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Database: UniProt/SWISS-PROT
Entry: MYC_RAT
LinkDB: 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   01-OCT-2014, entry version 134.
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; Sciurognathi;
OC   Muroidea; Muridae; 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 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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
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.,
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]
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
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 NO66. The heterodimer
CC       MYC:MAX interacts with ABI1; the interaction may enhance MYC:MAX
CC       transcriptional activity. {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 (By similarity).
CC       {ECO:0000250}.
CC   -!- DISEASE: Note=Overexpression of C-Myc is implicated in the
CC       etiology of a variety of hematopoietic tumors.
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   -!- SIMILARITY: Contains 1 bHLH (basic helix-loop-helix) domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00981}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH91699.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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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; 353-434.
DR   BioGrid; 246723; 3.
DR   DIP; DIP-28140N; -.
DR   IntAct; P09416; 2.
DR   MINT; MINT-4508782; -.
DR   PhosphoSite; P09416; -.
DR   PaxDb; P09416; -.
DR   PRIDE; P09416; -.
DR   GeneID; 24577; -.
DR   KEGG; rno:24577; -.
DR   UCSC; RGD:3130; rat.
DR   CTD; 4609; -.
DR   RGD; 3130; Myc.
DR   eggNOG; NOG42590; -.
DR   HOGENOM; HOG000043075; -.
DR   HOVERGEN; HBG000472; -.
DR   InParanoid; P09416; -.
DR   KO; K04377; -.
DR   PhylomeDB; P09416; -.
DR   NextBio; 603730; -.
DR   PRO; PR:P09416; -.
DR   ArrayExpress; P09416; -.
DR   Genevestigator; P09416; -.
DR   GO; GO:0030424; C:axon; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR   GO; GO:0005739; C:mitochondrion; IMP:GOC.
DR   GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR   GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:RGD.
DR   GO; GO:0005819; C:spindle; IEA:Ensembl.
DR   GO; GO:0000987; F:core promoter proximal region sequence-specific DNA binding; IEA:Ensembl.
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:0043565; F:sequence-specific DNA binding; IDA:RGD.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:RGD.
DR   GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
DR   GO; GO:0006865; P:amino acid transport; IMP:RGD.
DR   GO; GO:0001783; P:B cell apoptotic process; IEA:Ensembl.
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:0044336; P:canonical Wnt signaling pathway involved in negative regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0044337; P:canonical Wnt signaling pathway involved in positive regulation of apoptotic process; IEA:Ensembl.
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:0071322; P:cellular response to carbohydrate stimulus; IEP:RGD.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR   GO; GO:0035690; P:cellular response to drug; IEA:Ensembl.
DR   GO; GO:0071391; P:cellular response to estrogen stimulus; IEP:RGD.
DR   GO; GO:0071464; P:cellular response to hydrostatic pressure; IEP:RGD.
DR   GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
DR   GO; GO:0071407; P:cellular response to organic cyclic compound; 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; IEA:Ensembl.
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:0009100; P:glycoprotein metabolic process; IEP: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:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
DR   GO; GO:0046722; P:lactic acid secretion; IMP:RGD.
DR   GO; GO:0000165; P:MAPK cascade; ISS:UniProtKB.
DR   GO; GO:0042474; P:middle ear morphogenesis; IEA:Ensembl.
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:0032091; P:negative regulation of protein binding; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
DR   GO; GO:0009405; P:pathogenesis; TAS:RGD.
DR   GO; GO:0043473; P:pigmentation; IEA:Ensembl.
DR   GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IEA:Ensembl.
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; IEA:Ensembl.
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: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; ISS:UniProtKB.
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:2001022; P:positive regulation of response to DNA damage stimulus; ISS:UniProtKB.
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: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:0043279; P:response to alkaloid; IEA:Ensembl.
DR   GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR   GO; GO:0010332; P:response to gamma radiation; ISS:UniProtKB.
DR   GO; GO:0009611; P:response to wounding; IEP:RGD.
DR   GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl.
DR   GO; GO:0048705; P:skeletal system morphogenesis; IEA:Ensembl.
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   Gene3D; 4.10.280.10; -; 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   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; Complete proteome; DNA-binding; Glycoprotein;
KW   Nucleus; Phosphoprotein; Proto-oncogene; Reference proteome;
KW   Transcription; Transcription regulation; 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. {ECO:0000250}.
FT   MOD_RES      58     58       Phosphothreonine; by GSK3; alternate.
FT                                {ECO:0000250}.
FT   MOD_RES      62     62       Phosphoserine; by DYRK2, GSK3 and CDK2.
FT                                {ECO:0000250}.
FT   MOD_RES      71     71       Phosphoserine. {ECO:0000250}.
FT   MOD_RES     144    144       N6-acetyllysine; by PCAF. {ECO:0000250}.
FT   MOD_RES     149    149       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES     158    158       N6-acetyllysine; by PCAF. {ECO:0000250}.
FT   MOD_RES     162    162       Phosphoserine. {ECO:0000250}.
FT   MOD_RES     275    275       N6-acetyllysine; by PCAF. {ECO:0000250}.
FT   MOD_RES     317    317       N6-acetyllysine; by PCAF. {ECO:0000250}.
FT   MOD_RES     323    323       N6-acetyllysine; by PCAF. {ECO:0000250}.
FT   MOD_RES     329    329       Phosphoserine; by PIM2; in vitro.
FT                                {ECO:0000250}.
FT   MOD_RES     371    371       N6-acetyllysine; by PCAF. {ECO:0000250}.
FT   CARBOHYD     58     58       O-linked (GlcNAc); alternate.
FT                                {ECO:0000250}.
SQ   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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