P09416 (MYC_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 124.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·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 | Rattus norvegicus (Rat) [Reference proteome] | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus![]() |
Protein attributes
| Sequence length | 439 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
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. |
| 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 PARP10. Interacts with KDM5A and KDM5B. Interacts (when phosphorylated at Thr-58 and Ser-62) with FBXW7 By similarity. Interacts with PIM2 By similarity. Interacts with NO66 By similarity. |
| Subcellular location | Nucleus › nucleoplasm By similarity. Nucleus › nucleolus By similarity. |
| Post-translational modification | Phosphorylated by PRKDC. Phosphorylated at Ser-62 by DYRK2; this primes the protein for subsequent phosphorylation by GSK3B at Thr-58. 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. |
| Involvement in disease | Overexpression of C-Myc is implicated in the etiology of a variety of hematopoietic tumors. |
| Biotechnological use | POU5F1/OCT4, SOX2, MYC/c-Myc and KLF4 are the four Yamanaka factors. When combined, these factors are sufficient to reprogram differentiated cells to an embryonic-like state designated iPS (induced pluripotent stem) cells. iPS cells exhibit the morphology and growth properties of ES cells and express ES cell marker genes. Ref.4 |
| Sequence similarities | Contains 1 bHLH (basic helix-loop-helix) domain. |
| Sequence caution | The sequence AAH91699.2 differs from that shown. Reason: Erroneous initiation. |
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_0000127300 | |||||
Regions | |||||||||
| Domain | 354 – 406 | 53 | bHLH | ||||||
| Region | 413 – 434 | 22 | Leucine-zipper | ||||||
| Compositional bias | 34 – 37 | 4 | Poly-Gln | ||||||
| Compositional bias | 89 – 92 | 4 | Poly-Gly | ||||||
| Compositional bias | 218 – 223 | 6 | Poly-Ser | ||||||
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 DYRK2, GSK3 and CDK2 By similarity | ||||||
| Modified residue | 71 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 144 | 1 | N6-acetyllysine; by PCAF By similarity | ||||||
| Modified residue | 149 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 158 | 1 | N6-acetyllysine; by PCAF By similarity | ||||||
| Modified residue | 162 | 1 | Phosphoserine 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 | 371 | 1 | N6-acetyllysine; by PCAF By similarity | ||||||
| Glycosylation | 58 | 1 | O-linked (GlcNAc); alternate By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Characterization of rat c-myc and adjacent regions." Hayashi K., Makino R., Kawamura H., Arisawa A., Yoneda K. Nucleic Acids Res. 15:6419-6436(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | Shull J.D., Buckles L.K. Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: ACI/SegHsd and Brown Norway/SsNHsd. Tissue: Spleen. |
| [3] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Ovary. |
| [4] | "Direct reprogramming of rat neural precursor cells and fibroblasts into pluripotent stem cells." Chang M.Y., Kim D., Kim C.H., Kang H.C., Yang E., Moon J.I., Ko S., Park J., Park K.S., Lee K.A., Hwang D.Y., Chung Y., Lanza R., Kim K.S. PLoS ONE 5:E9838-E9838(2010) [PubMed] [Europe PMC] [Abstract] Cited for: BIOTECHNOLOGY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | Y00396 Genomic DNA. Translation: CAA68459.2. AY679729 mRNA. Translation: AAT92511.1. AY679730 mRNA. Translation: AAT92512.1. BC091699 mRNA. Translation: AAH91699.2. Different initiation. |
| IPI | IPI00214655. |
| PIR | TVRTMC. A26801. |
| RefSeq | NP_036735.2. NM_012603.2. |
| UniGene | Rn.12072. |
3D structure databases | |
| ProteinModelPortal | P09416. |
| SMR | P09416. Positions 353-434. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-28140N. |
| MINT | MINT-4508782. |
PTM databases | |
| PhosphoSite | P09416. |
Proteomic databases | |
| PaxDb | P09416. |
| PRIDE | P09416. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 24577. |
| KEGG | rno:24577. |
| UCSC | RGD:3130. rat. |
Organism-specific databases | |
| CTD | 4609. |
| RGD | 3130. Myc. |
Phylogenomic databases | |
| eggNOG | NOG42590. |
| HOGENOM | HOG000043075. |
| HOVERGEN | HBG000472. |
| InParanoid | P09416. |
| KO | K04377. |
| OrthoDB | EOG42RD7N. |
Gene expression databases | |
| ArrayExpress | P09416. |
| Genevestigator | P09416. |
| GermOnline | ENSRNOG00000004500. Rattus norvegicus. |
Family and domain databases | |
| Gene3D | 4.10.280.10. 1 hit. |
| InterPro | IPR011598. bHLH_dom. IPR003327. Myc-LZ. IPR002418. Tscrpt_reg_Myc. IPR012682. Tscrpt_reg_Myc_N. [Graphical view] |
| 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. BHLH. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 603730. |
Entry information
| Entry name | MYC_RAT | ||||||||
| Accession | Primary (citable) accession number: P09416 Secondary accession number(s): Q6B500 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
