MYC_HUMAN
ID MYC_HUMAN Reviewed; 439 AA.
AC P01106; A8WFE7; P01107; Q14026;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 263.
DE RecName: Full=Myc proto-oncogene protein;
DE AltName: Full=Class E basic helix-loop-helix protein 39;
DE Short=bHLHe39;
DE AltName: Full=Proto-oncogene c-Myc;
DE AltName: Full=Transcription factor p64;
GN Name=MYC; Synonyms=BHLHE39;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM 1).
RX PubMed=6414718; DOI=10.1016/0092-8674(83)90534-2;
RA Battey J., Moulding C., Taub R., Murphy W., Stewart T., Potter H.,
RA Lenoir G., Leder P.;
RT "The human c-myc oncogene: structural consequences of translocation into
RT the IgH locus in Burkitt lymphoma.";
RL Cell 34:779-787(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM 1).
RX PubMed=6321164; DOI=10.1002/j.1460-2075.1983.tb01749.x;
RA Bernard O., Cory S., Gerondakis S., Webb E., Adams J.M.;
RT "Sequence of the murine and human cellular myc oncogenes and two modes of
RT myc transcription resulting from chromosome translocation in B lymphoid
RT tumours.";
RL EMBO J. 2:2375-2383(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM 1).
RX PubMed=6298632; DOI=10.1038/301722a0;
RA Colby W.W., Chen E.Y., Smith D.H., Levinson A.D.;
RT "Identification and nucleotide sequence of a human locus homologous to the
RT v-myc oncogene of avian myelocytomatosis virus MC29.";
RL Nature 301:722-725(1983).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=6304538; DOI=10.1038/303725a0;
RA Watt R., Stanton L.W., Marcu K.B., Gallo R.C., Croce C.M., Rovera G.;
RT "Nucleotide sequence of cloned cDNA of human c-myc oncogene.";
RL Nature 303:725-728(1983).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ASP-39.
RX PubMed=6419122; DOI=10.1038/306760a0;
RA Rabbitts T.H., Hamlyn P.H., Baer R.;
RT "Altered nucleotide sequences of a translocated c-myc gene in Burkitt
RT lymphoma.";
RL Nature 306:760-765(1983).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM 1).
RX PubMed=6304729; DOI=10.1073/pnas.80.12.3642;
RA Watson D.K., Psallidopoulos M.C., Samuel K.P., Dalla-Favera R., Papas T.S.;
RT "Nucleotide sequence analysis of human c-myc locus, chicken homologue, and
RT myelocytomatosis virus MC29 transforming gene reveals a highly conserved
RT gene product.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:3642-3645(1983).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE [GENOMIC
RP DNA] OF 1-252.
RX PubMed=6547209; DOI=10.1038/309592a0;
RA Rabbitts T.H., Forster A., Hamlyn P., Baer R.;
RT "Effect of somatic mutation within translocated c-myc genes in Burkitt's
RT lymphoma.";
RL Nature 309:592-597(1984).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM 1).
RX PubMed=6714223; DOI=10.1002/j.1460-2075.1984.tb01816.x;
RA Gazin C., Dupont S., de Dinechin D., Hampe A., Masson J.-M., Martin P.,
RA Stehelin D., Galibert F.;
RT "Nucleotide sequence of the human c-myc locus: provocative open reading
RT frame within the first exon.";
RL EMBO J. 3:383-387(1984).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS 1 AND
RP 2).
RX PubMed=8444346; DOI=10.1016/0378-1119(93)90398-m;
RA Tachibana K., Takayama N., Matsuo K., Kato S., Yamamoto K., Ohyama K.,
RA Umezawa A., Takano T.;
RT "Allele-specific activation of the c-myc gene in an atypical Burkitt's
RT lymphoma carrying the t(2;8) chromosomal translocation 250 kb downstream
RT from c-myc.";
RL Gene 124:231-237(1993).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-11; CYS-160; ILE-170
RP AND VAL-322.
RG NIEHS SNPs program;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [13]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [14]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [15]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Cervix, Placenta, and Testis;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [16]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-170 (ISOFORM 1).
RC TISSUE=Promyelocytic leukemia;
RX PubMed=3540591; DOI=10.1128/mcb.6.10.3481-3489.1986;
RA Bentley D.L., Groudine M.;
RT "Novel promoter upstream of the human c-myc gene and regulation of c-myc
RT expression in B-cell lymphomas.";
RL Mol. Cell. Biol. 6:3481-3489(1986).
RN [17]
RP INVOLVEMENT IN BURKITT LYMPHOMA.
RX PubMed=2166998; DOI=10.1016/s0065-230x(08)60470-4;
RA Magrath I.;
RT "The pathogenesis of Burkitt's lymphoma.";
RL Adv. Cancer Res. 55:133-270(1990).
RN [18]
RP PHOSPHORYLATION.
RX PubMed=1597196; DOI=10.1111/j.1432-1033.1992.tb16964.x;
RA Iijima S., Teraoka H., Date T., Tsukada K.;
RT "DNA-activated protein kinase in Raji Burkitt's lymphoma cells.
RT Phosphorylation of c-Myc oncoprotein.";
RL Eur. J. Biochem. 206:595-603(1992).
RN [19]
RP INVOLVEMENT IN BURKITT LYMPHOMA, AND VARIANTS ASP-39; SER-57; ALA-59 AND
RP THR-86.
RX PubMed=8220424; DOI=10.1038/ng0993-56;
RA Bhatia K., Huppi K., Spangler G., Siwarski D., Iyer R., Magrath I.;
RT "Point mutations in the c-Myc transactivation domain are common in
RT Burkitt's lymphoma and mouse plasmacytomas.";
RL Nat. Genet. 5:56-61(1993).
RN [20]
RP PHOSPHORYLATION AT THR-58 AND SER-62.
RX PubMed=8386367; DOI=10.1073/pnas.90.8.3216;
RA Gupta S., Seth A., Davis R.J.;
RT "Transactivation of gene expression by Myc is inhibited by mutation at the
RT phosphorylation sites Thr-58 and Ser-62.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:3216-3220(1993).
RN [21]
RP GLYCOSYLATION AT THR-58.
RX PubMed=7642555; DOI=10.1074/jbc.270.32.18961;
RA Chou T.-Y., Hart G.W., Dang C.V.;
RT "c-Myc is glycosylated at threonine 58, a known phosphorylation site and a
RT mutational hot spot in lymphomas.";
RL J. Biol. Chem. 270:18961-18965(1995).
