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Myc proto-oncogene protein (Proto-oncogene c-Myc) (Transcription factor p64)

 MYC_RAT                 Reviewed;         439 AA.
P09416; Q6B500;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
25-OCT-2017, entry version 158.
RecName: Full=Myc proto-oncogene protein;
AltName: Full=Proto-oncogene c-Myc;
AltName: Full=Transcription factor p64;
Name=Myc;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3306601; DOI=10.1093/nar/15.16.6419;
Hayashi K., Makino R., Kawamura H., Arisawa A., Yoneda K.;
"Characterization of rat c-myc and adjacent regions.";
Nucleic Acids Res. 15:6419-6436(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=ACI/SegHsd, and Brown Norway/SsNHsd; TISSUE=Spleen;
Shull J.D., Buckles L.K.;
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Ovary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
BIOTECHNOLOGY.
PubMed=20352099; DOI=10.1371/journal.pone.0009838;
Chang M.Y., Kim D., Kim C.H., Kang H.C., Yang E., Moon J.I., Ko S.,
Park J., Park K.S., Lee K.A., Hwang D.Y., Chung Y., Lanza R.,
Kim K.S.;
"Direct reprogramming of rat neural precursor cells and fibroblasts
into pluripotent stem cells.";
PLoS ONE 5:E9838-E9838(2010).
[5]
FUNCTION IN TRANSCRIPTIONAL ACTIVATION, AND INTERACTION WITH ABI1.
PubMed=17304222; DOI=10.1038/sj.emboj.7601569;
Proepper C., Johannsen S., Liebau S., Dahl J., Vaida B., Bockmann J.,
Kreutz M.R., Gundelfinger E.D., Boeckers T.M.;
"Abelson interacting protein 1 (Abi-1) is essential for dendrite
morphogenesis and synapse formation.";
EMBO J. 26:1397-1409(2007).
-!- FUNCTION: Transcription factor that binds DNA in a non-specific
manner, yet also specifically recognizes the core sequence 5'-
CAC[GA]TG-3'. Activates the transcription of growth-related genes
(PubMed:17304222). Binds to the VEGFA promoter, promoting VEGFA
production and subsequent sprouting angiogenesis (By similarity).
{ECO:0000250|UniProtKB:P01106, ECO:0000269|PubMed:17304222}.
-!- SUBUNIT: Efficient DNA binding requires dimerization with another
bHLH protein. Binds DNA as a heterodimer with MAX (By similarity).
Interacts with TAF1C and SPAG9. Interacts with PARP10. Interacts
with KDM5A and KDM5B. Interacts (when phosphorylated at Thr-58 and
Ser-62) with FBXW7. Interacts with PIM2. Interacts with RIOX1 (By
similarity). The heterodimer MYC:MAX interacts with ABI1; the
interaction may enhance MYC:MAX transcriptional activity
(PubMed:17304222). Interacts with TRIM6 (By similarity). Interacts
with NPM1; the binary complex is recruited to the promoter of MYC
target genes and enhances their transcription (By similarity).
{ECO:0000250|UniProtKB:P01106, ECO:0000250|UniProtKB:P01108,
ECO:0000269|PubMed:17304222}.
-!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
{ECO:0000250|UniProtKB:P01106}. Nucleus, nucleolus
{ECO:0000250|UniProtKB:P01106}.
-!- PTM: Phosphorylated by PRKDC. Phosphorylated at Ser-62 by DYRK2;
this primes the protein for subsequent phosphorylation by GSK3B at
Thr-58. Phosphorylation at Thr-58 and Ser-62 by GSK3 is required
for ubiquitination and degradation by the proteasome (By
similarity). Phosphorylation at Ser-329 by PIM2 leads to the
stabilization of MYC. Phosphorylation at Ser-62 by CDK2 prevents
Ras-induced senescence (By similarity). {ECO:0000250}.
-!- PTM: Ubiquitinated by the SCF(FBXW7) complex when phosphorylated
at Thr-58 and Ser-62, leading to its degradation by the
proteasome. In the nucleoplasm, ubiquitination is counteracted by
USP28, which interacts with of FBXW7 (FBW7alpha), leading to its
deubiquitination and preventing degradation. Also
polyubiquitinated by the DCX(TRUSS) complex. Ubiquitinated by
TRIM6 in a phosphorylation-independent manner.
{ECO:0000250|UniProtKB:P01106, ECO:0000250|UniProtKB:P01108}.
-!- BIOTECHNOLOGY: POU5F1/OCT4, SOX2, MYC/c-Myc and KLF4 are the four
Yamanaka factors. When combined, these factors are sufficient to
reprogram differentiated cells to an embryonic-like state
designated iPS (induced pluripotent stem) cells. iPS cells exhibit
the morphology and growth properties of ES cells and express ES
cell marker genes. {ECO:0000269|PubMed:20352099}.
-!- SEQUENCE CAUTION:
Sequence=AAH91699.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; Y00396; CAA68459.2; -; Genomic_DNA.
EMBL; AY679729; AAT92511.1; -; mRNA.
EMBL; AY679730; AAT92512.1; -; mRNA.
EMBL; BC091699; AAH91699.2; ALT_INIT; mRNA.
PIR; A26801; TVRTMC.
RefSeq; NP_036735.2; NM_012603.2.
UniGene; Rn.12072; -.
ProteinModelPortal; P09416; -.
SMR; P09416; -.
BioGrid; 246723; 3.
CORUM; P09416; -.
DIP; DIP-28140N; -.
IntAct; P09416; 3.
MINT; MINT-4508782; -.
STRING; 10116.ENSRNOP00000006188; -.
iPTMnet; P09416; -.
PhosphoSitePlus; P09416; -.
PaxDb; P09416; -.
PRIDE; P09416; -.
Ensembl; ENSRNOT00000006188; ENSRNOP00000006188; ENSRNOG00000004500.
GeneID; 24577; -.
KEGG; rno:24577; -.
UCSC; RGD:3130; rat.
CTD; 4609; -.
RGD; 3130; Myc.
eggNOG; ENOG410IFSM; Eukaryota.
eggNOG; ENOG41124Q3; LUCA.
GeneTree; ENSGT00510000046414; -.
HOGENOM; HOG000043075; -.
HOVERGEN; HBG000472; -.
InParanoid; P09416; -.
KO; K04377; -.
PhylomeDB; P09416; -.
Reactome; R-RNO-5689880; Ub-specific processing proteases.
Reactome; R-RNO-8866911; TFAP2 (AP-2) family regulates transcription of cell cycle factors.
PRO; PR:P09416; -.
Proteomes; UP000002494; Chromosome 7.
ExpressionAtlas; P09416; baseline and differential.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005739; C:mitochondrion; IEA:GOC.
GO; GO:0005730; C:nucleolus; IDA:RGD.
GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0003677; F:DNA binding; IDA:RGD.
GO; GO:0003690; F:double-stranded DNA binding; IDA:RGD.
GO; GO:0070888; F:E-box binding; ISS:UniProtKB.
GO; GO:0032403; F:protein complex binding; ISS:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IPI:RGD.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:RGD.
GO; GO:0008134; F:transcription factor binding; IPI:RGD.
GO; GO:0006865; P:amino acid transport; IMP:RGD.
GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; ISS:UniProtKB.
GO; GO:0060070; P:canonical Wnt signaling pathway; ISS:UniProtKB.
GO; GO:0044330; P:canonical Wnt signaling pathway involved in positive regulation of wound healing; IMP:RGD.
GO; GO:0008283; P:cell proliferation; IMP:RGD.
GO; GO:0006879; P:cellular iron ion homeostasis; ISS:UniProtKB.
GO; GO:1904385; P:cellular response to angiotensin; IEP:RGD.
GO; GO:1903841; P:cellular response to arsenite(3-); IEP:RGD.
GO; GO:0071322; P:cellular response to carbohydrate stimulus; IEP:RGD.
GO; GO:0071409; P:cellular response to cycloheximide; IEP:RGD.
GO; GO:1904620; P:cellular response to dimethyl sulfoxide; IEP:RGD.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
GO; GO:0035690; P:cellular response to drug; IEP:RGD.
GO; GO:1990859; P:cellular response to endothelin; IEP:RGD.
GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEP:RGD.
GO; GO:0071391; P:cellular response to estrogen stimulus; IEP:RGD.
GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEP:RGD.
GO; GO:0071378; P:cellular response to growth hormone stimulus; IEP:RGD.
GO; GO:0071464; P:cellular response to hydrostatic pressure; IEP:RGD.
GO; GO:0032869; P:cellular response to insulin stimulus; IEP:RGD.
GO; GO:0071346; P:cellular response to interferon-gamma; IEP:RGD.
GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
GO; GO:1990858; P:cellular response to lectin; IEP:RGD.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
GO; GO:1904628; P:cellular response to phorbol 13-acetate 12-myristate; IEP:RGD.
GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IEP:RGD.
GO; GO:1990646; P:cellular response to prolactin; IEP:RGD.
GO; GO:1904586; P:cellular response to putrescine; IEP:RGD.
GO; GO:0071300; P:cellular response to retinoic acid; IEP:RGD.
GO; GO:0071394; P:cellular response to testosterone stimulus; IEP:RGD.
GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
GO; GO:0051276; P:chromosome organization; ISS:UniProtKB.
GO; GO:0006352; P:DNA-templated transcription, initiation; IDA:RGD.
GO; GO:0009812; P:flavonoid metabolic process; IEP:RGD.
GO; GO:0071966; P:fungal-type cell wall polysaccharide metabolic process; IEP:RGD.
GO; GO:0045023; P:G0 to G1 transition; IEP:RGD.
GO; GO:0006006; P:glucose metabolic process; IMP:RGD.
GO; GO:0021854; P:hypothalamus development; IEP:RGD.
GO; GO:0001701; P:in utero embryonic development; IEP:RGD.
GO; GO:0007007; P:inner mitochondrial membrane organization; IMP:RGD.
GO; GO:0046722; P:lactic acid secretion; IMP:RGD.
GO; GO:0097421; P:liver regeneration; IEP:RGD.
GO; GO:0000165; P:MAPK cascade; ISS:UniProtKB.
GO; GO:0060548; P:negative regulation of cell death; IMP:RGD.
GO; GO:0051782; P:negative regulation of cell division; ISS:UniProtKB.
GO; GO:0010629; P:negative regulation of gene expression; IMP:RGD.
GO; GO:0046325; P:negative regulation of glucose import; IMP:RGD.
GO; GO:0045656; P:negative regulation of monocyte differentiation; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:0001541; P:ovarian follicle development; IEP:RGD.
GO; GO:0030728; P:ovulation; IEP:RGD.
GO; GO:0009405; P:pathogenesis; TAS:RGD.
GO; GO:2001171; P:positive regulation of ATP biosynthetic process; IMP:RGD.
GO; GO:0045787; P:positive regulation of cell cycle; IMP:RGD.
GO; GO:0008284; P:positive regulation of cell proliferation; IGI:RGD.
GO; GO:1901857; P:positive regulation of cellular respiration; IMP:RGD.
GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
GO; GO:0043388; P:positive regulation of DNA binding; IMP:RGD.
GO; GO:2000573; P:positive regulation of DNA biosynthetic process; ISS:UniProtKB.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISS:UniProtKB.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:RGD.
GO; GO:0060252; P:positive regulation of glial cell proliferation; IMP:RGD.
GO; GO:0045821; P:positive regulation of glycolytic process; IMP:RGD.
GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; ISS:UniProtKB.
GO; GO:0090096; P:positive regulation of metanephric cap mesenchymal cell proliferation; ISS:UniProtKB.
GO; GO:0010918; P:positive regulation of mitochondrial membrane potential; IMP:RGD.
GO; GO:1903862; P:positive regulation of oxidative phosphorylation; IMP:RGD.
GO; GO:2001022; P:positive regulation of response to DNA damage stimulus; ISS:UniProtKB.
GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IMP:RGD.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:RGD.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:RGD.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0006848; P:pyruvate transport; IMP:RGD.
GO; GO:0000320; P:re-entry into mitotic cell cycle; IMP:RGD.
GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:RGD.
GO; GO:0002082; P:regulation of oxidative phosphorylation; IMP:RGD.
GO; GO:0032204; P:regulation of telomere maintenance; ISS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0045471; P:response to ethanol; IEP:RGD.
GO; GO:0010332; P:response to gamma radiation; ISS:UniProtKB.
GO; GO:0044752; P:response to human chorionic gonadotropin; IEP:RGD.
GO; GO:0009611; P:response to wounding; IEP:RGD.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; IDA:RGD.
GO; GO:0006351; P:transcription, DNA-templated; IDA:RGD.
GO; GO:0019087; P:transformation of host cell by virus; IMP:RGD.
CDD; cd00083; HLH; 1.
Gene3D; 4.10.280.10; -; 1.
InterPro; IPR011598; bHLH_dom.
InterPro; IPR036638; HLH_DNA-bd_sf.
InterPro; IPR003327; Myc-LZ.
InterPro; IPR002418; Tscrpt_reg_Myc.
InterPro; IPR012682; Tscrpt_reg_Myc_N.
Pfam; PF00010; HLH; 1.
Pfam; PF02344; Myc-LZ; 1.
Pfam; PF01056; Myc_N; 1.
PIRSF; PIRSF001705; Myc_protein; 1.
PRINTS; PR00044; LEUZIPPRMYC.
SMART; SM00353; HLH; 1.
SUPFAM; SSF47459; SSF47459; 1.
PROSITE; PS50888; BHLH; 1.
1: Evidence at protein level;
Acetylation; Activator; Complete proteome; DNA-binding; Glycoprotein;
Isopeptide bond; Nucleus; Phosphoprotein; Proto-oncogene;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 439 Myc proto-oncogene protein.
/FTId=PRO_0000127300.
DOMAIN 354 406 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
REGION 413 434 Leucine-zipper.
COMPBIAS 34 37 Poly-Gln.
COMPBIAS 89 92 Poly-Gly.
COMPBIAS 218 223 Poly-Ser.
MOD_RES 6 6 Phosphoserine.
{ECO:0000250|UniProtKB:P01106}.
MOD_RES 58 58 Phosphothreonine; by GSK3; alternate.
{ECO:0000250|UniProtKB:P01106}.
MOD_RES 62 62 Phosphoserine; by DYRK2, GSK3 and CDK2.
{ECO:0000250|UniProtKB:P01106}.
MOD_RES 71 71 Phosphoserine.
{ECO:0000250|UniProtKB:P01106}.
MOD_RES 144 144 N6-acetyllysine; by PCAF; alternate.
{ECO:0000250|UniProtKB:P01106}.
MOD_RES 149 149 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P01106}.
MOD_RES 158 158 N6-acetyllysine; by PCAF.
{ECO:0000250|UniProtKB:P01106}.
MOD_RES 162 162 Phosphoserine.
{ECO:0000250|UniProtKB:P01106}.
MOD_RES 275 275 N6-acetyllysine; by PCAF.
{ECO:0000250|UniProtKB:P01106}.
MOD_RES 293 293 Phosphoserine.
{ECO:0000250|UniProtKB:P01106}.
MOD_RES 317 317 N6-acetyllysine; by PCAF.
{ECO:0000250|UniProtKB:P01106}.
MOD_RES 323 323 N6-acetyllysine; by PCAF.
{ECO:0000250|UniProtKB:P01106}.
MOD_RES 329 329 Phosphoserine; by PIM2; in vitro.
{ECO:0000250|UniProtKB:P01108}.
MOD_RES 371 371 N6-acetyllysine; by PCAF.
{ECO:0000250|UniProtKB:P01106}.
CARBOHYD 58 58 O-linked (GlcNAc) threonine; alternate.
{ECO:0000250}.
CROSSLNK 52 52 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P01106}.
CROSSLNK 144 144 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P01106}.
CROSSLNK 149 149 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P01106}.
CROSSLNK 298 298 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P01106}.
SEQUENCE 439 AA; 48898 MW; 7547DCCECF74554F CRC64;
MPLNVSFANR NYDLDYDSVQ PYFICDEEEN FYHQQQQSEL QPPAPSEDIW KKFELLPTPP
LSPSRRSGLC SPSYVAVATS FSPREDDDGG GGNFSTADQL EMMTELLGGD MVNQSFICDP
DDETFIKNII IQDCMWSGFS AAAKLVSEKL ASYQAARKDS TSLSPARGHS VCSTSSLYLQ
DLTAAASECI DPSVVFPYPL NDSSSPKSCT SSDSTAFSSS SDSLLSSESS PRATPEPLVL
HEETPPTTSS DSEEEQDDEE EIDVVSVEKR QPPAKRSESG SSPSRGHSKP PHSPLVLKRC
HVSTHQHNYA APPSTRKDYP AAKRAKLDSG RVLKQISNNR KCSSPRSSDT EENDKRRTHN
VLERQRRNEL KRSFFALRDQ IPELENNEKA PKVVILKKAT AYILSVQADE HKLISEKDLL
RKRREQLKHK LEQLRNSGA


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