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P01108

- MYC_MOUSE

UniProt

P01108 - MYC_MOUSE

Protein

Myc proto-oncogene protein

Gene

Myc

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      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.

    GO - Molecular functioni

    1. core promoter proximal region sequence-specific DNA binding Source: MGI
    2. DNA binding Source: MGI
    3. E-box binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein complex binding Source: UniProtKB
    6. sequence-specific DNA binding transcription factor activity Source: UniProtKB

    GO - Biological processi

    1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: MGI
    2. B cell apoptotic process Source: MGI
    3. branching involved in ureteric bud morphogenesis Source: UniProtKB
    4. canonical Wnt signaling pathway Source: UniProtKB
    5. canonical Wnt signaling pathway involved in negative regulation of apoptotic process Source: MGI
    6. canonical Wnt signaling pathway involved in positive regulation of apoptotic process Source: MGI
    7. cellular iron ion homeostasis Source: UniProtKB
    8. cellular response to DNA damage stimulus Source: UniProtKB
    9. cellular response to drug Source: UniProtKB
    10. chromatin remodeling Source: UniProtKB
    11. chromosome organization Source: UniProtKB
    12. detection of mechanical stimulus involved in sensory perception of sound Source: MGI
    13. intrinsic apoptotic signaling pathway in response to DNA damage Source: MGI
    14. MAPK cascade Source: UniProtKB
    15. middle ear morphogenesis Source: MGI
    16. negative regulation of cell division Source: UniProtKB
    17. negative regulation of monocyte differentiation Source: UniProtKB
    18. negative regulation of protein binding Source: MGI
    19. negative regulation of transcription from RNA polymerase II promoter Source: MGI
    20. pigmentation Source: MGI
    21. positive regulation of apoptotic signaling pathway Source: MGI
    22. positive regulation of B cell apoptotic process Source: MGI
    23. positive regulation of catalytic activity Source: MGI
    24. positive regulation of cell proliferation Source: MGI
    25. positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    26. positive regulation of DNA biosynthetic process Source: UniProtKB
    27. positive regulation of epithelial cell proliferation Source: UniProtKB
    28. positive regulation of fibroblast proliferation Source: UniProtKB
    29. positive regulation of mesenchymal cell proliferation Source: UniProtKB
    30. positive regulation of metanephric cap mesenchymal cell proliferation Source: UniProtKB
    31. positive regulation of response to DNA damage stimulus Source: UniProtKB
    32. positive regulation of transcription, DNA-templated Source: UniProtKB
    33. positive regulation of transcription from RNA polymerase II promoter Source: MGI
    34. protein processing Source: MGI
    35. regulation of apoptotic process Source: MGI
    36. regulation of gene expression Source: MGI
    37. regulation of telomere maintenance Source: UniProtKB
    38. regulation of transcription, DNA-templated Source: MGI
    39. response to alkaloid Source: MGI
    40. response to gamma radiation Source: UniProtKB
    41. response to radiation Source: MGI
    42. skeletal muscle cell differentiation Source: MGI
    43. skeletal system morphogenesis Source: MGI
    44. transcription, DNA-templated Source: UniProtKB-KW
    45. Wnt signaling pathway Source: MGI

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_223647. Cyclin A:Cdk2-associated events at S phase entry.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Myc proto-oncogene protein
    Alternative name(s):
    Proto-oncogene c-Myc
    Transcription factor p64
    Gene namesi
    Name:Myc
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 15

    Organism-specific databases

    MGIiMGI:97250. Myc.

    Subcellular locationi

    Nucleusnucleoplasm By similarity. Nucleusnucleolus By similarity

    GO - Cellular componenti

    1. axon Source: MGI
    2. nuclear body Source: MGI
    3. nucleolus Source: UniProtKB
    4. nucleoplasm Source: UniProtKB
    5. nucleus Source: MGI
    6. spindle Source: MGI

    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

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi329 – 3291S → A: Reduces phosphorylation by PIM2 by 60%, and decreases the transcriptional activity of MYC. 1 Publication

    Keywords - Diseasei

    Proto-oncogene

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 439439Myc proto-oncogene proteinPRO_0000127296Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei8 – 81PhosphothreonineBy 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-acetyllysine1 Publication
    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 vitro1 Publication
    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. Phosphorylation at Ser-62 by CDK2 prevents Ras-induced senescence By similarity. Phosphorylation at Ser-329 by PIM2 leads to the stabilization of MYC.By similarity1 Publication
    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

    PRIDEiP01108.

    PTM databases

    PhosphoSiteiP01108.

    Expressioni

    Developmental stagei

    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.1 Publication

    Gene expression databases

    ArrayExpressiP01108.
    BgeeiP01108.
    CleanExiMM_MYC.
    GenevestigatoriP01108.

    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.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MaxP285746EBI-1183114,EBI-1183003
    Trim32Q8CH722EBI-1183114,EBI-773837

    Protein-protein interaction databases

    BioGridi201635. 15 interactions.
    DIPiDIP-1064N.
    IntActiP01108. 13 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliP01108.
    SMRiP01108. 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

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG42590.
    GeneTreeiENSGT00510000046414.
    HOVERGENiHBG000472.
    InParanoidiP01108.
    KOiK04377.
    OrthoDBiEOG7GJ6CX.
    PhylomeDBiP01108.

    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.

    P01108-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPLNVNFTNR NYDLDYDSVQ PYFICDEEEN FYHQQQQSEL QPPAPSEDIW    50
    KKFELLPTPP LSPSRRSGLC SPSYVAVATS FSPREDDDGG GGNFSTADQL 100
    EMMTELLGGD MVNQSFICDP DDETFIKNII IQDCMWSGFS AAAKLVSEKL 150
    ASYQAARKDS TSLSPARGHS VCSTSSLYLQ DLTAAASECI DPSVVFPYPL 200
    NDSSSPKSCT SSDSTAFSPS SDSLLSSESS PRASPEPLVL HEETPPTTSS 250
    DSEEEQEDEE EIDVVSVEKR QTPAKRSESG SSPSRGHSKP PHSPLVLKRC 300
    HVSTHQHNYA APPSTRKDYP AAKRAKLDSG RVLKQISNNR KCSSPRSSDT 350
    EENDKRRTHN VLERQRRNEL KRSFFALRDQ IPELENNEKA PKVVILKKAT 400
    AYILSIQADE HKLTSEKDLL RKRREQLKHK LEQLRNSGA 439
    Length:439
    Mass (Da):48,971
    Last modified:July 21, 1986 - v1
    Checksum:i3FCA39BFFD6FC59E
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti39 – 391E → D in K00683. (PubMed:6412145)Curated
    Sequence conflicti101 – 1011E → Q in AAB59728. (PubMed:6321164)Curated
    Sequence conflicti284 – 2841S → F in AAB59728. (PubMed:6321164)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS49615.1.
    PIRiA93337. TVMS.
    RefSeqiNP_001170823.1. NM_001177352.1.
    NP_001170824.1. NM_001177353.1.
    NP_001170825.1. NM_001177354.1.
    UniGeneiMm.2444.

    Genome annotation databases

    EnsembliENSMUST00000159327; ENSMUSP00000124758; ENSMUSG00000022346.
    ENSMUST00000160009; ENSMUSP00000123852; ENSMUSG00000022346.
    ENSMUST00000161976; ENSMUSP00000123821; ENSMUSG00000022346.
    GeneIDi17869.
    KEGGimmu:17869.
    UCSCiuc007vyh.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSi CCDS49615.1.
    PIRi A93337. TVMS.
    RefSeqi NP_001170823.1. NM_001177352.1.
    NP_001170824.1. NM_001177353.1.
    NP_001170825.1. NM_001177354.1.
    UniGenei Mm.2444.

    3D structure databases

    ProteinModelPortali P01108.
    SMRi P01108. Positions 353-434.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201635. 15 interactions.
    DIPi DIP-1064N.
    IntActi P01108. 13 interactions.

    PTM databases

    PhosphoSitei P01108.

    Proteomic databases

    PRIDEi P01108.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000159327 ; ENSMUSP00000124758 ; ENSMUSG00000022346 .
    ENSMUST00000160009 ; ENSMUSP00000123852 ; ENSMUSG00000022346 .
    ENSMUST00000161976 ; ENSMUSP00000123821 ; ENSMUSG00000022346 .
    GeneIDi 17869.
    KEGGi mmu:17869.
    UCSCi uc007vyh.1. mouse.

    Organism-specific databases

    CTDi 4609.
    MGIi MGI:97250. Myc.

    Phylogenomic databases

    eggNOGi NOG42590.
    GeneTreei ENSGT00510000046414.
    HOVERGENi HBG000472.
    InParanoidi P01108.
    KOi K04377.
    OrthoDBi EOG7GJ6CX.
    PhylomeDBi P01108.

    Enzyme and pathway databases

    Reactomei REACT_223647. Cyclin A:Cdk2-associated events at S phase entry.

    Miscellaneous databases

    ChiTaRSi MYC. mouse.
    NextBioi 292641.
    PROi P01108.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P01108.
    Bgeei P01108.
    CleanExi MM_MYC.
    Genevestigatori P01108.

    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. "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.
      , 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. "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.
    8. "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.
    9. "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.
    10. "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.

    Entry informationi

    Entry nameiMYC_MOUSE
    AccessioniPrimary (citable) accession number: P01108
    Secondary accession number(s): P70247, Q3UM70, Q61422
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 156 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3