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P01106 (MYC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 192. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myc proto-oncogene protein
Alternative name(s):
Class E basic helix-loop-helix protein 39
Short name=bHLHe39
Proto-oncogene c-Myc
Transcription factor p64
Gene names
Name:MYC
Synonyms:BHLHE39
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length439 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. Activates the transcription of growth-related genes.

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. Interacts (when phosphorylated at Thr-58 and Ser-62) with FBXW7. Interacts with PIM2. Interacts with NO66. The heterodimer MYC:MAX interacts with ABI1; the interaction may enhance MYC:MAX transcriptional activity. Ref.23 Ref.25 Ref.26 Ref.29 Ref.30 Ref.31 Ref.32

Subcellular location

Nucleusnucleoplasm. Nucleusnucleolus Ref.32.

Post-translational modification

Phosphorylated by PRKDC. Phosphorylation at Ser-329 by PIM2 leads to the stabilization of MYC By similarity. Phosphorylation at Ser-62 by CDK2 prevents Ras-induced senescence. Phosphorylated at Ser-62 by DYRK2; this primes the protein for subsequent phosphorylation by GSK3B at Thr-58. Phosphorylation at Thr-58 and Ser-62 by GSK3 is required for ubiquitination and degradation by the proteasome. Ref.18 Ref.20 Ref.22 Ref.23 Ref.32 Ref.36 Ref.37 Ref.41

Ubiquitinated by the SCF(FBXW7) complex when phosphorylated at Thr-58 and Ser-62, leading to its degradation by the proteasome. In the nucleoplasm, ubiquitination is counteracted by USP28, which interacts with isoform 1 of FBXW7 (FBW7alpha), leading to its deubiquitination and preventing degradation. In the nucleolus, however, ubiquitination is not counteracted by USP28, due to the lack of interaction between isoform 4of FBXW7 (FBW7gamma) and USP28, explaining the selective MYC degradation in the nucleolus. Also polyubiquitinated by the DCX(TRUSS) complex. Ref.18 Ref.20 Ref.22 Ref.23 Ref.32 Ref.36 Ref.37 Ref.41

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.

Burkitt lymphoma (BL) [MIM:113970]: A form of undifferentiated malignant lymphoma commonly manifested as a large osteolytic lesion in the jaw or as an abdominal mass.
Note: The gene represented in this entry is involved in disease pathogenesis. Chromosomal aberrations involving MYC are usually found in Burkitt lymphoma. Translocations t(8;14), t(8;22) or t(2;8) which juxtapose MYC to one of the heavy or light chain immunoglobulin gene loci.

Biotechnological use

POU5F1/OCT4, SOX2, MYC/c-Myc and KLF4 are the four Yamanaka factors. When combined, these factors are sufficient to reprogram differentiated cells to an embryonic-like state designated iPS (induced pluripotent stem) cells. iPS cells exhibit the morphology and growth properties of ES cells and express ES cell marker genes. Ref.28

Sequence similarities

Contains 1 bHLH (basic helix-loop-helix) domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DiseaseProto-oncogene
   LigandDNA-binding
   Molecular functionActivator
   PTMAcetylation
Glycoprotein
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processMAPK cascade

Inferred from mutant phenotype Ref.29. Source: UniProtKB

Notch signaling pathway

Traceable author statement. Source: Reactome

branching involved in ureteric bud morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

canonical Wnt signaling pathway

Inferred from direct assay PubMed 21533051. Source: UniProtKB

cell cycle arrest

Inferred from direct assay PubMed 10962037. Source: UniProtKB

cellular iron ion homeostasis

Inferred from direct assay PubMed 9924025. Source: UniProtKB

cellular response to DNA damage stimulus

Inferred from direct assay Ref.29. Source: UniProtKB

cellular response to UV

Inferred from expression pattern Ref.29. Source: UniProtKB

cellular response to drug

Inferred from direct assay Ref.29PubMed 19179467. Source: UniProtKB

chromatin remodeling

Inferred from direct assay PubMed 21533051. Source: UniProtKB

chromosome organization

Inferred from direct assay PubMed 10962037. Source: UniProtKB

energy reserve metabolic process

Non-traceable author statement PubMed 9924025. Source: UniProtKB

fibroblast apoptotic process

Traceable author statement PubMed 10962037. Source: UniProtKB

gene expression

Traceable author statement. Source: Reactome

negative regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell division

Inferred from direct assay PubMed 10962037. Source: UniProtKB

negative regulation of fibroblast proliferation

Inferred from direct assay PubMed 10962037. Source: UniProtKB

negative regulation of monocyte differentiation

Inferred from mutant phenotype PubMed 9924025. Source: UniProtKB

negative regulation of stress-activated MAPK cascade

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 9924025. Source: UniProtKB

oxygen transport

Non-traceable author statement PubMed 9924025. Source: UniProtKB

positive regulation of DNA biosynthetic process

Inferred from mutant phenotype PubMed 9924025. Source: UniProtKB

positive regulation of cell proliferation

Inferred from direct assay PubMed 15994933. Source: MGI

positive regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from direct assay PubMed 19179467. Source: UniProtKB

