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P06876

- MYB_MOUSE

UniProt

P06876 - MYB_MOUSE

Protein

Transcriptional activator Myb

Gene

Myb

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Transcriptional activator; DNA-binding protein that specifically recognize the sequence 5'-YAAC[GT]G-3'. Plays an important role in the control of proliferation and differentiation of hematopoietic progenitor cells.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi63 – 8624H-T-H motifPROSITE-ProRule annotationAdd
    BLAST
    DNA bindingi115 – 13824H-T-H motifPROSITE-ProRule annotationAdd
    BLAST
    DNA bindingi166 – 18924H-T-H motifPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. chromatin binding Source: InterPro
    2. DNA binding Source: MGI
    3. protein binding Source: IntAct
    4. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
    5. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: NTNU_SB
    6. sequence-specific DNA binding transcription factor activity Source: MGI

    GO - Biological processi

    1. B cell differentiation Source: MGI
    2. calcium ion transport Source: MGI
    3. chromatin remodeling Source: Ensembl
    4. embryonic digestive tract development Source: MGI
    5. G1/S transition of mitotic cell cycle Source: MGI
    6. homeostasis of number of cells Source: MGI
    7. in utero embryonic development Source: MGI
    8. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    9. positive regulation of histone H3-K4 methylation Source: Ensembl
    10. positive regulation of histone H3-K9 methylation Source: Ensembl
    11. positive regulation of T-helper cell differentiation Source: Ensembl
    12. positive regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
    13. regulation of gene expression Source: MGI
    14. regulation of transcription, DNA-templated Source: MGI
    15. thymus development Source: MGI

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_198649. Factors involved in megakaryocyte development and platelet production.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcriptional activator Myb
    Alternative name(s):
    Proto-oncogene c-Myb
    Gene namesi
    Name:Myb
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:97249. Myb.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleoplasm Source: Reactome
    2. nucleus Source: MGI

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Keywords - Diseasei

    Proto-oncogene

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 636636Transcriptional activator MybPRO_0000197049Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei467 – 4671N6-acetyllysineBy similarity
    Modified residuei476 – 4761N6-acetyllysineBy similarity

    Post-translational modificationi

    Ubiquitinated; mediated by SIAH1 and leading to its subsequent proteasomal degradation.By similarity
    Phosphorylated by NLK on multiple sites, which induces proteasomal degradation.
    Phosphorylated by HIPK1. This phosphorylation reduces MYB transcription factor activity but not MYB protein levels By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiP06876.

    PTM databases

    PhosphoSiteiP06876.

    Expressioni

    Gene expression databases

    ArrayExpressiP06876.
    BgeeiP06876.
    CleanExiMM_MYB.
    GenevestigatoriP06876.

    Interactioni

    Subunit structurei

    Binds to HIPK1 By similarity. Interacts with HIPK2, MAF, MYBBP1A and NLK.By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Hipk2Q9QZR52EBI-366934,EBI-366905

    Protein-protein interaction databases

    BioGridi201631. 11 interactions.
    IntActiP06876. 2 interactions.

    Structurei

    Secondary structure

    1
    636
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi45 – 5814
    Helixi63 – 686
    Helixi75 – 8612
    Beta strandi92 – 943
    Helixi97 – 11014
    Helixi115 – 1195
    Helixi127 – 13610
    Beta strandi140 – 1423
    Beta strandi144 – 1463
    Helixi149 – 16214
    Helixi163 – 1653
    Helixi166 – 1705
    Beta strandi173 – 1753
    Helixi178 – 18811
    Helixi189 – 1913
    Helixi292 – 31120

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GUUX-ray1.60A38-89[»]
    1GV2X-ray1.68A89-193[»]
    1GV5X-ray1.58A90-141[»]
    1GVDX-ray1.45A90-141[»]
    1H88X-ray2.80C37-193[»]
    1H89X-ray2.45C37-193[»]
    1IDYNMR-A141-193[»]
    1IDZNMR-A141-193[»]
    1MBENMR-A38-89[»]
    1MBFNMR-A38-89[»]
    1MBGNMR-A90-141[»]
    1MBHNMR-A90-141[»]
    1MBJNMR-A142-193[»]
    1MBKNMR-A142-193[»]
    1MSENMR-C90-193[»]
    1MSFNMR-C90-193[»]
    1SB0NMR-B291-315[»]
    2AGHNMR-A291-315[»]
    ProteinModelPortaliP06876.
    SMRiP06876. Positions 38-193.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06876.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini35 – 8652HTH myb-type 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini87 – 14256HTH myb-type 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini143 – 19351HTH myb-type 3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni90 – 193104Interaction with HIPK2 and NLKAdd
    BLAST
    Regioni275 – 32753Transcriptional activation domainBy similarityAdd
    BLAST
    Regioni328 – 460133Negative regulatory domainAdd
    BLAST
    Regioni375 – 39622Leucine-zipperAdd
    BLAST

    Domaini

    Comprised of 3 domains; an N-terminal DNA-binding domain, a centrally located transcriptional activation domain and a C-terminal domain involved in transcriptional repression.
    C-terminal truncated mutants display increased transactivation.

    Sequence similaritiesi

    Contains 3 HTH myb-type DNA-binding domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5147.
    GeneTreeiENSGT00390000001038.
    HOVERGENiHBG007964.
    KOiK09420.
    OMAiHGCLPEE.
    OrthoDBiEOG7H791P.
    TreeFamiTF326257.

    Family and domain databases

    Gene3Di1.10.10.60. 3 hits.
    InterProiIPR015395. C-myb_C.
    IPR009057. Homeodomain-like.
    IPR017930. Myb_dom.
    IPR001005. SANT/Myb.
    IPR012642. Tscrpt_reg_Wos2-domain.
    [Graphical view]
    PfamiPF09316. Cmyb_C. 1 hit.
    PF07988. LMSTEN. 1 hit.
    PF00249. Myb_DNA-binding. 1 hit.
    [Graphical view]
    SMARTiSM00717. SANT. 3 hits.
    [Graphical view]
    SUPFAMiSSF46689. SSF46689. 2 hits.
    PROSITEiPS51294. HTH_MYB. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P06876-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARRPRHSIY SSDEDDEDIE MCDHDYDGLL PKSGKRHLGK TRWTREEDEK    50
    LKKLVEQNGT DDWKVIANYL PNRTDVQCQH RWQKVLNPEL IKGPWTKEED 100
    QRVIELVQKY GPKRWSVIAK HLKGRIGKQC RERWHNHLNP EVKKTSWTEE 150
    EDRIIYQAHK RLGNRWAEIA KLLPGRTDNA IKNHWNSTMR RKVEQEGYLQ 200
    EPSKASQTPV ATSFQKNNHL MGFGHASPPS QLSPSGQSSV NSEYPYYHIA 250
    EAQNISSHVP YPVALHVNIV NVPQPAAAAI QRHYNDEDPE KEKRIKELEL 300
    LLMSTENELK GQQALPTQNH TCSYPGWHST SIVDQTRPHG DSAPVSCLGE 350
    HHATPSLPAD PGSLPEESAS PARCMIVHQG TILDNVKNLL EFAETLQFID 400
    SFLNTSSNHE SSGLDAPTLP STPLIGHKLT PCRDQTVKTQ KENSIFRTPA 450
    IKRSILESSP RTPTPFKHAL AAQEIKYGPL KMLPQTPSHA VEDLQDVIKQ 500
    ESDESGIVAE FQESGPPLLK KIKQEVESPT EKSGNFFCSN HWAENSLSTQ 550
    LFSQASPVAD APNILTSSVL MTPVSEDEDN VLKAFTVPKN RPLVGPLQPC 600
    SGAWEPASCG KTEDQMTASG PARKYVNAFS ARTLVM 636
    Length:636
    Mass (Da):71,422
    Last modified:July 27, 2011 - v2
    Checksum:i0C6308E584726D01
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti105 – 1051E → K in CAA26552. (PubMed:2998780)Curated
    Sequence conflicti201 – 2011E → K in CAA26552. (PubMed:2998780)Curated
    Sequence conflicti267 – 2671V → A in AAB59713. (PubMed:3010282)Curated
    Sequence conflicti402 – 4021F → V in AAA39786. (PubMed:3014527)Curated
    Sequence conflicti411 – 4111S → N in CAA26552. (PubMed:2998780)Curated
    Sequence conflicti500 – 5001Q → R in CAA26552. (PubMed:2998780)Curated
    Sequence conflicti500 – 5001Q → R in AAH11513. (PubMed:15489334)Curated
    Sequence conflicti525 – 5251E → A in CAA26552. (PubMed:2998780)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M21169 Genomic DNA. Translation: AAA39782.1.
    M12848 mRNA. Translation: AAB59713.1.
    X02774 mRNA. Translation: CAA26552.1.
    M20210 Genomic DNA. Translation: AAA39783.1.
    AC153556 Genomic DNA. No translation available.
    BC011513 mRNA. Translation: AAH11513.1.
    X04099
    , X04100, X04101, X04102, X04103, X04104 Genomic DNA. Translation: CAA27724.1.
    X16389 Genomic DNA. Translation: CAA34425.1.
    X16390 Genomic DNA. Translation: CAA34426.1.
    M13989 Genomic DNA. Translation: AAA39787.1.
    K03547 Genomic DNA. Translation: AAA39786.1.
    CCDSiCCDS35861.1.
    PIRiA25285. TVMSMB.
    RefSeqiNP_001185843.1. NM_001198914.1.
    NP_034978.3. NM_010848.3.
    UniGeneiMm.473872.
    Mm.52109.

    Genome annotation databases

    EnsembliENSMUST00000020158; ENSMUSP00000020158; ENSMUSG00000019982.
    GeneIDi17863.
    KEGGimmu:17863.
    UCSCiuc007eog.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M21169 Genomic DNA. Translation: AAA39782.1 .
    M12848 mRNA. Translation: AAB59713.1 .
    X02774 mRNA. Translation: CAA26552.1 .
    M20210 Genomic DNA. Translation: AAA39783.1 .
    AC153556 Genomic DNA. No translation available.
    BC011513 mRNA. Translation: AAH11513.1 .
    X04099
    , X04100 , X04101 , X04102 , X04103 , X04104 Genomic DNA. Translation: CAA27724.1 .
    X16389 Genomic DNA. Translation: CAA34425.1 .
    X16390 Genomic DNA. Translation: CAA34426.1 .
    M13989 Genomic DNA. Translation: AAA39787.1 .
    K03547 Genomic DNA. Translation: AAA39786.1 .
    CCDSi CCDS35861.1.
    PIRi A25285. TVMSMB.
    RefSeqi NP_001185843.1. NM_001198914.1.
    NP_034978.3. NM_010848.3.
    UniGenei Mm.473872.
    Mm.52109.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GUU X-ray 1.60 A 38-89 [» ]
    1GV2 X-ray 1.68 A 89-193 [» ]
    1GV5 X-ray 1.58 A 90-141 [» ]
    1GVD X-ray 1.45 A 90-141 [» ]
    1H88 X-ray 2.80 C 37-193 [» ]
    1H89 X-ray 2.45 C 37-193 [» ]
    1IDY NMR - A 141-193 [» ]
    1IDZ NMR - A 141-193 [» ]
    1MBE NMR - A 38-89 [» ]
    1MBF NMR - A 38-89 [» ]
    1MBG NMR - A 90-141 [» ]
    1MBH NMR - A 90-141 [» ]
    1MBJ NMR - A 142-193 [» ]
    1MBK NMR - A 142-193 [» ]
    1MSE NMR - C 90-193 [» ]
    1MSF NMR - C 90-193 [» ]
    1SB0 NMR - B 291-315 [» ]
    2AGH NMR - A 291-315 [» ]
    ProteinModelPortali P06876.
    SMRi P06876. Positions 38-193.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201631. 11 interactions.
    IntActi P06876. 2 interactions.

    PTM databases

    PhosphoSitei P06876.

    Proteomic databases

    PRIDEi P06876.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000020158 ; ENSMUSP00000020158 ; ENSMUSG00000019982 .
    GeneIDi 17863.
    KEGGi mmu:17863.
    UCSCi uc007eog.1. mouse.

    Organism-specific databases

    CTDi 4602.
    MGIi MGI:97249. Myb.

    Phylogenomic databases

    eggNOGi COG5147.
    GeneTreei ENSGT00390000001038.
    HOVERGENi HBG007964.
    KOi K09420.
    OMAi HGCLPEE.
    OrthoDBi EOG7H791P.
    TreeFami TF326257.

    Enzyme and pathway databases

    Reactomei REACT_198649. Factors involved in megakaryocyte development and platelet production.

    Miscellaneous databases

    EvolutionaryTracei P06876.
    NextBioi 292625.
    PROi P06876.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P06876.
    Bgeei P06876.
    CleanExi MM_MYB.
    Genevestigatori P06876.

    Family and domain databases

    Gene3Di 1.10.10.60. 3 hits.
    InterProi IPR015395. C-myb_C.
    IPR009057. Homeodomain-like.
    IPR017930. Myb_dom.
    IPR001005. SANT/Myb.
    IPR012642. Tscrpt_reg_Wos2-domain.
    [Graphical view ]
    Pfami PF09316. Cmyb_C. 1 hit.
    PF07988. LMSTEN. 1 hit.
    PF00249. Myb_DNA-binding. 1 hit.
    [Graphical view ]
    SMARTi SM00717. SANT. 3 hits.
    [Graphical view ]
    SUPFAMi SSF46689. SSF46689. 2 hits.
    PROSITEi PS51294. HTH_MYB. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Murine myb protooncogene mRNA: cDNA sequence and evidence for 5' heterogeneity."
      Bender T.P., Kuehl W.M.
      Proc. Natl. Acad. Sci. U.S.A. 83:3204-3208(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    2. "Nucleotide sequence of cDNA clones of the murine myb proto-oncogene."
      Gonda T.J., Gough N.M., Dunn A.R., de Blaquiere J.
      EMBO J. 4:2003-2008(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Multiple c-myb transcript cap sites are variously utilized in cells of mouse haemopoietic origin."
      Watson R.J., Dyson P.J., McMahon J.
      EMBO J. 6:1643-1651(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "Aberrant splicing events that are induced by proviral integration: implications for myb oncogene activation."
      Rosson D., Dugan D., Reddy E.P.
      Proc. Natl. Acad. Sci. U.S.A. 84:3171-3175(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    6. "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.
    7. "Structure and biological activity of the transcriptional initiation sequences of the murine c-myb oncogene."
      Sobieszczuk P.W., Gonda T.J., Dunn A.R.
      Nucleic Acids Res. 17:9593-9611(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-47.
    8. "Two modes of c-myb activation in virus-induced mouse myeloid tumors."
      Shen-Ong G.L.C., Morse H.C. III, Potter M., Mushinski F.
      Mol. Cell. Biol. 6:380-392(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 72-636.
    9. "Structural organization and nucleotide sequence of mouse c-myb oncogene: activation in ABPL tumors is due to viral integration in an intron which results in the deletion of the 5' coding sequences."
      Lavu S., Reddy E.P.
      Nucleic Acids Res. 14:5309-5320(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 72-401.
    10. "Truncation of the c-myb gene by a retroviral integration in an interleukin 3-dependent myeloid leukemia cell line."
      Weinstein Y., Ihle J.N., Lavu S., Reddy P.E.
      Proc. Natl. Acad. Sci. U.S.A. 83:5010-5014(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 388-402.
    11. "Activation of c-myb by carboxy-terminal truncation: relationship to transformation of murine haemopoietic cells in vitro."
      Gonda T.J., Buckmaster C., Ramsay R.G.
