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P09416 (MYC_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Myc proto-oncogene protein
Alternative name(s):
Proto-oncogene c-Myc
Transcription factor p64
Gene names
Name:Myc
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length439 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. Activates the transcription of growth-related genes. Ref.5

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. Interacts with PIM2. Interacts with NO66. The heterodimer MYC:MAX interacts with ABI1; the interaction may enhance MYC:MAX transcriptional activity. Ref.5

Subcellular location

Nucleusnucleoplasm By similarity. Nucleusnucleolus 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. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   DiseaseProto-oncogene
   LigandDNA-binding
   Molecular functionActivator
   PTMAcetylation
Glycoprotein
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

DNA-templated transcription, initiation

Inferred from direct assay Ref.1. Source: RGD

G0 to G1 transition

Inferred from expression pattern PubMed 23119170. Source: RGD

MAPK cascade

Inferred from sequence or structural similarity. Source: UniProtKB

activation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from electronic annotation. Source: Ensembl

amino acid transport

Inferred from mutant phenotype PubMed 22842522. Source: RGD

branching involved in ureteric bud morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

canonical Wnt signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

canonical Wnt signaling pathway involved in negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

canonical Wnt signaling pathway involved in positive regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

canonical Wnt signaling pathway involved in positive regulation of wound healing

Inferred from mutant phenotype PubMed 21975427. Source: RGD

cell proliferation

Inferred from mutant phenotype PubMed 20639453. Source: RGD

cellular iron ion homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to DNA damage stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to carbohydrate stimulus

Inferred from expression pattern PubMed 20694826. Source: RGD

cellular response to drug

Inferred from electronic annotation. Source: Ensembl

cellular response to estrogen stimulus

Inferred from expression pattern PubMed 21980073. Source: RGD

cellular response to hydrostatic pressure

Inferred from expression pattern PubMed 22644739. Source: RGD

cellular response to interleukin-1

Inferred from expression pattern PubMed 22706317. Source: RGD

cellular response to organic cyclic compound

Inferred from expression pattern PubMed 21980073. Source: RGD

chromatin remodeling

Inferred from sequence or structural similarity. Source: UniProtKB

chromosome organization

Inferred from sequence or structural similarity. Source: UniProtKB

detection of mechanical stimulus involved in sensory perception of sound

Inferred from electronic annotation. Source: Ensembl

flavonoid metabolic process

Inferred from expression pattern PubMed 22528217PubMed 22819302. Source: RGD

fungal-type cell wall polysaccharide metabolic process

Inferred from expression pattern PubMed 22060291. Source: RGD

glucose metabolic process

Inferred from mutant phenotype PubMed 12480946. Source: RGD

glycoprotein metabolic process

Inferred from expression pattern PubMed 22445893PubMed 22639698. Source: RGD

hypothalamus development

Inferred from expression pattern PubMed 23291449. Source: RGD

inner mitochondrial membrane organization

Inferred from mutant phenotype PubMed 22629444. Source: RGD

intrinsic apoptotic signaling pathway in response to DNA damage

Inferred from electronic annotation. Source: Ensembl

lactic acid secretion

Inferred from mutant phenotype PubMed 22842522. Source: RGD

middle ear morphogenesis

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell death

Inferred from mutant phenotype PubMed 22100782. Source: RGD

negative regulation of cell division

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of gene expression

Inferred from mutant phenotype PubMed 23349663. Source: RGD

negative regulation of glucose import

Inferred from mutant phenotype PubMed 22842522. Source: RGD

negative regulation of monocyte differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of protein binding

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 9924025. Source: UniProtKB

pathogenesis

Traceable author statement PubMed 11687580. Source: RGD

pigmentation

Inferred from electronic annotation. Source: Ensembl

positive regulation of ATP biosynthetic process

Inferred from mutant phenotype PubMed 22629444. Source: RGD

positive regulation of B cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of DNA biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell cycle

Inferred from mutant phenotype PubMed 22210745. Source: RGD

positive regulation of cell proliferation

Inferred from genetic interaction PubMed 21980073. Source: RGD

positive regulation of cellular respiration

Inferred from mutant phenotype PubMed 22842522. Source: RGD

positive regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of epithelial cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of fibroblast proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of glycolytic process

Inferred from mutant phenotype PubMed 22842522. Source: RGD

positive regulation of mesenchymal cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of metanephric cap mesenchymal cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of mitochondrial membrane potential

Inferred from mutant phenotype PubMed 22629444. Source: RGD

positive regulation of response to DNA damage stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 12480946. Source: RGD

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 18818310. Source: UniProtKB

pyruvate transport

Inferred from mutant phenotype PubMed 22842522. Source: RGD

regulation of mitotic cell cycle

Inferred from mutant phenotype PubMed 12070150. Source: RGD

regulation of oxidative phosphorylation

Inferred from mutant phenotype PubMed 22629444. Source: RGD

regulation of telomere maintenance

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from direct assay PubMed 11799123. Source: RGD

response to alkaloid

Inferred from electronic annotation. Source: Ensembl

response to estradiol

Inferred from expression pattern PubMed 23027806. Source: RGD

response to gamma radiation

Inferred from sequence or structural similarity. Source: UniProtKB

response to wounding

Inferred from expression pattern PubMed 20694826. Source: RGD

skeletal muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

skeletal system morphogenesis

Inferred from electronic annotation. Source: Ensembl

transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 15139290. Source: RGD

transcription, DNA-templated

Inferred from direct assay PubMed 15139290. Source: RGD

transformation of host cell by virus

Inferred from mutant phenotype PubMed 16256070. Source: RGD

   Cellular_componentaxon

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 9130602. Source: RGD

mitochondrion

Inferred from mutant phenotype PubMed 22629444. Source: GOC

nuclear body

Inferred from electronic annotation. Source: Ensembl

nucleolus

Inferred from sequence or structural similarity. Source: UniProtKB

nucleoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 16150871PubMed 9130602. Source: RGD

spindle

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionDNA binding

Inferred from direct assay PubMed 11799123. Source: RGD

E-box binding

Inferred from sequence or structural similarity. Source: UniProtKB

core promoter proximal region sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

double-stranded DNA binding

Inferred from direct assay PubMed 15139290. Source: RGD

protein complex binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein heterodimerization activity

