ID MYC_RAT Reviewed; 453 AA. AC P09416; A0A8L2Q2H7; Q6B500; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 22-FEB-2023, sequence version 2. DT 27-MAR-2024, entry version 198. DE RecName: Full=Myc proto-oncogene protein; DE AltName: Full=Proto-oncogene c-Myc; DE AltName: Full=Transcription factor p64; GN Name=Myc; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3306601; DOI=10.1093/nar/15.16.6419; RA Hayashi K., Makino R., Kawamura H., Arisawa A., Yoneda K.; RT "Characterization of rat c-myc and adjacent regions."; RL Nucleic Acids Res. 15:6419-6436(1987). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=ACI/SegHsd, and Brown Norway/SsNHsd; TISSUE=Spleen; RA Shull J.D., Buckles L.K.; RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway; RX PubMed=15057822; DOI=10.1038/nature02426; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., RA Mockrin S., Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into mammalian RT evolution."; RL Nature 428:493-521(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Ovary; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP ALTERNATIVE TRANSLATION INITIATION. RX PubMed=3277717; DOI=10.1016/0092-8674(88)90507-7; RA Hann S.R., King M.W., Bentley D.L., Anderson C.W., Eisenman R.N.; RT "A non-AUG translational initiation in c-myc exon 1 generates an N- RT terminally distinct protein whose synthesis is disrupted in Burkitt's RT lymphomas."; RL Cell 52:185-195(1988). RN [6] RP BIOTECHNOLOGY. RX PubMed=20352099; DOI=10.1371/journal.pone.0009838; RA Chang M.Y., Kim D., Kim C.H., Kang H.C., Yang E., Moon J.I., Ko S., RA Park J., Park K.S., Lee K.A., Hwang D.Y., Chung Y., Lanza R., Kim K.S.; RT "Direct reprogramming of rat neural precursor cells and fibroblasts into RT pluripotent stem cells."; RL PLoS ONE 5:E9838-E9838(2010). RN [7] RP FUNCTION IN TRANSCRIPTIONAL ACTIVATION, AND INTERACTION WITH ABI1. RX PubMed=17304222; DOI=10.1038/sj.emboj.7601569; RA Proepper C., Johannsen S., Liebau S., Dahl J., Vaida B., Bockmann J., RA Kreutz M.R., Gundelfinger E.D., Boeckers T.M.; RT "Abelson interacting protein 1 (Abi-1) is essential for dendrite RT morphogenesis and synapse formation."; RL EMBO J. 26:1397-1409(2007). CC -!- FUNCTION: Transcription factor that binds DNA in a non-specific manner, CC yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. CC Activates the transcription of growth-related genes (PubMed:17304222). CC Binds to the VEGFA promoter, promoting VEGFA production and subsequent CC sprouting angiogenesis (By similarity). Regulator of somatic CC reprogramming, controls self-renewal of embryonic stem cells. Functions CC with TAF6L to activate target gene expression through RNA polymerase II CC pause release (By similarity). Positively regulates transcription of CC HNRNPA1, HNRNPA2 and PTBP1 which in turn regulate splicing of pyruvate CC kinase PKM by binding repressively to sequences flanking PKM exon 9, CC inhibiting exon 9 inclusion and resulting in exon 10 inclusion and CC production of the PKM M2 isoform (By similarity). CC {ECO:0000250|UniProtKB:P01106, ECO:0000250|UniProtKB:P01108, CC ECO:0000269|PubMed:17304222}. CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH CC protein. Binds DNA as a heterodimer with MAX (By similarity). Interacts CC with TAF1C and SPAG9. Interacts with PARP10. Interacts with KDM5A and CC KDM5B. Interacts (when phosphorylated at Thr-72 and Ser-76) with FBXW7. CC Interacts with PIM2. Interacts with RIOX1 (By similarity). The CC heterodimer MYC:MAX interacts with ABI1; the interaction may enhance CC MYC:MAX transcriptional activity (PubMed:17304222). Interacts with CC TRIM6 (By similarity). Interacts with NPM1; the binary complex is CC recruited to the promoter of MYC target genes and enhances their CC transcription (By similarity). Interacts with CIP2A; leading to the CC stabilization of MYC (By similarity). Interacts with NUP205 (By CC similarity). {ECO:0000250|UniProtKB:P01106, CC ECO:0000250|UniProtKB:P01108, ECO:0000269|PubMed:17304222}. CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm CC {ECO:0000250|UniProtKB:P01106}. Nucleus, nucleolus CC {ECO:0000250|UniProtKB:P01106}. Nucleus {ECO:0000250|UniProtKB:P01106}. CC Cytoplasm {ECO:0000250|UniProtKB:P01106}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=2; CC Name=2; Synonyms=c-myc 1 {ECO:0000303|PubMed:3277717}; CC IsoId=P09416-1; Sequence=Displayed; CC Name=1; Synonyms=c-myc 2 {ECO:0000303|PubMed:3277717}; CC IsoId=P09416-2; Sequence=VSP_061785; CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large CC number of yeast and animal transcription factors. CC {ECO:0000250|UniProtKB:P01106}. CC -!- PTM: Phosphorylated by PRKDC (By similarity). Phosphorylation at Ser- CC 343 by PIM2 leads to the stabilization of MYC (By similarity). CC Phosphorylation at Ser-76 by CDK2 prevents Ras-induced senescence. CC Phosphorylated at Ser-76 by DYRK2; this primes the protein for CC subsequent phosphorylation by GSK3B at Thr-72. Phosphorylation at Thr- CC 72 and Ser-76 by GSK3 is required for ubiquitination and degradation by CC the proteasome. Dephosphorylation at Ser-76 by protein phosphatase 2A CC (PPP2CA) promotes its degradation; interaction with PPP2CA is enhanced CC by AMBRA1 (By similarity). {ECO:0000250|UniProtKB:P01106, CC ECO:0000250|UniProtKB:P01108}. CC -!- PTM: Ubiquitinated by the SCF(FBXW7) complex when phosphorylated at CC Thr-72 and Ser-76, leading to its degradation by the proteasome. CC Ubiquitination is counteracted by USP28 in the nucleoplasm and USP36 in CC the nucleolus, both interacting with of FBXW7, leading to its CC deubiquitination and preventing degradation. Also polyubiquitinated by CC the DCX(TRPC4AP) complex. Ubiquitinated by TRIM6 in a phosphorylation- CC independent manner. {ECO:0000250|UniProtKB:P01106, CC ECO:0000250|UniProtKB:P01108}. CC -!- BIOTECHNOLOGY: POU5F1/OCT4, SOX2, MYC/c-Myc and KLF4 are the four CC Yamanaka factors. When combined, these factors are sufficient to CC reprogram differentiated cells to an embryonic-like state designated CC iPS (induced pluripotent stem) cells. iPS cells exhibit the morphology CC and growth properties of ES cells and express ES cell marker genes. CC {ECO:0000269|PubMed:20352099}. CC -!- MISCELLANEOUS: Alternative translation initiation from an upstream, in- CC frame non-ATG (CTG) codon or a downstream ATG start site results in the CC production of 2 isoforms with distinct N-termini, shown in this entry CC as isoform 2 and isoform 1, respectively. {ECO:0000305|PubMed:3277717}. CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative translation CC initiation from a CTG codon, which is translated as Met. {ECO:0000305, CC ECO:0000305|PubMed:3277717}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH91699.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Y00396; CAA68459.2; -; Genomic_DNA. DR EMBL; AY679729; AAT92511.1; -; mRNA. DR EMBL; AY679730; AAT92512.1; -; mRNA. DR EMBL; BC091699; AAH91699.2; ALT_INIT; mRNA. DR PIR; A26801; TVRTMC. DR RefSeq; NP_036735.2; NM_012603.2. [P09416-1] DR PDB; 7LQT; NMR; -; A=27-44. DR PDBsum; 7LQT; -. DR AlphaFoldDB; P09416; -. DR SMR; P09416; -. DR BioGRID; 246723; 4. DR CORUM; P09416; -. DR DIP; DIP-28140N; -. DR IntAct; P09416; 3. DR MINT; P09416; -. DR STRING; 10116.ENSRNOP00000006188; -. DR ChEMBL; CHEMBL4105894; -. DR GlyCosmos; P09416; 1 site, No reported glycans. DR GlyGen; P09416; 1 site. DR iPTMnet; P09416; -. DR PhosphoSitePlus; P09416; -. DR PaxDb; 10116-ENSRNOP00000006188; -. DR Ensembl; ENSRNOT00055041035; ENSRNOP00055033365; ENSRNOG00055023910. DR Ensembl; ENSRNOT00060006663; ENSRNOP00060005003; ENSRNOG00060003990. DR Ensembl; ENSRNOT00065006804; ENSRNOP00065004679; ENSRNOG00065004691. DR GeneID; 24577; -. DR KEGG; rno:24577; -. DR UCSC; RGD:3130; rat. [P09416-1] DR AGR; RGD:3130; -. DR CTD; 4609; -. DR RGD; 3130; Myc. DR VEuPathDB; HostDB:ENSRNOG00000004500; -. DR eggNOG; KOG2483; Eukaryota. DR InParanoid; P09416; -. DR OrthoDB; 3039999at2759; -. DR PhylomeDB; P09416; -. DR Reactome; R-RNO-5689880; Ub-specific processing proteases. DR Reactome; R-RNO-8866911; TFAP2 (AP-2) family regulates transcription of cell cycle factors. DR PRO; PR:P09416; -. DR Proteomes; UP000002494; Chromosome 7. DR Bgee; ENSRNOG00000004500; Expressed in spleen and 19 other cell types or tissues. DR ExpressionAtlas; P09416; baseline and differential. DR GO; GO:0030424; C:axon; ISO:RGD. DR GO; GO:0000785; C:chromatin; ISO:RGD. DR GO; GO:0000791; C:euchromatin; ISO:RGD. DR GO; GO:0005739; C:mitochondrion; IEA:GOC. DR GO; GO:0071943; C:Myc-Max complex; ISO:RGD. DR GO; GO:0016604; C:nuclear body; ISO:RGD. DR GO; GO:0005635; C:nuclear envelope; ISO:RGD. DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB. DR GO; GO:0044195; C:nucleoplasmic reticulum; ISO:RGD. DR GO; GO:0005634; C:nucleus; ISO:RGD. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD. DR GO; GO:0032991; C:protein-containing complex; ISO:RGD. DR GO; GO:0090571; C:RNA polymerase II transcription repressor complex; ISO:RGD. DR GO; GO:0005791; C:rough endoplasmic reticulum; ISO:RGD. DR GO; GO:0005819; C:spindle; ISO:RGD. DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISO:RGD. DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; ISO:RGD. DR GO; GO:0003677; F:DNA binding; IDA:RGD. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:RGD. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:UniProtKB. DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:RGD. DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:RGD. DR GO; GO:0003690; F:double-stranded DNA binding; IDA:RGD. DR GO; GO:0070888; F:E-box binding; ISS:UniProtKB. DR GO; GO:0071074; F:eukaryotic initiation factor eIF2 binding; ISO:RGD. DR GO; GO:0003729; F:mRNA binding; ISO:RGD. DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro. DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD. DR GO; GO:1905761; F:SCF ubiquitin ligase complex binding; ISO:RGD. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD. DR GO; GO:0001221; F:transcription coregulator binding; ISO:RGD. DR GO; GO:0140537; F:transcription regulator activator activity; ISO:RGD. DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD. DR GO; GO:1990863; P:acinar cell proliferation; ISO:RGD. DR GO; GO:0006865; P:amino acid transport; IMP:RGD. DR GO; GO:0001783; P:B cell apoptotic process; ISO:RGD. DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; ISS:UniProtKB. DR GO; GO:0008283; P:cell population proliferation; ISO:RGD. DR GO; GO:1904385; P:cellular response to angiotensin; IEP:RGD. DR GO; GO:1903841; P:cellular response to arsenite(3-); IEP:RGD. DR GO; GO:0071322; P:cellular response to carbohydrate stimulus; IEP:RGD. DR GO; GO:0071409; P:cellular response to cycloheximide; IEP:RGD. DR GO; GO:0071345; P:cellular response to cytokine stimulus; IEP:RGD. DR GO; GO:1904620; P:cellular response to dimethyl sulfoxide; IEP:RGD. DR GO; GO:1990859; P:cellular response to endothelin; IEP:RGD. DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEP:RGD. DR GO; GO:0071391; P:cellular response to estrogen stimulus; IEP:RGD. DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEP:RGD. DR GO; GO:0071378; P:cellular response to growth hormone stimulus; IEP:RGD. DR GO; GO:0071464; P:cellular response to hydrostatic pressure; IEP:RGD. DR GO; GO:0071456; P:cellular response to hypoxia; ISO:RGD. DR GO; GO:0032869; P:cellular response to insulin stimulus; IEP:RGD. DR GO; GO:0035457; P:cellular response to interferon-alpha; ISO:RGD. DR GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD. DR GO; GO:1990858; P:cellular response to lectin; IEP:RGD. DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD. DR GO; GO:1904628; P:cellular response to phorbol 13-acetate 12-myristate; IEP:RGD. DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IEP:RGD. DR GO; GO:1990646; P:cellular response to prolactin; IEP:RGD. DR GO; GO:1904586; P:cellular response to putrescine; IEP:RGD. DR GO; GO:0071300; P:cellular response to retinoic acid; IEP:RGD. DR GO; GO:0071394; P:cellular response to testosterone stimulus; IEP:RGD. DR GO; GO:0071346; P:cellular response to type II interferon; IEP:RGD. DR GO; GO:0034644; P:cellular response to UV; ISO:RGD. DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEP:RGD. DR GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB. DR GO; GO:0051276; P:chromosome organization; ISS:UniProtKB. DR GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; ISO:RGD. DR GO; GO:0006974; P:DNA damage response; ISS:UniProtKB. DR GO; GO:0006346; P:DNA methylation-dependent heterochromatin formation; ISO:RGD. DR GO; GO:0006351; P:DNA-templated transcription; IDA:RGD. DR GO; GO:0006352; P:DNA-templated transcription initiation; IDA:RGD. DR GO; GO:0070371; P:ERK1 and ERK2 cascade; ISO:RGD. DR GO; GO:0045023; P:G0 to G1 transition; IEP:RGD. DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISS:UniProtKB. DR GO; GO:0006006; P:glucose metabolic process; IMP:RGD. DR GO; GO:0021854; P:hypothalamus development; IEP:RGD. DR GO; GO:0001701; P:in utero embryonic development; IEP:RGD. DR GO; GO:0007007; P:inner mitochondrial membrane organization; IMP:RGD. DR GO; GO:0006879; P:intracellular iron ion homeostasis; ISS:UniProtKB. DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; ISO:RGD. DR GO; GO:0046722; P:lactic acid secretion; IMP:RGD. DR GO; GO:0097421; P:liver regeneration; IEP:RGD. DR GO; GO:0000165; P:MAPK cascade; ISS:UniProtKB. DR GO; GO:0042474; P:middle ear morphogenesis; ISO:RGD. DR GO; GO:0051450; P:myoblast proliferation; IEP:RGD. DR GO; GO:0014902; P:myotube differentiation; ISO:RGD. DR GO; GO:0051782; P:negative regulation of cell division; ISS:UniProtKB. DR GO; GO:1904036; P:negative regulation of epithelial cell apoptotic process; IMP:RGD. DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; ISO:RGD. DR GO; GO:0010629; P:negative regulation of gene expression; IMP:RGD. DR GO; GO:0046325; P:negative regulation of glucose import; IMP:RGD. DR GO; GO:0045656; P:negative regulation of monocyte differentiation; ISS:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB. DR GO; GO:0001866; P:NK T cell proliferation; ISO:RGD. DR GO; GO:0001541; P:ovarian follicle development; IEP:RGD. DR GO; GO:0043473; P:pigmentation; ISO:RGD. DR GO; GO:1904699; P:positive regulation of acinar cell proliferation; ISO:RGD. DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; ISO:RGD. DR GO; GO:2001171; P:positive regulation of ATP biosynthetic process; IMP:RGD. DR GO; GO:0002904; P:positive regulation of B cell apoptotic process; ISO:RGD. DR GO; GO:0045787; P:positive regulation of cell cycle; IMP:RGD. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IGI:RGD. DR GO; GO:1901857; P:positive regulation of cellular respiration; IMP:RGD. DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISS:UniProtKB. DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:RGD. DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD. DR GO; GO:0060252; P:positive regulation of glial cell proliferation; IMP:RGD. DR GO; GO:0045821; P:positive regulation of glycolytic process; IMP:RGD. DR GO; GO:1902255; P:positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator; ISO:RGD. DR GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; ISS:UniProtKB. DR GO; GO:0090096; P:positive regulation of metanephric cap mesenchymal cell proliferation; ISS:UniProtKB. DR GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:RGD. DR GO; GO:0010918; P:positive regulation of mitochondrial membrane potential; IMP:RGD. DR GO; GO:1903862; P:positive regulation of oxidative phosphorylation; IMP:RGD. DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IMP:RGD. DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:RGD. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:RGD. DR GO; GO:0060261; P:positive regulation of transcription initiation by RNA polymerase II; ISO:RGD. DR GO; GO:0016485; P:protein processing; ISO:RGD. DR GO; GO:0032986; P:protein-DNA complex disassembly; ISO:RGD. DR GO; GO:0006848; P:pyruvate transport; IMP:RGD. DR GO; GO:0000320; P:re-entry into mitotic cell cycle; IMP:RGD. DR GO; GO:0042981; P:regulation of apoptotic process; ISO:RGD. DR GO; GO:0010564; P:regulation of cell cycle process; ISO:RGD. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:RGD. DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD. DR GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:RGD. DR GO; GO:0002082; P:regulation of oxidative phosphorylation; IMP:RGD. DR GO; GO:1904672; P:regulation of somatic stem cell population maintenance; ISS:UniProtKB. DR GO; GO:0032204; P:regulation of telomere maintenance; ISS:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0043279; P:response to alkaloid; ISO:RGD. DR GO; GO:0032355; P:response to estradiol; IEP:RGD. DR GO; GO:0045471; P:response to ethanol; IEP:RGD. DR GO; GO:0010332; P:response to gamma radiation; ISS:UniProtKB. DR GO; GO:0044752; P:response to human chorionic gonadotropin; IEP:RGD. DR GO; GO:0009314; P:response to radiation; ISO:RGD. DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:RGD. DR GO; GO:0035914; P:skeletal muscle cell differentiation; ISO:RGD. DR GO; GO:0048705; P:skeletal system morphogenesis; ISO:RGD. DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:RGD. DR GO; GO:0016055; P:Wnt signaling pathway; ISO:RGD. DR CDD; cd11458; bHLHzip_c-Myc; 1. DR Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1. DR InterPro; IPR011598; bHLH_dom. DR InterPro; IPR036638; HLH_DNA-bd_sf. DR InterPro; IPR003327; Myc-LZ. DR InterPro; IPR002418; Tscrpt_reg_Myc. DR InterPro; IPR012682; Tscrpt_reg_Myc_N. DR PANTHER; PTHR45851; MYC PROTO-ONCOGENE; 1. DR PANTHER; PTHR45851:SF1; MYC PROTO-ONCOGENE PROTEIN; 1. DR Pfam; PF00010; HLH; 1. DR Pfam; PF02344; Myc-LZ; 1. DR Pfam; PF01056; Myc_N; 1. DR PIRSF; PIRSF001705; Myc_protein; 1. DR PRINTS; PR00044; LEUZIPPRMYC. DR SMART; SM00353; HLH; 1. DR SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 1. DR PROSITE; PS50888; BHLH; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Alternative initiation; Cytoplasm; KW DNA-binding; Glycoprotein; Isopeptide bond; Nucleus; Phosphoprotein; KW Proto-oncogene; Reference proteome; Transcription; KW Transcription regulation; Ubl conjugation. FT CHAIN 1..453 FT /note="Myc proto-oncogene protein" FT /id="PRO_0000127300" FT DOMAIN 368..420 FT /note="bHLH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981" FT REGION 216..373 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 427..448 FT /note="Leucine-zipper" FT MOTIF 115..123 FT /note="9aaTAD" FT /evidence="ECO:0000250|UniProtKB:P01106" FT COMPBIAS 216..247 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 359..373 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 20 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P01106" FT MOD_RES 72 FT /note="Phosphothreonine; by GSK3; alternate" FT /evidence="ECO:0000250|UniProtKB:P01106" FT MOD_RES 76 FT /note="Phosphoserine; by DYRK2, GSK3 and CDK2" FT /evidence="ECO:0000250|UniProtKB:P01106" FT MOD_RES 85 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P01106" FT MOD_RES 158 FT /note="N6-acetyllysine; by PCAF; alternate" FT /evidence="ECO:0000250|UniProtKB:P01106" FT MOD_RES 163 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P01106" FT MOD_RES 172 FT /note="N6-acetyllysine; by PCAF" FT /evidence="ECO:0000250|UniProtKB:P01106" FT MOD_RES 176 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P01106" FT MOD_RES 289 FT /note="N6-acetyllysine; by PCAF" FT /evidence="ECO:0000250|UniProtKB:P01106" FT MOD_RES 307 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P01106" FT MOD_RES 331 FT /note="N6-acetyllysine; by PCAF" FT /evidence="ECO:0000250|UniProtKB:P01106" FT MOD_RES 337 FT /note="N6-acetyllysine; by PCAF" FT /evidence="ECO:0000250|UniProtKB:P01106" FT MOD_RES 343 FT /note="Phosphoserine; by PIM2; in vitro" FT /evidence="ECO:0000250|UniProtKB:P01108" FT MOD_RES 385 FT /note="N6-acetyllysine; by PCAF" FT /evidence="ECO:0000250|UniProtKB:P01106" FT CARBOHYD 72 FT /note="O-linked (GlcNAc) threonine; alternate" FT /evidence="ECO:0000250" FT CROSSLNK 66 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P01106" FT CROSSLNK 158 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P01106" FT CROSSLNK 163 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P01106" FT CROSSLNK 312 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P01106" FT VAR_SEQ 1..14 FT /note="Missing (in isoform 1)" FT /id="VSP_061785" FT TURN 21..23 FT /evidence="ECO:0007829|PDB:7LQT" SQ SEQUENCE 453 AA; 50561 MW; A64D6B02AF52E47F CRC64; MNFLWEVENP TVTTMPLNVS FANRNYDLDY DSVQPYFICD EEENFYHQQQ QSELQPPAPS EDIWKKFELL PTPPLSPSRR SGLCSPSYVA VATSFSPRED DDGGGGNFST ADQLEMMTEL LGGDMVNQSF ICDPDDETFI KNIIIQDCMW SGFSAAAKLV SEKLASYQAA RKDSTSLSPA RGHSVCSTSS LYLQDLTAAA SECIDPSVVF PYPLNDSSSP KSCTSSDSTA FSSSSDSLLS SESSPRATPE PLVLHEETPP TTSSDSEEEQ DDEEEIDVVS VEKRQPPAKR SESGSSPSRG HSKPPHSPLV LKRCHVSTHQ HNYAAPPSTR KDYPAAKRAK LDSGRVLKQI SNNRKCSSPR SSDTEENDKR RTHNVLERQR RNELKRSFFA LRDQIPELEN NEKAPKVVIL KKATAYILSV QADEHKLISE KDLLRKRREQ LKHKLEQLRN SGA //