RN [22]
RP PHOSPHORYLATION AT THR-8.
RX PubMed=9315742; DOI=10.1016/s0014-5793(97)00992-7;
RA Alexandrov I., Shlyakhova L., Vartanian A., Zajac-Kaye M., Alexandrova N.;
RT "c-Raf kinase binds to N-terminal domain of c-Myc.";
RL FEBS Lett. 414:465-470(1997).
RN [23]
RP UBIQUITINATION, INTERACTION WITH FBXW7, PHOSPHORYLATION AT THR-58 AND
RP SER-62, AND MUTAGENESIS OF THR-58 AND SER-62.
RX PubMed=15103331; DOI=10.1038/sj.emboj.7600217;
RA Yada M., Hatakeyama S., Kamura T., Nishiyama M., Tsunematsu R., Imaki H.,
RA Ishida N., Okumura F., Nakayama K., Nakayama K.I.;
RT "Phosphorylation-dependent degradation of c-Myc is mediated by the F-box
RT protein Fbw7.";
RL EMBO J. 23:2116-2125(2004).
RN [24]
RP ACETYLATION AT LYS-143; LYS-157; LYS-275; LYS-317; LYS-323 AND LYS-371, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16126174; DOI=10.1016/j.bbrc.2005.08.075;
RA Zhang K., Faiola F., Martinez E.;
RT "Six lysine residues on c-Myc are direct substrates for acetylation by
RT p300.";
RL Biochem. Biophys. Res. Commun. 336:274-280(2005).
RN [25]
RP INTERACTION WITH TAF1C.
RX PubMed=15723054; DOI=10.1038/ncb1224;
RA Grandori C., Gomez-Roman N., Felton-Edkins Z.A., Ngouenet C.,
RA Galloway D.A., Eisenman R.N., White R.J.;
RT "c-Myc binds to human ribosomal DNA and stimulates transcription of rRNA
RT genes by RNA polymerase I.";
RL Nat. Cell Biol. 7:311-318(2005).
RN [26]
RP INTERACTION WITH PARP10.
RX PubMed=15674325; DOI=10.1038/sj.onc.1208410;
RA Yu M., Schreek S., Cerni C., Schamberger C., Lesniewicz K., Poreba E.,
RA Vervoorts J., Walsemann G., Groetzinger J., Kremmer E., Mehraein Y.,
RA Mertsching J., Kraft R., Austen M., Luescher-Firzlaff J., Luescher B.;
RT "PARP-10, a novel Myc-interacting protein with poly(ADP-ribose) polymerase
RT activity, inhibits transformation.";
RL Oncogene 24:1982-1993(2005).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-58, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [28]
RP INTERACTION WITH CIP2A.
RX PubMed=17632056; DOI=10.1016/j.cell.2007.04.044;
RA Junttila M.R., Puustinen P., Niemelae M., Ahola R., Arnold H.,
RA Boettzauw T., Ala-Aho R., Nielsen C., Ivaska J., Taya Y., Lu S.-L., Lin S.,
RA Chan E.K.L., Wang X.-J., Grenman R., Kast J., Kallunki T., Sears R.,
RA Kaehaeri V.-M., Westermarck J.;
RT "CIP2A inhibits PP2A in human malignancies.";
RL Cell 130:51-62(2007).
RN [29]
RP BIOTECHNOLOGY.
RX PubMed=18035408; DOI=10.1016/j.cell.2007.11.019;
RA Takahashi K., Tanabe K., Ohnuki M., Narita M., Ichisaka T., Tomoda K.,
RA Yamanaka S.;
RT "Induction of pluripotent stem cells from adult human fibroblasts by
RT defined factors.";
RL Cell 131:861-872(2007).
RN [30]
RP UBIQUITINATION, DEUBIQUITINATION BY USP28, AND INTERACTION WITH FBXW7.
RX PubMed=17873522; DOI=10.4161/cc.6.19.4804;
RA Popov N., Herold S., Llamazares M., Schulein C., Eilers M.;
RT "Fbw7 and Usp28 regulate myc protein stability in response to DNA damage.";
RL Cell Cycle 6:2327-2331(2007).
RN [31]
RP INTERACTION WITH KDM5A AND KDM5B.
RX PubMed=17311883; DOI=10.1101/gad.1523007;
RA Secombe J., Li L., Carlos L., Eisenman R.N.;
RT "The Trithorax group protein Lid is a trimethyl histone H3K4 demethylase
RT required for dMyc-induced cell growth.";
RL Genes Dev. 21:537-551(2007).
RN [32]
RP INTERACTION WITH RIOX1.
RX PubMed=17308053; DOI=10.1158/1535-7163.mct-06-0659;
RA Suzuki C., Takahashi K., Hayama S., Ishikawa N., Kato T., Ito T.,
RA Tsuchiya E., Nakamura Y., Daigo Y.;
RT "Identification of Myc-associated protein with JmjC domain as a novel
RT therapeutic target oncogene for lung cancer.";
RL Mol. Cancer Ther. 6:542-551(2007).
RN [33]
RP UBIQUITINATION, DEUBIQUITINATION BY USP28, INTERACTION WITH FBXW7,
RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-58 AND SER-62, AND MUTAGENESIS
RP OF THR-58 AND SER-62.
RX PubMed=17558397; DOI=10.1038/ncb1601;
RA Popov N., Wanzel M., Madiredjo M., Zhang D., Beijersbergen R., Bernards R.,
RA Moll R., Elledge S.J., Eilers M.;
RT "The ubiquitin-specific protease USP28 is required for MYC stability.";
RL Nat. Cell Biol. 9:765-774(2007).
RN [34]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-58; SER-62 AND SER-71, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [35]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [36]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-148, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [37]
RP REVIEW ON SENESCENCE, PHOSPHORYLATION AT SER-62 BY CDK2, AND MUTAGENESIS OF
RP THR-58 AND SER-62.
RX PubMed=20713526; DOI=10.1158/0008-5472.can-10-1383;
RA Hydbring P., Larsson L.-G.;
RT "Tipping the balance: Cdk2 enables Myc to suppress senescence.";
RL Cancer Res. 70:6687-6691(2010).
RN [38]
RP FUNCTION.
RX PubMed=20010808; DOI=10.1038/nature08697;
RA David C.J., Chen M., Assanah M., Canoll P., Manley J.L.;
RT "HnRNP proteins controlled by c-Myc deregulate pyruvate kinase mRNA
RT splicing in cancer.";
RL Nature 463:364-368(2010).
RN [39]
RP PHOSPHORYLATION AT SER-62 BY CDK2, AND MUTAGENESIS OF THR-58 AND SER-62.
RX PubMed=19966300; DOI=10.1073/pnas.0900121106;
RA Hydbring P., Bahram F., Su Y., Tronnersjoe S., Hoegstrand K.,
RA von der Lehr N., Sharifi H.R., Lilischkis R., Hein N., Wu S., Vervoorts J.,
RA Henriksson M., Grandien A., Luescher B., Larsson L.-G.;
RT "Phosphorylation by Cdk2 is required for Myc to repress Ras-induced
RT senescence in cotransformation.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:58-63(2010).
RN [40]
RP UBIQUITINATION.
RX PubMed=20551172; DOI=10.1101/gad.1920310;
RA Choi S.H., Wright J.B., Gerber S.A., Cole M.D.;
RT "Myc protein is stabilized by suppression of a novel E3 ligase complex in
RT cancer cells.";
RL Genes Dev. 24:1236-1241(2010).
RN [41]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 AND SER-161, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [42]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-58 AND SER-62, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [43]
RP PHOSPHORYLATION AT SER-62, AND MUTAGENESIS OF SER-62.
RX PubMed=22307329; DOI=10.1172/jci60818;
RA Taira N., Mimoto R., Kurata M., Yamaguchi T., Kitagawa M., Miki Y.,
RA Yoshida K.;
RT "DYRK2 priming phosphorylation of c-Jun and c-Myc modulates cell cycle
RT progression in human cancer cells.";
RL J. Clin. Invest. 122:859-872(2012).
RN [44]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; THR-58; SER-62; SER-71 AND
RP SER-293, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [45]
RP FUNCTION.
RX PubMed=24940000; DOI=10.7554/elife.02349;
RA Shi Y., Xu X., Zhang Q., Fu G., Mo Z., Wang G.S., Kishi S., Yang X.L.;
RT "tRNA synthetase counteracts c-Myc to develop functional vasculature.";
RL Elife 3:E02349-E02349(2014).
RN [46]
RP FUNCTION, AND INTERACTION WITH NPM1.
RX PubMed=25956029; DOI=10.1016/j.ajpath.2015.03.016;
RA Kim J.Y., Cho Y.E., Park J.H.;
RT "The nucleolar protein GLTSCR2 is an upstream negative regulator of the
RT oncogenic Nucleophosmin-MYC axis.";
RL Am. J. Pathol. 185:2061-2068(2015).
RN [47]
RP PHOSPHORYLATION AT SER-62.
RX PubMed=25803737; DOI=10.1080/15384101.2015.1021526;
RA Cianfanelli V., D'Orazio M., Cecconi F.;
RT "AMBRA1 and BECLIN 1 interplay in the crosstalk between autophagy and cell
RT proliferation.";
RL Cell Cycle 14:959-963(2015).
RN [48]
RP PHOSPHORYLATION AT SER-62, DEPHOSPHORYLATION, AND MUTAGENESIS OF SER-62.
RX PubMed=25438055; DOI=10.1038/ncb3072;
RA Cianfanelli V., Fuoco C., Lorente M., Salazar M., Quondamatteo F.,
RA Gherardini P.F., De Zio D., Nazio F., Antonioli M., D'Orazio M., Skobo T.,
RA Bordi M., Rohde M., Dalla Valle L., Helmer-Citterich M., Gretzmeier C.,
RA Dengjel J., Fimia G.M., Piacentini M., Di Bartolomeo S., Velasco G.,
RA Cecconi F.;
RT "AMBRA1 links autophagy to cell proliferation and tumorigenesis by
RT promoting c-Myc dephosphorylation and degradation.";
RL Nat. Cell Biol. 17:20-30(2015).
RN [49]
RP UBIQUITINATION, DEUBIQUITINATION BY USP36, INTERACTION WITH FBXW7, AND
RP SUBCELLULAR LOCATION.
RX PubMed=25775507; DOI=10.1073/pnas.1411713112;
RA Sun X.X., He X., Yin L., Komada M., Sears R.C., Dai M.S.;
RT "The nucleolar ubiquitin-specific protease USP36 deubiquitinates and
RT stabilizes c-Myc.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:3734-3739(2015).
RN [50]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-52; LYS-143; LYS-148 AND LYS-298,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [51]
RP UBIQUITINATION, AND MUTAGENESIS OF ARG-435.
RX PubMed=29779948; DOI=10.1016/j.cell.2018.04.028;
RA Koren I., Timms R.T., Kula T., Xu Q., Li M.Z., Elledge S.J.;
RT "The eukaryotic proteome is shaped by E3 ubiquitin ligases targeting C-
RT terminal degrons.";
RL Cell 173:1622-1635(2018).
RN [52]
RP 9AATAD MOTIF.
RX PubMed=34342803; DOI=10.1007/s12015-021-10225-8;
RA Piskacek M., Otasevic T., Repko M., Knight A.;
RT "The 9aaTAD Activation Domains in the Yamanaka Transcription Factors Oct4,
RT Sox2, Myc, and Klf4.";
RL Stem. Cell. Rev. Rep. 17:1934-1936(2021).
RN [53]
RP STRUCTURE BY NMR OF 402-434 IN COMPLEX WITH MAX.
RX PubMed=9680483; DOI=10.1006/jmbi.1998.1914;
RA Lavigne P., Crump M.P., Gagne S.M., Hodges R.S., Kay C.M., Sykes B.D.;
RT "Insights into the mechanism of heterodimerization from the 1H-NMR solution
RT structure of the c-Myc-Max heterodimeric leucine zipper.";
RL J. Mol. Biol. 281:165-181(1998).
RN [54]
RP CHROMOSOMAL TRANSLOCATION WITH BTG1.
RX PubMed=2069907; DOI=10.1002/gcc.2870030106;
RA Rimokh R., Rouault J.P., Wahbi K., Gadoux M., Lafage M., Archimbaud E.,
RA Charrin C., Gentilhomme O., Germain D., Samarut J.;
RT "A chromosome 12 coding region is juxtaposed to the MYC protooncogene locus
RT in a t(8;12)(q24;q22) translocation in a case of B-cell chronic lymphocytic
RT leukemia.";
RL Genes Chromosomes Cancer 3:24-36(1991).