positive regulation of epithelial cell proliferation

Inferred from direct assay PubMed 18987311. Source: UniProtKB

positive regulation of fibroblast proliferation

Inferred from direct assay PubMed 18987311PubMed 9924025. Source: UniProtKB

positive regulation of mesenchymal cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of metanephric cap mesenchymal cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of response to DNA damage stimulus

Inferred from direct assay PubMed 19179467. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 9924025. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 10962037Ref.32PubMed 18818310. Source: UniProtKB

regulation of gene expression

Inferred from direct assay PubMed 21447833. Source: MGI

regulation of telomere maintenance

Inferred from mutant phenotype PubMed 17765874. Source: BHF-UCL

response to drug

Inferred from expression pattern PubMed 18291362. Source: UniProtKB

response to gamma radiation

Inferred from direct assay PubMed 19179467. Source: UniProtKB

response to growth factor

Traceable author statement PubMed 18987311. Source: UniProtKB

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription, DNA-templated

Traceable author statement. Source: Reactome

transforming growth factor beta receptor signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentnucleolus

Inferred from direct assay Ref.32. Source: UniProtKB

nucleoplasm

Inferred from direct assay Ref.32. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 11793365. Source: UniProtKB

protein complex

Inferred from direct assay Ref.29. Source: UniProtKB

spindle

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionDNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

E-box binding

Inferred from direct assay PubMed 18818310. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 10597290PubMed 12706874Ref.23Ref.26PubMed 17314511Ref.29PubMed 20208519Ref.38PubMed 21807113PubMed 9308237PubMed 9708738. Source: UniProtKB

protein complex binding

Inferred from direct assay PubMed 18987311. Source: UniProtKB

repressing transcription factor binding

Inferred from physical interaction Ref.26. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 9924025. Source: UniProtKB

transcription factor binding

Inferred from physical interaction Ref.26. Source: UniProtKB

Complete GO annotation...

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 439439Myc proto-oncogene protein
PRO_0000127293

Regions

Domain354 – 40653bHLH
Region413 – 43422Leucine-zipper
Compositional bias33 – 375Poly-Gln
Compositional bias88 – 914Poly-Gly

Amino acid modifications

Modified residue61Phosphoserine Ref.39
Modified residue81Phosphothreonine; by RAF; in vitro Ref.22
Modified residue581Phosphothreonine; by GSK3; alternate Ref.20 Ref.23 Ref.27 Ref.32 Ref.33 Ref.40
Modified residue621Phosphoserine; by DYRK2, GSK3 and CDK2 Ref.20 Ref.23 Ref.32 Ref.33 Ref.36 Ref.37 Ref.40 Ref.41
Modified residue711Phosphoserine Ref.33
Modified residue1431N6-acetyllysine; by PCAF Ref.24
Modified residue1481N6-acetyllysine Ref.35
Modified residue1571N6-acetyllysine; by PCAF Ref.24
Modified residue1611Phosphoserine Ref.39
Modified residue2751N6-acetyllysine; by PCAF Ref.24
Modified residue3171N6-acetyllysine; by PCAF Ref.24
Modified residue3231N6-acetyllysine; by PCAF Ref.24
Modified residue3291Phosphoserine; by PIM2; in vitro By similarity
Modified residue3711N6-acetyllysine; by PCAF Ref.24
Glycosylation581O-linked (GlcNAc); alternate Ref.21
CAR_000033

Natural variations

Alternative sequence11M → MDFFRVVENQQPPATM in isoform 2.
VSP_037813
Natural variant111N → S. Ref.11
Corresponds to variant rs4645959 [ dbSNP | Ensembl ].
VAR_016327
Natural variant391E → D in a Burkitt lymphoma symple. Ref.5 Ref.19
VAR_063384
Natural variant571P → S in a Burkitt lymphoma sample. Ref.19
VAR_063385
Natural variant591P → A in a Burkitt lymphoma sample. Ref.19
VAR_063386
Natural variant861N → T in a Burkitt lymphoma sample. Ref.19
VAR_063387
Natural variant1601G → C. Ref.11
Corresponds to variant rs4645960 [ dbSNP | Ensembl ].
VAR_016328
Natural variant1701V → I. Ref.11
Corresponds to variant rs4645961 [ dbSNP | Ensembl ].
VAR_016329
Natural variant3221A → V. Ref.11
Corresponds to variant rs4645968 [ dbSNP | Ensembl ].
VAR_016330

