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Q03347

- RUNX1_MOUSE

UniProt

Q03347 - RUNX1_MOUSE

Protein

Runt-related transcription factor 1

Gene

Runx1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    CBF binds to the core site, 5'-PYGPYGGT-3', of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, LCK, IL-3 and GM-CSF promoters. Essential for the development of normal hematopoiesis. Isoform 4 shows higher binding activities for target genes and binds TCR-beta-E2 and RAG-1 target site with threefold higher affinity than other isoforms. It is less effective in the context of neutrophil terminal differentiation. Acts synergistically with ELF4 to transactivate the IL-3 promoter and with ELF2 to transactivate the BLK promoter. Inhibits KAT6B-dependent transcriptional activation By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei112 – 1121Chloride 1PROSITE-ProRule annotation
    Binding sitei116 – 1161Chloride 1; via amide nitrogenPROSITE-ProRule annotation
    Binding sitei139 – 1391Chloride 2PROSITE-ProRule annotation
    Binding sitei170 – 1701Chloride 2; via amide nitrogenPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: InterPro
    2. DNA binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. repressing transcription factor binding Source: MGI
    5. sequence-specific DNA binding transcription factor activity Source: MGI

    GO - Biological processi

    1. behavioral response to pain Source: MGI
    2. cellular response to transforming growth factor beta stimulus Source: MGI
    3. central nervous system development Source: MGI
    4. definitive hemopoiesis Source: MGI
    5. embryonic hemopoiesis Source: MGI
    6. hair follicle morphogenesis Source: MGI
    7. hemopoiesis Source: UniProtKB
    8. in utero embryonic development Source: MGI
    9. liver development Source: MGI
    10. myeloid progenitor cell differentiation Source: MGI
    11. neuron development Source: MGI
    12. neuron differentiation Source: MGI
    13. positive regulation of angiogenesis Source: UniProtKB
    14. positive regulation of granulocyte differentiation Source: UniProtKB
    15. positive regulation of transcription, DNA-templated Source: UniProtKB
    16. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    17. regulation of hair follicle cell proliferation Source: MGI
    18. regulation of signal transduction Source: MGI
    19. regulation of transcription, DNA-templated Source: MGI
    20. response to retinoic acid Source: BHF-UCL
    21. skeletal system development Source: MGI
    22. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Runt-related transcription factor 1
    Alternative name(s):
    Acute myeloid leukemia 1 protein
    Core-binding factor subunit alpha-2
    Short name:
    CBF-alpha-2
    Oncogene AML-1
    Polyomavirus enhancer-binding protein 2 alpha B subunit
    Short name:
    PEA2-alpha B
    Short name:
    PEBP2-alpha B
    SL3-3 enhancer factor 1 alpha B subunit
    SL3/AKV core-binding factor alpha B subunit
    Gene namesi
    Name:Runx1
    Synonyms:Aml1, Cbfa2, Pebp2ab
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:99852. Runx1.

