Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q01196

- RUNX1_HUMAN

UniProt

Q01196 - RUNX1_HUMAN

Protein

Runt-related transcription factor 1

Gene

RUNX1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 184 (01 Oct 2014)
      Sequence version 3 (25 Nov 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. The alpha subunit binds DNA and appears to have a role in the development of normal hematopoiesis. Isoform AML-1L interferes with the transactivation activity of RUNX1. Acts synergistically with ELF4 to transactivate the IL-3 promoter and with ELF2 to transactivate the mouse BLK promoter. Inhibits KAT6B-dependent transcriptional activation.4 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei112 – 1121Chloride 1
    Binding sitei116 – 1161Chloride 1; via amide nitrogen
    Binding sitei139 – 1391Chloride 2
    Binding sitei170 – 1701Chloride 2; via amide nitrogen
    Sitei177 – 1782Breakpoint for translocation to form AML1-EMV-1 (or AML1-EAP) in CML and T-MDS, to form AML1-MTG8 (ETO) in AML-M2, to form AML1-CBFA2T3 in therapy-related myeloid malignancies, to form AML1-MECOM in CML and to form type I MACROD1-RUNX1 fusion protein
    Sitei241 – 2422Breakpoint for translocation to form AML1-EAP in T-MDS and CML and to form type II MACROD1-RUNX1 fusion protein

    GO - Molecular functioni

    1. ATP binding Source: InterPro
    2. calcium ion binding Source: UniProtKB
    3. DNA binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein heterodimerization activity Source: UniProtKB
    6. protein homodimerization activity Source: UniProtKB
    7. regulatory region DNA binding Source: UniProtKB
    8. sequence-specific DNA binding transcription factor activity Source: UniProtKB
    9. transcription factor binding Source: UniProtKB

    GO - Biological processi

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

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    Chloride, DNA-binding

    Enzyme and pathway databases

    SignaLinkiQ01196.

    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 21

    Organism-specific databases

    HGNCiHGNC:10471. RUNX1.

    Subcellular locationi

    GO - Cellular componenti

    1. basement membrane Source: Ensembl
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration involving RUNX1/AML1 is a cause of M2 type acute myeloid leukemia (AML-M2). Translocation t(8;21)(q22;q22) with RUNX1T1.
    A chromosomal aberration involving RUNX1/AML1 is a cause of therapy-related myelodysplastic syndrome (T-MDS). Translocation t(3;21)(q26;q22) with EAP or MECOM.
    A chromosomal aberration involving RUNX1/AML1 is a cause of chronic myelogenous leukemia (CML). Translocation t(3;21)(q26;q22) with EAP or MECOM.
    A chromosomal aberration involving RUNX1/AML1 is found in childhood acute lymphoblastic leukemia (ALL). Translocation t(12;21)(p13;q22) with TEL. The translocation fuses the 3'-end of TEL to the alternate 5'-exon of AML-1H.
    A chromosomal aberration involving RUNX1 is found in acute leukemia. Translocation t(11,21)(q13;q22) that forms a MACROD1-RUNX1 fusion protein.
    Familial platelet disorder with associated myeloid malignancy (FPDMM) [MIM:601399]: Autosomal dominant disease characterized by qualitative and quantitative platelet defects, and propensity to develop acute myelogenous leukemia.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti139 – 1391R → Q in FPDMM. 1 Publication
    VAR_012128
    Natural varianti174 – 1741R → Q in FPDMM; impaired phosphorylation. 2 Publications
    VAR_012129
    A chromosomal aberration involving RUNX1/AML1 is found in therapy-related myeloid malignancies. Translocation t(16;21)(q24;q22) that forms a RUNX1-CBFA2T3 fusion protein.
    A chromosomal aberration involving RUNX1/AML1 is a cause of chronic myelomonocytic leukemia. Inversion inv(21)(q21;q22) with USP16.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi67 – 671S → R: Loss of heterodimerization and reduced EP300 phosphorylation induction. 1 Publication
    Mutagenesisi80 – 801R → A: Strongly reduces DNA-binding. 1 Publication
    Mutagenesisi83 – 831K → A: Strongly reduces DNA-binding. 2 Publications
    Mutagenesisi83 – 831K → E: Strongly reduces DNA-binding, impaired phosphorylation and reduced EP300 phosphorylation induction. 2 Publications
    Mutagenesisi84 – 841T → A: No effect on DNA binding. 1 Publication
    Mutagenesisi107 – 1071A → T: Loss of heterodimerization. 1 Publication
    Mutagenesisi108 – 1081G → R: Loss of heterodimerization and impaired phosphorylation. 2 Publications
    Mutagenesisi135 – 1351R → A: Strongly reduces DNA-binding. 1 Publication
    Mutagenesisi139 – 1391R → A: Strongly reduces DNA-binding. 1 Publication
    Mutagenesisi142 – 1421R → A: Strongly reduces DNA-binding. 1 Publication
    Mutagenesisi145 – 453309Missing: No DNA-binding. Add
    BLAST
    Mutagenesisi167 – 1671K → A: Reduces DNA-binding. 1 Publication
    Mutagenesisi169 – 1691T → A: Strongly reduces DNA-binding. 1 Publication
    Mutagenesisi171 – 1711D → A: Strongly reduces DNA-binding. 1 Publication
    Mutagenesisi174 – 1741R → A: Strongly reduces DNA-binding. 1 Publication
    Mutagenesisi177 – 1771R → A: Strongly reduces DNA-binding. 1 Publication
    Mutagenesisi249 – 2491S → A: Reduced phosphorylation. 1 Publication
    Mutagenesisi273 – 2731T → A: Reduced phosphorylation; when associated with A-276. 1 Publication
    Mutagenesisi276 – 2761S → A: Reduced phosphorylation; when associated with A-273. 1 Publication

    Keywords - Diseasei

    Disease mutation, Proto-oncogene

    Organism-specific databases

    MIMi601399. phenotype.
    Orphaneti102724. Acute myeloid leukemia with t(8;21)(q22;q22) translocation.
    521. Chronic myeloid leukemia.
    71290. Familial platelet syndrome with predisposition to acute myelogenous leukemia.
    248340. Isolated delta-storage pool disease.
    99860. Precursor B-cell acute lymphoblastic leukemia.
    PharmGKBiPA34884.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 453453Runt-related transcription factor 1PRO_0000174655Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei14 – 141Phosphothreonine3 Publications
    Modified residuei21 – 211Phosphoserine2 Publications
    Modified residuei24 – 241N6-acetyllysine1 Publication
    Modified residuei43 – 431N6-acetyllysine1 Publication
    Modified residuei249 – 2491Phosphoserine; by HIPK23 Publications
    Modified residuei266 – 2661Phosphoserine2 Publications
    Modified residuei268 – 2681Phosphoserine2 Publications
    Modified residuei273 – 2731Phosphothreonine; by HIPK22 Publications
    Modified residuei276 – 2761Phosphoserine; by HIPK23 Publications

    Post-translational modificationi

    Phosphorylated in its C-terminus upon IL-6 treatment. Phosphorylation enhances interaction with KAT6A.
    Methylated.1 Publication
    Phosphorylated in Ser-249 Thr-273 and Ser-276 by HIPK2 when associated with CBFB and DNA. This phosphorylation promotes subsequent EP300 phosphorylation.2 Publications

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ01196.
    PaxDbiQ01196.
    PRIDEiQ01196.

    PTM databases

    PhosphoSiteiQ01196.

    Expressioni

    Tissue specificityi

    Expressed in all tissues examined except brain and heart. Highest levels in thymus, bone marrow and peripheral blood.

    Gene expression databases

    ArrayExpressiQ01196.
    BgeeiQ01196.
    GenevestigatoriQ01196.

    Organism-specific databases

    HPAiHPA004176.

    Interactioni

    Subunit structurei

    Heterodimer with CBFB. RUNX1 binds DNA as a monomer and through the Runt domain. DNA-binding is increased by heterodimerization. Isoform AML-1L can neither bind DNA nor heterodimerize. Interacts with TLE1 and ALYREF/THOC4. Interacts with 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. Interacts with YAP1. Interacts with HIPK2 By similarity. Interaction with CDK6 prevents myeloid differentiation, reducing its transcription transactivation activity. Found in a complex with PRMT5, RUNX1 AND CBFB.By similarity14 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CBFBQ139512EBI-925904,EBI-718750
    CDK6Q005345EBI-925904,EBI-295663
    ELF2Q157232EBI-925904,EBI-956941
    groP163714EBI-925940,EBI-153866From a different organism.
    HIPK2Q9H2X64EBI-925904,EBI-348345
    TAL1P175422EBI-925904,EBI-1753878
    TLE1Q047244EBI-925940,EBI-711424

    Protein-protein interaction databases

    BioGridi107309. 69 interactions.
    DIPiDIP-36773N.
    IntActiQ01196. 16 interactions.
    MINTiMINT-153610.

    Structurei

    Secondary structure

    1
    453
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi54 – 574
    Beta strandi62 – 643
    Beta strandi70 – 734
    Beta strandi77 – 804
    Beta strandi82 – 843
    Beta strandi90 – 934
    Beta strandi102 – 1087
    Beta strandi110 – 1145
    Beta strandi117 – 1193
    Beta strandi121 – 1233
    Beta strandi128 – 1303
    Beta strandi146 – 1527
    Beta strandi154 – 1563
    Beta strandi158 – 1614
    Beta strandi166 – 1716
    Helixi175 – 1773

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CMONMR-A52-178[»]
    1CO1NMR-A61-175[»]
    1E50X-ray2.60A/C/E/G/Q/R50-183[»]
    1H9DX-ray2.60A/C50-183[»]
    1LJMX-ray2.50A/B51-181[»]
    ProteinModelPortaliQ01196.
    SMRiQ01196. Positions 50-212, 319-346.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ01196.

    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 DNA
    Regioni135 – 1439Interaction with DNA
    Regioni168 – 17710Interaction with DNA
    Regioni291 – 37181Interaction with KAT6AAdd
    BLAST
    Regioni307 – 40094Interaction with KAT6BBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi187 – 453267Pro/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.
    HOVERGENiHBG060268.
    KOiK08367.
    OMAiDPRQFPT.
    PhylomeDBiQ01196.
    TreeFamiTF321496.

    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 (11)i

    Sequence statusi: Complete.

    This entry describes 11 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform AML-1B (identifier: Q01196-1) [UniParc]FASTAAdd to Basket

    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 LGAPDAGAAL AGKLRSGDRS    50
    MVEVLADHPG ELVRTDSPNF LCSVLPTHWR CNKTLPIAFK VVALGDVPDG 100
    TLVTVMAGND ENYSAELRNA TAAMKNQVAR FNDLRFVGRS GRGKSFTLTI 150
    TVFTNPPQVA TYHRAIKITV DGPREPRRHR QKLDDQTKPG SLSFSERLSE 200
    LEQLRRTAMR VSPHHPAPTP NPRASLNHST AFNPQPQSQM QDTRQIQPSP 250
    PWSYDQSYQY LGSIASPSVH PATPISPGRA SGMTTLSAEL SSRLSTAPDL 300
    TAFSDPRQFP ALPSISDPRM HYPGAFTYSP TPVTSGIGIG MSAMGSATRY 350
    HTYLPPPYPG SSQAQGGPFQ ASSPSYHLYY GASAGSYQFS MVGGERSPPR 400
    ILPPCTNAST GSALLNPSLP NQSDVVEAEG SHSNSPTNMA PSARLEEAVW 450
    RPY 453
    Length:453
    Mass (Da):48,737
    Last modified:November 25, 2008 - v3
    Checksum:i4F1F193A7CADDBAB
    GO
    Isoform AML-1A (identifier: Q01196-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         440-453: APSARLEEAVWRPY → GGASCSRQARRDPGPWARTPSWGRGRPTDRISL

    Show »
    Length:472
    Mass (Da):50,701
    Checksum:i13349A060DC3B793
    GO
    Isoform AML-1C (identifier: Q01196-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         242-250: DTRQIQPSP → EEDTAPWRC
         251-453: Missing.

    Show »
    Length:250
    Mass (Da):27,427
    Checksum:iFADB4980D9FCA9D5
    GO
    Isoform AML-1E (identifier: Q01196-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         258-453: Missing.

    Show »
    Length:257
    Mass (Da):28,226
    Checksum:i10A5E857CB432487
    GO
    Isoform AML-1FA (identifier: Q01196-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         178-224: RHRQKLDDQT...HPAPTPNPRA → SKCIHLGLVH...GWQAPVKPKS
         225-453: Missing.