CC -!- FUNCTION: Transcription factor that binds DNA in a non-specific manner,
CC yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'
CC (PubMed:24940000, PubMed:25956029). Activates the transcription of
CC growth-related genes (PubMed:24940000, PubMed:25956029). Binds to the
CC VEGFA promoter, promoting VEGFA production and subsequent sprouting
CC angiogenesis (PubMed:24940000, PubMed:25956029). Regulator of somatic
CC reprogramming, controls self-renewal of embryonic stem cells (By
CC similarity). Functions with TAF6L to activate target gene expression
CC through RNA polymerase II pause release (By similarity). Positively
CC regulates transcription of HNRNPA1, HNRNPA2 and PTBP1 which in turn
CC regulate splicing of pyruvate kinase PKM by binding repressively to
CC sequences flanking PKM exon 9, inhibiting exon 9 inclusion and
CC resulting in exon 10 inclusion and production of the PKM M2 isoform
CC (PubMed:20010808). {ECO:0000250|UniProtKB:P01108,
CC ECO:0000269|PubMed:20010808, ECO:0000269|PubMed:24940000,
CC ECO:0000269|PubMed:25956029}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. Binds DNA as a heterodimer with MAX (PubMed:9680483).
CC Interacts with TAF1C and SPAG9. Interacts with PARP10. Interacts with
CC KDM5A and KDM5B. Interacts (when phosphorylated at Thr-58 and Ser-62)
CC with FBXW7(PubMed:25775507, PubMed:17558397). Interacts with PIM2.
CC Interacts with RIOX1. The heterodimer MYC:MAX interacts with ABI1; the
CC interaction may enhance MYC:MAX transcriptional activity. Interacts
CC with TRIM6 (By similarity). Interacts with NPM1; the binary complex is
CC recruited to the promoter of MYC target genes and enhances their
CC transcription (PubMed:25956029). Interacts with CIP2A; leading to the
CC stabilization of MYC (PubMed:17632056). {ECO:0000250|UniProtKB:P01108,
CC ECO:0000269|PubMed:15103331, ECO:0000269|PubMed:15674325,
CC ECO:0000269|PubMed:15723054, ECO:0000269|PubMed:17308053,
CC ECO:0000269|PubMed:17311883, ECO:0000269|PubMed:17558397,
CC ECO:0000269|PubMed:17632056, ECO:0000269|PubMed:17873522,
CC ECO:0000269|PubMed:25775507, ECO:0000269|PubMed:25956029,
CC ECO:0000269|PubMed:9680483}.
CC -!- INTERACTION:
CC P01106; Q9UBB4: ATXN10; NbExp=4; IntAct=EBI-447544, EBI-702390;
CC P01106; O15169: AXIN1; NbExp=10; IntAct=EBI-447544, EBI-710484;
CC P01106; O00499-10: BIN1; NbExp=3; IntAct=EBI-447544, EBI-7689134;
CC P01106; O00499-11: BIN1; NbExp=2; IntAct=EBI-447544, EBI-7689211;
CC P01106; Q15059: BRD3; NbExp=3; IntAct=EBI-447544, EBI-1383460;
CC P01106; P55212: CASP6; NbExp=3; IntAct=EBI-447544, EBI-718729;
CC P01106; P45973: CBX5; NbExp=3; IntAct=EBI-447544, EBI-78219;
CC P01106; Q8N163: CCAR2; NbExp=8; IntAct=EBI-447544, EBI-355410;
CC P01106; P06307: CCK; NbExp=3; IntAct=EBI-447544, EBI-6624398;
CC P01106; A5D8W4: CDH1; NbExp=3; IntAct=EBI-447544, EBI-7793316;
CC P01106; P11802: CDK4; NbExp=2; IntAct=EBI-447544, EBI-295644;
CC P01106; Q86XR8: CEP57; NbExp=3; IntAct=EBI-447544, EBI-308614;
CC P01106; P28329-3: CHAT; NbExp=3; IntAct=EBI-447544, EBI-25837549;
CC P01106; Q14839: CHD4; NbExp=2; IntAct=EBI-447544, EBI-372916;
CC P01106; O15111: CHUK; NbExp=3; IntAct=EBI-447544, EBI-81249;
CC P01106; Q8TCG1: CIP2A; NbExp=2; IntAct=EBI-447544, EBI-1379376;
CC P01106; Q01658: DR1; NbExp=3; IntAct=EBI-447544, EBI-750300;
CC P01106; Q15029: EFTUD2; NbExp=5; IntAct=EBI-447544, EBI-357897;
CC P01106; Q96L91: EP400; NbExp=6; IntAct=EBI-447544, EBI-399163;
CC P01106; Q96L91-2: EP400; NbExp=2; IntAct=EBI-447544, EBI-15698003;
CC P01106; Q969H0: FBXW7; NbExp=7; IntAct=EBI-447544, EBI-359574;
CC P01106; Q8N3Y1: FBXW8; NbExp=3; IntAct=EBI-447544, EBI-914770;
CC P01106; P22607: FGFR3; NbExp=3; IntAct=EBI-447544, EBI-348399;
CC P01106; O43524: FOXO3; NbExp=3; IntAct=EBI-447544, EBI-1644164;
CC P01106; P49841-2: GSK3B; NbExp=3; IntAct=EBI-447544, EBI-15870655;
CC P01106; P06396: GSN; NbExp=3; IntAct=EBI-447544, EBI-351506;
CC P01106; Q00403: GTF2B; NbExp=3; IntAct=EBI-447544, EBI-389564;
CC P01106; Q9Y5Q9: GTF3C3; NbExp=4; IntAct=EBI-447544, EBI-1054873;
CC P01106; Q92769: HDAC2; NbExp=2; IntAct=EBI-447544, EBI-301821;
CC P01106; O15379: HDAC3; NbExp=6; IntAct=EBI-447544, EBI-607682;
CC P01106; Q9Y6K9: IKBKG; NbExp=3; IntAct=EBI-447544, EBI-81279;
CC P01106; O60341: KDM1A; NbExp=4; IntAct=EBI-447544, EBI-710124;
CC P01106; O00629: KPNA4; NbExp=6; IntAct=EBI-447544, EBI-396343;
CC P01106; P13473-2: LAMP2; NbExp=3; IntAct=EBI-447544, EBI-21591415;
CC P01106; P61244: MAX; NbExp=38; IntAct=EBI-447544, EBI-751711;
CC P01106; O95983: MBD3; NbExp=3; IntAct=EBI-447544, EBI-1783068;
CC P01106; P33993: MCM7; NbExp=6; IntAct=EBI-447544, EBI-355924;
CC P01106; A9UHW6: MIF4GD; NbExp=2; IntAct=EBI-447544, EBI-373498;
CC P01106; O75928: PIAS2; NbExp=4; IntAct=EBI-447544, EBI-348555;
CC P01106; Q13526: PIN1; NbExp=5; IntAct=EBI-447544, EBI-714158;
CC P01106; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-447544, EBI-5280197;
CC P01106; P62913: RPL11; NbExp=3; IntAct=EBI-447544, EBI-354380;
CC P01106; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-447544, EBI-2623095;
CC P01106; O75182: SIN3B; NbExp=7; IntAct=EBI-447544, EBI-540462;
CC P01106; Q96EB6: SIRT1; NbExp=4; IntAct=EBI-447544, EBI-1802965;
CC P01106; Q8N6T7: SIRT6; NbExp=3; IntAct=EBI-447544, EBI-712415;
CC P01106; Q13309: SKP2; NbExp=2; IntAct=EBI-447544, EBI-456291;
CC P01106; Q8TAD8: SNIP1; NbExp=9; IntAct=EBI-447544, EBI-749336;
CC P01106; P08047: SP1; NbExp=4; IntAct=EBI-447544, EBI-298336;
CC P01106; P31948: STIP1; NbExp=3; IntAct=EBI-447544, EBI-1054052;
CC P01106; Q13148: TARDBP; NbExp=6; IntAct=EBI-447544, EBI-372899;
CC P01106; P37173: TGFBR2; NbExp=3; IntAct=EBI-447544, EBI-296151;
CC P01106; P11387: TOP1; NbExp=2; IntAct=EBI-447544, EBI-876302;
CC P01106; Q14669: TRIP12; NbExp=7; IntAct=EBI-447544, EBI-308443;
CC P01106; Q9Y4A5: TRRAP; NbExp=6; IntAct=EBI-447544, EBI-399128;
CC P01106; P0CG48: UBC; NbExp=5; IntAct=EBI-447544, EBI-3390054;
CC P01106; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-447544, EBI-741480;
CC P01106; P17480: UBTF; NbExp=2; IntAct=EBI-447544, EBI-396235;
CC P01106; Q13105: ZBTB17; NbExp=9; IntAct=EBI-447544, EBI-372156;
CC P01106; Q9Y649; NbExp=3; IntAct=EBI-447544, EBI-25900580;
CC P01106; P03129: E7; Xeno; NbExp=2; IntAct=EBI-447544, EBI-866453;
CC P01106; P04020: E7; Xeno; NbExp=2; IntAct=EBI-447544, EBI-7005254;
CC P01106; P06788: E7; Xeno; NbExp=5; IntAct=EBI-447544, EBI-1776887;
CC P01106; P03204: EBNA6; Xeno; NbExp=11; IntAct=EBI-447544, EBI-9255985;
CC P01106; P52164: Max; Xeno; NbExp=4; IntAct=EBI-447544, EBI-1184963;
CC P01106; Q62141: Sin3b; Xeno; NbExp=8; IntAct=EBI-447544, EBI-591450;
CC P01106; P03070; Xeno; NbExp=2; IntAct=EBI-447544, EBI-617698;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:17558397}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:17558397, ECO:0000269|PubMed:25775507}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P01106-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P01106-2; Sequence=VSP_037813;
CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC number of yeast and animal transcription factors.
CC {ECO:0000269|PubMed:34342803}.
CC -!- PTM: Phosphorylated by PRKDC (PubMed:1597196). Phosphorylation at Ser-
CC 329 by PIM2 leads to the stabilization of MYC (By similarity).
CC Phosphorylation at Ser-62 by CDK2 prevents Ras-induced senescence
CC (PubMed:19966300, PubMed:20713526). Phosphorylated at Ser-62 by DYRK2;
CC this primes the protein for subsequent phosphorylation by GSK3B at Thr-
CC 58 (PubMed:22307329). Phosphorylation at Thr-58 and Ser-62 by GSK3 is
CC required for ubiquitination and degradation by the proteasome
CC (PubMed:15103331, PubMed:17558397, PubMed:8386367). Dephosphorylation
CC at Ser-62 by protein phosphatase 2A (PPP2CA) promotes its degradation;
CC interaction with PPP2CA is enhanced by AMBRA1 (PubMed:25803737,
CC PubMed:25438055). {ECO:0000250|UniProtKB:P01108,
CC ECO:0000269|PubMed:15103331, ECO:0000269|PubMed:1597196,
CC ECO:0000269|PubMed:17558397, ECO:0000269|PubMed:19966300,
CC ECO:0000269|PubMed:20713526, ECO:0000269|PubMed:22307329,
CC ECO:0000269|PubMed:25438055, ECO:0000269|PubMed:25803737,
CC ECO:0000269|PubMed:8386367}.
CC -!- PTM: Ubiquitinated by the SCF(FBXW7) complex when phosphorylated at
CC Thr-58 and Ser-62, leading to its degradation by the proteasome
CC (PubMed:15103331, PubMed:17558397, PubMed:25775507). In the
CC nucleoplasm, ubiquitination is counteracted by USP28, which interacts
CC with isoform 1 of FBXW7 (FBW7alpha), leading to its deubiquitination
CC and preventing degradation (PubMed:17873522, PubMed:17558397). In the
CC nucleolus, however, ubiquitination is not counteracted by USP28 but by
CC USP36, due to the lack of interaction between isoform 3 of FBXW7
CC (FBW7gamma) and USP28, explaining the selective MYC degradation in the
CC nucleolus (PubMed:17558397, PubMed:25775507). Also polyubiquitinated by
CC the DCX(TRPC4AP) complex (PubMed:20551172, PubMed:29779948).
CC Ubiquitinated by TRIM6 in a phosphorylation-independent manner (By
CC similarity). {ECO:0000250|UniProtKB:P01108,
CC ECO:0000269|PubMed:15103331, ECO:0000269|PubMed:17558397,
CC ECO:0000269|PubMed:17873522, ECO:0000269|PubMed:20551172,
CC ECO:0000269|PubMed:25775507, ECO:0000269|PubMed:29779948}.
CC -!- DISEASE: Note=A chromosomal aberration involving MYC may be a cause of
CC a form of B-cell chronic lymphocytic leukemia. Translocation
CC t(8;12)(q24;q22) with BTG1. {ECO:0000269|PubMed:2069907}.
CC -!- DISEASE: Burkitt lymphoma (BL) [MIM:113970]: A form of undifferentiated
CC malignant lymphoma commonly manifested as a large osteolytic lesion in
CC the jaw or as an abdominal mass. {ECO:0000269|PubMed:2166998,
CC ECO:0000269|PubMed:8220424}. Note=The gene represented in this entry is
CC involved in disease pathogenesis. Chromosomal aberrations involving MYC
CC are usually found in Burkitt lymphoma. Translocations t(8;14), t(8;22)
CC or t(2;8) which juxtapose MYC to one of the heavy or light chain
CC immunoglobulin gene loci.
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 designated
CC iPS (induced pluripotent stem) cells. iPS cells exhibit the morphology
CC and growth properties of ES cells and express ES cell marker genes.
CC {ECO:0000269|PubMed:18035408}.
CC -!- MISCELLANEOUS: [Isoform 2]: Initiates from CTG codon. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/MYCID27.html";
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/myc/";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Myc entry;
CC URL="https://en.wikipedia.org/wiki/Myc";
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DR EMBL; L00058; AAA59882.1; -; Genomic_DNA.
DR EMBL; L00057; AAA59882.1; JOINED; Genomic_DNA.
DR EMBL; K00535; AAA59880.1; -; Genomic_DNA.
DR EMBL; K00534; AAA59880.1; JOINED; Genomic_DNA.
DR EMBL; K00535; ABW69847.1; -; Genomic_DNA.
DR EMBL; K00534; ABW69847.1; JOINED; Genomic_DNA.
DR EMBL; X00196; CAA25015.2; -; Genomic_DNA.
DR EMBL; X00198; CAA25015.2; JOINED; Genomic_DNA.
DR EMBL; X00364; CAA25106.1; -; Genomic_DNA.
DR EMBL; V00568; CAA23831.1; -; mRNA.
DR EMBL; K01906; AAA59881.1; -; Genomic_DNA.
DR EMBL; K01905; AAA59881.1; JOINED; Genomic_DNA.
DR EMBL; K02276; AAA36340.1; -; mRNA.
DR EMBL; X00676; CAA25288.1; -; Genomic_DNA.
DR EMBL; D10493; BAA01374.2; -; Genomic_DNA.
DR EMBL; D10493; BAA01375.1; -; Genomic_DNA.
DR EMBL; BT019768; AAV38573.1; -; mRNA.
DR EMBL; AY214166; AAO21131.1; -; Genomic_DNA.
DR EMBL; AK312883; BAG35731.1; -; mRNA.
DR EMBL; AC103819; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471060; EAW92098.1; -; Genomic_DNA.
DR EMBL; BC000141; AAH00141.2; -; mRNA.
DR EMBL; BC000917; AAH00917.2; -; mRNA.
DR EMBL; BC058901; AAH58901.2; -; mRNA.
DR EMBL; M13929; AAA88092.1; -; mRNA.
DR CCDS; CCDS6359.2; -. [P01106-2]
DR PIR; A01349; TVHUM.
DR PIR; A01350; TVHUT.
DR RefSeq; NP_002458.2; NM_002467.4. [P01106-2]
DR PDB; 1A93; NMR; -; A=406-434.
DR PDB; 1EE4; X-ray; 2.10 A; C/D/E/F=320-328.
DR PDB; 1MV0; NMR; -; A=55-68.
DR PDB; 1NKP; X-ray; 1.80 A; A/D=353-434.
DR PDB; 2A93; NMR; -; A=406-434.
DR PDB; 2OR9; X-ray; 2.70 A; P=410-419.
DR PDB; 4Y7R; X-ray; 1.90 A; B=260-267.
DR PDB; 5I4Z; X-ray; 1.95 A; A/B=350-439.
DR PDB; 5I50; X-ray; 2.70 A; A/B=350-439.
DR PDB; 6C4U; X-ray; 2.60 A; G/H/I/J/K/L=54-62.
DR PDB; 6E16; X-ray; 2.40 A; A=96-125.
DR PDB; 6E24; X-ray; 3.00 A; A=96-125.
DR PDB; 6G6J; X-ray; 2.25 A; A/C=351-437.
DR PDB; 6G6K; X-ray; 1.35 A; A/C=351-437.
DR PDB; 6G6L; X-ray; 2.20 A; A/C/E/G=351-437.
DR PDBsum; 1A93; -.
DR PDBsum; 1EE4; -.
DR PDBsum; 1MV0; -.
DR PDBsum; 1NKP; -.
DR PDBsum; 2A93; -.
DR PDBsum; 2OR9; -.
DR PDBsum; 4Y7R; -.
DR PDBsum; 5I4Z; -.
DR PDBsum; 5I50; -.
DR PDBsum; 6C4U; -.
DR PDBsum; 6E16; -.
DR PDBsum; 6E24; -.
DR PDBsum; 6G6J; -.
DR PDBsum; 6G6K; -.
DR PDBsum; 6G6L; -.
DR AlphaFoldDB; P01106; -.
DR BMRB; P01106; -.
DR SMR; P01106; -.
DR BioGRID; 110694; 2036.
DR ComplexPortal; CPX-1123; FOXO3-MYC complex.
DR ComplexPortal; CPX-514; c-MYC-BIN1 complex.
DR ComplexPortal; CPX-91; Transcriptional activator Myc-Max complex.
DR CORUM; P01106; -.
DR DIP; DIP-28143N; -.
DR IntAct; P01106; 835.
DR MINT; P01106; -.
DR STRING; 9606.ENSP00000479618; -.
DR BindingDB; P01106; -.
DR ChEMBL; CHEMBL1250348; -.
DR DrugBank; DB00945; Acetylsalicylic acid.
DR DrugBank; DB08813; Nadroparin.
DR GlyConnect; 426; 1 O-Linked glycan (1 site).
DR GlyGen; P01106; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P01106; -.
DR PhosphoSitePlus; P01106; -.
DR BioMuta; MYC; -.
DR DMDM; 127619; -.
DR SWISS-2DPAGE; P01106; -.
DR EPD; P01106; -.
DR jPOST; P01106; -.
DR MassIVE; P01106; -.
DR MaxQB; P01106; -.
DR PaxDb; P01106; -.
DR PeptideAtlas; P01106; -.
DR PRIDE; P01106; -.
DR ProteomicsDB; 51318; -. [P01106-1]
DR ProteomicsDB; 51319; -. [P01106-2]
DR ABCD; P01106; 7 sequenced antibodies.
DR Antibodypedia; 3520; 4254 antibodies from 53 providers.
DR DNASU; 4609; -.
DR Ensembl; ENST00000377970.6; ENSP00000367207.3; ENSG00000136997.21. [P01106-1]
DR Ensembl; ENST00000621592.8; ENSP00000478887.2; ENSG00000136997.21. [P01106-2]
DR Ensembl; ENST00000652288.1; ENSP00000499105.1; ENSG00000136997.21. [P01106-1]
DR GeneID; 4609; -.
DR KEGG; hsa:4609; -.
DR MANE-Select; ENST00000621592.8; ENSP00000478887.2; NM_002467.6; NP_002458.2. [P01106-2]
DR UCSC; uc064qdj.1; human. [P01106-1]
DR CTD; 4609; -.
DR DisGeNET; 4609; -.
DR GeneCards; MYC; -.
DR HGNC; HGNC:7553; MYC.
DR HPA; ENSG00000136997; Low tissue specificity.
DR MalaCards; MYC; -.
DR MIM; 113970; phenotype.
DR MIM; 190080; gene.
DR neXtProt; NX_P01106; -.
DR OpenTargets; ENSG00000136997; -.
DR Orphanet; 543; Burkitt lymphoma.
DR Orphanet; 480541; High grade B-cell lymphoma with MYC and/ or BCL2 and/or BCL6 rearrangement.
DR Orphanet; 99861; Precursor T-cell acute lymphoblastic leukemia.
DR PharmGKB; PA31353; -.
DR VEuPathDB; HostDB:ENSG00000136997; -.
DR eggNOG; KOG2483; Eukaryota.
DR GeneTree; ENSGT00940000155285; -.
DR HOGENOM; CLU_052560_0_0_1; -.
DR InParanoid; P01106; -.
DR OMA; EQLRNCC; -.
DR PhylomeDB; P01106; -.
DR TreeFam; TF106001; -.
DR BioCyc; MetaCyc:ENSG00000136997-MON; -.
DR PathwayCommons; P01106; -.
DR Reactome; R-HSA-1362277; Transcription of E2F targets under negative control by DREAM complex.
DR Reactome; R-HSA-201556; Signaling by ALK.
DR Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
DR Reactome; R-HSA-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
DR Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
DR Reactome; R-HSA-4411364; Binding of TCF/LEF:CTNNB1 to target gene promoters.
DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-HSA-69202; Cyclin E associated events during G1/S transition.
DR Reactome; R-HSA-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR Reactome; R-HSA-8866911; TFAP2 (AP-2) family regulates transcription of cell cycle factors.
DR Reactome; R-HSA-8951430; RUNX3 regulates WNT signaling.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR Reactome; R-HSA-9616222; Transcriptional regulation of granulopoiesis.
DR Reactome; R-HSA-9759194; Nuclear events mediated by NFE2L2.
DR SignaLink; P01106; -.
DR SIGNOR; P01106; -.
DR BioGRID-ORCS; 4609; 813 hits in 1120 CRISPR screens.
DR ChiTaRS; MYC; human.
DR EvolutionaryTrace; P01106; -.
DR GeneWiki; Myc; -.
DR GenomeRNAi; 4609; -.
DR Pharos; P01106; Tchem.
DR PRO; PR:P01106; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P01106; protein.
DR Bgee; ENSG00000136997; Expressed in upper leg skin and 180 other tissues.
DR ExpressionAtlas; P01106; baseline and differential.
DR Genevisible; P01106; HS.
DR GO; GO:0000785; C:chromatin; IMP:BHF-UCL.
DR GO; GO:0071943; C:Myc-Max complex; IPI:ComplexPortal.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0090571; C:RNA polymerase II transcription repressor complex; IPI:ComplexPortal.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; IDA:ARUK-UCL.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IMP:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IMP:BHF-UCL.
DR GO; GO:0070888; F:E-box binding; IDA:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0001221; F:transcription coregulator binding; IPI:UniProtKB.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; ISS:UniProtKB.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IDA:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; IDA:CAFA.
DR GO; GO:0034644; P:cellular response to UV; IEP:UniProtKB.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IDA:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB.
DR GO; GO:0051276; P:chromosome organization; IDA:UniProtKB.
DR GO; GO:0006112; P:energy reserve metabolic process; NAS:UniProtKB.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IDA:CAFA.
DR GO; GO:0044346; P:fibroblast apoptotic process; TAS:UniProtKB.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IDA:UniProtKB.
DR GO; GO:0000165; P:MAPK cascade; IMP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0051782; P:negative regulation of cell division; IDA:UniProtKB.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IDA:UniProtKB.
DR GO; GO:0045656; P:negative regulation of monocyte differentiation; IMP:UniProtKB.
DR GO; GO:0032873; P:negative regulation of stress-activated MAPK cascade; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0015671; P:oxygen transport; NAS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:CAFA.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
DR GO; GO:2000573; P:positive regulation of DNA biosynthetic process; IMP:UniProtKB.
DR GO; GO:1905643; P:positive regulation of DNA methylation; IMP:BHF-UCL.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IDA:UniProtKB.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IDA:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:CAFA.
DR GO; GO:1902255; P:positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator; IDA:UniProtKB.
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:1902895; P:positive regulation of miRNA transcription; IDA:ARUK-UCL.
DR GO; GO:2001022; P:positive regulation of response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0051973; P:positive regulation of telomerase activity; ISS:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0032986; P:protein-DNA complex disassembly; IDA:CAFA.
DR GO; GO:0010564; P:regulation of cell cycle process; IDA:ComplexPortal.
DR GO; GO:0010468; P:regulation of gene expression; IDA:MGI.
DR GO; GO:1904672; P:regulation of somatic stem cell population maintenance; ISS:UniProtKB.
DR GO; GO:0032204; P:regulation of telomere maintenance; IMP:BHF-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0010332; P:response to gamma radiation; IDA:UniProtKB.
DR GO; GO:0070848; P:response to growth factor; TAS:UniProtKB.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:UniProtKB.
DR DisProt; DP00260; -.
DR Gene3D; 4.10.280.10; -; 1.