    Subcellular locationi

    GO - Cellular componenti

    1. basement membrane Source: MGI
    2. nucleus Source: MGI

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Mice with an Runx1 lacking the DNA-binding region are found to die between embryonic days 11.5 to 12.5 due to hemorrhaging in the central nervous system. This hemorrhaging is preceded by necrosis and hematopoiesis is blocked.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi80 – 801R → A: Interferes with DNA-binding. 1 Publication
    Mutagenesisi109 – 1091N → A: Interferes with heterodimerization. 1 Publication
    Mutagenesisi113 – 1131Y → A: Interferes with heterodimerization. 1 Publication
    Mutagenesisi142 – 1421R → A: Interferes with DNA-binding. 1 Publication
    Mutagenesisi144 – 1441K → M: Interferes with DNA-binding. 1 Publication
    Mutagenesisi149 – 1491T → A: Interferes with heterodimerization. 1 Publication
    Mutagenesisi170 – 1701V → A: No effect. 1 Publication
    Mutagenesisi171 – 1711D → A: Interferes with DNA-binding. 1 Publication
    Mutagenesisi174 – 1741R → A: Interferes with DNA-binding. 1 Publication
    Mutagenesisi177 – 1771R → A: Interferes with DNA-binding. 1 Publication
    Mutagenesisi249 – 2491S → A: Reduced phosphorylation. 1 Publication
    Mutagenesisi276 – 2761S → A: Reduced phosphorylation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 451451Runt-related transcription factor 1PRO_0000174656Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei14 – 141PhosphothreonineBy similarity
    Modified residuei21 – 211PhosphoserineBy similarity
    Modified residuei24 – 241N6-acetyllysineBy similarity
    Modified residuei43 – 431N6-acetyllysineBy similarity
    Modified residuei249 – 2491Phosphoserine; by HIPK21 Publication
    Modified residuei266 – 2661PhosphoserineBy similarity
    Modified residuei268 – 2681PhosphoserineBy similarity
    Modified residuei273 – 2731Phosphothreonine; by HIPK2By similarity
    Modified residuei276 – 2761Phosphoserine; by HIPK21 Publication

    Post-translational modificationi

    Phosphorylated in its C-terminus upon IL-6 treatment. Phosphorylation enhances interaction with KAT6A By similarity.By similarity
    Methylated.By similarity
    Phosphorylated in Ser-249 Thr-273 and Ser-276 by HIPK2 when associated with CBFB and DNA. This phosphorylation promotes subsequent EP300 phosphorylation.1 Publication

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    PaxDbiQ03347.
    PRIDEiQ03347.

    PTM databases

    PhosphoSiteiQ03347.

    Expressioni

    Tissue specificityi

    Isoform 4 is expressed at high levels in thymus, spleen and T-cell lines and at lower levels in myeloid cell lines and nonhematopoietic cells. Isoform 5 is expressed ubiquitously in lumbar vertebrae, brain, kidney, heart, muscle, ovary and osteoblast-like cell line MC3T3-E1.

    Developmental stagei

    Differentially expressed during hematopoietic differentiation. Isoform AML1-B is readily detectable in undifferentiated embryonic stem (es) cells and peak expression is seen on day 6 of differentiation, followed by a gradual decline thereafter. Isoform AML1-C is undetectable in undifferentiated es cells, but is gradually up-regulated along with differentiation and reaches its highest levels on day 8 and this expression is maintained through day 12. Isoform 5 is expressed at high levels at 6-8 dpc and then levels decrease on 12 dpc. Isoform 4 expression is high throughout T-cell development, declines with natural killer cell maturation, and appears to be transiently reduced and then restored during B-cell development.

    Gene expression databases

    CleanExiMM_RUNX1.
    GenevestigatoriQ03347.

    Interactioni

    Subunit structurei

    Heterodimer with CBFB. RUNX1 binds DNA as a monomer and through the Runt domain. DNA-binding is increased by heterodimerization. Interacts with TLE1 and ALYREF/THOC4. Interacts with HIPK2, ELF1, ELF2 and SPI1. Interacts via its Runt domain with the ELF4 N-terminal region. Interaction with ELF2 isoform 2 (NERF-1a) may act to repress RUNX1-mediated transactivation. Interacts with KAT6A and KAT6B. Interacts with SUV39H1, leading to abrogation of transactivating and DNA-binding properties of RUNX1 By similarity. Interacts with YAP1. Interaction with CDK6 prevents myeloid differentiation, reducing its transcription transactivation activity By similarity. Found in a complex with PRMT5, RUNX1 and CBFB.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Tbx21Q9JKD83EBI-3863873,EBI-3863870

    Protein-protein interaction databases

    BioGridi198519. 37 interactions.
    DIPiDIP-40723N.
    IntActiQ03347. 3 interactions.
    MINTiMINT-91306.