Experimental info

Mutagenesis581T → A: Impairs interaction with FBXW7 and subsequent degradation by the proteasome. Normal inhibition of Ras-induced senescence. Ref.23 Ref.32 Ref.36 Ref.37
Mutagenesis621S → A: Impairs interaction with FBXW7 and subsequent degradation by the proteasome. Impaired inhibition of Ras-induced senescence. Abolishes phosphorylation by DYRK2, and subsequent phosphorylation by GSK3B at Thr-58. Ref.23 Ref.32 Ref.36 Ref.37 Ref.41
Sequence conflict6 – 72SF → TI no nucleotide entry Ref.5
Sequence conflict101R → K no nucleotide entry Ref.5
Sequence conflict561L → LL no nucleotide entry Ref.5
Sequence conflict621S → P in CAA25288. Ref.7
Sequence conflict881G → D no nucleotide entry Ref.5
Sequence conflict921S → N no nucleotide entry Ref.5
Sequence conflict1141S → N no nucleotide entry Ref.5
Sequence conflict1201D → G no nucleotide entry Ref.5
Sequence conflict1711C → S no nucleotide entry Ref.5
Sequence conflict2031S → R no nucleotide entry Ref.5
Sequence conflict2301S → A no nucleotide entry Ref.5
Sequence conflict2401L → F no nucleotide entry Ref.5
Sequence conflict2451P → S no nucleotide entry Ref.5
Isoform 2:
Sequence conflict21D → N in BAA01374. Ref.7
Sequence conflict61V → E in BAA01374. Ref.7

Secondary structure

....... 439
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

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

FASTA43948,804
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 8B4107BB740689E5
Show »

FASTA45450,565

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ASP-39.
[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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-170 (ISOFORM 1).
Tissue: Promyelocytic leukemia.
[17]"The pathogenesis of Burkitt's lymphoma."
Magrath I.
Adv. Cancer Res. 55:133-270(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN BURKITT LYMPHOMA.
[18]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[19]"Point mutations in the c-Myc transactivation domain are common in Burkitt's lymphoma and mouse plasmacytomas."
Bhatia K., Huppi K., Spangler G., Siwarski D., Iyer R., Magrath I.
Nat. Genet. 5:56-61(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN BURKITT LYMPHOMA, VARIANTS ASP-39; SER-57; ALA-59 AND THR-86.
[20]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-58 AND SER-62.
[21]"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] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT THR-58.
[22]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-8.
[23]"Phosphorylation-dependent degradation of c-Myc is mediated by the F-box protein Fbw7."
Yada M., Hatakeyama S., Kamura T., Nishiyama M., Tsunematsu R., Imaki H., Ishida N., Okumura F., Nakayama K., Nakayama K.I.
EMBO J. 23:2116-2125(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, INTERACTION WITH FBXW7, PHOSPHORYLATION AT THR-58 AND SER-62, MUTAGENESIS OF THR-58 AND SER-62.
[24]"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] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-143; LYS-157; LYS-275; LYS-317; LYS-323 AND LYS-371, IDENTIFICATION BY MASS SPECTROMETRY.
[25]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TAF1C.
[26]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PARP10.
[27]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-58, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[28]"Induction of pluripotent stem cells from adult human fibroblasts by defined factors."
Takahashi K., Tanabe K., Ohnuki M., Narita M., Ichisaka T., Tomoda K., Yamanaka S.
Cell 131:861-872(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOTECHNOLOGY.
[29]"Fbw7 and Usp28 regulate myc protein stability in response to DNA damage."
Popov N., Herold S., Llamazares M., Schulein C., Eilers M.
Cell Cycle 6:2327-2331(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, DEUBIQUITINATION BY USP28, INTERACTION WITH FBXW7.
[30]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KDM5A AND KDM5B.
[31]"Identification of Myc-associated protein with JmjC domain as a novel therapeutic target oncogene for lung cancer."
Suzuki C., Takahashi K., Hayama S., Ishikawa N., Kato T., Ito T., Tsuchiya E., Nakamura Y., Daigo Y.
Mol. Cancer Ther. 6:542-551(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NO66.
[32]"The ubiquitin-specific protease USP28 is required for MYC stability."
Popov N., Wanzel M., Madiredjo M., Zhang D., Beijersbergen R., Bernards R., Moll R., Elledge S.J., Eilers M.
Nat. Cell Biol. 9:765-774(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, DEUBIQUITINATION BY USP28, INTERACTION WITH FBXW7, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-58 AND SER-62, MUTAGENESIS OF THR-58 AND SER-62.
[33]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-58; SER-62 AND SER-71, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[34]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[35]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-148, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[36]"Tipping the balance: Cdk2 enables Myc to suppress senescence."
Hydbring P., Larsson L.-G.
Cancer Res. 70:6687-6691(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON SENESCENCE, PHOSPHORYLATION AT SER-62 BY CDK2, MUTAGENESIS OF THR-58 AND SER-62.
[37]"Phosphorylation by Cdk2 is required for Myc to repress Ras-induced senescence in cotransformation."
Hydbring P., Bahram F., Su Y., Tronnersjoe S., Hoegstrand K., von der Lehr N., Sharifi H.R., Lilischkis R., Hein N., Wu S., Vervoorts J., Henriksson M., Grandien A., Luescher B., Larsson L.-G.
Proc. Natl. Acad. Sci. U.S.A. 107:58-63(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-62 BY CDK2, MUTAGENESIS OF THR-58 AND SER-62.
[38]"Myc protein is stabilized by suppression of a novel E3 ligase complex in cancer cells."
Choi S.H., Wright J.B., Gerber S.A., Cole M.D.
Genes Dev. 24:1236-1241(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION.
[39]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 AND SER-161, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[40]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-58 AND SER-62, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[41]"DYRK2 priming phosphorylation of c-Jun and c-Myc modulates cell cycle progression in human cancer cells."
Taira N., Mimoto R., Kurata M., Yamaguchi T., Kitagawa M., Miki Y., Yoshida K.
J. Clin. Invest. 122:859-872(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-62, MUTAGENESIS OF SER-62.
[42]"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] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 402-434 IN COMPLEX WITH MAX.
+Additional computationally mapped references.

