P01106 · MYC_HUMAN
- ProteinMyc proto-oncogene protein
- GeneMYC
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids454 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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).
Miscellaneous
Biotechnology
GO annotations
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMyc proto-oncogene protein
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP01106
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Burkitt lymphoma (BL)
- Note
- DescriptionA form of undifferentiated malignant lymphoma commonly manifested as a large osteolytic lesion in the jaw or as an abdominal mass.
- See alsoMIM:113970
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_016327 | 26 | in dbSNP:rs4645959 | |||
Sequence: N → S | ||||||
Natural variant | VAR_063384 | 54 | in a Burkitt lymphoma sample; dbSNP:rs121918684 | |||
Sequence: E → D | ||||||
Natural variant | VAR_063385 | 72 | in a Burkitt lymphoma sample; dbSNP:rs28933407 | |||
Sequence: P → S | ||||||
Mutagenesis | 73 | Impairs interaction with FBXW7 and subsequent degradation by the proteasome. Normal inhibition of Ras-induced senescence. | ||||
Sequence: T → A | ||||||
Natural variant | VAR_063386 | 74 | in a Burkitt lymphoma sample; dbSNP:rs121918685 | |||
Sequence: P → A | ||||||
Mutagenesis | 77 | 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. | ||||
Sequence: S → A | ||||||
Mutagenesis | 77 | Phospho-mimetic mutant; abolished regulation by AMBRA1. | ||||
Sequence: S → D | ||||||
Natural variant | VAR_063387 | 101 | in a Burkitt lymphoma sample; dbSNP:rs121918683 | |||
Sequence: N → T | ||||||
Natural variant | VAR_016328 | 175 | in dbSNP:rs4645960 | |||
Sequence: G → C | ||||||
Natural variant | VAR_016329 | 185 | in dbSNP:rs4645961 | |||
Sequence: V → I | ||||||
Natural variant | VAR_016330 | 337 | in dbSNP:rs4645968 | |||
Sequence: A → V | ||||||
Mutagenesis | 450 | Abolished ubiquitination and degradation by the DCX(TRPC4AP) complex. | ||||
Sequence: R → K |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,682 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data), cross-link, glycosylation.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000127293 | 1-454 | UniProt | Myc proto-oncogene protein | |||
Sequence: MDFFRVVENQQPPATMPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSGSPNPARGHSVCSTSSLYLQDLSAAASECIDPSVVFPYPLNDSSSPKSCASQDSSAFSPSSDSLLSSTESSPQGSPEPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQAPGKRSESGSPSAGGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRVKLDSVRVLRQISNNRKCTSPRSSDTEENVKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSVQAEEQKLISEEDLLRKRREQLKHKLEQLRNSCA | |||||||
Modified residue | 21 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 21 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 23 | UniProt | Phosphothreonine; by RAF; in vitro | ||||
Sequence: T | |||||||
Cross-link | 67 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 73 | UniProt | Phosphothreonine; by GSK3; alternate | ||||
Sequence: T | |||||||
Glycosylation | CAR_000033 | 73 | UniProt | O-linked (GlcNAc) threonine; alternate | |||
Sequence: T | |||||||
Modified residue (large scale data) | 73 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 77 | UniProt | Phosphoserine; by DYRK2, GSK3 and CDK2 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 77 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 79 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 82 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 86 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 86 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 88 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 93 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 158 | UniProt | N6-acetyllysine; by PCAF; alternate | ||||
Sequence: K | |||||||
Cross-link | 158 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue | 163 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 163 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue | 172 | UniProt | N6-acetyllysine; by PCAF | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 174 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 176 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 290 | UniProt | N6-acetyllysine; by PCAF | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 292 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 294 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 296 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 303 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 308 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 308 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 313 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 332 | UniProt | N6-acetyllysine; by PCAF | ||||
Sequence: K | |||||||
Modified residue | 338 | UniProt | N6-acetyllysine; by PCAF | ||||
Sequence: K | |||||||
Modified residue | 344 | UniProt | Phosphoserine; by PIM2; in vitro | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 358 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 359 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 363 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 365 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 386 | UniProt | N6-acetyllysine; by PCAF | ||||
Sequence: K |
Post-translational modification
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 Ser-77 by protein phosphatase 2A (PPP2CA) promotes its degradation; interaction with PPP2CA is enhanced by AMBRA1 (PubMed:25438055, PubMed:25803737).
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).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with TAF1C and SPAG9. Interacts with PARP10. Interacts with KDM5A and KDM5B. Interacts (when phosphorylated at Thr-73 and Ser-77) with FBXW7 (PubMed:17558397, PubMed:25775507).
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 (PubMed:25956029).
Interacts with CIP2A; leading to the stabilization of MYC (PubMed:17632056).
Interacts with NUP205 (PubMed:22719065).
Binary interactions
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for motif, compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 115-123 | 9aaTAD | ||||
Sequence: EMVTELLGG | ||||||
Compositional bias | 219-249 | Polar residues | ||||
Sequence: SPKSCASQDSSAFSPSSDSLLSSTESSPQGS | ||||||
Region | 219-310 | Disordered | ||||
Sequence: SPKSCASQDSSAFSPSSDSLLSSTESSPQGSPEPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQAPGKRSESGSPSAGGHSKPPHSPL | ||||||
Domain | 369-421 | bHLH | ||||
Sequence: VKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSV | ||||||
Motif | 370-379 | UBR5-degron | ||||
Sequence: KRRTHNVLER | ||||||
Region | 428-449 | Leucine-zipper | ||||
Sequence: LISEEDLLRKRREQLKHKLEQL |
Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing & Alternative initiation.