    Show »
    Length:224
    Mass (Da):24,049
    Checksum:i08A3748CC9F566E5
    GO
    Isoform AML-1FB (identifier: Q01196-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         178-188: RHRQKLDDQTK → NSLTWPRYPHI
         189-453: Missing.

    Show »
    Length:188
    Mass (Da):20,395
    Checksum:iD2B706A902D72B2A
    GO
    Isoform AML-1FC (identifier: Q01196-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         137-242: VGRSGRGKSF...NPQPQSQMQD → VDGPREPRRH...SPSVHPATPI
         243-453: Missing.

    Show »
    Length:242
    Mass (Da):26,509
    Checksum:i7DB647BA4D4BF366
    GO
    Isoform AML-1G (identifier: Q01196-8) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:480
    Mass (Da):51,818
    Checksum:i69582971F63E26D7
    GO
    Isoform AML-1H (identifier: Q01196-9) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:456
    Mass (Da):49,077
    Checksum:i9DE001CA7E9BA81B
    GO
    Isoform AML-1I (identifier: Q01196-10) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:468
    Mass (Da):50,173
    Checksum:i07A186F5A0EEB6E4
    GO
    Isoform AML-1L (identifier: Q01196-11) [UniParc]FASTAAdd to Basket

    Also known as: AML1-delta N

    The sequence of this isoform differs from the canonical sequence as follows:
         1-105: Missing.

    Show »
    Length:348
    Mass (Da):37,733
    Checksum:iD1E344B2E6586EC8
    GO

    Sequence cautioni

    The sequence AAC05246.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence AAC05247.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti412 – 4121S → F in AAA51720. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti139 – 1391R → Q in FPDMM. 1 Publication
    VAR_012128
    Natural varianti174 – 1741R → Q in FPDMM; impaired phosphorylation. 2 Publications
    VAR_012129
    Natural varianti431 – 4311S → R.
    Corresponds to variant rs1055308 [ dbSNP | Ensembl ].
    VAR_013177
    Natural varianti433 – 4331S → R.
    Corresponds to variant rs1055309 [ dbSNP | Ensembl ].
    VAR_013178

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 105105Missing in isoform AML-1L. 2 PublicationsVSP_005919Add
    BLAST
    Alternative sequencei1 – 55MRIPV → MASDSIFESFPSYPQCFMRE CILGMNPSRDVH in isoform AML-1G. 3 PublicationsVSP_005917
    Alternative sequencei1 – 55MRIPV → MNPSRDVH in isoform AML-1H. CuratedVSP_005916
    Alternative sequencei1 – 55MRIPV → MPAAPRGPAQGEAAARTRSR in isoform AML-1I. CuratedVSP_005918
    Alternative sequencei137 – 242106VGRSG…SQMQD → VDGPREPRRHRQKLDDQTKP GSLSFSERLSELEQLRRTAM RVSPHHPAPTPNPRASLNHS TAFNPQPQSQMQDTRQIQPS PPWSYDQSYQYLGSIASPSV HPATPI in isoform AML-1FC. CuratedVSP_005920Add
    BLAST
    Alternative sequencei178 – 22447RHRQK…PNPRA → SKCIHLGLVHPPGWYTLQAG ILRDHVSDSLGSTFPPGGWQ APVKPKS in isoform AML-1FA. CuratedVSP_005923Add
    BLAST
    Alternative sequencei178 – 18811RHRQKLDDQTK → NSLTWPRYPHI in isoform AML-1FB. CuratedVSP_005921Add
    BLAST
    Alternative sequencei189 – 453265Missing in isoform AML-1FB. CuratedVSP_005922Add
    BLAST
    Alternative sequencei225 – 453229Missing in isoform AML-1FA. CuratedVSP_005924Add
    BLAST
    Alternative sequencei242 – 2509DTRQIQPSP → EEDTAPWRC in isoform AML-1C. 1 PublicationVSP_005926
    Alternative sequencei243 – 453211Missing in isoform AML-1FC. CuratedVSP_005925Add
    BLAST
    Alternative sequencei251 – 453203Missing in isoform AML-1C. 1 PublicationVSP_005927Add
    BLAST
    Alternative sequencei258 – 453196Missing in isoform AML-1E. 1 PublicationVSP_005928Add
    BLAST
    Alternative sequencei440 – 45314APSAR…VWRPY → GGASCSRQARRDPGPWARTP SWGRGRPTDRISL in isoform AML-1A. 2 PublicationsVSP_005929Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L34598 mRNA. Translation: AAA51720.1.
    D43967 mRNA. Translation: BAA07902.1.
    D10570 mRNA. Translation: BAA01426.1.
    S76345 mRNA. Translation: AAB33729.1.
    S76346 mRNA. Translation: AAB33730.1.
    S76350 mRNA. Translation: AAB33731.1.
    S60998 mRNA. No translation available.
    X79549 mRNA. Translation: CAA56092.1.
    D43968 mRNA. Translation: BAA07903.1.
    D43969 mRNA. Translation: BAA07904.1.
    U19601 mRNA. Translation: AAB51691.1.
    L21756 mRNA. Translation: AAA03086.1. Different termination.
    S69002 mRNA. Translation: AAB29907.1. Different termination.
    D13979 mRNA. Translation: BAA03089.1.
    D14822 mRNA. Translation: BAA03559.1. Different termination.
    D14823 mRNA. Translation: BAA03560.1. Different termination.
    S78158 mRNA. Translation: AAB34819.2. Different termination.
    S78159 mRNA. Translation: AAB34820.2. Different termination.
    S50186 Genomic DNA. No translation available.
    S78496 mRNA. No translation available.
    S74092 Genomic DNA. No translation available.
    X90979 mRNA. Translation: CAA62466.1.
    X90976 mRNA. Translation: CAA62464.1.
    D89790 mRNA. Translation: BAA14022.1.
    D89788 mRNA. Translation: BAA14020.1.
    D89789 mRNA. Translation: BAA14021.1.
    AP000330 Genomic DNA. No translation available.
    AP000331 Genomic DNA. No translation available.
    AP000332 Genomic DNA. No translation available.
    AP000333 Genomic DNA. No translation available.
    AP000334 Genomic DNA. No translation available.
    AF015262 Genomic DNA. No translation available.
    CH471079 Genomic DNA. Translation: EAX09769.1.
    CH471079 Genomic DNA. Translation: EAX09770.1.
    BC136380 mRNA. Translation: AAI36381.1.
    BC136381 mRNA. Translation: AAI36382.1.
    BC144053 mRNA. Translation: AAI44054.1.
    AF025841 Genomic DNA. Translation: AAC05246.1. Different initiation.
    AF025841 Genomic DNA. Translation: AAC05247.1. Different initiation.
    AJ229043 Genomic DNA. Translation: CAA13070.1.
    CCDSiCCDS13639.1. [Q01196-8]
    CCDS42922.1. [Q01196-1]
    CCDS46646.1. [Q01196-3]
    PIRiI39443.
    S57842.
    RefSeqiNP_001001890.1. NM_001001890.2. [Q01196-1]
    NP_001116079.1. NM_001122607.1. [Q01196-3]
    NP_001745.2. NM_001754.4. [Q01196-8]
    XP_005261125.1. XM_005261068.2. [Q01196-10]
    UniGeneiHs.149261.
    Hs.612648.

    Genome annotation databases

    EnsembliENST00000300305; ENSP00000300305; ENSG00000159216. [Q01196-8]
    ENST00000344691; ENSP00000340690; ENSG00000159216. [Q01196-1]
    ENST00000358356; ENSP00000351123; ENSG00000159216. [Q01196-3]
    ENST00000416754; ENSP00000405158; ENSG00000159216.
    ENST00000437180; ENSP00000409227; ENSG00000159216. [Q01196-8]
    GeneIDi861.
    KEGGihsa:861.
    UCSCiuc002yuh.3. human. [Q01196-1]
    uc002yuk.4. human. [Q01196-8]
    uc002yuo.1. human. [Q01196-3]
    uc002yur.1. human. [Q01196-5]

