P49033 (MYC_HYLLA) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 73.
History...
Clusters with 
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Myc proto-oncogene protein Alternative name(s): Proto-oncogene c-Myc Transcription factor p64 | ||
| Gene names |
| ||
| Organism | Hylobates lar (Common gibbon) | ||
| Taxonomic identifier | 9580 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hylobatidae › Hylobates |
Protein attributes
| Sequence length | 439 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Participates in the regulation of gene transcription. Binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. Seems to activate the transcription of growth-related genes By similarity. |
| Subunit structure | Efficient DNA binding requires dimerization with another bHLH protein. Binds DNA as a heterodimer with MAX. Interacts with TAF1C and SPAG9. Interacts with KDM5A and KDM5B. Interacts (when phosphorylated at Thr-58 and Ser-62) with FBXW7 By similarity. Interacts with PIM2 By similarity. |
| Subcellular location | Nucleus › nucleoplasm By similarity. Nucleus › nucleolus By similarity. |
| Post-translational modification | Phosphorylated by PRKDC. Phosphorylation at Thr-58 and Ser-62 by GSK3 is required for ubiquitination and degradation by the proteasome By similarity. Phosphorylation at Ser-329 by PIM2 leads to the stabilization of MYC. Phosphorylation at Ser-62 by CDK2 prevents Ras-induced senescence By similarity. Ubiquitinated by the SCF(FBXW7) complex when phosphorylated at Thr-58 and Ser-62, leading to its degradation by the proteasome. In the nucleoplasm, ubiquitination is counteracted by USP28, which interacts with of FBXW7 (FBW7alpha), leading to its deubiquitination and preventing degradation. Also polyubiquitinated by the DCX(TRUSS) complex By similarity. |
| Sequence similarities | Contains 1 basic helix-loop-helix (bHLH) domain. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 439 | 439 | Myc proto-oncogene protein | PRO_0000127294 | |||||
Regions | |||||||||
| Domain | 368 – 407 | 40 | Helix-loop-helix motif | ||||||
| Domain | 413 – 434 | 22 | Leucine-zipper | ||||||
| DNA binding | 354 – 367 | 14 | Basic motif | ||||||
| Compositional bias | 33 – 37 | 5 | Poly-Gln | ||||||
| Compositional bias | 88 – 91 | 4 | Poly-Gly | ||||||
Amino acid modifications | |||||||||
| Modified residue | 6 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 58 | 1 | Phosphothreonine; by GSK3; alternate By similarity | ||||||
| Modified residue | 62 | 1 | Phosphoserine; by GSK3 and CDK2 By similarity | ||||||
| Modified residue | 71 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 143 | 1 | N6-acetyllysine; by PCAF By similarity | ||||||
| Modified residue | 148 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 157 | 1 | N6-acetyllysine; by PCAF By similarity | ||||||
| Modified residue | 275 | 1 | N6-acetyllysine; by PCAF By similarity | ||||||
| Modified residue | 317 | 1 | N6-acetyllysine; by PCAF By similarity | ||||||
| Modified residue | 323 | 1 | N6-acetyllysine; by PCAF By similarity | ||||||
| Modified residue | 329 | 1 | Phosphoserine; by PIM2; in vitro By similarity | ||||||
| Modified residue | 344 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 348 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 371 | 1 | N6-acetyllysine; by PCAF By similarity | ||||||
| Glycosylation | 58 | 1 | O-linked (GlcNAc); alternate By similarity | ||||||
Sequences
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References
| [1] | "Gibbon and marmoset c-myc nucleotide sequences." Eladari M.E., Mohammad-Ali K., Argaut C., Galibert F. Gene 116:231-243(1992) [PubMed: 1634119] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M88115 Genomic DNA. Translation: AAA35465.1. |
| PIR | JC1178. |
3D structure databases | |
| ProteinModelPortal | P49033. |
| SMR | P49033. Positions 353-434. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| HOVERGEN | HBG000472. |
Family and domain databases | |
| InterPro | IPR011598. HLH_DNA-bd. IPR003327. Myc-LZ. IPR002418. Tscrpt_reg_Myc. IPR012682. Tscrpt_reg_Myc_N. [Graphical view] |
| Gene3D | G3DSA:4.10.280.10. HLH_DNA_bd. 1 hit. |
| Pfam | PF00010. HLH. 1 hit. PF02344. Myc-LZ. 1 hit. PF01056. Myc_N. 1 hit. [Graphical view] |
| PIRSF | PIRSF001705. Myc_protein. 1 hit. |
| PRINTS | PR00044. LEUZIPPRMYC. |
| SMART | SM00353. HLH. 1 hit. [Graphical view] |
| SUPFAM | SSF47459. HLH_basic. 1 hit. |
| PROSITE | PS50888. HLH. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | MYC_HYLLA | ||||||||
| Accession | Primary (citable) accession number: P49033 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |