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P01108 (MYC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myc proto-oncogene protein
Alternative name(s):
Proto-oncogene c-Myc
Transcription factor p64
Gene names
Name:Myc
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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.8 Ref.10

Subcellular location

Nucleusnucleoplasm By similarity. Nucleusnucleolus By similarity.

Developmental stage

Expressed in the proliferating cells of the developing CNS and the epidermis. In the spinal cord at embryonic days 10.5, 11.5 and 12.5 dpc, expressed within a subset of cells in the proliferative ventricular zone, as well as in the differentiating cells at the ventral portion of the intermediate zone. Also detected in the roof plate and in the neural crest. At 14.5 dpc, found in regions containing differentiating postmitotic neurons. In the developing epidermis at 14.5 dpc, found in the dorsal lateral epidermis. At 17 dpc, expression is confined primarily to the proliferative malphigian layer of the epidermis and to the dermal papilla and primary germ cells in the dermis. Ref.6

Post-translational modification

Phosphorylated by PRKDC. 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. Phosphorylation at Ser-62 by CDK2 prevents Ras-induced senescence By similarity. Phosphorylation at Ser-329 by PIM2 leads to the stabilization of MYC. Ref.10

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 of FBXW7 (FBW7alpha), leading to its deubiquitination and preventing degradation. Also polyubiquitinated by the DCX(TRUSS) complex By similarity. Ref.10

Involvement in disease

Overexpression of C-Myc is implicated in the etiology of a variety of hematopoietic tumors.

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.9

Sequence similarities

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

Sequence caution

The sequence AAH06728.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   DiseaseProto-oncogene
   LigandDNA-binding
   Molecular functionActivator
   PTMAcetylation
Glycoprotein
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell apoptotic process

Inferred from mutant phenotype PubMed 12970677. Source: MGI

MAPK cascade

Inferred from sequence or structural similarity. Source: UniProtKB

Wnt signaling pathway

Inferred from direct assay PubMed 19056892. Source: MGI

activation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from direct assay PubMed 14517295. Source: MGI

branching involved in ureteric bud morphogenesis

Inferred from mutant phenotype PubMed 19161241. Source: UniProtKB

canonical Wnt signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

canonical Wnt signaling pathway involved in negative regulation of apoptotic process

Inferred from genetic interaction PubMed 17377531. Source: MGI

canonical Wnt signaling pathway involved in positive regulation of apoptotic process

Inferred from genetic interaction PubMed 17377531. Source: MGI

cellular iron ion homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to DNA damage stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to drug

Inferred from direct assay PubMed 19179467. Source: UniProtKB

chromatin remodeling

Inferred from sequence or structural similarity. Source: UniProtKB

chromosome organization

Inferred from sequence or structural similarity. Source: UniProtKB

detection of mechanical stimulus involved in sensory perception of sound

Inferred from mutant phenotype PubMed 17523175. Source: MGI

intrinsic apoptotic signaling pathway in response to DNA damage

Inferred from direct assay PubMed 14517295. Source: MGI

middle ear morphogenesis

Inferred from mutant phenotype PubMed 17523175. Source: MGI

negative regulation of cell division

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of monocyte differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of protein binding

Inferred from direct assay PubMed 18045875. Source: MGI

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 12196193. Source: MGI

pigmentation

Inferred from mutant phenotype PubMed 17523175. Source: MGI

positive regulation of B cell apoptotic process

Inferred from genetic interaction PubMed 11604501. Source: MGI

positive regulation of DNA biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of apoptotic signaling pathway

Inferred from direct assay PubMed 14517295. Source: MGI

positive regulation of catalytic activity

Inferred from mutant phenotype PubMed 17382917. Source: MGI

positive regulation of cell proliferation

Inferred from direct assay PubMed 12235125PubMed 14517295. Source: MGI

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

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of epithelial cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of fibroblast proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of mesenchymal cell proliferation