DR IDEAL; IID00012; -.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
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 3D-structure; Acetylation; Activator; Alternative splicing;
KW Chromosomal rearrangement; DNA-binding; Glycoprotein; Isopeptide bond;
KW Nucleus; Phosphoprotein; Proto-oncogene; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..439
FT /note="Myc proto-oncogene protein"
FT /id="PRO_0000127293"
FT DOMAIN 354..406
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 204..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..434
FT /note="Leucine-zipper"
FT MOTIF 100..108
FT /note="9aaTAD"
FT /evidence="ECO:0000269|PubMed:34342803"
FT COMPBIAS 204..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 8
FT /note="Phosphothreonine; by RAF; in vitro"
FT /evidence="ECO:0000269|PubMed:9315742"
FT MOD_RES 58
FT /note="Phosphothreonine; by GSK3; alternate"
FT /evidence="ECO:0000269|PubMed:15103331,
FT ECO:0000269|PubMed:17558397, ECO:0000269|PubMed:8386367,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 62
FT /note="Phosphoserine; by DYRK2, GSK3 and CDK2"
FT /evidence="ECO:0000269|PubMed:15103331,
FT ECO:0000269|PubMed:17558397, ECO:0000269|PubMed:19966300,
FT ECO:0000269|PubMed:20713526, ECO:0000269|PubMed:22307329,
FT ECO:0000269|PubMed:25438055, ECO:0000269|PubMed:25803737,
FT ECO:0000269|PubMed:8386367, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 143
FT /note="N6-acetyllysine; by PCAF; alternate"
FT /evidence="ECO:0000269|PubMed:16126174"
FT MOD_RES 148
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 157
FT /note="N6-acetyllysine; by PCAF"
FT /evidence="ECO:0000269|PubMed:16126174"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 275
FT /note="N6-acetyllysine; by PCAF"
FT /evidence="ECO:0000269|PubMed:16126174"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 317
FT /note="N6-acetyllysine; by PCAF"
FT /evidence="ECO:0000269|PubMed:16126174"
FT MOD_RES 323
FT /note="N6-acetyllysine; by PCAF"
FT /evidence="ECO:0000269|PubMed:16126174"
FT MOD_RES 329
FT /note="Phosphoserine; by PIM2; in vitro"
FT /evidence="ECO:0000250|UniProtKB:P01108"
FT MOD_RES 371
FT /note="N6-acetyllysine; by PCAF"
FT /evidence="ECO:0000269|PubMed:16126174"
FT CARBOHYD 58
FT /note="O-linked (GlcNAc) threonine; alternate"
FT /evidence="ECO:0000269|PubMed:7642555"
FT /id="CAR_000033"
FT CROSSLNK 52
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 143
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 148
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 298
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1
FT /note="M -> MDFFRVVENQQPPATM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037813"
FT VARIANT 11
FT /note="N -> S (in dbSNP:rs4645959)"
FT /evidence="ECO:0000269|Ref.11"
FT /id="VAR_016327"
FT VARIANT 39
FT /note="E -> D (in a Burkitt lymphoma sample;
FT dbSNP:rs121918684)"
FT /evidence="ECO:0000269|PubMed:6419122,
FT ECO:0000269|PubMed:8220424"
FT /id="VAR_063384"
FT VARIANT 57
FT /note="P -> S (in a Burkitt lymphoma sample;
FT dbSNP:rs28933407)"
FT /evidence="ECO:0000269|PubMed:8220424"
FT /id="VAR_063385"
FT VARIANT 59
FT /note="P -> A (in a Burkitt lymphoma sample;
FT dbSNP:rs121918685)"
FT /evidence="ECO:0000269|PubMed:8220424"
FT /id="VAR_063386"
FT VARIANT 86
FT /note="N -> T (in a Burkitt lymphoma sample;
FT dbSNP:rs121918683)"
FT /evidence="ECO:0000269|PubMed:8220424"
FT /id="VAR_063387"
FT VARIANT 160
FT /note="G -> C (in dbSNP:rs4645960)"
FT /evidence="ECO:0000269|Ref.11"
FT /id="VAR_016328"
FT VARIANT 170
FT /note="V -> I (in dbSNP:rs4645961)"
FT /evidence="ECO:0000269|Ref.11"
FT /id="VAR_016329"
FT VARIANT 322
FT /note="A -> V (in dbSNP:rs4645968)"
FT /evidence="ECO:0000269|Ref.11"
FT /id="VAR_016330"
FT MUTAGEN 58
FT /note="T->A: Impairs interaction with FBXW7 and subsequent
FT degradation by the proteasome. Normal inhibition of Ras-
FT induced senescence."
FT /evidence="ECO:0000269|PubMed:15103331,
FT ECO:0000269|PubMed:17558397, ECO:0000269|PubMed:19966300,
FT ECO:0000269|PubMed:20713526"
FT MUTAGEN 62
FT /note="S->A: Impairs interaction with FBXW7 and subsequent
FT degradation by the proteasome. Impaired inhibition of Ras-
FT induced senescence. Abolishes phosphorylation by DYRK2, and
FT subsequent phosphorylation by GSK3B at Thr-58."
FT /evidence="ECO:0000269|PubMed:15103331,
FT ECO:0000269|PubMed:17558397, ECO:0000269|PubMed:19966300,
FT ECO:0000269|PubMed:20713526, ECO:0000269|PubMed:22307329"
FT MUTAGEN 62
FT /note="S->D: Phospho-mimetic mutant; abolished regulation
FT by AMBRA1."
FT /evidence="ECO:0000269|PubMed:25438055"
FT MUTAGEN 435
FT /note="R->K: Abolished ubiquitination and degradation by
FT the DCX(TRPC4AP) complex."
FT /evidence="ECO:0000269|PubMed:29779948"
FT CONFLICT 6..7
FT /note="SF -> TI (in Ref. 5; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 10
FT /note="R -> K (in Ref. 5; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="L -> LL (in Ref. 5; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="S -> P (in Ref. 7; CAA25288)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="G -> D (in Ref. 5; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="S -> N (in Ref. 5; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="S -> N (in Ref. 5; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="D -> G (in Ref. 5; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="C -> S (in Ref. 5; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="S -> R (in Ref. 5; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="S -> A (in Ref. 5; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="L -> F (in Ref. 5; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="P -> S (in Ref. 5; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT HELIX 98..103
FT /evidence="ECO:0007829|PDB:6E16"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:6E16"
FT HELIX 351..378
FT /evidence="ECO:0007829|PDB:6G6K"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:6G6K"
FT HELIX 392..435
FT /evidence="ECO:0007829|PDB:6G6K"
FT CONFLICT P01106-2:2
FT /note="D -> N (in Ref. 7; BAA01374)"
FT /evidence="ECO:0000305"
FT CONFLICT P01106-2:6
FT /note="V -> E (in Ref. 7; BAA01374)"
FT /evidence="ECO:0000305"
SQ 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
