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

 MYC_PTEHP               Reviewed;         440 AA.
Q9MZT8;
15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-OCT-2017, entry version 88.
RecName: Full=Myc proto-oncogene protein;
AltName: Full=Proto-oncogene c-Myc;
AltName: Full=Transcription factor p64;
Name=MYC;
Pteropus hypomelanus (Island flying fox) (Variable flying fox).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Chiroptera; Megachiroptera;
Pteropodidae; Pteropodinae; Pteropus.
NCBI_TaxID=9405;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=12116424; DOI=10.1080/10635159950127367;
Miyamoto M.M., Porter C.A., Goodman M.;
"c-myc gene sequences and the phylogeny of bats and other eutherian
mammals.";
Syst. Biol. 49:501-514(2000).
-!- 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.
Phosphorylation at Ser-330 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}.
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EMBL; AF160487; AAF80395.1; -; Genomic_DNA.
EMBL; AF160486; AAF80395.1; JOINED; Genomic_DNA.
ProteinModelPortal; Q9MZT8; -.
SMR; Q9MZT8; -.
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.
3: Inferred from homology;
Acetylation; Activator; DNA-binding; Glycoprotein; Isopeptide bond;
Nucleus; Phosphoprotein; Proto-oncogene; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 440 Myc proto-oncogene protein.
/FTId=PRO_0000127299.
DOMAIN 355 407 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
REGION 414 435 Leucine-zipper.
COMPBIAS 34 37 Poly-Gln.
COMPBIAS 85 88 Poly-Asp.
COMPBIAS 89 92 Poly-Gly.
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 276 276 N6-acetyllysine; by PCAF.
{ECO:0000250|UniProtKB:P01106}.
MOD_RES 294 294 Phosphoserine.
{ECO:0000250|UniProtKB:P01106}.
MOD_RES 318 318 N6-acetyllysine; by PCAF.
{ECO:0000250|UniProtKB:P01106}.
MOD_RES 324 324 N6-acetyllysine; by PCAF.
{ECO:0000250|UniProtKB:P01106}.
MOD_RES 330 330 Phosphoserine; by PIM2; in vitro.
{ECO:0000250|UniProtKB:P01108}.
MOD_RES 372 372 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 299 299 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P01106}.
SEQUENCE 440 AA; 48796 MW; 95D61CEA3A7347AF CRC64;
MPLNVSFASR NYDLDYDSVQ PYFYCDEEEN FYHQQQQSEL QPPAPSEDIW KKFELLPTPP
LSPSRRSGLC SPSYVAAFAS FSPRDDDDGG GGSFSSADQL EMVTELLGGD MVNQSFICDP
DDETFIKNII IQDCMWSGFS AAAKLVSEKL ASYQAARKDG GSRSPARGHS ACSTSSLYLQ
DLSAAASECI DPSVVFPYPL NDSSSPKPCA SPDSTAFSPS SDSLLSSAAS SPRASPEPLV
LHEETPPTTS SDSEEEQEDE EEIDVVSVEK RQPPAKRSES GSPSAGSHSK PPHSPLVLKR
CHVSTHQHNY AAPPSTRKDY PPTKRAKLDS GRVLKQISNN RKCASPRSSD TEENDKRRTH
NVLERQRRNE LKRSFFALRD QIPELENNEK APKVVILKKA TAYILAIQAE EQKLISEKDL
LRKRREQLKH KLEQLRNSCA


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