P01106-2
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name2
- Synonymsc-myc 1
- NoteProduced by alternative translation initiation from a CTG codon, which is translated as Met.
- Length454
- Mass (Da)50,565
- Last updated2023-02-22 v2
- Checksum8B4107BB740689E5
P01106-1
- Name1
- Synonymsc-myc 2
- Differences from canonical
- 1-15: Missing
P01106-3
- Name3
- NoteProduced by alternative translation initiation from a CTG codon, which is translated as Met, and alternative splicing.
- Differences from canonical
- 10-11: QQ → Q
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H0YBG3 | H0YBG3_HUMAN | MYC | 184 | ||
Q16591 | Q16591_HUMAN | MYC | 188 | ||
Q14899 | Q14899_HUMAN | MYC | 114 | ||
A0A494C1T8 | A0A494C1T8_HUMAN | MYC | 339 | ||
A0A0B4J1R1 | A0A0B4J1R1_HUMAN | MYC | 257 |
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_061778 | 1-15 | in isoform 1 | |||
Sequence: Missing | ||||||
Sequence conflict | 2 | in Ref. 9; BAA01374 | ||||
Sequence: D → N | ||||||
Sequence conflict | 6 | in Ref. 9; BAA01374 | ||||
Sequence: V → E | ||||||
Alternative sequence | VSP_061779 | 10-11 | in isoform 3 | |||
Sequence: QQ → Q | ||||||
Sequence conflict | 21-22 | in Ref. 5; no nucleotide entry | ||||
Sequence: SF → TI | ||||||
Sequence conflict | 25 | in Ref. 5; no nucleotide entry | ||||
Sequence: R → K | ||||||
Sequence conflict | 71 | in Ref. 5; no nucleotide entry | ||||
Sequence: L → LL | ||||||
Sequence conflict | 77 | in Ref. 7; CAA25288 | ||||
Sequence: S → P | ||||||
Sequence conflict | 103 | in Ref. 5; no nucleotide entry | ||||
Sequence: G → D | ||||||
Sequence conflict | 107 | in Ref. 5; no nucleotide entry | ||||
Sequence: S → N | ||||||
Sequence conflict | 129 | in Ref. 5; no nucleotide entry | ||||
Sequence: S → N | ||||||
Sequence conflict | 135 | in Ref. 5; no nucleotide entry | ||||
Sequence: D → G | ||||||
Sequence conflict | 186 | in Ref. 5; no nucleotide entry | ||||
Sequence: C → S | ||||||
Sequence conflict | 218 | in Ref. 5; no nucleotide entry | ||||
Sequence: S → R | ||||||
Compositional bias | 219-249 | Polar residues | ||||
Sequence: SPKSCASQDSSAFSPSSDSLLSSTESSPQGS | ||||||
Sequence conflict | 245 | in Ref. 5; no nucleotide entry | ||||
Sequence: S → A | ||||||
Sequence conflict | 255 | in Ref. 5; no nucleotide entry | ||||
Sequence: L → F | ||||||
Sequence conflict | 260 | in Ref. 5; no nucleotide entry | ||||
Sequence: P → S |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L00058 EMBL· GenBank· DDBJ | AAA59882.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L00057 EMBL· GenBank· DDBJ | AAA59882.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
K00535 EMBL· GenBank· DDBJ | AAA59880.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
K00534 EMBL· GenBank· DDBJ | AAA59880.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
K00535 EMBL· GenBank· DDBJ | ABW69847.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
K00534 EMBL· GenBank· DDBJ | ABW69847.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X00196 EMBL· GenBank· DDBJ | CAA25015.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
X00198 EMBL· GenBank· DDBJ | CAA25015.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
X00364 EMBL· GenBank· DDBJ | CAA25106.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
V00568 EMBL· GenBank· DDBJ | CAA23831.1 EMBL· GenBank· DDBJ | mRNA | ||
K01906 EMBL· GenBank· DDBJ | AAA59881.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
K01905 EMBL· GenBank· DDBJ | AAA59881.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
K02276 EMBL· GenBank· DDBJ | AAA36340.1 EMBL· GenBank· DDBJ | mRNA | ||
X00676 EMBL· GenBank· DDBJ | CAA25288.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
D10493 EMBL· GenBank· DDBJ | BAA01374.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
D10493 EMBL· GenBank· DDBJ | BAA01375.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT019768 EMBL· GenBank· DDBJ | AAV38573.1 EMBL· GenBank· DDBJ | mRNA | ||
AY214166 EMBL· GenBank· DDBJ | AAO21131.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK312883 EMBL· GenBank· DDBJ | BAG35731.1 EMBL· GenBank· DDBJ | mRNA | ||
AC103819 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471060 EMBL· GenBank· DDBJ | EAW92098.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471060 EMBL· GenBank· DDBJ | EAW92100.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471060 EMBL· GenBank· DDBJ | EAW92101.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC000141 EMBL· GenBank· DDBJ | AAH00141.2 EMBL· GenBank· DDBJ | mRNA | ||
BC000917 EMBL· GenBank· DDBJ | AAH00917.2 EMBL· GenBank· DDBJ | mRNA | ||
BC058901 EMBL· GenBank· DDBJ | AAH58901.2 EMBL· GenBank· DDBJ | mRNA | ||
M13929 EMBL· GenBank· DDBJ | AAA88092.1 EMBL· GenBank· DDBJ | mRNA |