    Polymorphism databases

    DMDMi215274205.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L34598 mRNA. Translation: AAA51720.1 .
    D43967 mRNA. Translation: BAA07902.1 .
    D10570 mRNA. Translation: BAA01426.1 .
    S76345 mRNA. Translation: AAB33729.1 .
    S76346 mRNA. Translation: AAB33730.1 .
    S76350 mRNA. Translation: AAB33731.1 .
    S60998 mRNA. No translation available.
    X79549 mRNA. Translation: CAA56092.1 .
    D43968 mRNA. Translation: BAA07903.1 .
    D43969 mRNA. Translation: BAA07904.1 .
    U19601 mRNA. Translation: AAB51691.1 .
    L21756 mRNA. Translation: AAA03086.1 . Different termination.
    S69002 mRNA. Translation: AAB29907.1 . Different termination.
    D13979 mRNA. Translation: BAA03089.1 .
    D14822 mRNA. Translation: BAA03559.1 . Different termination.
    D14823 mRNA. Translation: BAA03560.1 . Different termination.
    S78158 mRNA. Translation: AAB34819.2 . Different termination.
    S78159 mRNA. Translation: AAB34820.2 . Different termination.
    S50186 Genomic DNA. No translation available.
    S78496 mRNA. No translation available.
    S74092 Genomic DNA. No translation available.
    X90979 mRNA. Translation: CAA62466.1 .
    X90976 mRNA. Translation: CAA62464.1 .
    D89790 mRNA. Translation: BAA14022.1 .
    D89788 mRNA. Translation: BAA14020.1 .
    D89789 mRNA. Translation: BAA14021.1 .
    AP000330 Genomic DNA. No translation available.
    AP000331 Genomic DNA. No translation available.
    AP000332 Genomic DNA. No translation available.
    AP000333 Genomic DNA. No translation available.
    AP000334 Genomic DNA. No translation available.
    AF015262 Genomic DNA. No translation available.
    CH471079 Genomic DNA. Translation: EAX09769.1 .
    CH471079 Genomic DNA. Translation: EAX09770.1 .
    BC136380 mRNA. Translation: AAI36381.1 .
    BC136381 mRNA. Translation: AAI36382.1 .
    BC144053 mRNA. Translation: AAI44054.1 .
    AF025841 Genomic DNA. Translation: AAC05246.1 . Different initiation.
    AF025841 Genomic DNA. Translation: AAC05247.1 . Different initiation.
    AJ229043 Genomic DNA. Translation: CAA13070.1 .
    CCDSi CCDS13639.1. [Q01196-8 ]
    CCDS42922.1. [Q01196-1 ]
    CCDS46646.1. [Q01196-3 ]
    PIRi I39443.
    S57842.
    RefSeqi NP_001001890.1. NM_001001890.2. [Q01196-1 ]
    NP_001116079.1. NM_001122607.1. [Q01196-3 ]
    NP_001745.2. NM_001754.4. [Q01196-8 ]
    XP_005261125.1. XM_005261068.2. [Q01196-10 ]
    UniGenei Hs.149261.
    Hs.612648.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CMO NMR - A 52-178 [» ]
    1CO1 NMR - A 61-175 [» ]
    1E50 X-ray 2.60 A/C/E/G/Q/R 50-183 [» ]
    1H9D X-ray 2.60 A/C 50-183 [» ]
    1LJM X-ray 2.50 A/B 51-181 [» ]
    ProteinModelPortali Q01196.
    SMRi Q01196. Positions 50-212, 319-346.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107309. 69 interactions.
    DIPi DIP-36773N.
    IntActi Q01196. 16 interactions.
    MINTi MINT-153610.

    Chemistry

    BindingDBi Q01196.
    ChEMBLi CHEMBL2093862.

    PTM databases

    PhosphoSitei Q01196.

    Polymorphism databases

    DMDMi 215274205.

    Proteomic databases

    MaxQBi Q01196.
    PaxDbi Q01196.
    PRIDEi Q01196.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000300305 ; ENSP00000300305 ; ENSG00000159216 . [Q01196-8 ]
    ENST00000344691 ; ENSP00000340690 ; ENSG00000159216 . [Q01196-1 ]
    ENST00000358356 ; ENSP00000351123 ; ENSG00000159216 . [Q01196-3 ]
    ENST00000416754 ; ENSP00000405158 ; ENSG00000159216 .
    ENST00000437180 ; ENSP00000409227 ; ENSG00000159216 . [Q01196-8 ]
    GeneIDi 861.
    KEGGi hsa:861.
    UCSCi uc002yuh.3. human. [Q01196-1 ]
    uc002yuk.4. human. [Q01196-8 ]
    uc002yuo.1. human. [Q01196-3 ]
    uc002yur.1. human. [Q01196-5 ]

    Organism-specific databases

    CTDi 861.
    GeneCardsi GC21M036160.
    HGNCi HGNC:10471. RUNX1.
    HPAi HPA004176.
    MIMi 151385. gene.
    601399. phenotype.
    neXtProti NX_Q01196.
    Orphaneti 102724. Acute myeloid leukemia with t(8;21)(q22;q22) translocation.
    521. Chronic myeloid leukemia.
    71290. Familial platelet syndrome with predisposition to acute myelogenous leukemia.
    248340. Isolated delta-storage pool disease.
    99860. Precursor B-cell acute lymphoblastic leukemia.
    PharmGKBi PA34884.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG123889.
    HOVERGENi HBG060268.
    KOi K08367.
    OMAi DPRQFPT.
    PhylomeDBi Q01196.
    TreeFami TF321496.

    Enzyme and pathway databases

    SignaLinki Q01196.

    Miscellaneous databases

    ChiTaRSi RUNX1. human.
    EvolutionaryTracei Q01196.
    GeneWikii RUNX1.
    GenomeRNAii 861.
    NextBioi 3580.
    PROi Q01196.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q01196.
    Bgeei Q01196.
    Genevestigatori Q01196.

    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. Ahn M.-Y., Bae S.C., Zhang Y.W., Shigesada K., Ito Y.
      Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "t(8;21) breakpoints on chromosome 21 in acute myeloid leukemia are clustered within a limited region of a single gene, AML1."
      Miyoshi H., Shimizu K., Kozu T., Maseki N., Kaneko Y., Ohki M.
      Proc. Natl. Acad. Sci. U.S.A. 88:10431-10434(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM AML-1C).
      Tissue: Leukocyte.
    3. "AML1 fusion transcripts in t(3;21) positive leukemia: evidence of molecular heterogeneity and usage of splicing sites frequently involved in the generation of normal AML1 transcripts."
      Sacchi N., Nisson P.E., Watkins P.C., Faustinella F., Wijsman J., Hagemeijer A.
      Genes Chromosomes Cancer 11:226-236(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE PRODUCTS, CHROMOSOMAL TRANSLOCATION WITH EAP.
    4. "Involvement of the AML1 gene in the t(3;21) in therapy-related leukemia and in chronic myeloid leukemia in blast crisis."
      Nucifora G., Birn D.J., Espinosa R. III, Erickson P., Lebeau M.M., Roulston D., McKeithan T.W., Drabkin H., Rowley J.D.
      Blood 81:2728-2734(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM AML-1E), CHROMOSOMAL TRANSLOCATION WITH ETO.
    5. "AML1, AML2, and AML3, the human members of the runt domain gene-family: cDNA structure, expression, and chromosomal localization."
      Levanon D., Negreanu V., Bernstein Y., Bar-Am I., Avivi L., Groner Y.
      Genomics 23:425-432(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM AML-1A).
      Tissue: Monocyte.
    6. "Alternative splicing and genomic structure of the AML1 gene involved in acute myeloid leukemia."
      Miyoshi H., Ohira M., Shimizu K., Mitani K., Hirai H., Imai T., Yokoyama K., Soeda E., Ohki M.
      Nucleic Acids Res. 23:2762-2769(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS AML-1B; AML-1A; AML-1G AND AML-1L).
    7. "The t(8;21) fusion protein interferes with AML-1B-dependent transcriptional activation."
      Meyers S., Lenny N., Hiebert S.W.
      Mol. Cell. Biol. 15:1974-1982(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM AML-1G).
      Tissue: B-cell.
    8. "A novel transcript encoding an N-terminally truncated AML1/PEBP2 alphaB protein interferes with transactivation and blocks granulocytic differentiation of 32Dcl3 myeloid cells."
      Zhang Y.-W., Bae S.-C., Huang G., Fu Y.-X., Lu J., Ahn M.-Y., Kanno Y., Kanno T., Ito Y.
      Mol. Cell. Biol. 17:4133-4145(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM AML-1L).
    9. "The DNA sequence of human chromosome 21."
      Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A.
      , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
      Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. "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] (ISOFORM AML-1G).
    12. "Generation of the AML1-EVI-1 fusion gene in the t(3;21)(q26;q22) causes blastic crisis in chronic myelocytic leukemia."
