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

 MYC_MARMO               Reviewed;         439 AA.
P22555;
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
15-DEC-1998, sequence version 2.
25-OCT-2017, entry version 106.
RecName: Full=Myc proto-oncogene protein;
AltName: Full=Proto-oncogene c-Myc;
AltName: Full=Transcription factor p64;
Name=MYC;
Marmota monax (Woodchuck).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha;
Sciuridae; Xerinae; Marmotini; Marmota.
NCBI_TaxID=9995;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Hepatoma;
PubMed=2644611;
Etiemble J., Moeroey T., Jacquemin E., Tiollais P., Buendia M.-A.;
"Fused transcripts of c-myc and a new cellular locus, hcr in a primary
liver tumor.";
Oncogene 4:51-57(1989).
-!- 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.
Binds to the VEGFA promoter, promoting VEGFA production and
subsequent sprouting angiogenesis. {ECO:0000250|UniProtKB:P01106}.
-!- 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. The
heterodimer MYC:MAX interacts with ABI1; the interaction may
enhance MYC:MAX transcriptional activity. 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}.
-!- 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}.
-!- SEQUENCE CAUTION:
Sequence=CAA31619.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; X13232; CAA31619.1; ALT_INIT; mRNA.
PIR; S03325; S03325.
ProteinModelPortal; P22555; -.
SMR; P22555; -.
HOVERGEN; HBG000472; -.
GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
GO; GO:0070888; F:E-box binding; ISS:UniProtKB.
GO; GO:0032403; F:protein complex binding; ISS:UniProtKB.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0060070; P:canonical Wnt signaling pathway; ISS:UniProtKB.
GO; GO:0006879; P:cellular iron ion homeostasis; ISS:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
GO; GO:0051276; P:chromosome organization; ISS:UniProtKB.
GO; GO:0000165; P:MAPK cascade; ISS:UniProtKB.
GO; GO:0051782; P:negative regulation of cell division; ISS:UniProtKB.
GO; GO:0045656; P:negative regulation of monocyte differentiation; ISS:UniProtKB.
GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
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; ISS:UniProtKB.
GO; GO:2001022; P:positive regulation of response to DNA damage stimulus; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0032204; P:regulation of telomere maintenance; ISS:UniProtKB.
GO; GO:0010332; P:response to gamma radiation; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
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.
2: Evidence at transcript level;
Acetylation; Activator; DNA-binding; Glycoprotein; Isopeptide bond;
Nucleus; Phosphoprotein; Proto-oncogene; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 439 Myc proto-oncogene protein.
/FTId=PRO_0000127295.
DOMAIN 354 406 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
REGION 413 434 Leucine-zipper.
COMPBIAS 33 37 Poly-Gln.
COMPBIAS 88 91 Poly-Gly.
COMPBIAS 172 175 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 143 143 N6-acetyllysine; by PCAF; alternate.
{ECO:0000250|UniProtKB:P01106}.
MOD_RES 148 148 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P01106}.
MOD_RES 157 157 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 143 143 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P01106}.
CROSSLNK 148 148 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; 48705 MW; 7DC4CF7775E9E285 CRC64;
MPLNVSFANR NYDLDYDSVQ PYFYCDEEEN FYQQQQQSEL QPPAPSEDIW KKFELLPTPP
LSPSRRSGLC SPPCVTVASF SPPGDDDGGG GSFSTADQLE MVTELLGGDM VNQSFICDPD
DETFIKNIII QDCMWSGFSA AAKLVSEKLA SYQAARKDTG CPSPARGHSG CSSSSLYLQD
LSPRASECID PSVVFPYPLN DSSSPKPCAS PDSTAFSPSS DSLLSSTESS PRASPEPLVL
HEETPPTTSS DSEEEQEDEE EIDVVSVEKR QPSARRSESV SPPAGSHSKP PHSPLVLKRC
HVSTHQHNYA APPSTRKDCP AAKRAKLDSG RVLKQISNNR KCASPRSSDT EENDKRRTHN
VLERQRRNEL KRSFFALRDQ IPELENNEKA PKVIILKKAT AYILSVQAEE QKLISEKDLL
RKRREQLKQK LEQLRNSCA


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