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P09416

- MYC_RAT

UniProt

P09416 - MYC_RAT

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Protein

Myc proto-oncogene protein

Gene

Myc

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  1. core promoter proximal region sequence-specific DNA binding Source: Ensembl
  2. DNA binding Source: RGD
  3. double-stranded DNA binding Source: RGD
  4. E-box binding Source: UniProtKB
  5. protein complex binding Source: UniProtKB
  6. protein heterodimerization activity Source: RGD
  7. sequence-specific DNA binding Source: RGD
  8. sequence-specific DNA binding transcription factor activity Source: RGD

GO - Biological processi

  1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
  2. amino acid transport Source: RGD
  3. B cell apoptotic process Source: Ensembl
  4. branching involved in ureteric bud morphogenesis Source: UniProtKB
  5. canonical Wnt signaling pathway Source: UniProtKB
  6. canonical Wnt signaling pathway involved in negative regulation of apoptotic process Source: Ensembl
  7. canonical Wnt signaling pathway involved in positive regulation of apoptotic process Source: Ensembl
  8. canonical Wnt signaling pathway involved in positive regulation of wound healing Source: RGD
  9. cell proliferation Source: RGD
  10. cellular iron ion homeostasis Source: UniProtKB
  11. cellular response to carbohydrate stimulus Source: RGD
  12. cellular response to DNA damage stimulus Source: UniProtKB
  13. cellular response to drug Source: Ensembl
  14. cellular response to estrogen stimulus Source: RGD
  15. cellular response to hydrostatic pressure Source: RGD
  16. cellular response to interleukin-1 Source: RGD
  17. cellular response to organic cyclic compound Source: RGD
  18. chromatin remodeling Source: UniProtKB
  19. chromosome organization Source: UniProtKB
  20. detection of mechanical stimulus involved in sensory perception of sound Source: Ensembl
  21. DNA-templated transcription, initiation Source: RGD
  22. flavonoid metabolic process Source: RGD
  23. fungal-type cell wall polysaccharide metabolic process Source: RGD
  24. G0 to G1 transition Source: RGD
  25. glucose metabolic process Source: RGD
  26. glycoprotein metabolic process Source: RGD
  27. hypothalamus development Source: RGD
  28. inner mitochondrial membrane organization Source: RGD
  29. intrinsic apoptotic signaling pathway in response to DNA damage Source: Ensembl
  30. in utero embryonic development Source: RGD
  31. lactic acid secretion Source: RGD
  32. MAPK cascade Source: UniProtKB
  33. middle ear morphogenesis Source: Ensembl
  34. negative regulation of cell death Source: RGD
  35. negative regulation of cell division Source: UniProtKB
  36. negative regulation of gene expression Source: RGD
  37. negative regulation of glucose import Source: RGD
  38. negative regulation of monocyte differentiation Source: UniProtKB
  39. negative regulation of protein binding Source: Ensembl
  40. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  41. pathogenesis Source: RGD
  42. pigmentation Source: Ensembl
  43. positive regulation of apoptotic signaling pathway Source: Ensembl
  44. positive regulation of ATP biosynthetic process Source: RGD
  45. positive regulation of B cell apoptotic process Source: Ensembl
  46. positive regulation of cell cycle Source: RGD
  47. positive regulation of cell proliferation Source: RGD
  48. positive regulation of cellular respiration Source: RGD
  49. positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  50. positive regulation of DNA biosynthetic process Source: UniProtKB
  51. positive regulation of epithelial cell proliferation Source: UniProtKB
  52. positive regulation of fibroblast proliferation Source: UniProtKB
  53. positive regulation of glycolytic process Source: RGD
  54. positive regulation of mesenchymal cell proliferation Source: UniProtKB
  55. positive regulation of metanephric cap mesenchymal cell proliferation Source: UniProtKB
  56. positive regulation of mitochondrial membrane potential Source: RGD
  57. positive regulation of response to DNA damage stimulus Source: UniProtKB
  58. positive regulation of transcription, DNA-templated Source: UniProtKB
  59. positive regulation of transcription from RNA polymerase II promoter Source: RGD
  60. pyruvate transport Source: RGD
  61. regulation of mitotic cell cycle Source: RGD
  62. regulation of oxidative phosphorylation Source: RGD
  63. regulation of telomere maintenance Source: UniProtKB
  64. regulation of transcription, DNA-templated Source: RGD
  65. response to alkaloid Source: Ensembl
  66. response to estradiol Source: RGD
  67. response to gamma radiation Source: UniProtKB
  68. response to wounding Source: RGD
  69. skeletal muscle cell differentiation Source: Ensembl
  70. skeletal system morphogenesis Source: Ensembl
  71. transcription, DNA-templated Source: RGD
  72. transcription from RNA polymerase II promoter Source: RGD
  73. transformation of host cell by virus Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Myc proto-oncogene protein
Alternative name(s):
Proto-oncogene c-Myc
Transcription factor p64
Gene namesi
Name:Myc
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi3130. Myc.

Subcellular locationi

Nucleusnucleoplasm By similarity. Nucleusnucleolus By similarity

GO - Cellular componenti

  1. axon Source: Ensembl
  2. cytoplasm Source: RGD
  3. mitochondrion Source: GOC
  4. nuclear body Source: Ensembl
  5. nucleolus Source: UniProtKB
  6. nucleoplasm Source: UniProtKB
  7. nucleus Source: RGD
  8. spindle Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

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

Biotechnological usei

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.1 Publication

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 439439Myc proto-oncogene proteinPRO_0000127300Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei6 – 61PhosphoserineBy similarity
Modified residuei58 – 581Phosphothreonine; by GSK3; alternateBy similarity
Glycosylationi58 – 581O-linked (GlcNAc); alternateBy similarity
Modified residuei62 – 621Phosphoserine; by DYRK2, GSK3 and CDK2By similarity
Modified residuei71 – 711PhosphoserineBy similarity
Modified residuei144 – 1441N6-acetyllysine; by PCAFBy similarity
Modified residuei149 – 1491N6-acetyllysineBy similarity
Modified residuei158 – 1581N6-acetyllysine; by PCAFBy similarity
Modified residuei162 – 1621PhosphoserineBy similarity
Modified residuei275 – 2751N6-acetyllysine; by PCAFBy similarity
Modified residuei317 – 3171N6-acetyllysine; by PCAFBy similarity
Modified residuei323 – 3231N6-acetyllysine; by PCAFBy similarity
Modified residuei329 – 3291Phosphoserine; by PIM2; in vitroBy similarity
Modified residuei371 – 3711N6-acetyllysine; by PCAFBy similarity

Post-translational modificationi

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 (By similarity). Phosphorylation at Ser-329 by PIM2 leads to the stabilization of MYC. Phosphorylation at Ser-62 by CDK2 prevents Ras-induced senescence (By similarity).By similarity
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).By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP09416.
PRIDEiP09416.

PTM databases

PhosphoSiteiP09416.

Expressioni

Gene expression databases

ExpressionAtlasiP09416. baseline and differential.
GenevestigatoriP09416.

Interactioni

Subunit structurei

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.1 Publication

Protein-protein interaction databases

BioGridi246723. 3 interactions.
DIPiDIP-28140N.
IntActiP09416. 2 interactions.
MINTiMINT-4508782.

Structurei

3D structure databases

ProteinModelPortaliP09416.
SMRiP09416. Positions 353-434.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini354 – 40653bHLHPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni413 – 43422Leucine-zipperAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi34 – 374Poly-Gln
Compositional biasi89 – 924Poly-Gly
Compositional biasi218 – 2236Poly-Ser

Sequence similaritiesi

Contains 1 bHLH (basic helix-loop-helix) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG42590.
HOGENOMiHOG000043075.
HOVERGENiHBG000472.
InParanoidiP09416.
KOiK04377.
PhylomeDBiP09416.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
IPR003327. Myc-LZ.
IPR002418. Tscrpt_reg_Myc.
IPR012682. Tscrpt_reg_Myc_N.
[Graphical view]
PfamiPF00010. HLH. 1 hit.
PF02344. Myc-LZ. 1 hit.
PF01056. Myc_N. 1 hit.
[Graphical view]
PIRSFiPIRSF001705. Myc_protein. 1 hit.
PRINTSiPR00044. LEUZIPPRMYC.
SMARTiSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P09416-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPLNVSFANR NYDLDYDSVQ PYFICDEEEN FYHQQQQSEL QPPAPSEDIW
60 70 80 90 100
KKFELLPTPP LSPSRRSGLC SPSYVAVATS FSPREDDDGG GGNFSTADQL
110 120 130 140 150
EMMTELLGGD MVNQSFICDP DDETFIKNII IQDCMWSGFS AAAKLVSEKL
160 170 180 190 200
ASYQAARKDS TSLSPARGHS VCSTSSLYLQ DLTAAASECI DPSVVFPYPL
210 220 230 240 250
NDSSSPKSCT SSDSTAFSSS SDSLLSSESS PRATPEPLVL HEETPPTTSS
260 270 280 290 300
DSEEEQDDEE EIDVVSVEKR QPPAKRSESG SSPSRGHSKP PHSPLVLKRC
310 320 330 340 350
HVSTHQHNYA APPSTRKDYP AAKRAKLDSG RVLKQISNNR KCSSPRSSDT
360 370 380 390 400
EENDKRRTHN VLERQRRNEL KRSFFALRDQ IPELENNEKA PKVVILKKAT
410 420 430
AYILSVQADE HKLISEKDLL RKRREQLKHK LEQLRNSGA
Length:439
Mass (Da):48,898
Last modified:July 1, 1989 - v1
Checksum:i7547DCCECF74554F
GO

Sequence cautioni

The sequence AAH91699.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00396 Genomic DNA. Translation: CAA68459.2.
AY679729 mRNA. Translation: AAT92511.1.
AY679730 mRNA. Translation: AAT92512.1.
BC091699 mRNA. Translation: AAH91699.2. Different initiation.
PIRiA26801. TVRTMC.
RefSeqiNP_036735.2. NM_012603.2.
UniGeneiRn.12072.

Genome annotation databases

GeneIDi24577.
KEGGirno:24577.
UCSCiRGD:3130. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00396 Genomic DNA. Translation: CAA68459.2 .
AY679729 mRNA. Translation: AAT92511.1 .
AY679730 mRNA. Translation: AAT92512.1 .
BC091699 mRNA. Translation: AAH91699.2 . Different initiation.
PIRi A26801. TVRTMC.
RefSeqi NP_036735.2. NM_012603.2.
UniGenei Rn.12072.

3D structure databases

ProteinModelPortali P09416.
SMRi P09416. Positions 353-434.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 246723. 3 interactions.
DIPi DIP-28140N.
IntActi P09416. 2 interactions.
MINTi MINT-4508782.

PTM databases

PhosphoSitei P09416.

Proteomic databases

PaxDbi P09416.
PRIDEi P09416.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 24577.
KEGGi rno:24577.
UCSCi RGD:3130. rat.

Organism-specific databases

CTDi 4609.
RGDi 3130. Myc.

Phylogenomic databases

eggNOGi NOG42590.
HOGENOMi HOG000043075.
HOVERGENi HBG000472.
InParanoidi P09416.
KOi K04377.
PhylomeDBi P09416.

Miscellaneous databases

NextBioi 603730.
PROi P09416.

Gene expression databases

ExpressionAtlasi P09416. baseline and differential.
Genevestigatori P09416.

Family and domain databases

Gene3Di 4.10.280.10. 1 hit.
InterProi IPR011598. bHLH_dom.
IPR003327. Myc-LZ.
IPR002418. Tscrpt_reg_Myc.
IPR012682. Tscrpt_reg_Myc_N.
[Graphical view ]
Pfami PF00010. HLH. 1 hit.
PF02344. Myc-LZ. 1 hit.
PF01056. Myc_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF001705. Myc_protein. 1 hit.
PRINTSi PR00044. LEUZIPPRMYC.
SMARTi SM00353. HLH. 1 hit.
[Graphical view ]
SUPFAMi SSF47459. SSF47459. 1 hit.
PROSITEi PS50888. BHLH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Shull J.D., Buckles L.K.
    Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: ACI/SegHsd and Brown Norway/SsNHsd.
    Tissue: Spleen.
  3. "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].
    Tissue: Ovary.
  4. "Direct reprogramming of rat neural precursor cells and fibroblasts into pluripotent stem cells."
    Chang M.Y., Kim D., Kim C.H., Kang H.C., Yang E., Moon J.I., Ko S., Park J., Park K.S., Lee K.A., Hwang D.Y., Chung Y., Lanza R., Kim K.S.
    PLoS ONE 5:E9838-E9838(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOTECHNOLOGY.
  5. "Abelson interacting protein 1 (Abi-1) is essential for dendrite morphogenesis and synapse formation."
    Proepper C., Johannsen S., Liebau S., Dahl J., Vaida B., Bockmann J., Kreutz M.R., Gundelfinger E.D., Boeckers T.M.
    EMBO J. 26:1397-1409(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TRANSCRIPTIONAL ACTIVATION, INTERACTION WITH ABI1.

Entry informationi

Entry nameiMYC_RAT
AccessioniPrimary (citable) accession number: P09416
Secondary accession number(s): Q6B500
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: October 29, 2014
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3