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Myc proto-oncogene protein (Class E basic helix-loop-helix protein 39) (bHLHe39) (Proto-oncogene c-Myc) (Transcription factor p64)

 MYC_HUMAN               Reviewed;         439 AA.
P01106; A8WFE7; P01107; Q14026;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 1.
30-AUG-2017, entry version 226.
RecName: Full=Myc proto-oncogene protein;
AltName: Full=Class E basic helix-loop-helix protein 39;
Short=bHLHe39;
AltName: Full=Proto-oncogene c-Myc;
AltName: Full=Transcription factor p64;
Name=MYC; Synonyms=BHLHE39;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM
1).
PubMed=6414718; DOI=10.1016/0092-8674(83)90534-2;
Battey J., Moulding C., Taub R., Murphy W., Stewart T., Potter H.,
Lenoir G., Leder P.;
"The human c-myc oncogene: structural consequences of translocation
into the IgH locus in Burkitt lymphoma.";
Cell 34:779-787(1983).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM
1).
PubMed=6321164;
Bernard O., Cory S., Gerondakis S., Webb E., Adams J.M.;
"Sequence of the murine and human cellular myc oncogenes and two modes
of myc transcription resulting from chromosome translocation in B
lymphoid tumours.";
EMBO J. 2:2375-2383(1983).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM
1).
PubMed=6298632; DOI=10.1038/301722a0;
Colby W.W., Chen E.Y., Smith D.H., Levinson A.D.;
"Identification and nucleotide sequence of a human locus homologous to
the v-myc oncogene of avian myelocytomatosis virus MC29.";
Nature 301:722-725(1983).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=6304538; DOI=10.1038/303725a0;
Watt R., Stanton L.W., Marcu K.B., Gallo R.C., Croce C.M., Rovera G.;
"Nucleotide sequence of cloned cDNA of human c-myc oncogene.";
Nature 303:725-728(1983).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ASP-39.
PubMed=6419122; DOI=10.1038/306760a0;
Rabbitts T.H., Hamlyn P.H., Baer R.;
"Altered nucleotide sequences of a translocated c-myc gene in Burkitt
lymphoma.";
Nature 306:760-765(1983).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM
1).
PubMed=6304729; DOI=10.1073/pnas.80.12.3642;
Watson D.K., Psallidopoulos M.C., Samuel K.P., Dalla-Favera R.,
Papas T.S.;
"Nucleotide sequence analysis of human c-myc locus, chicken homologue,
and myelocytomatosis virus MC29 transforming gene reveals a highly
conserved gene product.";
Proc. Natl. Acad. Sci. U.S.A. 80:3642-3645(1983).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
[GENOMIC DNA] OF 1-252.
PubMed=6547209; DOI=10.1038/309592a0;
Rabbitts T.H., Forster A., Hamlyn P., Baer R.;
"Effect of somatic mutation within translocated c-myc genes in
Burkitt's lymphoma.";
Nature 309:592-597(1984).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM
1).
PubMed=6714223;
Gazin C., Dupont S., de Dinechin D., Hampe A., Masson J.-M.,
Martin P., Stehelin D., Galibert F.;
"Nucleotide sequence of the human c-myc locus: provocative open
reading frame within the first exon.";
EMBO J. 3:383-387(1984).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS
1 AND 2).
PubMed=8444346; DOI=10.1016/0378-1119(93)90398-M;
Tachibana K., Takayama N., Matsuo K., Kato S., Yamamoto K., Ohyama K.,
Umezawa A., Takano T.;
"Allele-specific activation of the c-myc gene in an atypical Burkitt's
lymphoma carrying the t(2;8) chromosomal translocation 250 kb
downstream from c-myc.";
Gene 124:231-237(1993).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-11; CYS-160;
ILE-170 AND VAL-322.
NIEHS SNPs program;
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Uterus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[14]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[15]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Cervix, Placenta, and Testis;
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).
[16]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-170 (ISOFORM 1).
TISSUE=Promyelocytic leukemia;
PubMed=3540591; DOI=10.1128/MCB.6.10.3481;
Bentley D.L., Groudine M.;
"Novel promoter upstream of the human c-myc gene and regulation of c-
myc expression in B-cell lymphomas.";
Mol. Cell. Biol. 6:3481-3489(1986).
[17]
INVOLVEMENT IN BURKITT LYMPHOMA.
PubMed=2166998;
Magrath I.;
"The pathogenesis of Burkitt's lymphoma.";
Adv. Cancer Res. 55:133-270(1990).
[18]
PHOSPHORYLATION.
PubMed=1597196; DOI=10.1111/j.1432-1033.1992.tb16964.x;
Iijima S., Teraoka H., Date T., Tsukada K.;
"DNA-activated protein kinase in Raji Burkitt's lymphoma cells.
Phosphorylation of c-Myc oncoprotein.";
Eur. J. Biochem. 206:595-603(1992).
[19]
INVOLVEMENT IN BURKITT LYMPHOMA, AND VARIANTS ASP-39; SER-57; ALA-59
AND THR-86.
PubMed=8220424; DOI=10.1038/ng0993-56;
Bhatia K., Huppi K., Spangler G., Siwarski D., Iyer R., Magrath I.;
"Point mutations in the c-Myc transactivation domain are common in
Burkitt's lymphoma and mouse plasmacytomas.";
Nat. Genet. 5:56-61(1993).
[20]
PHOSPHORYLATION AT THR-58 AND SER-62.
PubMed=8386367; DOI=10.1073/pnas.90.8.3216;
Gupta S., Seth A., Davis R.J.;
"Transactivation of gene expression by Myc is inhibited by mutation at
the phosphorylation sites Thr-58 and Ser-62.";
Proc. Natl. Acad. Sci. U.S.A. 90:3216-3220(1993).
[21]
GLYCOSYLATION AT THR-58.
PubMed=7642555; DOI=10.1074/jbc.270.32.18961;
Chou T.-Y., Hart G.W., Dang C.V.;
"c-Myc is glycosylated at threonine 58, a known phosphorylation site
and a mutational hot spot in lymphomas.";
J. Biol. Chem. 270:18961-18965(1995).
[22]
PHOSPHORYLATION AT THR-8.
PubMed=9315742; DOI=10.1016/S0014-5793(97)00992-7;
Alexandrov I., Shlyakhova L., Vartanian A., Zajac-Kaye M.,
Alexandrova N.;
"c-Raf kinase binds to N-terminal domain of c-Myc.";
FEBS Lett. 414:465-470(1997).
[23]
UBIQUITINATION, INTERACTION WITH FBXW7, PHOSPHORYLATION AT THR-58 AND
SER-62, AND MUTAGENESIS OF THR-58 AND SER-62.
PubMed=15103331; DOI=10.1038/sj.emboj.7600217;
Yada M., Hatakeyama S., Kamura T., Nishiyama M., Tsunematsu R.,
Imaki H., Ishida N., Okumura F., Nakayama K., Nakayama K.I.;
"Phosphorylation-dependent degradation of c-Myc is mediated by the F-
box protein Fbw7.";
EMBO J. 23:2116-2125(2004).
[24]
ACETYLATION AT LYS-143; LYS-157; LYS-275; LYS-317; LYS-323 AND
LYS-371, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16126174; DOI=10.1016/j.bbrc.2005.08.075;
Zhang K., Faiola F., Martinez E.;
"Six lysine residues on c-Myc are direct substrates for acetylation by
p300.";
Biochem. Biophys. Res. Commun. 336:274-280(2005).
[25]
INTERACTION WITH TAF1C.
PubMed=15723054; DOI=10.1038/ncb1224;
Grandori C., Gomez-Roman N., Felton-Edkins Z.A., Ngouenet C.,
Galloway D.A., Eisenman R.N., White R.J.;
"c-Myc binds to human ribosomal DNA and stimulates transcription of
rRNA genes by RNA polymerase I.";
Nat. Cell Biol. 7:311-318(2005).
[26]
INTERACTION WITH PARP10.
PubMed=15674325; DOI=10.1038/sj.onc.1208410;
Yu M., Schreek S., Cerni C., Schamberger C., Lesniewicz K., Poreba E.,
Vervoorts J., Walsemann G., Groetzinger J., Kremmer E., Mehraein Y.,
Mertsching J., Kraft R., Austen M., Luescher-Firzlaff J., Luescher B.;
"PARP-10, a novel Myc-interacting protein with poly(ADP-ribose)
polymerase activity, inhibits transformation.";
Oncogene 24:1982-1993(2005).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-58, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[28]
BIOTECHNOLOGY.
PubMed=18035408; DOI=10.1016/j.cell.2007.11.019;
Takahashi K., Tanabe K., Ohnuki M., Narita M., Ichisaka T., Tomoda K.,
Yamanaka S.;
"Induction of pluripotent stem cells from adult human fibroblasts by
defined factors.";
Cell 131:861-872(2007).
[29]
UBIQUITINATION, DEUBIQUITINATION BY USP28, AND INTERACTION WITH FBXW7.
PubMed=17873522; DOI=10.4161/cc.6.19.4804;
Popov N., Herold S., Llamazares M., Schulein C., Eilers M.;
"Fbw7 and Usp28 regulate myc protein stability in response to DNA
damage.";
Cell Cycle 6:2327-2331(2007).
[30]
INTERACTION WITH KDM5A AND KDM5B.
PubMed=17311883; DOI=10.1101/gad.1523007;
Secombe J., Li L., Carlos L., Eisenman R.N.;
"The Trithorax group protein Lid is a trimethyl histone H3K4
demethylase required for dMyc-induced cell growth.";
Genes Dev. 21:537-551(2007).
[31]
INTERACTION WITH RIOX1.
PubMed=17308053; DOI=10.1158/1535-7163.MCT-06-0659;
Suzuki C., Takahashi K., Hayama S., Ishikawa N., Kato T., Ito T.,
Tsuchiya E., Nakamura Y., Daigo Y.;
"Identification of Myc-associated protein with JmjC domain as a novel
therapeutic target oncogene for lung cancer.";
Mol. Cancer Ther. 6:542-551(2007).
[32]
UBIQUITINATION, DEUBIQUITINATION BY USP28, INTERACTION WITH FBXW7,
SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-58 AND SER-62, AND
MUTAGENESIS OF THR-58 AND SER-62.
PubMed=17558397; DOI=10.1038/ncb1601;
Popov N., Wanzel M., Madiredjo M., Zhang D., Beijersbergen R.,
Bernards R., Moll R., Elledge S.J., Eilers M.;
"The ubiquitin-specific protease USP28 is required for MYC
stability.";
Nat. Cell Biol. 9:765-774(2007).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-58; SER-62 AND SER-71,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[34]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[35]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-148, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[36]
REVIEW ON SENESCENCE, PHOSPHORYLATION AT SER-62 BY CDK2, AND
MUTAGENESIS OF THR-58 AND SER-62.
PubMed=20713526; DOI=10.1158/0008-5472.CAN-10-1383;
Hydbring P., Larsson L.-G.;
"Tipping the balance: Cdk2 enables Myc to suppress senescence.";
Cancer Res. 70:6687-6691(2010).
[37]
PHOSPHORYLATION AT SER-62 BY CDK2, AND MUTAGENESIS OF THR-58 AND
SER-62.
PubMed=19966300; DOI=10.1073/pnas.0900121106;
Hydbring P., Bahram F., Su Y., Tronnersjoe S., Hoegstrand K.,
von der Lehr N., Sharifi H.R., Lilischkis R., Hein N., Wu S.,
Vervoorts J., Henriksson M., Grandien A., Luescher B., Larsson L.-G.;
"Phosphorylation by Cdk2 is required for Myc to repress Ras-induced
senescence in cotransformation.";
Proc. Natl. Acad. Sci. U.S.A. 107:58-63(2010).
[38]
UBIQUITINATION.
PubMed=20551172; DOI=10.1101/gad.1920310;
Choi S.H., Wright J.B., Gerber S.A., Cole M.D.;
"Myc protein is stabilized by suppression of a novel E3 ligase complex
in cancer cells.";
Genes Dev. 24:1236-1241(2010).
[39]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 AND SER-161, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[40]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-58 AND SER-62, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[41]
PHOSPHORYLATION AT SER-62, AND MUTAGENESIS OF SER-62.
PubMed=22307329; DOI=10.1172/JCI60818;
Taira N., Mimoto R., Kurata M., Yamaguchi T., Kitagawa M., Miki Y.,
Yoshida K.;
"DYRK2 priming phosphorylation of c-Jun and c-Myc modulates cell cycle
progression in human cancer cells.";
J. Clin. Invest. 122:859-872(2012).
[42]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; THR-58; SER-62;
SER-71 AND SER-293, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[43]
FUNCTION, AND INTERACTION WITH NPM1.
PubMed=25956029; DOI=10.1016/j.ajpath.2015.03.016;
Kim J.Y., Cho Y.E., Park J.H.;
"The nucleolar protein GLTSCR2 is an upstream negative regulator of
the oncogenic Nucleophosmin-MYC axis.";
Am. J. Pathol. 185:2061-2068(2015).
[44]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-52; LYS-143; LYS-148 AND
LYS-298, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[45]
STRUCTURE BY NMR OF 402-434 IN COMPLEX WITH MAX.
PubMed=9680483; DOI=10.1006/jmbi.1998.1914;
Lavigne P., Crump M.P., Gagne S.M., Hodges R.S., Kay C.M., Sykes B.D.;
"Insights into the mechanism of heterodimerization from the 1H-NMR
solution structure of the c-Myc-Max heterodimeric leucine zipper.";
J. Mol. Biol. 281:165-181(1998).
[46]
CHROMOSOMAL TRANSLOCATION WITH BTG1.
PubMed=2069907; DOI=10.1002/gcc.2870030106;
Rimokh R., Rouault J.P., Wahbi K., Gadoux M., Lafage M.,
Archimbaud E., Charrin C., Gentilhomme O., Germain D., Samarut J.;
"A chromosome 12 coding region is juxtaposed to the MYC protooncogene
locus in a t(8;12)(q24;q22) translocation in a case of B-cell chronic
lymphocytic leukemia.";
Genes Chromosomes Cancer 3:24-36(1991).
-!- 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.
{ECO:0000269|PubMed:25956029}.
-!- SUBUNIT: Efficient DNA binding requires dimerization with another
bHLH protein. Binds DNA as a heterodimer with MAX. 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
(PubMed:25956029). {ECO:0000250|UniProtKB:P01108,
ECO:0000269|PubMed:15103331, ECO:0000269|PubMed:15674325,
ECO:0000269|PubMed:15723054, ECO:0000269|PubMed:17308053,
ECO:0000269|PubMed:17311883, ECO:0000269|PubMed:17558397,
ECO:0000269|PubMed:17873522, ECO:0000269|PubMed:25956029,
ECO:0000269|PubMed:9680483}.
-!- INTERACTION:
P03070:- (xeno); NbExp=2; IntAct=EBI-447544, EBI-617698;
O15169:AXIN1; NbExp=10; IntAct=EBI-447544, EBI-710484;
O00499-10:BIN1; NbExp=3; IntAct=EBI-447544, EBI-7689134;
O00499-11:BIN1; NbExp=2; IntAct=EBI-447544, EBI-7689211;
Q15059:BRD3; NbExp=3; IntAct=EBI-447544, EBI-1383460;
Q8N163:CCAR2; NbExp=8; IntAct=EBI-447544, EBI-355410;
P11802:CDK4; NbExp=2; IntAct=EBI-447544, EBI-295644;
Q86XR8:CEP57; NbExp=3; IntAct=EBI-447544, EBI-308614;
Q14839:CHD4; NbExp=2; IntAct=EBI-447544, EBI-372916;
O15111:CHUK; NbExp=3; IntAct=EBI-447544, EBI-81249;
P03129:E7 (xeno); NbExp=2; IntAct=EBI-447544, EBI-866453;
P04020:E7 (xeno); NbExp=2; IntAct=EBI-447544, EBI-7005254;
P06788:E7 (xeno); NbExp=5; IntAct=EBI-447544, EBI-1776887;
P03204:EBNA6 (xeno); NbExp=11; IntAct=EBI-447544, EBI-9255985;
Q15029:EFTUD2; NbExp=5; IntAct=EBI-447544, EBI-357897;
Q969H0:FBXW7; NbExp=4; IntAct=EBI-447544, EBI-359574;
Q8N3Y1:FBXW8; NbExp=3; IntAct=EBI-447544, EBI-914770;
O43524:FOXO3; NbExp=3; IntAct=EBI-447544, EBI-1644164;
Q92769:HDAC2; NbExp=2; IntAct=EBI-447544, EBI-301821;
O15379:HDAC3; NbExp=6; IntAct=EBI-447544, EBI-607682;
Q9Y6K9:IKBKG; NbExp=3; IntAct=EBI-447544, EBI-81279;
Q8TCG1:KIAA1524; NbExp=2; IntAct=EBI-447544, EBI-1379376;
P61244:MAX; NbExp=31; IntAct=EBI-447544, EBI-751711;
P52164:Max (xeno); NbExp=4; IntAct=EBI-447544, EBI-1184963;
P33993:MCM7; NbExp=6; IntAct=EBI-447544, EBI-355924;
O75928:PIAS2; NbExp=4; IntAct=EBI-447544, EBI-348555;
P62913:RPL11; NbExp=3; IntAct=EBI-447544, EBI-354380;
O75182:SIN3B; NbExp=7; IntAct=EBI-447544, EBI-540462;
Q62141:Sin3b (xeno); NbExp=8; IntAct=EBI-447544, EBI-591450;
Q96EB6:SIRT1; NbExp=4; IntAct=EBI-447544, EBI-1802965;
Q8N6T7:SIRT6; NbExp=3; IntAct=EBI-447544, EBI-712415;
Q13309:SKP2; NbExp=2; IntAct=EBI-447544, EBI-456291;
Q8TAD8:SNIP1; NbExp=9; IntAct=EBI-447544, EBI-749336;
P08047:SP1; NbExp=4; IntAct=EBI-447544, EBI-298336;
P11387:TOP1; NbExp=2; IntAct=EBI-447544, EBI-876302;
Q9Y4A5:TRRAP; NbExp=4; IntAct=EBI-447544, EBI-399128;
P0CG48:UBC; NbExp=5; IntAct=EBI-447544, EBI-3390054;
P17480:UBTF; NbExp=2; IntAct=EBI-447544, EBI-396235;
Q13105:ZBTB17; NbExp=9; IntAct=EBI-447544, EBI-372156;
-!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
{ECO:0000269|PubMed:17558397}. Nucleus, nucleolus
{ECO:0000269|PubMed:17558397}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P01106-1; Sequence=Displayed;
Name=2;
IsoId=P01106-2; Sequence=VSP_037813;
Note=Initiates from CTG codon. Ref.7 (BAA01374) sequence is in
conflict in position: 2:D->N. Ref.7 (BAA01374) sequence is in
conflict in position: 6:V->E. {ECO:0000305};
-!- PTM: Phosphorylated by PRKDC. Phosphorylation at Ser-329 by PIM2
leads to the stabilization of MYC (By similarity). Phosphorylation
at Ser-62 by CDK2 prevents Ras-induced senescence. 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. {ECO:0000250, ECO:0000269|PubMed:15103331,
ECO:0000269|PubMed:17558397, ECO:0000269|PubMed:19966300,
ECO:0000269|PubMed:20713526, ECO:0000269|PubMed:22307329,
ECO:0000269|PubMed:8386367}.
-!- 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 isoform 1 of FBXW7 (FBW7alpha),
leading to its deubiquitination and preventing degradation. In the
nucleolus, however, ubiquitination is not counteracted by USP28,
due to the lack of interaction between isoform 4 of FBXW7
(FBW7gamma) and USP28, explaining the selective MYC degradation in
the nucleolus. Also polyubiquitinated by the DCX(TRUSS) complex.
Ubiquitinated by TRIM6 in a phosphorylation-independent manner (By
similarity). {ECO:0000250|UniProtKB:P01108,
ECO:0000269|PubMed:15103331, ECO:0000269|PubMed:17558397,
ECO:0000269|PubMed:19966300, ECO:0000269|PubMed:20713526,
ECO:0000269|PubMed:22307329, ECO:0000269|PubMed:8386367}.
-!- DISEASE: Note=A chromosomal aberration involving MYC may be a
cause of a form of B-cell chronic lymphocytic leukemia.
Translocation t(8;12)(q24;q22) with BTG1.
{ECO:0000269|PubMed:2069907}.
-!- DISEASE: Burkitt lymphoma (BL) [MIM:113970]: A form of
undifferentiated malignant lymphoma commonly manifested as a large
osteolytic lesion in the jaw or as an abdominal mass.
{ECO:0000269|PubMed:2166998, ECO:0000269|PubMed:8220424}. Note=The
gene represented in this entry is involved in disease
pathogenesis. Chromosomal aberrations involving MYC are usually
found in Burkitt lymphoma. Translocations t(8;14), t(8;22) or
t(2;8) which juxtapose MYC to one of the heavy or light chain
immunoglobulin gene loci.
-!- 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:18035408}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/MYCID27.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/myc/";
-!- WEB RESOURCE: Name=Wikipedia; Note=Myc entry;
URL="https://en.wikipedia.org/wiki/Myc";
-----------------------------------------------------------------------
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EMBL; L00058; AAA59882.1; -; Genomic_DNA.
EMBL; L00057; AAA59882.1; JOINED; Genomic_DNA.
EMBL; K00535; AAA59880.1; -; Genomic_DNA.
EMBL; K00534; AAA59880.1; JOINED; Genomic_DNA.
EMBL; K00535; ABW69847.1; -; Genomic_DNA.
EMBL; K00534; ABW69847.1; JOINED; Genomic_DNA.
EMBL; X00196; CAA25015.2; -; Genomic_DNA.
EMBL; X00198; CAA25015.2; JOINED; Genomic_DNA.
EMBL; X00364; CAA25106.1; -; Genomic_DNA.
EMBL; V00568; CAA23831.1; -; mRNA.
EMBL; K01906; AAA59881.1; -; Genomic_DNA.
EMBL; K01905; AAA59881.1; JOINED; Genomic_DNA.
EMBL; K02276; AAA36340.1; -; mRNA.
EMBL; X00676; CAA25288.1; -; Genomic_DNA.
EMBL; D10493; BAA01374.2; -; Genomic_DNA.
EMBL; D10493; BAA01375.1; -; Genomic_DNA.
EMBL; BT019768; AAV38573.1; -; mRNA.
EMBL; AY214166; AAO21131.1; -; Genomic_DNA.
EMBL; AK312883; BAG35731.1; -; mRNA.
EMBL; AC103819; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471060; EAW92098.1; -; Genomic_DNA.
EMBL; BC000141; AAH00141.2; -; mRNA.
EMBL; BC000917; AAH00917.2; -; mRNA.
EMBL; BC058901; AAH58901.2; -; mRNA.
EMBL; M13929; AAA88092.1; -; mRNA.
CCDS; CCDS6359.2; -. [P01106-2]
PIR; A01349; TVHUM.
PIR; A01350; TVHUT.
RefSeq; NP_002458.2; NM_002467.4. [P01106-2]
UniGene; Hs.202453; -.
PDB; 1A93; NMR; -; A=406-434.
PDB; 1EE4; X-ray; 2.10 A; C/D/E/F=320-328.
