulation of transcription by RNA polymerase II | 8521822|10723141 |
| Gene | MAX | GO:0000785 | chromatin | 12837246 |
| Gene | MAX | GO:0000977 | RNA polymerase II transcription regulatory region sequence-specific DNA binding | 8425219|8521822 |
| Gene | MAX | GO:0000981 | DNA-binding transcription factor activity, RNA polymerase II-specific | 8425218 |
| Gene | MAX | GO:0001227 | DNA-binding transcription repressor activity, RNA polymerase II-specific | 8521822 |
| Gene | MAX | GO:0001227 | DNA-binding transcription repressor activity, RNA polymerase II-specific | 26070438 |
| Gene | MAX | GO:0003677 | DNA binding | 9399572 |
| Gene | MAX | GO:0005634 | nucleus | 10723141|15358760 |
| Gene | MAX | GO:0006357 | regulation of transcription by RNA polymerase II | 8425218 |
| Gene | MAX | GO:0032993 | protein-DNA complex | 9399572 |
| Gene | MAX | GO:0045893 | positive regulation of DNA-templated transcription | 8425218 |
| Gene | MAX | GO:0071339 | MLL1 complex | 15960975 |
| Gene | MAX | GO:0090575 | RNA polymerase II transcription regulator complex | 8425219|8521822 |
| Gene | MAX | GO:1990837 | sequence-specific double-stranded DNA binding | 28473536 |
AS Summary |
Information of the canonical protein with experimentally identified structure from PDB (2023). |
| UniProt Acc | File name | PDB ID | Method | Resolution | Chain | Start | End |
| P61244-1 | P61244-1_1hlo_A.pdb | 1HLO | X-ray | 2.8 | A | 4 | 92 |
ASpdb's canonical and alternatively spliced isoform information. |
| accession_id | gene_name | canonical_id | alternative_id | canonical_length | alternative_length | canonical_start | canonical_end | type | originalSEQ | variationSEQ | alternative_start | alternative_end |
| P61244 | MAX | P61244-1 | P61244-2 | 160 | 151 | 13 | 21 | Deletion | none | none | 12 | 12 |
| P61244 | MAX | P61244-1 | P61244-3 | 160 | 103 | 99 | 160 | Substitution | VRALEKARSSAQLQTNYPSSDNSLYTNAKGSTISAFDGGSDSSSESEPEEPQSRKKLRMEAS | GESES | 99 | 103 |
| P61244 | MAX | P61244-1 | P61244-4 | 160 | 134 | 99 | 160 | Substitution | VRALEKARSSAQLQTNYPSSDNSLYTNAKGSTISAFDGGSDSSSESEPEEPQSRKKLRMEAS | GEHPSSWGSWPCCAPARSGFGTWACRVRASHGVCAQ | 99 | 134 |
| P61244 | MAX | P61244-1 | P61244-5 | 160 | 96 | 58 | 160 | Substitution | ASRAQILDKATEYIQYMRRKNHTHQQDIDDLKRQNALLEQQVRALEKARSSAQLQTNYPSSDNSLYTNAKGSTISAFDGGSDSSSESEPEEPQSRKKLRMEAS | LYFLFWKLCTPVLHRQSLMQKCHTFISSYQVHKKKECKI | 58 | 96 |
| P61244 | MAX | P61244-1 | P61244-6 | 160 | 83 | 58 | 160 | Substitution | ASRAQILDKATEYIQYMRRKNHTHQQDIDDLKRQNALLEQQVRALEKARSSAQLQTNYPSSDNSLYTNAKGSTISAFDGGSDSSSESEPEEPQSRKKLRMEAS | GTKMKLTLPPVFPYEHLPFPTVFCHG | 58 | 83 |
Multiple sequence alignment of our canonical and alternatively spliced MAX |
Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of MAX |
| UniProt-id | ENSG | ENST | ENSP |
| P61244-1 | ENSG00000125952.21 | ENST00000358664.9 | ENSP00000351490.4 |
| P61244-2 | ENSG00000125952.21 | ENST00000358402.8 | ENSP00000351175.4 |
| P61244-3 | ENSG00000125952.21 | ENST00000394606.6 | ENSP00000378104.2 |
| P61244-3 | ENSG00000125952.21 | ENST00000553928.5 | ENSP00000451907.1 |
| P61244-3 | ENSG00000125952.21 | ENST00000556979.6 | ENSP00000452378.1 |
| P61244-4 | ENSG00000125952.21 | ENST00000284165.10 | ENSP00000284165.6 |
| P61244-5 | ENSG00000125952.21 | ENST00000246163.2 | ENSP00000246163.2 |
| P61244-6 | ENSG00000125952.21 | ENST00000341653.6 | ENSP00000342482.2 |
| UniProt-id | NM ID | NP ID |
| P61244-1 | NM_002382.4 | NP_002373.3 |
| P61244-2 | NM_145112.2 | NP_660087.1 |
| P61244-3 | NM_145113.2 | NP_660088.1 |
| P61244-5 | NM_145114.2 | NP_660089.1 |
| P61244-6 | NM_197957.3 | NP_932061.1 |
Amino acid sequences of our canonical and alternatively spliced MAX |
| accession_id | Protein sequence |
| P61244-1 | MSDNDDIEVESDEEQPRFQSAADKRAHHNALERKRRDHIKDSFHSLRDSVPSLQGEKASRAQILDKATEYIQYMRRKNHTHQQDIDDLKR |
| P61244-2 | MSDNDDIEVESDADKRAHHNALERKRRDHIKDSFHSLRDSVPSLQGEKASRAQILDKATEYIQYMRRKNHTHQQDIDDLKRQNALLEQQV |
| P61244-3 | MSDNDDIEVESDEEQPRFQSAADKRAHHNALERKRRDHIKDSFHSLRDSVPSLQGEKASRAQILDKATEYIQYMRRKNHTHQQDIDDLKR |
| P61244-4 | MSDNDDIEVESDEEQPRFQSAADKRAHHNALERKRRDHIKDSFHSLRDSVPSLQGEKASRAQILDKATEYIQYMRRKNHTHQQDIDDLKR |
| P61244-5 | MSDNDDIEVESDEEQPRFQSAADKRAHHNALERKRRDHIKDSFHSLRDSVPSLQGEKLYFLFWKLCTPVLHRQSLMQKCHTFISSYQVHK |
| P61244-6 |
Protein Functional Features |
Main function of this protein. (from UniProt) |
| MAX (go to UniProt):P61244 |
Retention 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 * Minus value of BPloci means that the break pointn is located before the CDS. |
| - Retained protein feature among the 13 regional features. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| P61244 | Domain | 23 | 74 | Note=BHLH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00981 | Type=Substitution;Start=58;End=160 |
| P61244 | Domain | 23 | 74 | Note=BHLH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00981 | Type=Substitution;Start=58;End=160 |
| P61244 | Region | 1 | 40 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=13;End=21 |
| P61244 | Region | 81 | 102 | Note=Leucine-zipper | Type=Substitution;Start=99;End=160 |
| P61244 | Region | 81 | 102 | Note=Leucine-zipper | Type=Substitution;Start=99;End=160 |
| P61244 | Region | 81 | 102 | Note=Leucine-zipper | Type=Substitution;Start=58;End=160 |
| P61244 | Region | 81 | 102 | Note=Leucine-zipper | Type=Substitution;Start=58;End=160 |
| P61244 | Region | 103 | 160 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=99;End=160 |
| P61244 | Region | 103 | 160 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=99;End=160 |
| P61244 | Region | 103 | 160 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=58;End=160 |
| P61244 | Region | 103 | 160 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=58;End=160 |
| P61244 | Motif | 152 | 156 | Note=Nuclear localization signal | Type=Substitution;Start=99;End=160 |
| P61244 | Motif | 152 | 156 | Note=Nuclear localization signal | Type=Substitution;Start=99;End=160 |
| P61244 | Motif | 152 | 156 | Note=Nuclear localization signal | Type=Substitution;Start=58;End=160 |
| P61244 | Motif | 152 | 156 | Note=Nuclear localization signal | Type=Substitution;Start=58;End=160 |
| P61244 | Compositional bias | 13 | 40 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=13;End=21 |
| P61244 | Compositional bias | 103 | 144 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=99;End=160 |
| P61244 | Compositional bias | 103 | 144 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=99;End=160 |
| P61244 | Compositional bias | 103 | 144 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=58;End=160 |
| P61244 | Compositional bias | 103 | 144 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=58;End=160 |
| P61244 | Compositional bias | 145 | 160 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=99;End=160 |
| P61244 | Compositional bias | 145 | 160 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=99;End=160 |
| P61244 | Compositional bias | 145 | 160 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=58;End=160 |
| P61244 | Compositional bias | 145 | 160 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=58;End=160 |
Gene Isoform Structures and Expression Levels for MAX |
Gene 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. |
Expression levels of gene isoforms across GTEx. |
Expression levels of gene isoforms across TCGA. |
Protein Structures |
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 |
pLDDT score distribution of the predicted protein structures from AlphaFold2* AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. |
Ramachandran Plot of Protein Structures |
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 |
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| Ramachandran plot of P61244-2 |
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| Ramachandran plot of P61244-3 |
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| Ramachandran plot of P61244-4 |
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| Ramachandran plot of P61244-5 |
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| Ramachandran plot of P61244-6 |
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Potential Active Site Information |
The potential binding sites of these proteins were identified using SiteMap, a module of the Schrodinger suite. |
| UniProt-id | Site score | Size | D score | Volume | Exposure | Enclosure | Contact | Phobic | Philic | Balance | Don/Acc | Residues |
| P61244-1 | 0.599 | 20 | 0.546 | 59.682 | 0.672 | 0.625 | 0.8 | 0.565 | 0.765 | 0.739 | 0.545 | 40,43,44,47,57,58,60,63
|
| P61244-2 | 0.603 | 24 | 0.546 | 59.339 | 0.692 | 0.614 | 0.784 | 0.669 | 0.869 | 0.769 | 0.865 | 31,34,35,38,48,49,51,54
|
| P61244-3 | 0.532 | 13 | 0.538 | 35.672 | 0.854 | 0.477 | 0.58 | 1.009 | 0.267 | 3.784 | 0.651 | 50,52,66,69,70,73
|
| P61244-4 | 0.558 | 13 | 0.546 | 36.358 | 0.8 | 0.545 | 0.791 | 1.133 | 0.367 | 3.089 | 0.515 | 51,52,66,69,70,73,76
|
| P61244-5 | 0.998 | 54 | 1.068 | 110.789 | 0.465 | 0.753 | 1.038 | 3.359 | 0.231 | 14.564 | 1.885 | 40,43,44,46,47,53,55,58,59,61,62
|
| P61244-6 | 0.447 | 9 | 0.384 | 37.73 | 0.862 | 0.53 | 0.615 | 0.263 | 0.663 | 0.396 | 2.45 | 44,47,53,56,58
|
Protein Structure and Feature Comparision |
Protein Structure Comparision Using Template Modeling Scores (TM-score). |
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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 |
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 |
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 |
Protein Feature Comparison of the protein sequendary structures among the protiens. |
Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens. |
Protein-Protein Interaction |
Interactors from UniProt. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
Interactors from STRING. |
| Gene name | Interactors |
Related Drugs to MAX |
Drugs targeting this gene/protein. (DrugBank) |
| UniProt accession | Gene name | DrugBank ID | Drug name | Drug group | Actions |
Related Diseases to MAX |
Previous studies relating to the alternative splicing of MAX and disease information from the MeSH term (PubMed) |
| Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
| MAX | 23707073 | EGFR 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. | D005909 | Glioblastoma |
Clinically important variants in MAX |
(ClinVar, 04/20/2024) |
| accession_id | uniprot_id | gene_name | Type | Variant | Clinical_significance |
|
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