      EMBO J. 8:1777-1783(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN C-TERMINAL.
    12. "Transformation by carboxyl-deleted Myb reflects increased transactivating capacity and disruption of a negative regulatory domain."
      Hu Y., Ramsay R.G., Kanei-Ishii C., Ishii S., Gonda T.J.
      Oncogene 6:1549-1553(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NEGATIVE REGULATORY DOMAIN.
    13. "Negative autoregulation of c-Myb activity by homodimer formation through the leucine zipper."
      Nomura T., Sakai N., Sarai A., Sudo T., Kanei-Ishii C., Ramsay R.G., Favier D., Gonda T.J., Ishii S.
      J. Biol. Chem. 268:21914-21923(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN LEUCINE-ZIPPER, NEGATIVE AUTOREGULATION.
    14. "Molecular cloning reveals that the p160 Myb-binding protein is a novel, predominantly nucleolar protein which may play a role in transactivation by Myb."
      Tavner F.J., Simpson R., Tashiro S., Favier D., Jenkins N.A., Gilbert D.J., Copeland N.G., Macmillan E.M., Lutwyche J., Keough R.A., Ishii S., Gonda T.J.
      Mol. Cell. Biol. 18:989-1002(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MYBBP1A1.
    15. "c-Maf interacts with c-Myb to regulate transcription of an early myeloid gene during differentiation."
      Hedge S.P., Kumar A., Kurschner C., Shapiro L.H.
      Mol. Cell. Biol. 18:2729-2737(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAF.
    16. "Wnt-1 signal induces phosphorylation and degradation of c-Myb protein via TAK1, HIPK2, and NLK."
      Kanei-Ishii C., Ninomiya-Tsuji J., Tanikawa J., Nomura T., Ishitani T., Kishida S., Kokura K., Kurahashi T., Ichikawa-Iwata E., Kim Y., Matsumoto K., Ishii S.
      Genes Dev. 18:816-829(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIPK2 AND NLK.
    17. "c-Maf interacts with c-Myb to down-regulate Bcl-2 expression and increase apoptosis in peripheral CD4 cells."
      Peng S., Lalani S., Leavenworth J.W., Ho I.-C., Pauza M.E.
      Eur. J. Immunol. 37:2868-2880(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAF.
    18. "Solution structure of a DNA-binding unit of Myb: a helix-turn-helix-related motif with conserved tryptophans forming a hydrophobic core."
      Ogata K., Hojo H., Aimoto S., Nakai T., Nakamura H., Sarai A., Ishii S., Nishimura Y.
      Proc. Natl. Acad. Sci. U.S.A. 89:6428-6432(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 142-193.
    19. "Secondary structure of the DNA-binding domain of the c-Myb oncoprotein in solution. A multidimensional double and triple heteronuclear NMR study."
      Jamin N., Gabrielsen O.S., Gilles N., Lirsac P.-N., Toma F.
      Eur. J. Biochem. 216:147-154(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 89-192.
    20. "Comparison of the free and DNA-complexed forms of the DNA-binding domain from c-Myb."
      Ogata K., Morikawa S., Nakamura H., Hojo H., Yoshimura S., Zhang R., Aimoto S., Ametani Y., Hirata Z., Sarai A., Ishii S., Nishimura Y.
      Nat. Struct. Biol. 2:309-320(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 38-89; 90-141 AND 142-193.
    21. "A small engineered protein lacks structural uniqueness by increasing the side-chain conformational entropy."
      Furukawa K., Oda M., Nakamura H.
      Proc. Natl. Acad. Sci. U.S.A. 93:13583-13588(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 140-193.
    22. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 35-193 IN COMPLEX WITH HUMAN CEBPB.

    Entry informationi

    Entry nameiMYB_MOUSE
    AccessioniPrimary (citable) accession number: P06876
    Secondary accession number(s): E9QMG8, Q61929
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 151 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3