Myc
entrez
17869
canonical
uniprot
P01108
canonical
ensembl
ENSMUSG00000022346
resolver
ensp
ENSMUSP00000022971
resolver
ensp
ENSMUSP00000123821
resolver
ensp
ENSMUSP00000124758
resolver
ensp
ENSMUSP00000130285
resolver
genesymbol
Myc
resolver
uniprot
A0A087WSQ0
resolver
uniprot
B2RSN1
resolver
uniprot
F6PX41
resolver
uniprot
F8WID3
resolver
uniprot
P70247
resolver
uniprot
Q3UM70
resolver
uniprot
Q61422
resolver
uniprot_entry
MYC_MOUSE
resolver
uniprot_sec
A0A087WSQ0
resolver
uniprot_sec
B2RSN1
resolver
uniprot_sec
F6PX41
resolver
uniprot_sec
F8WID3
resolver
uniprot_sec
P70247
resolver
uniprot_sec
Q3UM70
resolver
uniprot_sec
Q61422
resolver
amino_acid_sequence
MDFLWALETPQTATTMPLNVNFTNRNYDLDYDSVQPYFICDEEENFYHQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVATSFSPREDDDGGGGNFSTADQLEMMTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSTSLSPARGHSVCSTSSLYLQDLTAAASECIDPSVVFPYPLNDSSSPKSCTSSDSTAFSPSSDSLLSSESSPRASPEPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQTPAKRSESGSSPSRGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRAKLDSGRVLKQISNNRKCSSPRSSDTEENDKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSIQADEHKLTSEKDLLRKRREQLKHKLEQLRNSGA
uniprot
proteins
function
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. Binds to the VEGFA promoter, promoting VEGFA production and subsequent sprouting angiogenesis. Regulator of somatic reprogramming, controls self-renewal of embryonic stem cells. Functions with TAF6L to activate target gene expression through RNA polymerase II pause release (PubMed:31005419). Positively regulates transcription of HNRNPA1, HNRNPA2 and PTBP1 which in turn regulate splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform (By similarity). {ECO:0000250|UniProtKB:P01106, ECO:0000269|PubMed:31005419}.
uniprot
proteins
mass_dalton
50678
uniprot
proteins
mutagenesis
MUTAGEN 73; /note="T->A: Does not affect interaction with TRIM6."; /evidence="ECO:0000269|PubMed:22328504"; MUTAGEN 77; /note="S->A: Does not affect interaction with TRIM6."; /evidence="ECO:0000269|PubMed:22328504"; MUTAGEN 344; /note="S->A: Reduces phosphorylation by PIM2 by 60%, and decreases the transcriptional activity of MYC."; /evidence="ECO:0000269|PubMed:18438430
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by PRKDC (By similarity). Phosphorylation at Ser-344 by PIM2 leads to the stabilization of MYC (PubMed:18438430). Phosphorylation at Ser-77 by CDK2 prevents Ras-induced senescence. Phosphorylated at Ser-77 by DYRK2; this primes the protein for subsequent phosphorylation by GSK3B at Thr-73. Phosphorylation at Thr-73 and Ser-77 by GSK3 is required for ubiquitination and degradation by the proteasome. Dephosphorylation at multiple sites by the PNUTS-PP1 complex promotes MYC stability by preventing ubiquitination by the SCF(FBXW7) complex. Dephosphorylation at Ser-77 by protein phosphatase 2A (PPP2CA) promotes its degradation; interaction with PPP2CA is enhanced by AMBRA1 (By similarity). {ECO:0000250|UniProtKB:P01106, ECO:0000269|PubMed:18438430}.; PTM: Ubiquitinated by the SCF(FBXW7) complex when phosphorylated at Thr-73 and Ser-77, 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(TRPC4AP) complex (By similarity). Ubiquitinated by UBR5 when not forming a heterodimer with another bHLH protein, leading to its degradation: UBR5 recognizes and binds a degron that is only available upon heterodimer dissociation (By similarity). Ubiquitinated by TRIM6 in a phosphorylation-independent manner (PubMed:22328504). {ECO:0000250|UniProtKB:P01106, ECO:0000269|PubMed:22328504}.
uniprot
proteins
pubmed
12391307
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
1628829
uniprot
proteins
pubmed
16904174
uniprot
proteins
pubmed
18438430
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
22328504
uniprot
proteins
pubmed
22510880
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
31005419
uniprot
proteins
pubmed
3277717
uniprot
proteins
pubmed
6321164
uniprot
proteins
pubmed
6412145
uniprot
proteins
pubmed
6462227
uniprot
proteins
pubmed
8521822
uniprot
proteins
pubmed
8617250
uniprot
proteins
sequence_length
454
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P01106}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P01106}. Nucleus {ECO:0000250|UniProtKB:P01106}. Cytoplasm {ECO:0000250|UniProtKB:P01106}. Chromosome {ECO:0000250|UniProtKB:P01106}. Note=Association with chromatin is reduced by hyperphosphorylation. Localization to the nucleolus is dependent on HEATR1. {ECO:0000250|UniProtKB:P01106}.
uniprot
proteins