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UniProtKB/Swiss-Prot entry P01106


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MYC_HUMAN
Primary accession number P01106
Secondary accession numbers P01107 Q14026
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on August 13, 1987 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 133)
Name and origin of the protein
Protein name Myc proto-oncogene protein
Synonyms c-Myc
Transcription factor p64
Gene name
Name: MYC
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0092-8674(83)90534-2; PubMed=6414718 [NCBI, ExPASy, EBI, Israel, Japan]
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].
PubMed=6321164 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1038/301722a0; PubMed=6298632 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1038/303725a0; PubMed=6304538 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1038/306760a0; PubMed=6419122 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1073/pnas.80.12.3642; PubMed=6304729 [NCBI, ExPASy, EBI, Israel, Japan]
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 [GENOMIC DNA].
PubMed=6714223 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0378-1119(93)90398-M; PubMed=8444346 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.
[10]
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.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cervix, Placenta, and Testis;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-252.
DOI=10.1038/309592a0; PubMed=6547209 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[13]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-170.
TISSUE=Promyelocytic leukemia;
PubMed=3540591 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[14]
PHOSPHORYLATION.
DOI=10.1111/j.1432-1033.1992.tb16964.x; PubMed=1597196 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[15]
PHOSPHORYLATION AT THR-58 AND SER-62.
DOI=10.1073/pnas.90.8.3216; PubMed=8386367 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[16]
GLYCOSYLATION AT THR-58.
DOI=10.1074/jbc.270.32.18961; PubMed=7642555 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[17]
PHOSPHORYLATION AT THR-8.
DOI=10.1016/S0014-5793(97)00992-7; PubMed=9315742 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[18]
ACETYLATION AT LYS-143; LYS-157; LYS-275; LYS-317; LYS-323 AND LYS-371, AND MASS SPECTROMETRY.
DOI=10.1016/j.bbrc.2005.08.075; PubMed=16126174 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[19]
INTERACTION WITH TAF1C.
DOI=10.1038/ncb1224; PubMed=15723054 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[20]
INTERACTION WITH PARP10.
DOI=10.1038/sj.onc.1208410; PubMed=15674325 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-58 AND SER-62, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[22]
INTERACTION WITH KDM5A AND KDM5B.
DOI=10.1101/gad.1523007; PubMed=17311883 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-58; SER-62 AND SER-71, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[24]
STRUCTURE BY NMR OF 402-434 IN COMPLEX WITH MAX.
DOI=10.1006/jmbi.1998.1914; PubMed=9680483 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L00058; AAA59882.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00057; AAA59882.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
K00535; AAA59880.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
K00534; AAA59880.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X00196; CAA25015.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X00198; CAA25015.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X00364; CAA25106.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
V00568; CAA23831.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
K02276; AAA36340.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
K01906; AAA59881.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
K01905; AAA59881.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D10493; BAA01375.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D10493; BAA01374.2; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT019768; AAV38573.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY214166; AAO21131.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000141; AAH00141.2; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000917; AAH00917.2; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC058901; AAH58901.2; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X00676; CAA25288.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M13929; AAA88092.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00745564; -.
PIR A01349; TVHUM.
A01350; TVHUT.
RefSeq NP_002458.2; -.
UniGene Hs.202453
3D structure databases
PDB
1A93; NMR; -; A=406-434.[ExPASy / RCSB / EBI]
1EE4; X-ray; 2.10 A; C/D/E/F=320-328.[ExPASy / RCSB / EBI]
1MV0; NMR; -; A=55-68.[ExPASy / RCSB / EBI]
1NKP; X-ray; 1.80 A; A/D=353-434.[ExPASy / RCSB / EBI]
2A93; NMR; -; A=406-434.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1A93; -.
1EE4; -.
1MV0; -.
1NKP; -.
2A93; -.
DisProt DP00260; -.
ModBase P01106.
Protein-protein interaction databases
DIP DIP:28143N; -.
IntAct P01106; 237.
PTM databases
GlycoSuiteDB P01106; -.
PhosphoSite P01106; -.
Enzyme and pathway databases
Pathway_Interaction_DB wnt_canonical_pathway; Canonical Wnt signaling pathway.
ceramidepathway; Ceramide signaling pathway.
foxm1pathway; FOXM1 transcription factor network.
il2_pi3kpathway; IL2 signaling events mediated by PI3K.
il2_stat5pathway; IL2 signaling events mediated by STAT5.
il2_1pathway; IL2-mediated signaling events.
il6_7pathway; IL6-mediated signaling events.
pdgfrbpathway; PDGFR-beta signaling pathway.
ps1pathway; Presenilin action in Notch and Wnt signaling.
smad2_3nuclearpathway; Regulation of nuclear SMAD2/3 signaling.
telomerasepathway; Regulation of Telomerase.
2D gel databases
SWISS-2DPAGE P01106; -.
Organism-specific databases
GeneCards GC08P128817; -.
H-InvDB HIX0007784; -.
HGNC HGNC:7553; MYC.
GenAtlas MYC.
MIM 190080; gene. [NCBI / EBI]
Orphanet 543; Burkitt lymphoma.
PharmGKB PA31353; -.
Gene expression databases
ArrayExpress P01106; -.
Bgee P01106; -.
CleanEx HS_MYC; -.
GermOnline ENSG00000136997; Homo sapiens.
Ontologies
GO
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0003700; Molecular function: transcription factor activity (traceable author statement from ProtInc).
GO:0007050; Biological process: cell cycle arrest (traceable author statement from ProtInc).
GO:0008283; Biological process: cell proliferation (traceable author statement from ProtInc).
GO:0006879; Biological process: cellular iron ion homeostasis (traceable author statement from ProtInc).
GO:0008284; Biological process: positive regulation of cell proliferation (inferred from direct assay from MGI).
GO:0032204; Biological process: regulation of telomere maintenance (inferred from mutant phenotype from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR001092; HLH_basic.
IPR011598; HLH_DNA_bd.
IPR003327; Myc-LZ.
IPR002418; Tscrpt_reg_Myc.
IPR012682; Tscrpt_reg_Myc_N.
Graphical view of domain structure.
Gene3D G3DSA:4.10.280.10; HLH_DNA_bd; 1.
Pfam PF00010; HLH; 1.
PF02344; Myc-LZ; 1.
PF01056; Myc_N; 1.
Pfam graphical view of domain structure.
PRINTS PR00044; LEUZIPPRMYC.
SMART SM00353; HLH; 1.
SMART graphical view of domain structure.
PROSITE PS50888; HLH; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P01106; -.
Genome annotation databases
Ensembl ENSG00000136997; Homo sapiens. [Contig view]
GeneID 4609; -.
KEGG hsa:4609; -.
Phylogenomic databases
HOGENOM P01106; -.
HOVERGEN P01106; -.
Other
NextBio 17740; -.
SOURCE MYC; Homo sapiens.
ProtoNet P01106.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Activator; Chromosomal rearrangement; DNA-binding; Glycoprotein; Nucleus; Phosphoprotein; Polymorphism; Proto-oncogene; Transcription; Transcription regulation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   439  439     Myc proto-oncogene protein. PRO_0000127293
DOMAIN   368   407  40     Helix-loop-helix motif. 
DOMAIN   413   434  22     Leucine-zipper (Potential). 
DNA_BIND   354   367  14     Basic motif. 
COMPBIAS   33    37  5     Poly-Gln. 
COMPBIAS   88    91  4     Poly-Gly. 
MOD_RES   8     8        Phosphothreonine; by RAF; in vitro. 
MOD_RES   58    58        Phosphothreonine; alternate. 
MOD_RES   62    62        Phosphoserine. 
MOD_RES   71    71        Phosphoserine. 
MOD_RES   143   143        N6-acetyllysine; by PCAF. 
MOD_RES   157   157        N6-acetyllysine; by PCAF. 
MOD_RES   275   275        N6-acetyllysine; by PCAF. 
MOD_RES   317   317        N6-acetyllysine; by PCAF. 
MOD_RES   323   323        N6-acetyllysine; by PCAF. 
MOD_RES   371   371        N6-acetyllysine; by PCAF. 
CARBOHYD   58    58        O-linked (GlcNAc); alternate [GlycoSuiteDB]. CAR_000033
VARIANT   11    11  1     N -> S (in dbSNP:rs4645959 [NCBI]). VAR_016327 
VARIANT   160   160  1     G -> C (in dbSNP:rs4645960 [NCBI]). VAR_016328 
VARIANT   170   170  1     V -> I (in dbSNP:rs4645961 [NCBI]). VAR_016329 
VARIANT   322   322  1     A -> V (in dbSNP:rs4645968 [NCBI]). VAR_016330 
CONFLICT   6     7        SF -> TI (in Ref. 5). 
CONFLICT   10    10        R -> K (in Ref. 5). 
CONFLICT   39    39        E -> D (in Ref. 5). 
CONFLICT   56    56        L -> LL (in Ref. 5). 
CONFLICT   62    62        S -> P (in Ref. 12; CAA25288). 
CONFLICT   88    88        G -> D (in Ref. 5). 
CONFLICT   92    92        S -> N (in Ref. 5). 
CONFLICT   114   114        S -> N (in Ref. 5). 
CONFLICT   120   120        D -> G (in Ref. 5). 
CONFLICT   171   171        C -> S (in Ref. 5). 
CONFLICT   203   203        S -> R (in Ref. 5). 
CONFLICT   230   230        S -> A (in Ref. 5). 
CONFLICT   240   240        L -> F (in Ref. 5). 
CONFLICT   245   245        P -> S (in Ref. 5). 
HELIX   353   378  26      
HELIX   382   384  3      
HELIX   392   434  43      
Sequence information
Length: 439 AA [This is the length of the unprocessed precursor] Molecular weight: 48804 Da [This is the MW of the unprocessed precursor] CRC64: ED5C028029A4C5D1 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPLNVSFTNR NYDLDYDSVQ PYFYCDEEEN FYQQQQQSEL QPPAPSEDIW KKFELLPTPP 

        70         80         90        100        110        120 
LSPSRRSGLC SPSYVAVTPF SLRGDNDGGG GSFSTADQLE MVTELLGGDM VNQSFICDPD 

       130        140        150        160        170        180 
DETFIKNIII QDCMWSGFSA AAKLVSEKLA SYQAARKDSG SPNPARGHSV CSTSSLYLQD 

       190        200        210        220        230        240 
LSAAASECID PSVVFPYPLN DSSSPKSCAS QDSSAFSPSS DSLLSSTESS PQGSPEPLVL 

       250        260        270        280        290        300 
HEETPPTTSS DSEEEQEDEE EIDVVSVEKR QAPGKRSESG SPSAGGHSKP PHSPLVLKRC 

       310        320        330        340        350        360 
HVSTHQHNYA APPSTRKDYP AAKRVKLDSV RVLRQISNNR KCTSPRSSDT EENVKRRTHN 

       370        380        390        400        410        420 
VLERQRRNEL KRSFFALRDQ IPELENNEKA PKVVILKKAT AYILSVQAEE QKLISEEDLL 

       430 
RKRREQLKHK LEQLRNSCA 

P01106 in FASTA format

View entry in raw text format (no links)
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