    Structurei

    Secondary structure

    1
    451
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi51 – 577
    Turni59 – 613
    Beta strandi62 – 643
    Beta strandi70 – 723
    Beta strandi77 – 804
    Beta strandi90 – 956
    Beta strandi102 – 1098
    Beta strandi112 – 1154
    Beta strandi117 – 1193
    Beta strandi121 – 1255
    Beta strandi128 – 1303
    Beta strandi146 – 1527
    Beta strandi154 – 1563
    Beta strandi158 – 1614
    Beta strandi166 – 1716
    Helixi194 – 20310
    Helixi205 – 2106

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EANX-ray1.70A46-185[»]
    1EAOX-ray1.40A/B46-185[»]
    1EAQX-ray1.25A/B46-185[»]
    1HJBX-ray3.00C/F60-182[»]
    1HJCX-ray2.65A/D60-182[»]
    1IO4X-ray3.00C60-182[»]
    2J6WX-ray2.60A/B46-185[»]
    4L0YX-ray2.50A1-242[»]
    4L0ZX-ray2.70A1-242[»]
    4L18X-ray2.30A/E48-214[»]
    ProteinModelPortaliQ03347.
    SMRiQ03347. Positions 50-212, 319-345.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ03347.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini50 – 178129RuntPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni80 – 845Interaction with DNABy similarity
    Regioni135 – 1439Interaction with DNABy similarity
    Regioni168 – 17710Interaction with DNABy similarity
    Regioni291 – 37080Interaction with KAT6ABy similarityAdd
    BLAST
    Regioni307 – 39993Interaction with KAT6BBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi187 – 451265Pro/Ser/Thr-richAdd
    BLAST

    Domaini

    A proline/serine/threonine rich region at the C-terminus is necessary for transcriptional activation of target genes.

    Sequence similaritiesi

    Contains 1 Runt domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG123889.
    HOGENOMiHOG000045616.
    HOVERGENiHBG060268.
    InParanoidiQ03347.
    PhylomeDBiQ03347.

    Family and domain databases

    Gene3Di2.60.40.720. 1 hit.
    4.10.770.10. 1 hit.
    InterProiIPR000040. AML1_Runt.
    IPR008967. p53-like_TF_DNA-bd.
    IPR012346. p53/RUNT-type_TF_DNA-bd.
    IPR013524. Runt_dom.
    IPR027384. Runx_central_dom.
    IPR013711. RunxI_C_dom.
    IPR016554. TF_Runt-rel_RUNX.
    [Graphical view]
    PANTHERiPTHR11950. PTHR11950. 1 hit.
    PfamiPF00853. Runt. 1 hit.
    PF08504. RunxI. 1 hit.
    [Graphical view]
    PIRSFiPIRSF009374. TF_Runt-rel_RUNX. 1 hit.
    PRINTSiPR00967. ONCOGENEAML1.
    SUPFAMiSSF49417. SSF49417. 1 hit.
    PROSITEiPS51062. RUNT. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q03347-1) [UniParc]FASTAAdd to Basket

    Also known as: AML1-B, PEB2-alpha B1

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MRIPVDASTS RRFTPPSTAL SPGKMSEALP LGAPDGGPAL ASKLRSGDRS    50
    MVEVLADHPG ELVRTDSPNF LCSVLPTHWR CNKTLPIAFK VVALGDVPDG 100
    TLVTVMAGND ENYSAELRNA TAAMKNQVAR FNDLRFVGRS GRGKSFTLTI 150
    TVFTNPPQVA TYHRAIKITV DGPREPRRHR QKLDDQTKPG SLSFSERLSE 200
    LEQLRRTAMR VSPHHPAPTP NPRASLNHST AFNPQPQSQM QDARQIQPSP 250
    PWSYDQSYQY LGSITSSSVH PATPISPGRA SGMTSLSAEL SSRLSTAPDL 300
    TAFGDPRQFP TLPSISDPRM HYPGAFTYSP PVTSGIGIGM SAMSSASRYH 350
    TYLPPPYPGS SQAQAGPFQT GSPSYHLYYG ASAGSYQFSM VGGERSPPRI 400
    LPPCTNASTG AALLNPSLPS QSDVVETEGS HSNSPTNMPP ARLEEAVWRP 450
    Y 451
    Length:451
    Mass (Da):48,610
    Last modified:November 1, 1996 - v1
    Checksum:i06B9E9BA01A6469C
    GO
    Isoform 2 (identifier: Q03347-2) [UniParc]FASTAAdd to Basket

    Also known as: PEB2-alpha B2

    The sequence of this isoform differs from the canonical sequence as follows:
         178-178: R → N
         179-242: Missing.

    Show »
    Length:387
    Mass (Da):41,299
    Checksum:iCB505325F9D4ED81
    GO
    Isoform 3 (identifier: Q03347-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         92-182: VALGDVPDGT...PREPRRHRQK → LLPEEGGGRS...ASEVSKREFF
         183-451: Missing.

    Show »
    Length:163
    Mass (Da):17,571
    Checksum:iAE48F53C5FF9A096
    GO
    Isoform 4 (identifier: Q03347-4) [UniParc]FASTAAdd to Basket

    Also known as: AML1-C

    The sequence of this isoform differs from the canonical sequence as follows:
         1-5: MRIPV → MASDSIFESFPSYPQCFMR

    Show »
    Length:465
    Mass (Da):50,238
    Checksum:i8C7E357BAA92E2E5
    GO
    Isoform 5 (identifier: Q03347-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         242-303: DARQIQPSPP...LSTAPDLTAF → KNPTEPTTLC...EYLYSEKCGC
         304-451: Missing.

    Show »
    Length:303
    Mass (Da):33,485
    Checksum:iED89962B59A0EC94
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti37 – 382GP → A in CAA65976. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 55MRIPV → MASDSIFESFPSYPQCFMR in isoform 4. CuratedVSP_005930
    Alternative sequencei92 – 18291VALGD…RHRQK → LLPEEGGGRSRWRSADGQSE PRGQRLRRLLKGAACSRSLW SFSLSLGWGGDAALPWRPSG GSASEVSKREFF in isoform 3. 1 PublicationVSP_005931Add
    BLAST
    Alternative sequencei178 – 1781R → N in isoform 2. 1 PublicationVSP_005932
    Alternative sequencei179 – 24264Missing in isoform 2. 1 PublicationVSP_005933Add
    BLAST
    Alternative sequencei183 – 451269Missing in isoform 3. 1 PublicationVSP_005934Add
    BLAST
    Alternative sequencei242 – 30362DARQI…DLTAF → KNPTEPTTLCLCWSPRRRKH RGCQAFLGALRELLKPRSIS WEPNEENAVPSAEYLYSEKC GC in isoform 5. CuratedVSP_005935Add
    BLAST
    Alternative sequencei304 – 451148Missing in isoform 5. CuratedVSP_005936Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D26532 mRNA. Translation: BAA05535.1.
    D13802 mRNA. Translation: BAA02960.1.
    X97306 mRNA. Translation: CAA65976.1.
    AB046930 mRNA. Translation: BAB08105.1.
    AF345649 mRNA. Translation: AAK29784.1.
    AF193030 Genomic DNA. Translation: AAG32957.1.
    CCDSiCCDS28339.1. [Q03347-2]
    CCDS49916.1. [Q03347-1]
    CCDS49917.1. [Q03347-4]
    PIRiA56017.
    UniGeneiMm.4081.
    Mm.470227.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D26532 mRNA. Translation: BAA05535.1 .
    D13802 mRNA. Translation: BAA02960.1 .
    X97306 mRNA. Translation: CAA65976.1 .
    AB046930 mRNA. Translation: BAB08105.1 .
    AF345649 mRNA. Translation: AAK29784.1 .
    AF193030 Genomic DNA. Translation: AAG32957.1 .
    CCDSi CCDS28339.1. [Q03347-2 ]
    CCDS49916.1. [Q03347-1 ]
    CCDS49917.1. [Q03347-4 ]
    PIRi A56017.
    UniGenei Mm.4081.
    Mm.470227.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EAN X-ray 1.70 A 46-185 [» ]
    1EAO X-ray 1.40 A/B 46-185 [» ]
    1EAQ X-ray 1.25 A/B 46-185 [» ]
    1HJB X-ray 3.00 C/F 60-182 [» ]
    1HJC X-ray 2.65 A/D 60-182 [» ]
    1IO4 X-ray 3.00 C 60-182 [» ]
    2J6W X-ray 2.60 A/B 46-185 [» ]
    4L0Y X-ray 2.50 A 1-242 [» ]
    4L0Z X-ray 2.70 A 1-242 [» ]
    4L18 X-ray 2.30 A/E 48-214 [» ]
    ProteinModelPortali Q03347.
    SMRi Q03347. Positions 50-212, 319-345.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198519. 37 interactions.
    DIPi DIP-40723N.
    IntActi Q03347. 3 interactions.
    MINTi MINT-91306.