Inferred from mutant phenotype PubMed 19161241. Source: UniProtKB

positive regulation of metanephric cap mesenchymal cell proliferation

Inferred from mutant phenotype PubMed 19161241. Source: UniProtKB

positive regulation of response to DNA damage stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 17382917. Source: MGI

positive regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

protein processing

Inferred from mutant phenotype PubMed 12970677. Source: MGI

regulation of apoptotic process

Inferred from direct assay PubMed 12235125. Source: MGI

regulation of gene expression

Inferred from direct assay PubMed 11438662. Source: MGI

regulation of telomere maintenance

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from genetic interaction Ref.6. Source: MGI

response to alkaloid

Inferred from mutant phenotype PubMed 12970677. Source: MGI

response to gamma radiation

Inferred from sequence or structural similarity. Source: UniProtKB

response to radiation

Inferred from direct assay PubMed 14517295. Source: MGI

skeletal muscle cell differentiation

Inferred from mutant phenotype PubMed 22147266. Source: MGI

skeletal system morphogenesis

Inferred from mutant phenotype PubMed 17523175. Source: MGI

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentaxon

Inferred from direct assay PubMed 10482234. Source: MGI

nuclear body

Inferred from direct assay PubMed 15735755. Source: MGI

nucleolus

Inferred from sequence or structural similarity. Source: UniProtKB

nucleoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 11872843PubMed 17631878PubMed 19796622. Source: MGI

spindle

Inferred from direct assay PubMed 15509711. Source: MGI

   Molecular_functionDNA binding

Inferred from direct assay PubMed 12970171PubMed 14560010. Source: MGI

E-box binding

Inferred from sequence or structural similarity. Source: UniProtKB

core promoter proximal region sequence-specific DNA binding

Inferred from direct assay PubMed 15511642. Source: MGI

protein binding

Inferred from physical interaction Ref.10. Source: UniProtKB

protein complex binding

Inferred from sequence or structural similarity. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 439439Myc proto-oncogene protein
PRO_0000127296

Regions

Domain354 – 40653bHLH
Region413 – 43422Leucine-zipper
Compositional bias34 – 374Poly-Gln
Compositional bias89 – 924Poly-Gly

Amino acid modifications

Modified residue81Phosphothreonine By similarity
Modified residue581Phosphothreonine; by GSK3; alternate By similarity
Modified residue621Phosphoserine; by DYRK2, GSK3 and CDK2 By similarity
Modified residue711Phosphoserine By similarity
Modified residue1441N6-acetyllysine; by PCAF By similarity
Modified residue1491N6-acetyllysine Ref.11
Modified residue1581N6-acetyllysine; by PCAF By similarity
Modified residue1621Phosphoserine By similarity
Modified residue2751N6-acetyllysine; by PCAF By similarity
Modified residue3171N6-acetyllysine; by PCAF By similarity
Modified residue3231N6-acetyllysine; by PCAF By similarity
Modified residue3291Phosphoserine; by PIM2; in vitro Ref.10
Modified residue3711N6-acetyllysine; by PCAF By similarity
Glycosylation581O-linked (GlcNAc); alternate By similarity

Experimental info

Mutagenesis3291S → A: Reduces phosphorylation by PIM2 by 60%, and decreases the transcriptional activity of MYC. Ref.10
Sequence conflict391E → D in K00683. Ref.5
Sequence conflict1011E → Q in AAB59728. Ref.1
Sequence conflict2841S → F in AAB59728. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P01108 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 3FCA39BFFD6FC59E

FASTA43948,971
        10         20         30         40         50         60 
MPLNVNFTNR NYDLDYDSVQ PYFICDEEEN FYHQQQQSEL QPPAPSEDIW KKFELLPTPP 

        70         80         90        100        110        120 
LSPSRRSGLC SPSYVAVATS FSPREDDDGG GGNFSTADQL EMMTELLGGD MVNQSFICDP 

       130        140        150        160        170        180 
DDETFIKNII IQDCMWSGFS AAAKLVSEKL ASYQAARKDS TSLSPARGHS VCSTSSLYLQ 

       190        200        210        220        230        240 
DLTAAASECI DPSVVFPYPL NDSSSPKSCT SSDSTAFSPS SDSLLSSESS PRASPEPLVL 

       250        260        270        280        290        300 
HEETPPTTSS DSEEEQEDEE EIDVVSVEKR QTPAKRSESG SSPSRGHSKP PHSPLVLKRC 

       310        320        330        340        350        360 
HVSTHQHNYA APPSTRKDYP AAKRAKLDSG RVLKQISNNR KCSSPRSSDT EENDKRRTHN 

       370        380        390        400        410        420 
VLERQRRNEL KRSFFALRDQ IPELENNEKA PKVVILKKAT AYILSIQADE HKLTSEKDLL 

       430 
RKRREQLKHK LEQLRNSGA 

« Hide

References

« Hide 'large scale' references
[1]"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].
Strain: BALB/c.
Tissue: Spleen.
[2]"Nucleotide sequence comparison of normal and translocated murine c-myc genes."
Stanton L.W., Fahrlander P.D., Tesser P.M., Marcu K.B.
Nature 310:423-425(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Embryo, Mammary gland and Thymus.
[4]"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].
Strain: FVB/N.
Tissue: Mammary gland.
[5]"Reciprocal chromosome translocation between c-myc and immunoglobulin gamma 2b genes."
Neuberger M.S., Calabi F.
Nature 305:240-243(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-252.
[6]"Mad3 and Mad4: novel Max-interacting transcriptional repressors that suppress c-myc dependent transformation and are expressed during neural and epidermal differentiation."
Hurlin P.J., Queva C., Koskinen P.J., Steingrimsson E., Ayer D.E., Copeland N.G., Jenkins N.A., Eisenman R.N.
EMBO J. 14:5646-5659(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
[7]Erratum
Hurlin P.J., Queva C., Koskinen P.J., Steingrimsson E., Ayer D.E., Copeland N.G., Jenkins N.A., Eisenman R.N.
EMBO J. 15:2030-2030(1996) [PubMed] [Europe PMC] [Abstract]
[8]"JLP: a scaffolding protein that tethers JNK/p38MAPK signaling modules and transcription factors."
Lee C.M., Onesime D., Reddy C.D., Dhanasekaran N., Reddy E.P.
Proc. Natl. Acad. Sci. U.S.A. 99:14189-14194(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SPAG9.
[9]"Induction of pluripotent stem cells from mouse embryonic and adult fibroblast cultures by defined factors."
Takahashi K., Yamanaka S.
Cell 126:663-676(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOTECHNOLOGY.
[10]"Pim kinase-dependent inhibition of c-Myc degradation."
Zhang Y., Wang Z., Li X., Magnuson N.S.
Oncogene 27:4809-4819(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-329, MUTAGENESIS OF SER-329, INTERACTION WITH PIM2.
[11]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-149, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L00039, L00038 Genomic DNA. Translation: AAB59728.1.
X01023 mRNA. Translation: CAA25508.1.
AK087961 mRNA. Translation: BAC40060.1.
AK133952 mRNA. Translation: BAE21948.1.
AK145084 mRNA. Translation: BAE26228.1.
BC006728 mRNA. Translation: AAH06728.2. Different initiation.
K00683 Genomic DNA. No translation available.
CCDSCCDS49615.1.
PIRTVMS. A93337.
RefSeqNP_001170823.1. NM_001177352.1.
NP_001170824.1. NM_001177353.1.
NP_001170825.1. NM_001177354.1.
UniGeneMm.2444.

3D structure databases

ProteinModelPortalP01108.
SMRP01108. Positions 353-434.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201635. 15 interactions.
DIPDIP-1064N.
IntActP01108. 13 interactions.

PTM databases

PhosphoSiteP01108.

Proteomic databases

PRIDEP01108.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000159327; ENSMUSP00000124758; ENSMUSG00000022346.
ENSMUST00000160009; ENSMUSP00000123852; ENSMUSG00000022346.
ENSMUST00000161976; ENSMUSP00000123821; ENSMUSG00000022346.
GeneID17869.
KEGGmmu:17869.
UCSCuc007vyh.1. mouse.

Organism-specific databases

CTD4609.
MGIMGI:97250. Myc.

Phylogenomic databases

eggNOGNOG42590.
GeneTreeENSGT00510000046414.
HOVERGENHBG000472.
InParanoidP01108.
KOK04377.
OrthoDBEOG7GJ6CX.
PhylomeDBP01108.

Gene expression databases

ArrayExpressP01108.
BgeeP01108.
CleanExMM_MYC.
GenevestigatorP01108.

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. mouse.
NextBio292641.
PROP01108.
SOURCESearch...

Entry information

Entry nameMYC_MOUSE
AccessionPrimary (citable) accession number: P01108
Secondary accession number(s): P70247, Q3UM70, Q61422
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 154 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot