MYC
entrez
4609
canonical
uniprot
P01106
canonical
ensembl
ENSG00000136997
resolver
ensp
ENSP00000430235
resolver
ensp
ENSP00000478887
resolver
genesymbol
MYC
resolver
genesymbol_syn
BHLHE39
resolver
hgnc
HGNC:7553
resolver
uniprot
A0A024R9L7
resolver
uniprot
A0A087WUS5
resolver
uniprot
A8WFE7
resolver
uniprot
H0YBT0
resolver
uniprot
P01107
resolver
uniprot
Q14026
resolver
uniprot_entry
MYC_HUMAN
resolver
uniprot_sec
A0A024R9L7
resolver
uniprot_sec
A0A087WUS5
resolver
uniprot_sec
A8WFE7
resolver
uniprot_sec
H0YBT0
resolver
uniprot_sec
P01107
resolver
uniprot_sec
Q14026
resolver
amino_acid_sequence
MDFFRVVENQQPPATMPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSGSPNPARGHSVCSTSSLYLQDLSAAASECIDPSVVFPYPLNDSSSPKSCASQDSSAFSPSSDSLLSSTESSPQGSPEPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQAPGKRSESGSPSAGGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRVKLDSVRVLRQISNNRKCTSPRSSDTEENVKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSVQAEEQKLISEEDLLRKRREQLKHKLEQLRNSCA
uniprot
proteins
disease_involvement
DISEASE: Note=A chromosomal aberration involving MYC may be a cause of a form of B-cell chronic lymphocytic leukemia. Translocation t(8;12)(q24;q22) with BTG1. {ECO:0000269|PubMed:2069907}.; DISEASE: Burkitt lymphoma (BL) [MIM:113970]: A form of undifferentiated malignant lymphoma commonly manifested as a large osteolytic lesion in the jaw or as an abdominal mass. {ECO:0000269|PubMed:2166998, ECO:0000269|PubMed:8220424}. Note=The gene represented in this entry is involved in disease pathogenesis. Chromosomal aberrations involving MYC are usually found in Burkitt lymphoma. Translocations t(8;14), t(8;22) or t(2;8) which juxtapose MYC to one of the heavy or light chain immunoglobulin gene loci.
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' (PubMed:24940000, PubMed:25956029). Activates the transcription of growth-related genes (PubMed:24940000, PubMed:25956029). Binds to the VEGFA promoter, promoting VEGFA production and subsequent sprouting angiogenesis (PubMed:24940000, PubMed:25956029). Regulator of somatic reprogramming, controls self-renewal of embryonic stem cells (By similarity). Functions with TAF6L to activate target gene expression through RNA polymerase II pause release (By similarity). 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 (PubMed:20010808). {ECO:0000250|UniProtKB:P01108, ECO:0000269|PubMed:20010808, ECO:0000269|PubMed:24940000, ECO:0000269|PubMed:25956029}.
uniprot
proteins
mass_dalton
50565
uniprot
proteins
mutagenesis
MUTAGEN 73; /note="T->A: Impairs interaction with FBXW7 and subsequent degradation by the proteasome. Normal inhibition of Ras-induced senescence."; /evidence="ECO:0000269|PubMed:15103331, ECO:0000269|PubMed:17558397, ECO:0000269|PubMed:19966300, ECO:0000269|PubMed:20713526"; MUTAGEN 77; /note="S->A: Impairs interaction with FBXW7 and subsequent degradation by the proteasome. Impaired inhibition of Ras-induced senescence. Abolishes phosphorylation by DYRK2, and subsequent phosphorylation by GSK3B at Thr-73."; /evidence="ECO:0000269|PubMed:15103331, ECO:0000269|PubMed:17558397, ECO:0000269|PubMed:19966300, ECO:0000269|PubMed:20713526, ECO:0000269|PubMed:22307329"; MUTAGEN 77; /note="S->D: Phospho-mimetic mutant; abolished regulation by AMBRA1."; /evidence="ECO:0000269|PubMed:25438055"; MUTAGEN 450; /note="R->K: Abolished ubiquitination and degradation by the DCX(TRPC4AP) complex."; /evidence="ECO:0000269|PubMed:29779948
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by PRKDC (PubMed:1597196). Phosphorylation at Ser-344 by PIM2 leads to the stabilization of MYC (By similarity). Phosphorylation at Ser-77 by CDK2 prevents Ras-induced senescence (PubMed:19966300, PubMed:20713526). Phosphorylated at Ser-77 by DYRK2; this primes the protein for subsequent phosphorylation by GSK3B at Thr-73 (PubMed:22307329). Phosphorylation at Thr-73 and Ser-77 by GSK3 is required for ubiquitination and degradation by the proteasome (PubMed:15103331, PubMed:17558397, PubMed:8386367). Dephosphorylation at multiple sites by the PNUTS-PP1 complex promotes MYC stability by preventing ubiquitination by the SCF(FBXW7) complex (PubMed:30158517). Dephosphorylation at Ser-77 by protein phosphatase 2A (PPP2CA) promotes its degradation; interaction with PPP2CA is enhanced by AMBRA1 (PubMed:25438055, PubMed:25803737). {ECO:0000250|UniProtKB:P01108, ECO:0000269|PubMed:15103331, ECO:0000269|PubMed:1597196, ECO:0000269|PubMed:17558397, ECO:0000269|PubMed:19966300, ECO:0000269|PubMed:20713526, ECO:0000269|PubMed:22307329, ECO:0000269|PubMed:25438055, ECO:0000269|PubMed:25803737, ECO:0000269|PubMed:30158517, ECO:0000269|PubMed:8386367}.; PTM: Ubiquitinated by the SCF(FBXW7) complex when phosphorylated at Thr-73 and Ser-77, leading to its degradation by the proteasome (PubMed:15103331, PubMed:17558397, PubMed:25775507, PubMed:30158517). In the nucleoplasm, ubiquitination is counteracted by USP28, which interacts with isoform 1 of FBXW7 (FBW7alpha), leading to its deubiquitination and preventing degradation (PubMed:17558397, PubMed:17873522). In the nucleolus, however, ubiquitination is not counteracted by USP28 but by USP36, due to the lack of interaction between isoform 3 of FBXW7 (FBW7gamma) and USP28, explaining the selective MYC degradation in the nucleolus (PubMed:17558397, PubMed:25775507). Also polyubiquitinated by the DCX(TRPC4AP) complex (PubMed:20551172, PubMed:29779948). 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 (PubMed:33208877, PubMed:37478862). Ubiquitinated by TRIM6 in a phosphorylation-independent manner (By similarity). {ECO:0000250|UniProtKB:P01108, ECO:0000269|PubMed:15103331, ECO:0000269|PubMed:17558397, ECO:0000269|PubMed:17873522, ECO:0000269|PubMed:20551172, ECO:0000269|PubMed:25775507, ECO:0000269|PubMed:29779948, ECO:0000269|PubMed:30158517, ECO:0000269|PubMed:33208877, ECO:0000269|PubMed:37478862}.
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15103331
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15674325
uniprot
proteins
pubmed
15723054
uniprot
proteins
pubmed
1597196
uniprot
proteins
pubmed
16126174
uniprot
proteins
pubmed
16421571
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17308053
uniprot
proteins
pubmed
17311883
uniprot
proteins
pubmed
17558397
uniprot
proteins
pubmed
17632056
uniprot
proteins
pubmed
17873522
uniprot
proteins
pubmed
18035408
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19966300
uniprot
proteins
pubmed
20010808
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20551172
uniprot
proteins
pubmed
2069907
uniprot
proteins
pubmed
20713526
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
2166998
uniprot
proteins
pubmed
22307329
uniprot
proteins
pubmed
22719065
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24940000
uniprot
proteins
pubmed
25438055
uniprot
proteins
pubmed
25775507
uniprot
proteins
pubmed
25803737
uniprot
proteins
pubmed
25925585
uniprot
proteins
pubmed
25956029
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
29779948
uniprot
proteins
pubmed
30158517
uniprot
proteins
pubmed
3277717
uniprot
proteins
pubmed
33208877
uniprot
proteins
pubmed
34342803
uniprot
proteins
pubmed
3540591
uniprot
proteins
pubmed
37478862
uniprot
proteins
pubmed
38225354
uniprot
proteins
pubmed
6298632
uniprot
proteins
pubmed
6304538
uniprot
proteins
pubmed
6304729
uniprot
proteins
pubmed
6321164
uniprot
proteins
pubmed
6414718
uniprot
proteins
pubmed
6419122
uniprot
proteins
pubmed
6547209
uniprot
proteins
pubmed
6714223
uniprot
proteins
pubmed
7642555
uniprot
proteins
pubmed
8220424
uniprot
proteins
pubmed
8386367
uniprot
proteins
pubmed
8444346
uniprot
proteins
pubmed
9315742
uniprot
proteins
pubmed
9680483
uniprot
proteins
sequence_length
454
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:17558397}. Nucleus, nucleolus {ECO:0000269|PubMed:17558397, ECO:0000269|PubMed:25775507, ECO:0000269|PubMed:38225354}. Nucleus {ECO:0000269|PubMed:22719065, ECO:0000269|PubMed:38225354}. Cytoplasm {ECO:0000269|PubMed:22719065}. Chromosome {ECO:0000269|PubMed:30158517}. Note=Association with chromatin is reduced by hyperphosphorylation (PubMed:30158517). Localization to the nucleolus is dependent on HEATR1 (PubMed:38225354). {ECO:0000269|PubMed:30158517, ECO:0000269|PubMed:38225354}.
uniprot
proteins