Reviewed, UniProtKB/Swiss-Prot P01106 (MYC_HUMAN)

Names and origin

Protein names

Recommended name:
    Myc proto-oncogene protein
Alternative name(s):
    Proto-oncogene c-Myc
    Transcription factor p64
    Class E basic helix-loop-helix protein 39
      Short name=bHLHe39

Gene names

Name:	MYC
Synonyms:	BHLHE39

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	439 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Participates in the regulation of gene transcription. Binds DNA in a non-specific manner, yet also specifically 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 KDM5A and KDM5B. Ref.22 Ref.23 Ref.25
Subcellular location	Nucleus.
Post-translational modification	Phosphorylated by PRKDC. Ref.17 Ref.18 Ref.20 Ref.24 Ref.26 Ref.27
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.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Disease	Proto-oncogene
Ligand	DNA-binding
Molecular function	Activator
PTM	Acetylation Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	branching involved in ureteric bud morphogenesis Inferred from sequence or structural similarity. Source: UniProtKB cell cycle arrest Traceable author statement. Source: ProtInc cell proliferation Traceable author statement. Source: ProtInc cellular iron ion homeostasis Traceable author statement. Source: ProtInc positive regulation of metanephric cap mesenchymal cell proliferation Inferred from sequence or structural similarity. Source: UniProtKB regulation of telomere maintenance Inferred from mutant phenotype. Source: UniProtKB regulation of transcription from RNA polymerase II promoter Traceable author statement. Source: ProtInc transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from direct assay. Source: MGI
Molecular function	protein binding Inferred from physical interaction. Source: UniProtKB transcription factor activity Traceable author statement. Source: ProtInc
Complete GO annotation...

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

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P01106-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P01106-2) The sequence of this isoform differs from the canonical sequence as follows:      1-1: M → MDFFRVVENQQPPATM
Note: Initiates from CTG codon.
Sequence annotation (Features)
	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
	Sequence conflict	2	1	D → N in BAA01374. Ref.7
	Sequence conflict	6	1	V → E in BAA01374. Ref.7

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

40

Helix-loop-helix motif

Domain

413 – 434

22

Leucine-zipper

DNA binding

354 – 367

14

Basic motif

Compositional bias

33 – 37

5

Poly-Gln

Compositional bias

88 – 91

4

Poly-Gly

Amino acid modifications

Modified residue

6

1

Phosphoserine Ref.27

Modified residue

8

1

Phosphothreonine; by RAF; in vitro Ref.20

Modified residue

58

1

Phosphothreonine; alternate Ref.18 Ref.24 Ref.26

Modified residue

62

1

Phosphoserine Ref.18 Ref.24 Ref.26

Modified residue

71

1

Phosphoserine Ref.26

Modified residue

143

1

N6-acetyllysine; by PCAF Ref.21

Modified residue

148

1

N6-acetyllysine Ref.28

Modified residue

157

1

N6-acetyllysine; by PCAF Ref.21

Modified residue

275

1

N6-acetyllysine; by PCAF Ref.21

Modified residue

317

1

N6-acetyllysine; by PCAF Ref.21

Modified residue

323

1

N6-acetyllysine; by PCAF Ref.21

Modified residue

344

1

Phosphoserine Ref.27

Modified residue

348

1

Phosphoserine Ref.27

Modified residue

371

1

N6-acetyllysine; by PCAF Ref.21

Glycosylation

58

1

O-linked (GlcNAc); alternate Ref.19

CAR_000033

Natural variations

Alternative sequence

1

1

M → MDFFRVVENQQPPATM in isoform 2.

VSP_037813

Natural variant

11

1

N → S: dbSNP rs4645959. Ref.11

VAR_016327

Natural variant

160

1

G → C: dbSNP rs4645960. Ref.11

VAR_016328

Natural variant

170

1

V → I: dbSNP rs4645961. Ref.11

VAR_016329

Natural variant

322

1

A → V: dbSNP rs4645968. Ref.11

VAR_016330

Experimental info

Sequence conflict

6 – 7

2

SF → TI Ref.5

Sequence conflict

10

1

R → K Ref.5

Sequence conflict

39

1

E → D Ref.5

Sequence conflict

56

1

L → LL Ref.5

Sequence conflict

62

1

S → P in CAA25288. Ref.7

Sequence conflict

88

1

G → D Ref.5

Sequence conflict

92

1

S → N Ref.5

Sequence conflict

114

1

S → N Ref.5

Sequence conflict

120

1

D → G Ref.5

Sequence conflict

171

1

C → S Ref.5

Sequence conflict

203

1

S → R Ref.5

Sequence conflict

230

1

S → A Ref.5

Sequence conflict

240

1

L → F Ref.5

Sequence conflict

245

1

P → S Ref.5

Secondary structure

1

.

.

.

.

.

.

.

439

Helix Strand Turn

Details...

Helix

353 – 378

26

Helix

382 – 384

3

Helix

392 – 434

43

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 13, 1987. Version 1. Checksum: ED5C028029A4C5D1	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
	Isoform 2. Checksum: 8B4107BB740689E5	FASTA	454	50,565
	10 20 30 40 50 60 MDFFRVVENQ QPPATMPLNV SFTNRNYDLD YDSVQPYFYC DEEENFYQQQ QQSELQPPAP 70 80 90 100 110 120 SEDIWKKFEL LPTPPLSPSR RSGLCSPSYV AVTPFSLRGD NDGGGGSFST ADQLEMVTEL 130 140 150 160 170 180 LGGDMVNQSF ICDPDDETFI KNIIIQDCMW SGFSAAAKLV SEKLASYQAA RKDSGSPNPA 190 200 210 220 230 240 RGHSVCSTSS LYLQDLSAAA SECIDPSVVF PYPLNDSSSP KSCASQDSSA FSPSSDSLLS 250 260 270 280 290 300 STESSPQGSP EPLVLHEETP PTTSSDSEEE QEDEEEIDVV SVEKRQAPGK RSESGSPSAG 310 320 330 340 350 360 GHSKPPHSPL VLKRCHVSTH QHNYAAPPST RKDYPAAKRV KLDSVRVLRQ ISNNRKCTSP 370 380 390 400 410 420 RSSDTEENVK RRTHNVLERQ RRNELKRSFF ALRDQIPELE NNEKAPKVVI LKKATAYILS 430 440 450 VQAEEQKLIS EEDLLRKRRE QLKHKLEQLR NSCA