PDB; 1MV0; NMR; -; A=55-68.
PDB; 1NKP; X-ray; 1.80 A; A/D=353-434.
PDB; 2A93; NMR; -; A=406-434.
PDB; 2OR9; X-ray; 2.70 A; P=410-419.
PDB; 4Y7R; X-ray; 1.90 A; B=260-267.
PDB; 5I4Z; X-ray; 1.95 A; A/B=350-439.
PDB; 5I50; X-ray; 2.70 A; A/B=350-439.
PDBsum; 1A93; -.
PDBsum; 1EE4; -.
PDBsum; 1MV0; -.
PDBsum; 1NKP; -.
PDBsum; 2A93; -.
PDBsum; 2OR9; -.
PDBsum; 4Y7R; -.
PDBsum; 5I4Z; -.
PDBsum; 5I50; -.
DisProt; DP00260; -.
ProteinModelPortal; P01106; -.
SMR; P01106; -.
BioGrid; 110694; 617.
DIP; DIP-28143N; -.
IntAct; P01106; 712.
MINT; MINT-257327; -.
STRING; 9606.ENSP00000367207; -.
BindingDB; P01106; -.
ChEMBL; CHEMBL1250348; -.
DrugBank; DB08813; Nadroparin.
iPTMnet; P01106; -.
PhosphoSitePlus; P01106; -.
UniCarbKB; P01106; -.
BioMuta; MYC; -.
DMDM; 127619; -.
SWISS-2DPAGE; P01106; -.
EPD; P01106; -.
MaxQB; P01106; -.
PaxDb; P01106; -.
PeptideAtlas; P01106; -.
PRIDE; P01106; -.
DNASU; 4609; -.
Ensembl; ENST00000377970; ENSP00000367207; ENSG00000136997. [P01106-1]
Ensembl; ENST00000613283; ENSP00000479618; ENSG00000136997. [P01106-2]
GeneID; 4609; -.
KEGG; hsa:4609; -.
UCSC; uc064qdj.1; human. [P01106-1]
CTD; 4609; -.
DisGeNET; 4609; -.
GeneCards; MYC; -.
H-InvDB; HIX0007784; -.
HGNC; HGNC:7553; MYC.
HPA; CAB000084; -.
HPA; CAB010307; -.
HPA; HPA055893; -.
HPA; HPA066556; -.
MalaCards; MYC; -.
MIM; 113970; phenotype.
MIM; 190080; gene.
neXtProt; NX_P01106; -.
OpenTargets; ENSG00000136997; -.
Orphanet; 543; Burkitt lymphoma.
Orphanet; 99861; Precursor T-cell acute lymphoblastic leukemia.
PharmGKB; PA31353; -.
eggNOG; ENOG410IFSM; Eukaryota.
eggNOG; ENOG41124Q3; LUCA.
GeneTree; ENSGT00510000046414; -.
HOGENOM; HOG000043075; -.
HOVERGEN; HBG000472; -.
InParanoid; P01106; -.
KO; K04377; -.
PhylomeDB; P01106; -.
TreeFam; TF106001; -.
BioCyc; MetaCyc:ENSG00000136997-MONOMER; -.
Reactome; R-HSA-1362277; Transcription of E2F targets under negative control by DREAM complex.
Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
Reactome; R-HSA-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
Reactome; R-HSA-4411364; Binding of TCF/LEF:CTNNB1 to target gene promoters.
Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
Reactome; R-HSA-69202; Cyclin E associated events during G1/S transition.
Reactome; R-HSA-69656; Cyclin A:Cdk2-associated events at S phase entry.
Reactome; R-HSA-8866911; TFAP2 (AP-2) family regulates transcription of cell cycle factors.
Reactome; R-HSA-8951430; RUNX3 regulates WNT signaling.
SignaLink; P01106; -.
SIGNOR; P01106; -.
ChiTaRS; MYC; human.
EvolutionaryTrace; P01106; -.
GeneWiki; Myc; -.
GenomeRNAi; 4609; -.
PRO; PR:P01106; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000136997; -.
CleanEx; HS_MYC; -.
ExpressionAtlas; P01106; baseline and differential.
Genevisible; P01106; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0033613; F:activating transcription factor binding; IPI:CAFA.
GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
GO; GO:0070888; F:E-box binding; IDA:UniProtKB.
GO; GO:0032403; F:protein complex binding; IDA:UniProtKB.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0070491; F:repressing transcription factor binding; IPI:UniProtKB.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IMP:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:NTNU_SB.
GO; GO:1904837; P:beta-catenin-TCF complex assembly; TAS:Reactome.
GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; ISS:UniProtKB.
GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:UniProtKB.
GO; GO:0007050; P:cell cycle arrest; IDA:UniProtKB.
GO; GO:0006879; P:cellular iron ion homeostasis; IDA:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0035690; P:cellular response to drug; IDA:UniProtKB.
GO; GO:0071456; P:cellular response to hypoxia; IDA:CAFA.
GO; GO:0034644; P:cellular response to UV; IEP:UniProtKB.
GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB.
GO; GO:0051276; P:chromosome organization; IDA:UniProtKB.
GO; GO:0006112; P:energy reserve metabolic process; NAS:UniProtKB.
GO; GO:0070371; P:ERK1 and ERK2 cascade; IDA:CAFA.
GO; GO:0044346; P:fibroblast apoptotic process; TAS:UniProtKB.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0000165; P:MAPK cascade; IMP:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0051782; P:negative regulation of cell division; IDA:UniProtKB.
GO; GO:0048147; P:negative regulation of fibroblast proliferation; IDA:UniProtKB.
GO; GO:0045656; P:negative regulation of monocyte differentiation; IMP:UniProtKB.
GO; GO:0032873; P:negative regulation of stress-activated MAPK cascade; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0007219; P:Notch signaling pathway; TAS:Reactome.
GO; GO:0015671; P:oxygen transport; NAS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:CAFA.
GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:2000573; P:positive regulation of DNA biosynthetic process; IMP:UniProtKB.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IDA:UniProtKB.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IDA:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IDA:CAFA.
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:2001022; P:positive regulation of response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0051973; P:positive regulation of telomerase activity; ISS:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:NTNU_SB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0032986; P:protein-DNA complex disassembly; IDA:CAFA.
GO; GO:0010468; P:regulation of gene expression; IDA:MGI.
GO; GO:0032204; P:regulation of telomere maintenance; IMP:BHF-UCL.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0042493; P:response to drug; IEP:UniProtKB.
GO; GO:0010332; P:response to gamma radiation; IDA:UniProtKB.
GO; GO:0070848; P:response to growth factor; TAS:UniProtKB.
CDD; cd00083; HLH; 1.
Gene3D; 4.10.280.10; -; 1.
InterPro; IPR011598; bHLH_dom.
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;
3D-structure; Acetylation; Activator; Alternative splicing;
Chromosomal rearrangement; Complete proteome; DNA-binding;
Glycoprotein; Isopeptide bond; Nucleus; Phosphoprotein; Polymorphism;
Proto-oncogene; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 439 Myc proto-oncogene protein.
/FTId=PRO_0000127293.
DOMAIN 354 406 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
REGION 413 434 Leucine-zipper.
COMPBIAS 33 37 Poly-Gln.
COMPBIAS 88 91 Poly-Gly.
MOD_RES 6 6 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 8 8 Phosphothreonine; by RAF; in vitro.
{ECO:0000269|PubMed:9315742}.
MOD_RES 58 58 Phosphothreonine; by GSK3; alternate.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:15103331,
ECO:0000269|PubMed:17558397,
ECO:0000269|PubMed:8386367}.
MOD_RES 62 62 Phosphoserine; by DYRK2, GSK3 and CDK2.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:15103331,
ECO:0000269|PubMed:17558397,
ECO:0000269|PubMed:19966300,
ECO:0000269|PubMed:20713526,
ECO:0000269|PubMed:22307329,
ECO:0000269|PubMed:8386367}.
MOD_RES 71 71 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 143 143 N6-acetyllysine; by PCAF; alternate.
{ECO:0000269|PubMed:16126174}.
MOD_RES 148 148 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 157 157 N6-acetyllysine; by PCAF.
{ECO:0000269|PubMed:16126174}.
MOD_RES 161 161 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 275 275 N6-acetyllysine; by PCAF.
{ECO:0000269|PubMed:16126174}.
MOD_RES 293 293 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 317 317 N6-acetyllysine; by PCAF.
{ECO:0000269|PubMed:16126174}.
MOD_RES 323 323 N6-acetyllysine; by PCAF.
{ECO:0000269|PubMed:16126174}.
MOD_RES 329 329 Phosphoserine; by PIM2; in vitro.
{ECO:0000250|UniProtKB:P01108}.
MOD_RES 371 371 N6-acetyllysine; by PCAF.
{ECO:0000269|PubMed:16126174}.
CARBOHYD 58 58 O-linked (GlcNAc) threonine; alternate.
{ECO:0000269|PubMed:7642555}.
/FTId=CAR_000033.
CROSSLNK 52 52 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 143 143 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 148 148 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 298 298 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 1 M -> MDFFRVVENQQPPATM (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_037813.
VARIANT 11 11 N -> S (in dbSNP:rs4645959).
{ECO:0000269|Ref.11}.
/FTId=VAR_016327.
VARIANT 39 39 E -> D (in a Burkitt lymphoma symple;
dbSNP:rs121918684).
{ECO:0000269|PubMed:6419122,
ECO:0000269|PubMed:8220424}.
/FTId=VAR_063384.
VARIANT 57 57 P -> S (in a Burkitt lymphoma sample;
dbSNP:rs28933407).
{ECO:0000269|PubMed:8220424}.
/FTId=VAR_063385.
VARIANT 59 59 P -> A (in a Burkitt lymphoma sample;
dbSNP:rs121918685).
{ECO:0000269|PubMed:8220424}.
/FTId=VAR_063386.
VARIANT 86 86 N -> T (in a Burkitt lymphoma sample;
dbSNP:rs121918683).
{ECO:0000269|PubMed:8220424}.
/FTId=VAR_063387.
VARIANT 160 160 G -> C (in dbSNP:rs4645960).
{ECO:0000269|Ref.11}.
/FTId=VAR_016328.
VARIANT 170 170 V -> I (in dbSNP:rs4645961).
{ECO:0000269|Ref.11}.
/FTId=VAR_016329.
VARIANT 322 322 A -> V (in dbSNP:rs4645968).
{ECO:0000269|Ref.11}.
/FTId=VAR_016330.
MUTAGEN 58 58 T->A: Impairs interaction with FBXW7 and
subsequent degradation by the proteasome.
Normal inhibition of Ras-induced
senescence. {ECO:0000269|PubMed:15103331,
ECO:0000269|PubMed:17558397,
ECO:0000269|PubMed:19966300,
ECO:0000269|PubMed:20713526}.
MUTAGEN 62 62 S->A: Impairs interaction with FBXW7 and
subsequent degradation by the proteasome.
Impaired inhibition of Ras-induced
senescence. Abolishes phosphorylation by
DYRK2, and subsequent phosphorylation by
GSK3B at Thr-58.
{ECO:0000269|PubMed:15103331,
ECO:0000269|PubMed:17558397,
ECO:0000269|PubMed:19966300,
ECO:0000269|PubMed:20713526,
ECO:0000269|PubMed:22307329}.
CONFLICT 6 7 SF -> TI (in Ref. 5; no nucleotide
entry). {ECO:0000305}.
CONFLICT 10 10 R -> K (in Ref. 5; no nucleotide entry).
{ECO:0000305}.
CONFLICT 56 56 L -> LL (in Ref. 5; no nucleotide entry).
{ECO:0000305}.
CONFLICT 62 62 S -> P (in Ref. 7; CAA25288).
{ECO:0000305}.
CONFLICT 88 88 G -> D (in Ref. 5; no nucleotide entry).
{ECO:0000305}.
CONFLICT 92 92 S -> N (in Ref. 5; no nucleotide entry).
{ECO:0000305}.
CONFLICT 114 114 S -> N (in Ref. 5; no nucleotide entry).
{ECO:0000305}.
CONFLICT 120 120 D -> G (in Ref. 5; no nucleotide entry).
{ECO:0000305}.
CONFLICT 171 171 C -> S (in Ref. 5; no nucleotide entry).
{ECO:0000305}.
CONFLICT 203 203 S -> R (in Ref. 5; no nucleotide entry).
{ECO:0000305}.
CONFLICT 230 230 S -> A (in Ref. 5; no nucleotide entry).
{ECO:0000305}.
CONFLICT 240 240 L -> F (in Ref. 5; no nucleotide entry).
{ECO:0000305}.
CONFLICT 245 245 P -> S (in Ref. 5; no nucleotide entry).
{ECO:0000305}.
HELIX 353 378 {ECO:0000244|PDB:1NKP}.
HELIX 382 384 {ECO:0000244|PDB:1NKP}.
HELIX 392 434 {ECO:0000244|PDB:1NKP}.
SEQUENCE 439 AA; 48804 MW; ED5C028029A4C5D1 CRC64;
MPLNVSFTNR NYDLDYDSVQ PYFYCDEEEN FYQQQQQSEL QPPAPSEDIW KKFELLPTPP
LSPSRRSGLC SPSYVAVTPF SLRGDNDGGG GSFSTADQLE MVTELLGGDM VNQSFICDPD
DETFIKNIII QDCMWSGFSA AAKLVSEKLA SYQAARKDSG SPNPARGHSV CSTSSLYLQD
LSAAASECID PSVVFPYPLN DSSSPKSCAS QDSSAFSPSS DSLLSSTESS PQGSPEPLVL
HEETPPTTSS DSEEEQEDEE EIDVVSVEKR QAPGKRSESG SPSAGGHSKP PHSPLVLKRC
HVSTHQHNYA APPSTRKDYP AAKRVKLDSV RVLRQISNNR KCTSPRSSDT EENVKRRTHN
VLERQRRNEL KRSFFALRDQ IPELENNEKA PKVVILKKAT AYILSVQAEE QKLISEEDLL
RKRREQLKHK LEQLRNSCA


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