Database: UniProt/SWISS-PROT
Entry: MYC_RAT
Original site: MYC_RAT 
ID   MYC_RAT                 Reviewed;         439 AA.
AC   P09416; Q6B500;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   30-AUG-2017, entry version 156.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
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]
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]
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
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.,
RA   Kim K.S.;
RT   "Direct reprogramming of rat neural precursor cells and fibroblasts
RT   into pluripotent stem cells.";
RL   PLoS ONE 5:E9838-E9838(2010).
RN   [5]
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
CC       manner, yet also specifically recognizes the core sequence 5'-
CC       CAC[GA]TG-3'. Activates the transcription of growth-related genes.
CC       {ECO:0000269|PubMed:17304222}.
CC   -!- SUBUNIT: Efficient DNA binding requires dimerization with another
CC       bHLH protein. Binds DNA as a heterodimer with MAX. Interacts with
CC       TAF1C and SPAG9. Interacts with PARP10. Interacts with KDM5A and
CC       KDM5B. Interacts (when phosphorylated at Thr-58 and Ser-62) with
CC       FBXW7. Interacts with PIM2. Interacts with RIOX1. The heterodimer
CC       MYC:MAX interacts with ABI1; the interaction may enhance MYC:MAX
CC       transcriptional activity. Interacts with TRIM6 (By similarity).
CC       Interacts with NPM1; the binary complex is recruited to the
CC       promoter of MYC target genes and enhances their transcription (By
CC       similarity). {ECO:0000250|UniProtKB:P01106,
CC       ECO:0000250|UniProtKB:P01108, ECO:0000269|PubMed:17304222}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. Nucleus,
CC       nucleolus {ECO:0000250}.
CC   -!- PTM: Phosphorylated by PRKDC. Phosphorylated at Ser-62 by DYRK2;
CC       this primes the protein for subsequent phosphorylation by GSK3B at
CC       Thr-58. Phosphorylation at Thr-58 and Ser-62 by GSK3 is required
CC       for ubiquitination and degradation by the proteasome (By
CC       similarity). Phosphorylation at Ser-329 by PIM2 leads to the
CC       stabilization of MYC. Phosphorylation at Ser-62 by CDK2 prevents
CC       Ras-induced senescence (By similarity). {ECO:0000250}.
CC   -!- PTM: Ubiquitinated by the SCF(FBXW7) complex when phosphorylated
CC       at Thr-58 and Ser-62, leading to its degradation by the
CC       proteasome. In the nucleoplasm, ubiquitination is counteracted by
CC       USP28, which interacts with of FBXW7 (FBW7alpha), leading to its
CC       deubiquitination and preventing degradation. Also
CC       polyubiquitinated by the DCX(TRUSS) complex. Ubiquitinated by
CC       TRIM6 in a phosphorylation-independent manner.
CC       {ECO:0000250|UniProtKB:P01106, 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
CC       designated iPS (induced pluripotent stem) cells. iPS cells exhibit
CC       the morphology and growth properties of ES cells and express ES
CC       cell marker genes. {ECO:0000269|PubMed:20352099}.
CC       Sequence=AAH91699.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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.
DR   UniGene; Rn.12072; -.
DR   ProteinModelPortal; P09416; -.
DR   SMR; P09416; -.
DR   BioGrid; 246723; 3.
DR   DIP; DIP-28140N; -.
DR   IntAct; P09416; 3.
DR   MINT; MINT-4508782; -.
DR   STRING; 10116.ENSRNOP00000006188; -.
DR   iPTMnet; P09416; -.
DR   PhosphoSitePlus; P09416; -.
DR   PaxDb; P09416; -.
DR   PRIDE; P09416; -.
DR   Ensembl; ENSRNOT00000006188; ENSRNOP00000006188; ENSRNOG00000004500.
DR   GeneID; 24577; -.
DR   KEGG; rno:24577; -.
DR   UCSC; RGD:3130; rat.
DR   CTD; 4609; -.
DR   RGD; 3130; Myc.
DR   eggNOG; ENOG410IFSM; Eukaryota.
DR   eggNOG; ENOG41124Q3; LUCA.
DR   GeneTree; ENSGT00510000046414; -.
DR   HOGENOM; HOG000043075; -.
DR   HOVERGEN; HBG000472; -.
DR   InParanoid; P09416; -.
DR   KO; K04377; -.
DR   PhylomeDB; P09416; -.
DR   PRO; PR:P09416; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   ExpressionAtlas; P09416; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR   GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR   GO; GO:0005730; C:nucleolus; IDA:RGD.
DR   GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:RGD.
DR   GO; GO:0003677; F:DNA binding; IDA: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:0032403; F:protein complex binding; ISS:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:RGD.
DR   GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISS:UniProtKB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
DR   GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:RGD.
DR   GO; GO:0008134; F:transcription factor binding; IPI:RGD.
DR   GO; GO:0006865; P:amino acid transport; IMP:RGD.
DR   GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; ISS:UniProtKB.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; ISS:UniProtKB.
DR   GO; GO:0044330; P:canonical Wnt signaling pathway involved in positive regulation of wound healing; IMP:RGD.
DR   GO; GO:0008283; P:cell proliferation; IMP:RGD.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; ISS:UniProtKB.
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:1904620; P:cellular response to dimethyl sulfoxide; IEP:RGD.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR   GO; GO:0035690; P:cellular response to drug; 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:0032869; P:cellular response to insulin stimulus; IEP:RGD.
DR   GO; GO:0071346; P:cellular response to interferon-gamma; IEP: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:0006338; P:chromatin remodeling; ISS:UniProtKB.
DR   GO; GO:0051276; P:chromosome organization; ISS:UniProtKB.
DR   GO; GO:0006352; P:DNA-templated transcription, initiation; IDA:RGD.
DR   GO; GO:0009812; P:flavonoid metabolic process; IEP:RGD.
DR   GO; GO:0071966; P:fungal-type cell wall polysaccharide metabolic process; IEP:RGD.
DR   GO; GO:0045023; P:G0 to G1 transition; IEP:RGD.
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: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:0060548; P:negative regulation of cell death; IMP:RGD.
DR   GO; GO:0051782; P:negative regulation of cell division; ISS:UniProtKB.
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 from RNA polymerase II promoter; IMP:UniProtKB.
DR   GO; GO:0001541; P:ovarian follicle development; IEP:RGD.
DR   GO; GO:0030728; P:ovulation; IEP:RGD.
DR   GO; GO:0009405; P:pathogenesis; TAS:RGD.
DR   GO; GO:2001171; P:positive regulation of ATP biosynthetic process; IMP:RGD.
DR   GO; GO:0045787; P:positive regulation of cell cycle; IMP:RGD.
DR   GO; GO:0008284; P:positive regulation of cell 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:0043388; P:positive regulation of DNA binding; IMP:RGD.
DR   GO; GO:2000573; P:positive regulation of DNA biosynthetic process; ISS: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: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: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: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:2001022; P:positive regulation of response to DNA damage stimulus; ISS:UniProtKB.
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 from RNA polymerase II promoter; IMP:RGD.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
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:0007346; P:regulation of mitotic cell cycle; IMP:RGD.
DR   GO; GO:0002082; P:regulation of oxidative phosphorylation; IMP:RGD.
DR   GO; GO:0032204; P:regulation of telomere maintenance; ISS:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA: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:0009611; P:response to wounding; IEP:RGD.
DR   GO; GO:0006366; P:transcription from RNA polymerase II promoter; IDA:RGD.
DR   GO; GO:0006351; P:transcription, DNA-templated; IDA:RGD.
DR   GO; GO:0019087; P:transformation of host cell by virus; IMP:RGD.
DR   CDD; cd00083; HLH; 1.
DR   Gene3D;; -; 1.
DR   InterPro; IPR011598; bHLH_dom.
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   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; SSF47459; 1.
DR   PROSITE; PS50888; BHLH; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; Complete proteome; DNA-binding; Glycoprotein;
KW   Isopeptide bond; Nucleus; Phosphoprotein; Proto-oncogene;
KW   Reference proteome; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   CHAIN         1    439       Myc proto-oncogene protein.
FT                                /FTId=PRO_0000127300.
FT   DOMAIN      354    406       bHLH. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00981}.
FT   REGION      413    434       Leucine-zipper.
FT   COMPBIAS     34     37       Poly-Gln.
FT   COMPBIAS     89     92       Poly-Gly.
FT   COMPBIAS    218    223       Poly-Ser.
FT   MOD_RES       6      6       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P01106}.
FT   MOD_RES      58     58       Phosphothreonine; by GSK3; alternate.
FT                                {ECO:0000250|UniProtKB:P01106}.
FT   MOD_RES      62     62       Phosphoserine; by DYRK2, GSK3 and CDK2.
FT                                {ECO:0000250|UniProtKB:P01106}.
FT   MOD_RES      71     71       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P01106}.
FT   MOD_RES     144    144       N6-acetyllysine; by PCAF; alternate.
FT                                {ECO:0000250|UniProtKB:P01106}.
FT   MOD_RES     149    149       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P01106}.
FT   MOD_RES     158    158       N6-acetyllysine; by PCAF.
FT                                {ECO:0000250|UniProtKB:P01106}.
FT   MOD_RES     162    162       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P01106}.
FT   MOD_RES     275    275       N6-acetyllysine; by PCAF.
FT                                {ECO:0000250|UniProtKB:P01106}.
FT   MOD_RES     293    293       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P01106}.
FT   MOD_RES     317    317       N6-acetyllysine; by PCAF.
FT                                {ECO:0000250|UniProtKB:P01106}.
FT   MOD_RES     323    323       N6-acetyllysine; by PCAF.
FT                                {ECO:0000250|UniProtKB:P01106}.
FT   MOD_RES     329    329       Phosphoserine; by PIM2; in vitro.
FT                                {ECO:0000250|UniProtKB:P01108}.
FT   MOD_RES     371    371       N6-acetyllysine; by PCAF.
FT                                {ECO:0000250|UniProtKB:P01106}.
FT   CARBOHYD     58     58       O-linked (GlcNAc) threonine; alternate.
FT                                {ECO:0000250}.
FT   CROSSLNK     52     52       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:P01106}.
FT   CROSSLNK    144    144       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2);
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:P01106}.
FT   CROSSLNK    149    149       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2);
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:P01106}.
FT   CROSSLNK    298    298       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:P01106}.
SQ   SEQUENCE   439 AA;  48898 MW;  7547DCCECF74554F CRC64;
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