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Protein

Myc proto-oncogene protein

Gene

Myc

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  • DNA binding Source: RGD
  • double-stranded DNA binding Source: RGD
  • E-box binding Source: UniProtKB
  • protein complex binding Source: UniProtKB
  • protein heterodimerization activity Source: RGD
  • sequence-specific DNA binding Source: RGD
  • transcription factor activity, sequence-specific DNA binding Source: RGD
  • transcription factor binding Source: RGD

GO - Biological processi

  • amino acid transport Source: RGD
  • branching involved in ureteric bud morphogenesis Source: UniProtKB
  • canonical Wnt signaling pathway Source: UniProtKB
  • canonical Wnt signaling pathway involved in positive regulation of wound healing Source: RGD
  • cell proliferation Source: RGD
  • cellular iron ion homeostasis Source: UniProtKB
  • cellular response to angiotensin Source: RGD
  • cellular response to arsenite(3-) Source: RGD
  • cellular response to carbohydrate stimulus Source: RGD
  • cellular response to cycloheximide Source: RGD
  • cellular response to dimethyl sulfoxide Source: RGD
  • cellular response to DNA damage stimulus Source: UniProtKB
  • cellular response to drug Source: RGD
  • cellular response to endothelin Source: RGD
  • cellular response to epidermal growth factor stimulus Source: RGD
  • cellular response to estrogen stimulus Source: RGD
  • cellular response to fibroblast growth factor stimulus Source: RGD
  • cellular response to growth hormone stimulus Source: RGD
  • cellular response to hydrostatic pressure Source: RGD
  • cellular response to insulin stimulus Source: RGD
  • cellular response to interferon-gamma Source: RGD
  • cellular response to interleukin-1 Source: RGD
  • cellular response to lectin Source: RGD
  • cellular response to organic cyclic compound Source: RGD
  • cellular response to phorbol 13-acetate 12-myristate Source: RGD
  • cellular response to platelet-derived growth factor stimulus Source: RGD
  • cellular response to prolactin Source: RGD
  • cellular response to putrescine Source: RGD
  • cellular response to retinoic acid Source: RGD
  • cellular response to testosterone stimulus Source: RGD
  • chromatin remodeling Source: UniProtKB
  • chromosome organization Source: UniProtKB
  • DNA-templated transcription, initiation Source: RGD
  • flavonoid metabolic process Source: RGD
  • fungal-type cell wall polysaccharide metabolic process Source: RGD
  • G0 to G1 transition Source: RGD
  • glucose metabolic process Source: RGD
  • hypothalamus development Source: RGD
  • inner mitochondrial membrane organization Source: RGD
  • in utero embryonic development Source: RGD
  • lactic acid secretion Source: RGD
  • liver regeneration Source: RGD
  • MAPK cascade Source: UniProtKB
  • negative regulation of cell death Source: RGD
  • negative regulation of cell division Source: UniProtKB
  • negative regulation of gene expression Source: RGD
  • negative regulation of glucose import Source: RGD
  • negative regulation of monocyte differentiation Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • ovarian follicle development Source: RGD
  • ovulation Source: RGD
  • pathogenesis Source: RGD
  • positive regulation of ATP biosynthetic process Source: RGD
  • positive regulation of cell cycle Source: RGD
  • positive regulation of cell proliferation Source: RGD
  • positive regulation of cellular respiration Source: RGD
  • positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • positive regulation of DNA binding Source: RGD
  • positive regulation of DNA biosynthetic process Source: UniProtKB
  • positive regulation of epithelial cell proliferation Source: UniProtKB
  • positive regulation of fibroblast proliferation Source: UniProtKB
  • positive regulation of glial cell proliferation Source: RGD
  • positive regulation of glycolytic process Source: RGD
  • positive regulation of mesenchymal cell proliferation Source: UniProtKB
  • positive regulation of metanephric cap mesenchymal cell proliferation Source: UniProtKB
  • positive regulation of mitochondrial membrane potential Source: RGD
  • positive regulation of oxidative phosphorylation Source: RGD
  • positive regulation of response to DNA damage stimulus Source: UniProtKB
  • positive regulation of smooth muscle cell migration Source: RGD
  • positive regulation of smooth muscle cell proliferation Source: RGD
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: RGD
  • pyruvate transport Source: RGD
  • re-entry into mitotic cell cycle Source: RGD
  • regulation of mitotic cell cycle Source: RGD
  • regulation of oxidative phosphorylation Source: RGD
  • regulation of telomere maintenance Source: UniProtKB
  • regulation of transcription, DNA-templated Source: RGD
  • response to estradiol Source: RGD
  • response to ethanol Source: RGD
  • response to gamma radiation Source: UniProtKB
  • response to human chorionic gonadotropin Source: RGD
  • response to wounding Source: RGD
  • transcription, DNA-templated Source: RGD
  • transcription from RNA polymerase II promoter Source: RGD
  • transformation of host cell by virus Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-RNO-8866911. TFAP2 (AP-2) family regulates transcription of cell cycle factors.