    PTM databases

    PhosphoSitei Q03347.

    Proteomic databases

    PaxDbi Q03347.
    PRIDEi Q03347.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    MGIi MGI:99852. Runx1.

    Phylogenomic databases

    eggNOGi NOG123889.
    HOGENOMi HOG000045616.
    HOVERGENi HBG060268.
    InParanoidi Q03347.
    PhylomeDBi Q03347.

    Miscellaneous databases

    EvolutionaryTracei Q03347.
    NextBioi 281140.
    PROi Q03347.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_RUNX1.
    Genevestigatori Q03347.

    Family and domain databases

    Gene3Di 2.60.40.720. 1 hit.
    4.10.770.10. 1 hit.
    InterProi IPR000040. AML1_Runt.
    IPR008967. p53-like_TF_DNA-bd.
    IPR012346. p53/RUNT-type_TF_DNA-bd.
    IPR013524. Runt_dom.
    IPR027384. Runx_central_dom.
    IPR013711. RunxI_C_dom.
    IPR016554. TF_Runt-rel_RUNX.
    [Graphical view ]
    PANTHERi PTHR11950. PTHR11950. 1 hit.
    Pfami PF00853. Runt. 1 hit.
    PF08504. RunxI. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF009374. TF_Runt-rel_RUNX. 1 hit.
    PRINTSi PR00967. ONCOGENEAML1.
    SUPFAMi SSF49417. SSF49417. 1 hit.
    PROSITEi PS51062. RUNT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation of PEBP2 alpha B cDNA representing the mouse homolog of human acute myeloid leukemia gene, AML1."
      Bae S.-C., Yamaguchi-Iwai Y., Ogawa E., Maruyama M., Inuzuka M., Kagoshima H., Shigesada K., Satake M., Ito Y.
      Oncogene 8:809-814(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Fibroblast.
    2. "PEBP2 alpha B/mouse AML1 consists of multiple isoforms that possess differential transactivation potentials."
      Bae S.-C., Ogawa E., Maruyama M., Oka H., Satake M., Shigesada K., Jenkins N.A., Gilbert D.J., Copeland N.G., Ito Y.
      Mol. Cell. Biol. 14:3242-3252(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Fibroblast.
    3. Calabi F.
      Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
      Strain: BALB/c.
      Tissue: Thymus.
    4. "Identification and expression of a novel 3'-exon of mouse Runx1/Pebp2alphaB/Cbfa2/AML1 gene."
      Tsuji K., Noda M.
      Biochem. Biophys. Res. Commun. 274:171-176(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
    5. "Identification of an alternatively spliced form of the mouse AML1/RUNX1 gene transcript AML1c and its expression in early hematopoietic development."
      Fujita Y., Nishimura M., Taniwaki M., Abe T., Okuda T.
      Biochem. Biophys. Res. Commun. 281:1248-1255(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
      Strain: 129/Ola.
      Tissue: Embryo.
    6. "Expression and function of a stem cell promoter for the murine CBFalpha2 gene: distinct roles and regulation in natural killer and T cell development."
      Telfer J.C., Rothenberg E.V.
      Dev. Biol. 229:363-382(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 4).
      Strain: C57BL/6.
      Tissue: Thymus.
    7. "AML1, the target of multiple chromosomal translocations in human leukemia, is essential for normal fetal liver hematopoiesis."
      Okuda T., van Deursen J., Hiebert S.W., Grosveld G., Downing J.R.
      Cell 84:321-330(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN LIVER HEMATOPOIESIS.
    8. "The histone- and PRMT5-associated protein COPR5 is required for myogenic differentiation."
      Paul C., Sardet C., Fabbrizio E.
      Cell Death Differ. 19:900-908(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH PRMT5; RUNX1 AND CBFB.
    9. "Disruption of the Cbfa2 gene causes necrosis and hemorrhaging in the central nervous system and blocks definitive hematopoiesis."
      Wang Q., Stacy T., Binder M., Marin-Padilla M., Sharpe A.H., Speck N.A.
      Proc. Natl. Acad. Sci. U.S.A. 93:3444-3449(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN NECROSIS AND HEMORRHAGING.
    10. "Roles of HIPK1 and HIPK2 in AML1- and p300-dependent transcription, hematopoiesis and blood vessel formation."
      Aikawa Y., Nguyen L.A., Isono K., Takakura N., Tagata Y., Schmitz M.L., Koseki H., Kitabayashi I.
      EMBO J. 25:3955-3965(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIPK2, PHOSPHORYLATION AT SER-249 AND SER-276 BY HIPK2, MUTAGENESIS OF SER-249 AND SER-276.
    11. "Crystallization and preliminary X-ray analyses of quaternary, ternary and binary protein-DNA complexes with involvement of AML1/Runx-1/CBFalpha Runt domain, CBFbeta and the C/EBPbeta bZip region."
      Tahirov T.H., Inoue-Bungo T., Sasaki M., Shiina M., Kimura K., Sato K., Kumasaka T., Yamamoto M., Kamiya N., Ogata K.
      Acta Crystallogr. D 57:850-853(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 62-177 IN COMPLEX WITH CEBPB; CBFB AND DNA.
    12. "Structural analyses of DNA recognition by the AML1/Runx-1 Runt domain and its allosteric control by CBFbeta."
      Tahirov T.H., Inoue-Bungo T., Morii H., Fujikawa A., Sasaki M., Kimura K., Shiina M., Sato K., Kumasaka T., Yamamoto M., Ishii S., Ogata K.
      Cell 104:755-767(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 60-182 IN COMPLEX WITH CEBPB; CBFB AND DNA, MUTAGENESIS OF ARG-80; ASN-109; TYR-113; ARG-142; LYS-144; THR-149; VAL-170; ASP-171; ARG-174 AND ARG-177.
    13. "The RUNX1 Runt domain at 1.25A resolution: a structural switch and specifically bound chloride ions modulate DNA binding."
      Baeckstroem S., Wolf-Watz M., Grundstroem C., Haerd T., Grundstroem T., Sauer U.H.
      J. Mol. Biol. 322:259-272(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 60-173.

    Entry informationi

    Entry nameiRUNX1_MOUSE
    AccessioniPrimary (citable) accession number: Q03347
    Secondary accession number(s): O08598
    , Q62049, Q9ESB9, Q9ET65
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 146 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

    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