Myc proto-oncogene protein - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P01106 (MYC_HUMAN)

Last modified November 25, 2008. Version 127. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Myc proto-oncogene protein
Alternative name(s):
    c-Myc
    Transcription factor p64

Gene names

Name:

MYC

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	439 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Participates in the regulation of gene transcription. Binds DNA both in a non-specific manner and also specifically to recognizes the core sequence 5'-CAC[GA]TG-3'. Seems to activate the transcription of growth-related genes.
Subunit structure	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 JARID1A and JARID1B.
Subcellular location	Nucleus.
Post-translational modification	Phosphorylated by PRKDC.
Involvement in disease	Overexpression of MYC is implicated in the etiology of a variety of hematopoietic tumors. 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.
Sequence similarities	Contains 1 basic helix-loop-helix (bHLH) domain.
Sequence caution	The sequence BAA01374.2 differs from that shown. Reason: Erroneous gene model prediction.

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Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Chromosomal rearrangement Polymorphism
Disease	Proto-oncogene
Ligand	DNA-binding
Molecular function	Activator
PTM	Acetylation Glycoprotein Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	cell cycle arrest Traceable author statement. Source: ProtInc cellular iron ion homeostasis Traceable author statement. Source: ProtInc positive regulation of cell proliferation Inferred from direct assay. Source: MGI regulation of transcription from RNA polymerase II promoter Traceable author statement. Source: ProtInc
Molecular function	protein binding Inferred from physical interaction. Source: UniProtKB transcription factor activity Traceable author statement. Source: ProtInc
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
	P03070	1	EBI-447544,EBI-617698	From a different organism.
CHD4	Q14839	1	EBI-447544,EBI-372916
EFTUD2	Q15029	2	EBI-447544,EBI-357897
EP300	Q09472	1	EBI-447544,EBI-447295
FBXW7	Q969H0	1	EBI-447544,EBI-359574
FBXW8	Q8N3Y1	1	EBI-447544,EBI-914770
KIAA1524	Q8TCG1	2	EBI-447544,EBI-1379376
KIAA1967	Q8N163	2	EBI-447544,EBI-355410
MAX	P61244	8	EBI-447544,EBI-878388
Max	P52164	2	EBI-447544,EBI-1184963	From a different organism.
MCM7	P33993	2	EBI-447544,EBI-355924
PIAS2	O75928	2	EBI-447544,EBI-348555
SKP2	Q13309	2	EBI-447544,EBI-456291
SNIP1	Q8TAD8	5	EBI-447544,EBI-749336
SP1	P08047	2	EBI-447544,EBI-298336
TRRAP	Q9Y4A5	2	EBI-447544,EBI-399128
vIRF-3	Q9DUN1	1	EBI-447544,EBI-1647907	From a different organism.
ZBTB17	Q13105	1	EBI-447544,EBI-372156

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 439

439

Myc proto-oncogene protein

PRO_0000127293

Regions

Domain

368 – 407

Helix-loop-helix motif

Domain

413 – 434

Leucine-zipper Potential

DNA binding

354 – 367

Basic motif

Compositional bias

33 – 37

Poly-Gln

Compositional bias

88 – 91

Poly-Gly

Amino acid modifications

Modified residue

Phosphothreonine; by RAF; in vitro

Modified residue

Phosphothreonine; alternate

Modified residue

Phosphoserine

Modified residue

143

N6-acetyllysine; by PCAF

Modified residue

157

N6-acetyllysine; by PCAF

Modified residue

275

N6-acetyllysine; by PCAF

Modified residue

317

N6-acetyllysine; by PCAF

Modified residue

323

N6-acetyllysine; by PCAF

Modified residue

371

N6-acetyllysine; by PCAF

Glycosylation

O-linked (GlcNAc); alternate

CAR_000033

Natural variations

Natural variant

N → S: dbSNP rs4645959.

VAR_016327

Natural variant

160

G → C: dbSNP rs4645960.

VAR_016328

Natural variant

170

V → I: dbSNP rs4645961.

VAR_016329

Natural variant

322

A → V: dbSNP rs4645968.

VAR_016330

Experimental info

Sequence conflict

6 – 7

SF → TI Ref.5

Sequence conflict

R → K Ref.5

Sequence conflict

E → D Ref.5

Sequence conflict

L → LL Ref.5

Sequence conflict

S → P in CAA25288. Ref.12

Sequence conflict

G → D Ref.5

Sequence conflict

S → N Ref.5

Sequence conflict

114

S → N Ref.5

Sequence conflict

120

D → G Ref.5

Sequence conflict

171

C → S Ref.5

Sequence conflict

203

S → R Ref.5

Sequence conflict

230

S → A Ref.5

Sequence conflict

240

L → F Ref.5

Sequence conflict

245

P → S Ref.5

Secondary structure

439

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P01106-1 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: ED5C028029A4C5D1
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FASTA

439

48,804

        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

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The human c-myc oncogene: structural consequences of translocation into the IgH locus in Burkitt lymphoma." Battey J., Moulding C., Taub R., Murphy W., Stewart T., Potter H., Lenoir G., Leder P. Cell 34:779-787(1983) [PubMed: 6414718] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Sequence of the murine and human cellular myc oncogenes and two modes of myc transcription resulting from chromosome translocation in B lymphoid tumours." Bernard O., Cory S., Gerondakis S., Webb E., Adams J.M. EMBO J. 2:2375-2383(1983) [PubMed: 6321164] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Identification and nucleotide sequence of a human locus homologous to the v-myc oncogene of avian myelocytomatosis virus MC29." Colby W.W., Chen E.Y., Smith D.H., Levinson A.D. Nature 301:722-725(1983) [PubMed: 6298632] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Nucleotide sequence of cloned cDNA of human c-myc oncogene." Watt R., Stanton L.W., Marcu K.B., Gallo R.C., Croce C.M., Rovera G. Nature 303:725-728(1983) [PubMed: 6304538] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]	"Altered nucleotide sequences of a translocated c-myc gene in Burkitt lymphoma." Rabbitts T.H., Hamlyn P.H., Baer R. Nature 306:760-765(1983) [PubMed: 6419122] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]	"Nucleotide sequence analysis of human c-myc locus, chicken homologue, and myelocytomatosis virus MC29 transforming gene reveals a highly conserved gene product." Watson D.K., Psallidopoulos M.C., Samuel K.P., Dalla-Favera R., Papas T.S. Proc. Natl. Acad. Sci. U.S.A. 80:3642-3645(1983) [PubMed: 6304729] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]	"Nucleotide sequence of the human c-myc locus: provocative open reading frame within the first exon." Gazin C., Dupont S., de Dinechin D., Hampe A., Masson J.-M., Martin P., Stehelin D., Galibert F. EMBO J. 3:383-387(1984) [PubMed: 6714223] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]	"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." Tachibana K., Takayama N., Matsuo K., Kato S., Yamamoto K., Ohyama K., Umezawa A., Takano T. Gene 124:231-237(1993) [PubMed: 8444346] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[9]	"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu)." Rieder M.J., Livingston R.J., Daniels M.R., Montoya M.A., Chung M.-W., Miyamoto K.E., Nguyen C.P., Nguyen D.A., Poel C.L., Robertson P.D., Schackwitz W.S., Sherwood J.K., Witrak L.A., Nickerson D.A. Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-11; CYS-160; ILE-170 AND VAL-322.
[10]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." 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. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[11]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Cervix, Placenta and Testis.
[12]	"Effect of somatic mutation within translocated c-myc genes in Burkitt's lymphoma." Rabbitts T.H., Forster A., Hamlyn P., Baer R. Nature 309:592-597(1984) [PubMed: 6547209] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-252.
[13]	"Novel promoter upstream of the human c-myc gene and regulation of c-myc expression in B-cell lymphomas." Bentley D.L., Groudine M. Mol. Cell. Biol. 6:3481-3489(1986) [PubMed: 3540591] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-170. Tissue: Promyelocytic leukemia.
[14]	"DNA-activated protein kinase in Raji Burkitt's lymphoma cells. Phosphorylation of c-Myc oncoprotein." Iijima S., Teraoka H., Date T., Tsukada K. Eur. J. Biochem. 206:595-603(1992) [PubMed: 1597196] [Abstract] Cited for: PHOSPHORYLATION.
[15]	"Transactivation of gene expression by Myc is inhibited by mutation at the phosphorylation sites Thr-58 and Ser-62." Gupta S., Seth A., Davis R.J. Proc. Natl. Acad. Sci. U.S.A. 90:3216-3220(1993) [PubMed: 8386367] [Abstract] Cited for: PHOSPHORYLATION AT THR-58 AND SER-62.
[16]	"c-Myc is glycosylated at threonine 58, a known phosphorylation site and a mutational hot spot in lymphomas." Chou T.-Y., Hart G.W., Dang C.V. J. Biol. Chem. 270:18961-18965(1995) [PubMed: 7642555] [Abstract] Cited for: GLYCOSYLATION AT THR-58.
[17]	"c-Raf kinase binds to N-terminal domain of c-Myc." Alexandrov I., Shlyakhova L., Vartanian A., Zajac-Kaye M., Alexandrova N. FEBS Lett. 414:465-470(1997) [PubMed: 9315742] [Abstract] Cited for: PHOSPHORYLATION AT THR-8.
[18]	"Six lysine residues on c-Myc are direct substrates for acetylation by p300." Zhang K., Faiola F., Martinez E. Biochem. Biophys. Res. Commun. 336:274-280(2005) [PubMed: 16126174] [Abstract] Cited for: ACETYLATION AT LYS-143; LYS-157; LYS-275; LYS-317; LYS-323 AND LYS-371, MASS SPECTROMETRY.
[19]	"c-Myc binds to human ribosomal DNA and stimulates transcription of rRNA genes by RNA polymerase I." Grandori C., Gomez-Roman N., Felton-Edkins Z.A., Ngouenet C., Galloway D.A., Eisenman R.N., White R.J. Nat. Cell Biol. 7:311-318(2005) [PubMed: 15723054] [Abstract] Cited for: INTERACTION WITH TAF1C.
[20]	"PARP-10, a novel Myc-interacting protein with poly(ADP-ribose) polymerase activity, inhibits transformation." 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. Oncogene 24:1982-1993(2005) [PubMed: 15674325] [Abstract] Cited for: INTERACTION WITH PARP10.
[21]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-58 AND SER-62, MASS SPECTROMETRY. Tissue: Epithelium.
[22]	"The Trithorax group protein Lid is a trimethyl histone H3K4 demethylase required for dMyc-induced cell growth." Secombe J., Li L., Carlos L., Eisenman R.N. Genes Dev. 21:537-551(2007) [PubMed: 17311883] [Abstract] Cited for: INTERACTION WITH JARID1A AND JARID1B.
[23]	"Insights into the mechanism of heterodimerization from the 1H-NMR solution structure of the c-Myc-Max heterodimeric leucine zipper." Lavigne P., Crump M.P., Gagne S.M., Hodges R.S., Kay C.M., Sykes B.D. J. Mol. Biol. 281:165-181(1998) [PubMed: 9680483] [Abstract] Cited for: STRUCTURE BY NMR OF 402-434 IN COMPLEX WITH MAX.
+	Additional computationally mapped references.