Names & Taxonomyi

Protein namesi
Recommended name:
Myc proto-oncogene protein
Alternative name(s):
Proto-oncogene c-Myc
Transcription factor p64
Gene namesi
Name:Myc
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 7

Organism-specific databases

RGDi3130. Myc.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: RGD
  • mitochondrion Source: GOC
  • nucleolus Source: UniProtKB
  • nucleoplasm Source: UniProtKB
  • nucleus Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Biotechnological usei

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.1 Publication

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001273001 – 439Myc proto-oncogene proteinAdd BLAST439

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei6PhosphoserineBy similarity1
Modified residuei58Phosphothreonine; by GSK3; alternateBy similarity1
Glycosylationi58O-linked (GlcNAc); alternateBy similarity1
Modified residuei62Phosphoserine; by DYRK2, GSK3 and CDK2By similarity1
Modified residuei71PhosphoserineBy similarity1
Modified residuei144N6-acetyllysine; by PCAFBy similarity1
Modified residuei149N6-acetyllysineBy similarity1
Modified residuei158N6-acetyllysine; by PCAFBy similarity1
Modified residuei162PhosphoserineBy similarity1
Modified residuei275N6-acetyllysine; by PCAFBy similarity1
Modified residuei293PhosphoserineBy similarity1
Modified residuei317N6-acetyllysine; by PCAFBy similarity1
Modified residuei323N6-acetyllysine; by PCAFBy similarity1
Modified residuei329Phosphoserine; by PIM2; in vitroBy similarity1
Modified residuei371N6-acetyllysine; by PCAFBy similarity1

Post-translational modificationi

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).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. Ubiquitinated by TRIM6 in a phosphorylation-independent manner.By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP09416.
PRIDEiP09416.

PTM databases

iPTMnetiP09416.
PhosphoSitePlusiP09416.

Expressioni

Gene expression databases

BgeeiENSRNOG00000004500.
ExpressionAtlasiP09416. baseline and differential.

Interactioni

Subunit structurei

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. Interacts with TRIM6 (By similarity).By similarity1 Publication

GO - Molecular functioni

  • protein complex binding Source: UniProtKB
  • protein heterodimerization activity Source: RGD
  • transcription factor binding Source: RGD

Protein-protein interaction databases

BioGridi246723. 3 interactors.
DIPiDIP-28140N.
IntActiP09416. 3 interactors.
MINTiMINT-4508782.
STRINGi10116.ENSRNOP00000006188.

Structurei

3D structure databases

ProteinModelPortaliP09416.
SMRiP09416.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini354 – 406bHLHPROSITE-ProRule annotationAdd BLAST53

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni413 – 434Leucine-zipperAdd BLAST22

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi34 – 37Poly-Gln4
Compositional biasi89 – 92Poly-Gly4
Compositional biasi218 – 223Poly-Ser6

