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Protein

Myc proto-oncogene protein

Gene

MYC

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
Status
Reviewed-Annotation score: -Experimental evidence at transcript 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. Binds to the VEGFA promoter, promoting VEGFA production and subsequent sprouting angiogenesis.By similarity

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionActivator, DNA-binding
Biological processTranscription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Myc proto-oncogene protein
Alternative name(s):
Proto-oncogene c-Myc
Transcription factor p64
Gene namesi
Name:MYC
OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
Proteomesi
  • UP000002254 Componenti: Unplaced

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001272901 – 439Myc proto-oncogene proteinAdd BLAST439

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei6PhosphoserineBy similarity1
Cross-linki52Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei58Phosphothreonine; by GSK3; alternateBy similarity1
Glycosylationi58O-linked (GlcNAc) threonine; alternateBy similarity1
Modified residuei62Phosphoserine; by DYRK2, GSK3 and CDK2By similarity1
Modified residuei71PhosphoserineBy similarity1
Modified residuei143N6-acetyllysine; by PCAF; alternateBy similarity1
Cross-linki143Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei148N6-acetyllysine; alternateBy similarity1
Cross-linki148Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei157N6-acetyllysine; by PCAFBy similarity1
Modified residuei161PhosphoserineBy similarity1
Modified residuei275N6-acetyllysine; by PCAFBy similarity1
Modified residuei293PhosphoserineBy similarity1
Cross-linki298Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
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. Ubiquitination is counteracted by USP28 in the nucleoplasm and USP36 in the nucleolus, both interacting with of FBXW7, 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, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ28350
PRIDEiQ28350

Interactioni

Subunit structurei

Efficient DNA binding requires dimerization with another bHLH protein. Binds DNA as a heterodimer with MAX (By similarity). 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 RIOX1. The heterodimer MYC:MAX interacts with ABI1; the interaction may enhance MYC:MAX transcriptional activity. Interacts with TRIM6 (By similarity). Interacts with NPM1; the binary complex is recruited to the promoter of MYC target genes and enhances their transcription (By similarity). Interacts with CIP2A; leading to the stabilization of MYC (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000001523

Structurei

3D structure databases

ProteinModelPortaliQ28350
SMRiQ28350
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 biasi33 – 37Poly-Gln5
Compositional biasi88 – 91Poly-Gly4

Phylogenomic databases

eggNOGiENOG410IFSM Eukaryota
ENOG41124Q3 LUCA
HOGENOMiHOG000043075
HOVERGENiHBG000472
InParanoidiQ28350
KOiK04377

Family and domain databases

CDDicd00083 HLH, 1 hit
Gene3Di4.10.280.10, 1 hit
InterProiView protein in InterPro
IPR011598 bHLH_dom
IPR036638 HLH_DNA-bd_sf
IPR003327 Myc-LZ
IPR002418 Tscrpt_reg_Myc
IPR012682 Tscrpt_reg_Myc_N
PfamiView protein in Pfam
PF00010 HLH, 1 hit
PF02344 Myc-LZ, 1 hit
PF01056 Myc_N, 1 hit
PIRSFiPIRSF001705 Myc_protein, 1 hit
PRINTSiPR00044 LEUZIPPRMYC
SMARTiView protein in SMART
SM00353 HLH, 1 hit
SUPFAMiSSF47459 SSF47459, 1 hit
PROSITEiView protein in PROSITE
PS50888 BHLH, 1 hit

Sequencei

Sequence statusi: Complete.

Q28350-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPLNVSFANR NYDLDYDSVQ PYFYCDEEEN FYQQQQQSEL QPPAPSEDIW
60 70 80 90 100
KKFELLPTPP LSPSRRSGLC SPSYVAVASF SPRGDDDGGG GSFSTADQLE
110 120 130 140 150
MVTELLGGDM VNQSFICDPD DETFIKNIII QDCMWSGFSA AAKLVSEKLA
160 170 180 190 200
SYQAARKDSG SPSPARGPGG CSTSSLYLQD LSAAASECID PSVVFPYPLN
210 220 230 240 250
DSSSPKPCAS PDSAAFSPSS DSLLSSAESS PRASPEPLAL HEETPPTTSS
260 270 280 290 300
DSEEEQEDEE EIDVVSVEKR QAPAKRSESG SPSAGGHSKP PHSPLVLKRC
310 320 330 340 350
HVSTHQHNYA APPSTRKDYP AAKRARLDSG RVLKQISNNR KCASPRSSDT
360 370 380 390 400
EENDKRRTHN VLERQRRNEL KRSFFALRDQ IPELENNEKA PKVVILKKAT
410 420 430
AYILSVQAEE QKLLSEKDLL RKRREQLKHK LEQLRNSGA
Length:439
Mass (Da):48,410
Last modified:November 1, 1996 - v1
Checksum:i9A1D9F31C66C7C8B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95367 mRNA Translation: CAA64654.1
RefSeqiNP_001003246.2, NM_001003246.2
UniGeneiCfa.3786

Genome annotation databases

GeneIDi403924
KEGGicfa:403924

Similar proteinsi

Entry informationi

Entry nameiMYC_CANLF
AccessioniPrimary (citable) accession number: Q28350
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: May 23, 2018
This is version 129 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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