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Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Wikipedia

Myc entry

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Cross-references

Sequence databases

L00058, L00057 Genomic DNA. Translation: AAA59882.1.
K00535, K00534 Genomic DNA. Translation: AAA59880.1.
X00196, X00198 Genomic DNA. Translation: CAA25015.2.
X00364 Genomic DNA. Translation: CAA25106.1.
V00568 mRNA. Translation: CAA23831.1.
K02276 mRNA. Translation: AAA36340.1.
K01906, K01905 Genomic DNA. Translation: AAA59881.1.
D10493 Genomic DNA. Translation: BAA01375.1.
D10493 Genomic DNA. Translation: BAA01374.2. Sequence problems.
AY214166 Genomic DNA. Translation: AAO21131.1.
BT019768 mRNA. Translation: AAV38573.1.
BC000141 mRNA. Translation: AAH00141.2. Different initiation.
BC000917 mRNA. Translation: AAH00917.2. Different initiation.
BC058901 mRNA. Translation: AAH58901.2. Different initiation.
X00676 Genomic DNA. Translation: CAA25288.1.
M13929 mRNA. Translation: AAA88092.1.

PIR

TVHUM. A01349.
TVHUT. A01350.

RefSeq

NP_002458.2.

UniGene

Hs.202453

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A93	NMR	-	A	406-434	[»]
1EE4	X-ray	2.10	C/D/E/F	320-328	[»]
1MV0	NMR	-	A	55-68	[»]
1NKP	X-ray	1.80	A/D	353-434	[»]
2A93	NMR	-	A	406-434	[»]