IED Industry Enzyme Database

Detail Information for IndEnz0002015473
IED ID IndEnz0002015473
Enzyme Type ID protease015473
Protein Name Myc proto-oncogene protein
Class E basic helix-loop-helix protein 39
bHLHe39
Proto-oncogene c-Myc
Transcription factor p64
Gene Name MYC BHLHE39
Organism Homo sapiens (Human)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSGSPNPARGHSVCSTSSLYLQDLSAAASECIDPSVVFPYPLNDSSSPKSCASQDSSAFSPSSDSLLSSTESSPQGSPEPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQAPGKRSESGSPSAGGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRVKLDSVRVLRQISNNRKCTSPRSSDTEENVKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSVQAEEQKLISEEDLLRKRREQLKHKLEQLRNSCA
Enzyme Length 439
Uniprot Accession Number P01106
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme 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}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Alternative sequence (1); Chain (1); Compositional bias (1); Cross-link (4); Domain (1); Glycosylation (1); Helix (5); Modified residue (15); Motif (1); Mutagenesis (4); Natural variant (8); Region (2); Sequence conflict (15)
Keywords 3D-structure;Acetylation;Activator;Alternative splicing;Chromosomal rearrangement;DNA-binding;Glycoprotein;Isopeptide bond;Nucleus;Phosphoprotein;Proto-oncogene;Reference proteome;Transcription;Transcription regulation;Ubl conjugation
Interact With Q9UBB4; O15169; O00499-10; O00499-11; Q15059; P55212; P45973; Q8N163; P06307; A5D8W4; P11802; Q86XR8; P28329-3; Q14839; O15111; Q8TCG1; Q01658; Q15029; Q96L91; Q96L91-2; Q969H0; Q8N3Y1; P22607; O43524; P49841-2; P06396; Q00403; Q9Y5Q9; Q92769; O15379; Q9Y6K9; O60341; P13473-2; P61244; O95983; P33993; A9UHW6; O75928; Q13526; O75400-2; P62913; Q9Y371; O75182; Q96EB6; Q8N6T7; Q13309; Q8TAD8; P08047; P31948; Q13148; P37173; P11387; Q14669; Q9Y4A5; P0CG48; Q9UMX0; P17480; Q13105; Q9Y649; P03129; P04020; P06788; P03204; P52164; Q62141; P03070
Induction
Subcellular Location SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:17558397}. Nucleus, nucleolus {ECO:0000269|PubMed:17558397, ECO:0000269|PubMed:25775507}.
Modified Residue MOD_RES 6; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"; MOD_RES 8; /note="Phosphothreonine; by RAF; in vitro"; /evidence="ECO:0000269|PubMed:9315742"; MOD_RES 58; /note="Phosphothreonine; by GSK3; alternate"; /evidence="ECO:0000269|PubMed:15103331, ECO:0000269|PubMed:17558397, ECO:0000269|PubMed:8386367, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"; MOD_RES 62; /note="Phosphoserine; by DYRK2, GSK3 and CDK2"; /evidence="ECO:0000269|PubMed:15103331, 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:8386367, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"; MOD_RES 71; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"; MOD_RES 143; /note="N6-acetyllysine; by PCAF; alternate"; /evidence="ECO:0000269|PubMed:16126174"; MOD_RES 148; /note="N6-acetyllysine; alternate"; /evidence="ECO:0007744|PubMed:19608861"; MOD_RES 157; /note="N6-acetyllysine; by PCAF"; /evidence="ECO:0000269|PubMed:16126174"; MOD_RES 161; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:20068231"; MOD_RES 275; /note="N6-acetyllysine; by PCAF"; /evidence="ECO:0000269|PubMed:16126174"; MOD_RES 293; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 317; /note="N6-acetyllysine; by PCAF"; /evidence="ECO:0000269|PubMed:16126174"; MOD_RES 323; /note="N6-acetyllysine; by PCAF"; /evidence="ECO:0000269|PubMed:16126174"; MOD_RES 329; /note="Phosphoserine; by PIM2; in vitro"; /evidence="ECO:0000250|UniProtKB:P01108"; MOD_RES 371; /note="N6-acetyllysine; by PCAF"; /evidence="ECO:0000269|PubMed:16126174"
Post Translational Modification PTM: Phosphorylated by PRKDC (PubMed:1597196). Phosphorylation at Ser-329 by PIM2 leads to the stabilization of MYC (By similarity). Phosphorylation at Ser-62 by CDK2 prevents Ras-induced senescence (PubMed:19966300, PubMed:20713526). Phosphorylated at Ser-62 by DYRK2; this primes the protein for subsequent phosphorylation by GSK3B at Thr-58 (PubMed:22307329). Phosphorylation at Thr-58 and Ser-62 by GSK3 is required for ubiquitination and degradation by the proteasome (PubMed:15103331, PubMed:17558397, PubMed:8386367). Dephosphorylation at Ser-62 by protein phosphatase 2A (PPP2CA) promotes its degradation; interaction with PPP2CA is enhanced by AMBRA1 (PubMed:25803737, PubMed:25438055). {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:8386367}.; PTM: Ubiquitinated by the SCF(FBXW7) complex when phosphorylated at Thr-58 and Ser-62, leading to its degradation by the proteasome (PubMed:15103331, PubMed:17558397, PubMed:25775507). In the nucleoplasm, ubiquitination is counteracted by USP28, which interacts with isoform 1 of FBXW7 (FBW7alpha), leading to its deubiquitination and preventing degradation (PubMed:17873522, PubMed:17558397). 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 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}.
Signal Peptide
Structure 3D NMR spectroscopy (3); X-ray crystallography (12)
Cross Reference PDB 1A93; 1EE4; 1MV0; 1NKP; 2A93; 2OR9; 4Y7R; 5I4Z; 5I50; 6C4U; 6E16; 6E24; 6G6J; 6G6K; 6G6L;
Mapped Pubmed ID 10022608; 10224279; 10454584; 10551811; 10597290; 10706881; 10713166; 10745017; 10825194; 10866684; 10867011; 11018017; 11120780; 11182042; 11243879; 11404481; 11443860; 11672531; 11679086; 11777933; 11795828; 11804592; 11817538; 11840336; 11848444; 11848471; 11850082; 11861398; 11877042; 11877298; 11891322; 11904304; 11909963; 11916966; 11956070; 11960382; 11968011; 12027803; 12031912; 12032779; 12049739; 12072203; 12077335; 12082260; 12149248; 12150994; 12177005; 12209953; 12213716; 12223483; 12226097; 12237776; 12356725; 12360279; 12362975; 12379776; 12394763; 12420224; 12435808; 12452058; 12490316; 12509468; 12529648; 12538578; 12545156; 12553908; 12562237; 12600988; 12637327; 12637527; 12646176; 12673205; 12676581; 12688321; 12721301; 12729735; 12776177; 12783888; 12808131; 12818373; 12821782; 12824159; 12829833; 12842909; 12855588; 12869508; 12909717; 12970749; 1332967; 14517214; 14532990; 14563837; 14576301; 14625288; 14645543; 14645547; 14663479; 14663583; 14672406; 14697225; 14724288; 14744757; 14760071; 14769798; 14991929; 15048125; 15071503; 15077166; 15083194; 15108364; 15126105; 15150404; 15160911; 15190416; 15191563; 15192039; 15198123; 15199070; 15199147; 15243561; 15282543; 15286700; 15287031; 15355849; 15361884; 15457447; 15459488; 15467756; 15468060; 15474507; 15514030; 15516975; 15522869; 15528212; 15580293; 15595642; 15601838; 15629428; 15645079; 15663936; 15688026; 15697230; 15716988; 15723053; 15739117; 15743499; 15756435; 15763593; 15769738; 15800668; 15839202; 15856024; 15878876; 15929079; 15937962; 15944709; 15950906; 15965094; 15972952; 15983063; 15986448; 15991278; 15992821; 16007143; 16085756; 16094360; 16107691; 16107734; 16116477; 16139224; 16167342; 16169462; 16172399; 16173081; 16174239; 16201965; 16205115; 16210249; 16247449; 16260605; 16263084; 16269333; 16287840; 16293596; 16295419; 1630819; 16308474; 16328057; 16352593; 16367922; 16376880; 16378632; 16397018; 16410719; 16410805; 16423995; 16423996; 16432227; 16452238; 16466700; 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9708738; 9727977; 9874564;
Motif MOTIF 100..108; /note=9aaTAD; /evidence=ECO:0000269|PubMed:34342803
Gene Encoded By
Mass 48,804
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda