MYC_MOUSE
ID MYC_MOUSE Reviewed; 439 AA.
AC P01108; P70247; Q3UM70; Q61422;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 217.
DE RecName: Full=Myc proto-oncogene protein;
DE AltName: Full=Proto-oncogene c-Myc;
DE AltName: Full=Transcription factor p64;
GN Name=Myc;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ; TISSUE=Spleen;
RX PubMed=6321164; DOI=10.1002/j.1460-2075.1983.tb01749.x;
RA Bernard O., Cory S., Gerondakis S., Webb E., Adams J.M.;
RT "Sequence of the murine and human cellular myc oncogenes and two modes of
RT myc transcription resulting from chromosome translocation in B lymphoid
RT tumours.";
RL EMBO J. 2:2375-2383(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6462227; DOI=10.1038/310423a0;
RA Stanton L.W., Fahrlander P.D., Tesser P.M., Marcu K.B.;
RT "Nucleotide sequence comparison of normal and translocated murine c-myc
RT genes.";
RL Nature 310:423-425(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Mammary gland, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-252.
RX PubMed=6412145; DOI=10.1038/305240a0;
RA Neuberger M.S., Calabi F.;
RT "Reciprocal chromosome translocation between c-myc and immunoglobulin gamma
RT 2b genes.";
RL Nature 305:240-243(1983).
RN [6]
RP DEVELOPMENTAL STAGE.
RX PubMed=8521822; DOI=10.1002/j.1460-2075.1995.tb00252.x;
RA Hurlin P.J., Queva C., Koskinen P.J., Steingrimsson E., Ayer D.E.,
RA Copeland N.G., Jenkins N.A., Eisenman R.N.;
RT "Mad3 and Mad4: novel Max-interacting transcriptional repressors that
RT suppress c-myc dependent transformation and are expressed during neural and
RT epidermal differentiation.";
RL EMBO J. 14:5646-5659(1995).
RN [7]
RP ERRATUM OF PUBMED:8521822.
RX PubMed=8617250; DOI=10.1002/j.1460-2075.1996.tb00555.x;
RA Hurlin P.J., Queva C., Koskinen P.J., Steingrimsson E., Ayer D.E.,
RA Copeland N.G., Jenkins N.A., Eisenman R.N.;
RL EMBO J. 15:2030-2030(1996).
RN [8]
RP INTERACTION WITH SPAG9.
RX PubMed=12391307; DOI=10.1073/pnas.232310199;
RA Lee C.M., Onesime D., Reddy C.D., Dhanasekaran N., Reddy E.P.;
RT "JLP: a scaffolding protein that tethers JNK/p38MAPK signaling modules and
RT transcription factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14189-14194(2002).
RN [9]
RP BIOTECHNOLOGY.
RX PubMed=16904174; DOI=10.1016/j.cell.2006.07.024;
RA Takahashi K., Yamanaka S.;
RT "Induction of pluripotent stem cells from mouse embryonic and adult
RT fibroblast cultures by defined factors.";
RL Cell 126:663-676(2006).
RN [10]
RP PHOSPHORYLATION AT SER-329, MUTAGENESIS OF SER-329, AND INTERACTION WITH
RP PIM2.
RX PubMed=18438430; DOI=10.1038/onc.2008.123;
RA Zhang Y., Wang Z., Li X., Magnuson N.S.;
RT "Pim kinase-dependent inhibition of c-Myc degradation.";
RL Oncogene 27:4809-4819(2008).
RN [11]
RP MUTAGENESIS OF THR-58 AND SER-62, INTERACTION WITH TRIM6, AND
RP UBIQUITINATION.
RX PubMed=22328504; DOI=10.1242/jcs.095273;
RA Sato T., Okumura F., Ariga T., Hatakeyama S.;
RT "TRIM6 interacts with Myc and maintains the pluripotency of mouse embryonic
RT stem cells.";
RL J. Cell Sci. 125:1544-1555(2012).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-149, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [13]
RP FUNCTION.
RX PubMed=31005419; DOI=10.1016/j.molcel.2019.03.025;
RA Seruggia D., Oti M., Tripathi P., Canver M.C., LeBlanc L.,
RA Di Giammartino D.C., Bullen M.J., Nefzger C.M., Sun Y.B.Y., Farouni R.,
RA Polo J.M., Pinello L., Apostolou E., Kim J., Orkin S.H., Das P.P.;
RT "TAF5L and TAF6L Maintain Self-Renewal of Embryonic Stem Cells via the MYC
RT Regulatory Network.";
RL Mol. Cell 74:1148.E7-1163.E7(2019).
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. Binds to the VEGFA
CC promoter, promoting VEGFA production and subsequent sprouting
CC angiogenesis. Regulator of somatic reprogramming, controls self-renewal
CC of embryonic stem cells. Functions with TAF6L to activate target gene
CC expression through RNA polymerase II pause release (PubMed:31005419).
CC Positively regulates transcription of HNRNPA1, HNRNPA2 and PTBP1 which
CC in turn regulate splicing of pyruvate kinase PKM by binding
CC repressively to sequences flanking PKM exon 9, inhibiting exon 9
CC inclusion and resulting in exon 10 inclusion and production of the PKM
CC M2 isoform (By similarity). {ECO:0000250|UniProtKB:P01106,
CC ECO:0000269|PubMed:31005419}.
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-58 and Ser-62) with FBXW7.
CC Interacts with PIM2 (PubMed:18438430). Interacts with RIOX1. The
CC heterodimer MYC:MAX interacts with ABI1; the interaction may enhance
CC MYC:MAX transcriptional activity (By similarity). Interacts with TRIM6
CC (PubMed:22328504). Interacts with NPM1; the binary complex is recruited
CC to the promoter of MYC target genes and enhances their transcription
CC (By similarity). Interacts with CIP2A; leading to the stabilization of
CC MYC (By similarity). {ECO:0000250|UniProtKB:P01106,
CC ECO:0000269|PubMed:12391307, ECO:0000269|PubMed:18438430,
CC ECO:0000269|PubMed:22328504}.
CC -!- INTERACTION:
CC P01108; P28574: Max; NbExp=7; IntAct=EBI-1183114, EBI-1183003;
CC P01108; Q8CH72: Trim32; NbExp=2; IntAct=EBI-1183114, EBI-773837;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:P01106}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P01106}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the proliferating cells of the
CC developing CNS and the epidermis. In the spinal cord at embryonic days
CC 10.5, 11.5 and 12.5 dpc, expressed within a subset of cells in the
CC proliferative ventricular zone, as well as in the differentiating cells
CC at the ventral portion of the intermediate zone. Also detected in the
CC roof plate and in the neural crest. At 14.5 dpc, found in regions
CC containing differentiating postmitotic neurons. In the developing
CC epidermis at 14.5 dpc, found in the dorsal lateral epidermis. At 17
CC dpc, expression is confined primarily to the proliferative malphigian
CC layer of the epidermis and to the dermal papilla and primary germ cells
CC in the dermis. {ECO:0000269|PubMed:8521822}.
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 329 by PIM2 leads to the stabilization of MYC (PubMed:18438430).
CC Phosphorylation at Ser-62 by CDK2 prevents Ras-induced senescence.
CC Phosphorylated at Ser-62 by DYRK2; this primes the protein for
CC subsequent phosphorylation by GSK3B at Thr-58. Phosphorylation at Thr-
CC 58 and Ser-62 by GSK3 is required for ubiquitination and degradation by
CC the proteasome. Dephosphorylation at Ser-62 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:0000269|PubMed:18438430}.
CC -!- PTM: Ubiquitinated by the SCF(FBXW7) complex when phosphorylated at
CC Thr-58 and Ser-62, 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 (By similarity). Ubiquitinated by TRIM6 in a
CC phosphorylation-independent manner (PubMed:22328504).
CC {ECO:0000250|UniProtKB:P01106, ECO:0000269|PubMed:22328504}.
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:16904174}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH06728.2; 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; L00039; AAB59728.1; -; Genomic_DNA.
DR EMBL; L00038; AAB59728.1; JOINED; Genomic_DNA.
DR EMBL; X01023; CAA25508.1; -; mRNA.
DR EMBL; AK087961; BAC40060.1; -; mRNA.
DR EMBL; AK133952; BAE21948.1; -; mRNA.
DR EMBL; AK145084; BAE26228.1; -; mRNA.
DR EMBL; BC006728; AAH06728.2; ALT_INIT; mRNA.
DR EMBL; K00683; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS49615.1; -.
DR PIR; A93337; TVMS.
DR RefSeq; NP_001170823.1; NM_001177352.1.
DR RefSeq; NP_001170824.1; NM_001177353.1.
DR RefSeq; NP_001170825.1; NM_001177354.1.
DR AlphaFoldDB; P01108; -.
DR SMR; P01108; -.
DR BioGRID; 201635; 33.
DR ComplexPortal; CPX-1144; FOXO3-MYC complex.
DR ComplexPortal; CPX-744; c-MYC-BIN1 complex.
DR ComplexPortal; CPX-97; Transcriptional activator Myc-Max complex.
DR CORUM; P01108; -.
DR DIP; DIP-1064N; -.
DR IntAct; P01108; 17.
DR STRING; 10090.ENSMUSP00000022971; -.
DR GlyGen; P01108; 1 site.
DR iPTMnet; P01108; -.
DR PhosphoSitePlus; P01108; -.
DR EPD; P01108; -.
DR MaxQB; P01108; -.
DR PaxDb; P01108; -.
DR PeptideAtlas; P01108; -.
DR PRIDE; P01108; -.
DR ProteomicsDB; 293593; -.
DR DNASU; 17869; -.
DR Ensembl; ENSMUST00000159327; ENSMUSP00000124758; ENSMUSG00000022346.
DR Ensembl; ENSMUST00000160009; ENSMUSP00000123852; ENSMUSG00000022346.
DR Ensembl; ENSMUST00000161976; ENSMUSP00000123821; ENSMUSG00000022346.
DR GeneID; 17869; -.
DR KEGG; mmu:17869; -.
DR UCSC; uc007vyh.2; mouse.
DR CTD; 4609; -.
DR MGI; MGI:97250; Myc.
DR VEuPathDB; HostDB:ENSMUSG00000022346; -.
DR eggNOG; KOG2483; Eukaryota.
DR GeneTree; ENSGT00940000155285; -.
DR HOGENOM; CLU_052560_0_0_1; -.
DR InParanoid; P01108; -.
DR OMA; EQLRNCC; -.
DR PhylomeDB; P01108; -.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR Reactome; R-MMU-8866911; TFAP2 (AP-2) family regulates transcription of cell cycle factors.
DR BioGRID-ORCS; 17869; 29 hits in 76 CRISPR screens.
DR ChiTaRS; Myc; mouse.
DR PRO; PR:P01108; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P01108; protein.
DR Bgee; ENSMUSG00000022346; Expressed in ectoplacental cone and 266 other tissues.
DR ExpressionAtlas; P01108; baseline and differential.
DR Genevisible; P01108; MM.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0000791; C:euchromatin; IDA:BHF-UCL.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0071943; C:Myc-Max complex; IPI:ComplexPortal.
DR GO; GO:0016604; C:nuclear body; IDA:MGI.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0090571; C:RNA polymerase II transcription repressor complex; ISO:MGI.
DR GO; GO:0005819; C:spindle; IDA:MGI.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
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:MGI.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
DR GO; GO:0070888; F:E-box binding; ISS:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0044877; F:protein-containing complex binding; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0001221; F:transcription coregulator binding; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:1990863; P:acinar cell proliferation; IGI:MGI.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:MGI.
DR GO; GO:0006865; P:amino acid transport; ISO:MGI.
DR GO; GO:0001783; P:B cell apoptotic process; IMP:MGI.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IMP:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IGI:MGI.
DR GO; GO:0006879; P:cellular iron ion homeostasis; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:MGI.
DR GO; GO:0071456; P:cellular response to hypoxia; ISO:MGI.
DR GO; GO:0035457; P:cellular response to interferon-alpha; IDA:MGI.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IDA:UniProtKB.
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; IMP:MGI.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; ISO:MGI.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0006006; P:glucose metabolic process; ISO:MGI.
DR GO; GO:0007007; P:inner mitochondrial membrane organization; ISO:MGI.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IDA:MGI.
DR GO; GO:0046722; P:lactic acid secretion; ISO:MGI.
DR GO; GO:0000165; P:MAPK cascade; ISS:UniProtKB.
DR GO; GO:0042474; P:middle ear morphogenesis; IMP:MGI.
DR GO; GO:0014902; P:myotube differentiation; IMP:MGI.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
DR GO; GO:0051782; P:negative regulation of cell division; ISS:UniProtKB.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0046325; P:negative regulation of glucose import; ISO:MGI.
DR GO; GO:0045656; P:negative regulation of monocyte differentiation; ISS:UniProtKB.
DR GO; GO:0032091; P:negative regulation of protein binding; IDA:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0001866; P:NK T cell proliferation; IMP:MGI.
DR GO; GO:0043473; P:pigmentation; IMP:MGI.
DR GO; GO:1904699; P:positive regulation of acinar cell proliferation; IGI:MGI.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IDA:MGI.
DR GO; GO:2001171; P:positive regulation of ATP biosynthetic process; ISO:MGI.
DR GO; GO:0002904; P:positive regulation of B cell apoptotic process; IGI:MGI.
DR GO; GO:0043085; P:positive regulation of catalytic activity; IMP:MGI.
DR GO; GO:0045787; P:positive regulation of cell cycle; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:MGI.
DR GO; GO:1901857; P:positive regulation of cellular respiration; ISO:MGI.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
DR GO; GO:0043388; P:positive regulation of DNA binding; ISO:MGI.
DR GO; GO:2000573; P:positive regulation of DNA biosynthetic process; ISS:UniProtKB.
DR GO; GO:1905643; P:positive regulation of DNA methylation; ISO:MGI.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISS:UniProtKB.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0060252; P:positive regulation of glial cell proliferation; ISO:MGI.
DR GO; GO:0045821; P:positive regulation of glycolytic process; ISO:MGI.
DR GO; GO:1902255; P:positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator; ISO:MGI.
DR GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IMP:UniProtKB.
DR GO; GO:0090096; P:positive regulation of metanephric cap mesenchymal cell proliferation; IMP:UniProtKB.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:MGI.
DR GO; GO:0010918; P:positive regulation of mitochondrial membrane potential; ISO:MGI.
DR GO; GO:1903862; P:positive regulation of oxidative phosphorylation; ISO:MGI.
DR GO; GO:2001022; P:positive regulation of response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; ISO:MGI.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0051973; P:positive regulation of telomerase activity; IMP:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IDA:CACAO.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL.
DR GO; GO:0016485; P:protein processing; IMP:MGI.
DR GO; GO:0032986; P:protein-DNA complex disassembly; ISO:MGI.
DR GO; GO:0006848; P:pyruvate transport; ISO:MGI.
DR GO; GO:0000320; P:re-entry into mitotic cell cycle; ISO:MGI.
DR GO; GO:0042981; P:regulation of apoptotic process; IDA:MGI.
DR GO; GO:0010564; P:regulation of cell cycle process; ISO:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IDA:MGI.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; ISO:MGI.
DR GO; GO:0002082; P:regulation of oxidative phosphorylation; ISO:MGI.
DR GO; GO:1904672; P:regulation of somatic stem cell population maintenance; IDA: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:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0043279; P:response to alkaloid; IMP:MGI.
DR GO; GO:0010332; P:response to gamma radiation; ISS:UniProtKB.
DR GO; GO:0009314; P:response to radiation; IDA:MGI.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IMP:MGI.
DR GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0006351; P:transcription, DNA-templated; ISO:MGI.
DR GO; GO:0019087; P:transformation of host cell by virus; ISO:MGI.
DR GO; GO:0016055; P:Wnt signaling pathway; IDA:MGI.
DR Gene3D; 4.10.280.10; -; 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 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; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; DNA-binding; Glycoprotein; Isopeptide bond;
KW Nucleus; Phosphoprotein; Proto-oncogene; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..439
FT /note="Myc proto-oncogene protein"
FT /id="PRO_0000127296"
FT DOMAIN 354..406
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 205..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..434
FT /note="Leucine-zipper"
FT MOTIF 101..109
FT /note="9aaTAD"
FT /evidence="ECO:0000250|UniProtKB:P01106"
FT COMPBIAS 205..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 8
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P01106"
FT MOD_RES 58
FT /note="Phosphothreonine; by GSK3; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01106"
FT MOD_RES 62
FT /note="Phosphoserine; by DYRK2, GSK3 and CDK2"
FT /evidence="ECO:0000250|UniProtKB:P01106"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01106"
FT MOD_RES 144
FT /note="N6-acetyllysine; by PCAF; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01106"
FT MOD_RES 149
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 158
FT /note="N6-acetyllysine; by PCAF"
FT /evidence="ECO:0000250|UniProtKB:P01106"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01106"
FT MOD_RES 275
FT /note="N6-acetyllysine; by PCAF"
FT /evidence="ECO:0000250|UniProtKB:P01106"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01106"
FT MOD_RES 317
FT /note="N6-acetyllysine; by PCAF"
FT /evidence="ECO:0000250|UniProtKB:P01106"
FT MOD_RES 323
FT /note="N6-acetyllysine; by PCAF"
FT /evidence="ECO:0000250|UniProtKB:P01106"
FT MOD_RES 329
FT /note="Phosphoserine; by PIM2; in vitro"
FT /evidence="ECO:0000269|PubMed:18438430"
FT MOD_RES 371
FT /note="N6-acetyllysine; by PCAF"
FT /evidence="ECO:0000250|UniProtKB:P01106"
FT CARBOHYD 58
FT /note="O-linked (GlcNAc) threonine; alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 52
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P01106"
FT CROSSLNK 144
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P01106"
FT CROSSLNK 149
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P01106"
FT CROSSLNK 298
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P01106"
FT MUTAGEN 58
FT /note="T->A: Does not affect interaction with TRIM6."
FT /evidence="ECO:0000269|PubMed:22328504"
FT MUTAGEN 62
FT /note="S->A: Does not affect interaction with TRIM6."
FT /evidence="ECO:0000269|PubMed:22328504"
FT MUTAGEN 329
FT /note="S->A: Reduces phosphorylation by PIM2 by 60%, and
FT decreases the transcriptional activity of MYC."
FT /evidence="ECO:0000269|PubMed:18438430"
FT CONFLICT 39
FT /note="E -> D (in Ref. 5; K00683)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="E -> Q (in Ref. 1; AAB59728)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="S -> F (in Ref. 1; AAB59728)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 439 AA; 48971 MW; 3FCA39BFFD6FC59E CRC64;
MPLNVNFTNR NYDLDYDSVQ PYFICDEEEN FYHQQQQSEL QPPAPSEDIW KKFELLPTPP
LSPSRRSGLC SPSYVAVATS FSPREDDDGG GGNFSTADQL EMMTELLGGD MVNQSFICDP
DDETFIKNII IQDCMWSGFS AAAKLVSEKL ASYQAARKDS TSLSPARGHS VCSTSSLYLQ
DLTAAASECI DPSVVFPYPL NDSSSPKSCT SSDSTAFSPS SDSLLSSESS PRASPEPLVL
HEETPPTTSS DSEEEQEDEE EIDVVSVEKR QTPAKRSESG SSPSRGHSKP PHSPLVLKRC
HVSTHQHNYA APPSTRKDYP AAKRAKLDSG RVLKQISNNR KCSSPRSSDT EENDKRRTHN
VLERQRRNEL KRSFFALRDQ IPELENNEKA PKVVILKKAT AYILSIQADE HKLTSEKDLL
RKRREQLKHK LEQLRNSGA