Sequence similaritiesi

Contains 1 bHLH (basic helix-loop-helix) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IFSM. Eukaryota.
ENOG41124Q3. LUCA.
GeneTreeiENSGT00510000046414.
HOGENOMiHOG000043075.
HOVERGENiHBG000472.
InParanoidiP09416.
KOiK04377.
PhylomeDBiP09416.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
IPR003327. Myc-LZ.
IPR002418. Tscrpt_reg_Myc.
IPR012682. Tscrpt_reg_Myc_N.
[Graphical view]
PfamiPF00010. HLH. 1 hit.
PF02344. Myc-LZ. 1 hit.
PF01056. Myc_N. 1 hit.
[Graphical view]
PIRSFiPIRSF001705. Myc_protein. 1 hit.
PRINTSiPR00044. LEUZIPPRMYC.
SMARTiSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P09416-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPLNVSFANR NYDLDYDSVQ PYFICDEEEN FYHQQQQSEL QPPAPSEDIW
60 70 80 90 100
KKFELLPTPP LSPSRRSGLC SPSYVAVATS FSPREDDDGG GGNFSTADQL
110 120 130 140 150
EMMTELLGGD MVNQSFICDP DDETFIKNII IQDCMWSGFS AAAKLVSEKL
160 170 180 190 200
ASYQAARKDS TSLSPARGHS VCSTSSLYLQ DLTAAASECI DPSVVFPYPL
210 220 230 240 250
NDSSSPKSCT SSDSTAFSSS SDSLLSSESS PRATPEPLVL HEETPPTTSS
260 270 280 290 300
DSEEEQDDEE EIDVVSVEKR QPPAKRSESG SSPSRGHSKP PHSPLVLKRC
310 320 330 340 350
HVSTHQHNYA APPSTRKDYP AAKRAKLDSG RVLKQISNNR KCSSPRSSDT
360 370 380 390 400
EENDKRRTHN VLERQRRNEL KRSFFALRDQ IPELENNEKA PKVVILKKAT
410 420 430
AYILSVQADE HKLISEKDLL RKRREQLKHK LEQLRNSGA
Length:439
Mass (Da):48,898
Last modified:July 1, 1989 - v1
Checksum:i7547DCCECF74554F
GO

Sequence cautioni

The sequence AAH91699 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00396 Genomic DNA. Translation: CAA68459.2.
AY679729 mRNA. Translation: AAT92511.1.
AY679730 mRNA. Translation: AAT92512.1.
BC091699 mRNA. Translation: AAH91699.2. Different initiation.
PIRiA26801. TVRTMC.
RefSeqiNP_036735.2. NM_012603.2.
UniGeneiRn.12072.

Genome annotation databases

EnsembliENSRNOT00000006188; ENSRNOP00000006188; ENSRNOG00000004500.
GeneIDi24577.
KEGGirno:24577.
UCSCiRGD:3130. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00396 Genomic DNA. Translation: CAA68459.2.
AY679729 mRNA. Translation: AAT92511.1.
AY679730 mRNA. Translation: AAT92512.1.
BC091699 mRNA. Translation: AAH91699.2. Different initiation.
PIRiA26801. TVRTMC.
RefSeqiNP_036735.2. NM_012603.2.
UniGeneiRn.12072.

3D structure databases

ProteinModelPortaliP09416.
SMRiP09416.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246723. 3 interactors.
DIPiDIP-28140N.
IntActiP09416. 3 interactors.
MINTiMINT-4508782.
STRINGi10116.ENSRNOP00000006188.

PTM databases

iPTMnetiP09416.
PhosphoSitePlusiP09416.

Proteomic databases

PaxDbiP09416.
PRIDEiP09416.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000006188; ENSRNOP00000006188; ENSRNOG00000004500.
GeneIDi24577.
KEGGirno:24577.
UCSCiRGD:3130. rat.

Organism-specific databases

CTDi4609.
RGDi3130. Myc.

Phylogenomic databases

eggNOGiENOG410IFSM. Eukaryota.
ENOG41124Q3. LUCA.
GeneTreeiENSGT00510000046414.
HOGENOMiHOG000043075.
HOVERGENiHBG000472.
InParanoidiP09416.
KOiK04377.
PhylomeDBiP09416.

Enzyme and pathway databases

ReactomeiR-RNO-8866911. TFAP2 (AP-2) family regulates transcription of cell cycle factors.

Miscellaneous databases

PROiP09416.

Gene expression databases

BgeeiENSRNOG00000004500.
ExpressionAtlasiP09416. baseline and differential.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
IPR003327. Myc-LZ.
IPR002418. Tscrpt_reg_Myc.
IPR012682. Tscrpt_reg_Myc_N.
[Graphical view]
PfamiPF00010. HLH. 1 hit.
PF02344. Myc-LZ. 1 hit.
PF01056. Myc_N. 1 hit.
[Graphical view]
PIRSFiPIRSF001705. Myc_protein. 1 hit.
PRINTSiPR00044. LEUZIPPRMYC.
SMARTiSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMYC_RAT
AccessioniPrimary (citable) accession number: P09416
Secondary accession number(s): Q6B500
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: November 30, 2016
This is version 151 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.