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], ALTERNATIVE SPLICING (ISOFORM 1).
[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], ALTERNATIVE SPLICING (ISOFORM 1).
[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], ALTERNATIVE SPLICING (ISOFORM 1).
[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] (ISOFORM 1).
[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] (ISOFORM 1).
[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], ALTERNATIVE SPLICING (ISOFORM 1).
[7]	"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 [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-252.
[8]	"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], ALTERNATIVE SPLICING (ISOFORM 1).
[9]	"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], ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
[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] (ISOFORM 1).
[11]	NIEHS SNPs program 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.
[12]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Uterus.
[13]	"DNA sequence and analysis of human chromosome 8." 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. Nature 439:331-335(2006) [PubMed: 16421571] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[14]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[15]	"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] (ISOFORM 2). Tissue: Cervix, Placenta and Testis.
[16]	"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 (ISOFORM 1). Tissue: Promyelocytic leukemia.
[17]	"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.
[18]	"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.
[19]	"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.
[20]	"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.
[21]	"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.
[22]	"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.
[23]	"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.
[24]	"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.
[25]	"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 KDM5A AND KDM5B.
[26]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-58; SER-62 AND SER-71, MASS SPECTROMETRY.
[27]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-344 AND SER-348, MASS SPECTROMETRY.
[28]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-148, MASS SPECTROMETRY.
[29]	"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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

NIEHS-SNPs

Wikipedia

Myc entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L00058, L00057 Genomic DNA. Translation: AAA59882.1.
K00535, K00534 Genomic DNA. Translation: AAA59880.1.
K00535, K00534 Genomic DNA. Translation: ABW69847.1.
X00196, X00198 Genomic DNA. Translation: CAA25015.2.
X00364 Genomic DNA. Translation: CAA25106.1.
V00568 mRNA. Translation: CAA23831.1.
K01906, K01905 Genomic DNA. Translation: AAA59881.1.
K02276 mRNA. Translation: AAA36340.1.
X00676 Genomic DNA. Translation: CAA25288.1.
D10493 Genomic DNA. Translation: BAA01374.2.
D10493 Genomic DNA. Translation: BAA01375.1.
BT019768 mRNA. Translation: AAV38573.1.
AY214166 Genomic DNA. Translation: AAO21131.1.
AK312883 mRNA. Translation: BAG35731.1.
AC103819 Genomic DNA. No translation available.
CH471060 Genomic DNA. Translation: EAW92098.1.
BC000141 mRNA. Translation: AAH00141.2.
BC000917 mRNA. Translation: AAH00917.2.
BC058901 mRNA. Translation: AAH58901.2.
M13929 mRNA. Translation: AAA88092.1.

IPI

IPI00033016.
IPI00935431.

PIR

TVHUM. A01349.
TVHUT. A01350.

RefSeq

NP_002458.2.

UniGene

Hs.202453

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

DisProt

DP00260.

ModBase

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Protein-protein interaction databases

DIP

DIP-28143N.

IntAct

P01106. 237 interactions.

STRING

P01106.

PTM databases

GlycoSuiteDB

P01106.

PhosphoSite

P01106.

2-D gel databases

SWISS-2DPAGE

P01106.

Proteomic databases

PRIDE

P01106.

Genome annotation databases

Ensembl

ENST00000377970; ENSP00000367207; ENSG00000136997; Homo sapiens. [Genome view]

GeneID

4609.

KEGG

hsa:4609.

Organism-specific databases

CTD

4609.

GeneCards

GC08P128817.

H-InvDB

HIX0007784.

HGNC

HGNC:7553. MYC.

MIM

190080. gene.

Orphanet

543. Burkitt lymphoma.

PharmGKB

PA31353.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG11147.

HOGENOM

HBG445611.

HOVERGEN

P01106.

InParanoid

P01106.

PhylomeDB

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.

Gene expression databases

ArrayExpress

P01106.

Bgee

P01106.

CleanEx

HS_MYC.

Genevestigator

P01106.

GermOnline

ENSG00000136997. Homo sapiens.

Family and domain databases

InterPro

IPR001092. HLH_DNA-bd_dom.
IPR011598. HLH_DNA_bd.
IPR003327. Myc-LZ.
IPR002418. Tscrpt_reg_Myc.
IPR012682. Tscrpt_reg_Myc_N.
[Graphical view]

Gene3D

G3DSA:4.10.280.10. HLH_DNA_bd. 1 hit.

Pfam

PF00010. HLH. 1 hit.
PF02344. Myc-LZ. 1 hit.
PF01056. Myc_N. 1 hit.
[Graphical view]

PRINTS

PR00044. LEUZIPPRMYC.

SMART

SM00353. HLH. 1 hit.
[Graphical view]

PROSITE

PS50888. HLH. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

17740.

SOURCE

Search...

Entry information

Entry name

MYC_HUMAN

Accession

Primary (citable) accession number: P01106
Secondary accession number(s): A8WFE7, P01107, Q14026

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	August 13, 1987
Last modified:	February 9, 2010
This is version 142 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.