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.
CCDSCCDS6359.2. [P01106-2]
PIRTVHUM. A01349.
TVHUT. A01350.
RefSeqNP_002458.2. NM_002467.4. [P01106-2]
UniGeneHs.202453.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A93NMR-A406-434[»]
1EE4X-ray2.10C/D/E/F320-328[»]
1MV0NMR-A55-68[»]
1NKPX-ray1.80A/D353-434[»]
2A93NMR-A406-434[»]
2OR9X-ray2.70P410-419[»]
DisProtDP00260.
ProteinModelPortalP01106.
SMRP01106. Positions 353-434.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110694. 565 interactions.
DIPDIP-28143N.
IntActP01106. 670 interactions.
MINTMINT-257327.
STRING9606.ENSP00000367207.

Chemistry

BindingDBP01106.
ChEMBLCHEMBL1250348.

PTM databases

PhosphoSiteP01106.
UniCarbKBP01106.

Polymorphism databases

DMDM127619.

2D gel databases

SWISS-2DPAGEP01106.

Proteomic databases

MaxQBP01106.
PaxDbP01106.
PRIDEP01106.

Protocols and materials databases

DNASU4609.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000377970; ENSP00000367207; ENSG00000136997.
GeneID4609.
KEGGhsa:4609.
UCSCuc003ysi.3. human. [P01106-2]
uc022bbe.1. human. [P01106-1]

Organism-specific databases

CTD4609.
GeneCardsGC08P128748.
H-InvDBHIX0007784.
HGNCHGNC:7553. MYC.
HPACAB000084.
CAB010307.
MIM113970. phenotype.
190080. gene.
neXtProtNX_P01106.
Orphanet543. Burkitt lymphoma.
99861. Precursor T-cell acute lymphoblastic leukemia.
PharmGKBPA31353.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG42590.
HOGENOMHOG000043075.
HOVERGENHBG000472.
InParanoidP01106.
KOK04377.
OrthoDBEOG7GJ6CX.
PhylomeDBP01106.
TreeFamTF106001.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000136997-MONOMER.
ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_71. Gene Expression.
SignaLinkP01106.

Gene expression databases

ArrayExpressP01106.
BgeeP01106.
CleanExHS_MYC.
GenevestigatorP01106.

Family and domain databases

Gene3D4.10.280.10. 1 hit.
InterProIPR011598. bHLH_dom.
IPR003327. Myc-LZ.
IPR002418. Tscrpt_reg_Myc.
IPR012682. Tscrpt_reg_Myc_N.
[Graphical view]
PfamPF00010. HLH. 1 hit.
PF02344. Myc-LZ. 1 hit.
PF01056. Myc_N. 1 hit.
[Graphical view]
PIRSFPIRSF001705. Myc_protein. 1 hit.
PRINTSPR00044. LEUZIPPRMYC.
SMARTSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMSSF47459. SSF47459. 1 hit.
PROSITEPS50888. BHLH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMYC. human.
EvolutionaryTraceP01106.
GeneWikiMyc.
GenomeRNAi4609.
NextBio17740.
PROP01106.
SOURCESearch...

Entry information

Entry nameMYC_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 192 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM