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P09416

- MYC_RAT

UniProt

P09416 - MYC_RAT

Protein

Myc proto-oncogene protein

Gene

Myc

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    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

    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

    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

    ArrayExpressiP09416.
    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

    MPLNVSFANR NYDLDYDSVQ PYFICDEEEN FYHQQQQSEL QPPAPSEDIW    50
    KKFELLPTPP LSPSRRSGLC SPSYVAVATS FSPREDDDGG GGNFSTADQL 100
    EMMTELLGGD MVNQSFICDP DDETFIKNII IQDCMWSGFS AAAKLVSEKL 150
    ASYQAARKDS TSLSPARGHS VCSTSSLYLQ DLTAAASECI DPSVVFPYPL 200
    NDSSSPKSCT SSDSTAFSSS SDSLLSSESS PRATPEPLVL HEETPPTTSS 250
    DSEEEQDDEE EIDVVSVEKR QPPAKRSESG SSPSRGHSKP PHSPLVLKRC 300
    HVSTHQHNYA APPSTRKDYP AAKRAKLDSG RVLKQISNNR KCSSPRSSDT 350
    EENDKRRTHN VLERQRRNEL KRSFFALRDQ IPELENNEKA PKVVILKKAT 400
    AYILSVQADE HKLISEKDLL RKRREQLKHK LEQLRNSGA 439
    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.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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

    ArrayExpressi P09416.
    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

    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 1, 2014
    This is version 134 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