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 13-NOV-2013, entry version 128.
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).
CC -!- FUNCTION: Participates in the regulation of gene transcription.
CC Binds DNA in a non-specific manner, yet also specifically
CC recognizes the core sequence 5'-CAC[GA]TG-3'. Seems to activate
CC the transcription of growth-related genes.
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 (By similarity). Interacts with PIM2 (By similarity).
CC Interacts with NO66 (By similarity).
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm (By similarity).
CC Nucleus, nucleolus (By similarity).
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).
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 -!- 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.
CC -!- SIMILARITY: Contains 1 bHLH (basic helix-loop-helix) domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH91699.2; Type=Erroneous initiation;
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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 IPI; IPI00214655; -.
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 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 NextBio; 603730; -.
DR PRO; PR:P09416; -.
DR ArrayExpress; P09416; -.
DR Genevestigator; P09416; -.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
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: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:0006865; P:amino acid transport; IMP:RGD.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; ISS:UniProtKB.
DR GO; GO:0044330; P:canonical Wnt receptor 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: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:0006338; P:chromatin remodeling; ISS:UniProtKB.
DR GO; GO:0006352; P:DNA-dependent transcription, initiation; IDA:RGD.
DR GO; GO:0009790; P:embryo development; IEP: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:0007007; P:inner mitochondrial membrane organization; IMP:RGD.
DR GO; GO:0046722; P:lactic acid secretion; IMP: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: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: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: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 glycolysis; IMP:RGD.
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: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:0006974; P:response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0032355; P:response to estradiol stimulus; 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:0006366; P:transcription from RNA polymerase II promoter; 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.
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 (By similarity).
FT MOD_RES 58 58 Phosphothreonine; by GSK3; alternate (By
FT similarity).
FT MOD_RES 62 62 Phosphoserine; by DYRK2, GSK3 and CDK2
FT (By similarity).
FT MOD_RES 71 71 Phosphoserine (By similarity).
FT MOD_RES 144 144 N6-acetyllysine; by PCAF (By similarity).
FT MOD_RES 149 149 N6-acetyllysine (By similarity).
FT MOD_RES 158 158 N6-acetyllysine; by PCAF (By similarity).
FT MOD_RES 162 162 Phosphoserine (By similarity).
FT MOD_RES 275 275 N6-acetyllysine; by PCAF (By similarity).
FT MOD_RES 317 317 N6-acetyllysine; by PCAF (By similarity).
FT MOD_RES 323 323 N6-acetyllysine; by PCAF (By similarity).
FT MOD_RES 329 329 Phosphoserine; by PIM2; in vitro (By
FT similarity).
FT MOD_RES 371 371 N6-acetyllysine; by PCAF (By similarity).
FT CARBOHYD 58 58 O-linked (GlcNAc); alternate (By
FT similarity).
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
//