Inferred from physical interaction PubMed 17341548. Source: RGD

sequence-specific DNA binding

Inferred from direct assay PubMed 15139290PubMed 17341548. Source: RGD

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 15139290. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 439439Myc proto-oncogene protein
PRO_0000127300

Regions

Domain354 – 40653bHLH
Region413 – 43422Leucine-zipper
Compositional bias34 – 374Poly-Gln
Compositional bias89 – 924Poly-Gly
Compositional bias218 – 2236Poly-Ser

Amino acid modifications

Modified residue61Phosphoserine By similarity
Modified residue581Phosphothreonine; by GSK3; alternate By similarity
Modified residue621Phosphoserine; by DYRK2, GSK3 and CDK2 By similarity
Modified residue711Phosphoserine By similarity
Modified residue1441N6-acetyllysine; by PCAF By similarity
Modified residue1491N6-acetyllysine By similarity
Modified residue1581N6-acetyllysine; by PCAF By similarity
Modified residue1621Phosphoserine By similarity
Modified residue2751N6-acetyllysine; by PCAF By similarity
Modified residue3171N6-acetyllysine; by PCAF By similarity
Modified residue3231N6-acetyllysine; by PCAF By similarity
Modified residue3291Phosphoserine; by PIM2; in vitro By similarity
Modified residue3711N6-acetyllysine; by PCAF By similarity
Glycosylation581O-linked (GlcNAc); alternate By similarity

Sequences

Sequence LengthMass (Da)Tools
P09416 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 7547DCCECF74554F

FASTA43948,898
        10         20         30         40         50         60 
MPLNVSFANR NYDLDYDSVQ PYFICDEEEN FYHQQQQSEL QPPAPSEDIW KKFELLPTPP 

        70         80         90        100        110        120 
LSPSRRSGLC SPSYVAVATS FSPREDDDGG GGNFSTADQL EMMTELLGGD MVNQSFICDP 

       130        140        150        160        170        180 
DDETFIKNII IQDCMWSGFS AAAKLVSEKL ASYQAARKDS TSLSPARGHS VCSTSSLYLQ 

       190        200        210        220        230        240 
DLTAAASECI DPSVVFPYPL NDSSSPKSCT SSDSTAFSSS SDSLLSSESS PRATPEPLVL 

       250        260        270        280        290        300 
HEETPPTTSS DSEEEQDDEE EIDVVSVEKR QPPAKRSESG SSPSRGHSKP PHSPLVLKRC 

       310        320        330        340        350        360 
HVSTHQHNYA APPSTRKDYP AAKRAKLDSG RVLKQISNNR KCSSPRSSDT EENDKRRTHN 

       370        380        390        400        410        420 
VLERQRRNEL KRSFFALRDQ IPELENNEKA PKVVILKKAT AYILSVQADE HKLISEKDLL 

       430 
RKRREQLKHK LEQLRNSGA 

« Hide

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.
[5]"Abelson interacting protein 1 (Abi-1) is essential for dendrite morphogenesis and synapse formation."
Proepper C., Johannsen S., Liebau S., Dahl J., Vaida B., Bockmann J., Kreutz M.R., Gundelfinger E.D., Boeckers T.M.
EMBO J. 26:1397-1409(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TRANSCRIPTIONAL ACTIVATION, INTERACTION WITH ABI1.
+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.
PIRTVRTMC. A26801.
RefSeqNP_036735.2. NM_012603.2.
UniGeneRn.12072.

3D structure databases

ProteinModelPortalP09416.
SMRP09416. Positions 353-434.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid246723. 3 interactions.
DIPDIP-28140N.
IntActP09416. 2 interactions.
MINTMINT-4508782.

PTM databases

PhosphoSiteP09416.

Proteomic databases

PaxDbP09416.
PRIDEP09416.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID24577.
KEGGrno:24577.
UCSCRGD:3130. rat.

Organism-specific databases

CTD4609.
RGD3130. Myc.

Phylogenomic databases

eggNOGNOG42590.
HOGENOMHOG000043075.
HOVERGENHBG000472.
InParanoidP09416.
KOK04377.
PhylomeDBP09416.

Gene expression databases

ArrayExpressP09416.
GenevestigatorP09416.

Family and domain databases

Gene3D4.10.280.10. 1 hit.
InterProIPR011598. bHLH_dom.
IPR003327. Myc-LZ.
IPR002418. Tscrpt_reg_Myc.
IPR012682. Tscrpt_reg_Myc_N.
[Graphical view]
PfamPF00010. HLH. 1 hit.
PF02344. Myc-LZ. 1 hit.
PF01056. Myc_N. 1 hit.
[Graphical view]
PIRSFPIRSF001705. Myc_protein. 1 hit.
PRINTSPR00044. LEUZIPPRMYC.
SMARTSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMSSF47459. SSF47459. 1 hit.
PROSITEPS50888. BHLH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio603730.
PROP09416.

Entry information

Entry nameMYC_RAT
AccessionPrimary (citable) accession number: P09416
Secondary accession number(s): Q6B500
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: July 9, 2014
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families