      Mitani K., Ogawa S., Tanaka T., Miyoshi H., Kurokawa M., Mano H., Yazaki Y., Ohki M., Hirai H.
      EMBO J. 13:504-510(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-177, CHROMOSOMAL TRANSLOCATION WITH MECOM IN CHRONIC MYELOCYTIC LEUKEMIA.
    13. "Expression of the human acute myeloid leukemia gene AML1 is regulated by two promoter regions."
      Ghozi M.C., Bernstein Y., Negreanu V., Levanon D., Groner Y.
      Proc. Natl. Acad. Sci. U.S.A. 93:1935-1940(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-90 (ISOFORMS AML-1H AND AML-1I).
    14. "A large variety of alternatively spliced and differentially expressed mRNAs are encoded by the human acute myeloid leukemia gene AML1."
      Levanon D., Bernstein Y., Negreanu V., Ghozi M.C., Bar-Am I., Aloya R., Goldenberg D., Lotem J., Groner Y.
      DNA Cell Biol. 15:175-185(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 440-453, ALTERNATIVE SPLICING.
      Tissue: Monocyte.
    15. "Sequencing and analysis of 960 kb between AML1 and CBR1 on chromosome 21q22.2."
      Blechschmidt K., Rump A., Nordsiek G., Drescher B., Weber J., Rosenthal A.
      Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19, ALTERNATIVE SPLICING (ISOFORM AML-1G).
    16. Cited for: SIMILARITY TO RUNT.
    17. "Identification of AML-1 and the (8;21) translocation protein (AML-1/ETO) as sequence-specific DNA-binding proteins: the runt homology domain is required for DNA binding and protein-protein interactions."
      Meyers S., Downing J.R., Hiebert S.W.
      Mol. Cell. Biol. 13:6336-6345(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENHANCER CORE BINDING SEQUENCE.
    18. "ALY, a context-dependent coactivator of LEF-1 and AML-1, is required for TCRalpha enhancer function."
      Bruhn L., Munnerlyn A., Grosschedl R.
      Genes Dev. 11:640-653(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ALYREF/THOC4.
    19. "The partner gene of AML1 in t(16;21) myeloid malignancies is a novel member of the MTG8(ETO) family."
      Gamou T., Kitamura E., Hosoda F., Shimuzu K., Hayashi Y., Nagase T., Yokoyama Y., Ohki M.
      Blood 91:4028-4037(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL TRANSLOCATION WITH CBFA2T3.
    20. "Transcriptional repression by AML1 and LEF-1 is mediated by the TLE/Groucho corepressors."
      Levanon D., Goldstein R.E., Bernstein Y., Tang H., Goldenberg D., Stifani S., Paroush Z., Groner Y.
      Proc. Natl. Acad. Sci. U.S.A. 95:11590-11595(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TLE1.
    21. "Functional and physical interactions between AML1 proteins and an ETS protein, MEF: implications for the pathogenesis of t(8;21)-positive leukemias."
      Mao S., Frank R.C., Zhang J., Miyazaki Y., Nimer S.D.
      Mol. Cell. Biol. 19:3635-3644(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ELF1; ELF2; ELF4 AND SPI1.
    22. "Activation of AML1-mediated transcription by MOZ and inhibition by the MOZ-CBP fusion protein."
      Kitabayashi I., Aikawa Y., Nguyen L.A., Yokoyama A., Ohki M.
      EMBO J. 20:7184-7196(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KAT6A, PHOSPHORYLATION.
    23. "MOZ and MORF histone acetyltransferases interact with the Runt-domain transcription factor Runx2."
      Pelletier N., Champagne N., Stifani S., Yang X.-J.
      Oncogene 21:2729-2740(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KAT6B, FUNCTION.
    24. "SUV39H1 interacts with AML1 and abrogates AML1 transactivity. AML1 is methylated in vivo."
      Chakraborty S., Sinha K.K., Senyuk V., Nucifora G.
      Oncogene 22:5229-5237(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SUV39H1, METHYLATION.
    25. "Isoforms of the Ets transcription factor NERF/ELF-2 physically interact with AML1 and mediate opposing effects on AML1-mediated transcription of the B cell-specific blk gene."
      Cho J.-Y., Akbarali Y., Zerbini L.F., Gu X., Boltax J., Wang Y., Oettgen P., Zhang D.-E., Libermann T.A.
      J. Biol. Chem. 279:19512-19522(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ELF2.
    26. Cited for: INTERACTION WITH SUV39H1.
    27. "Cdk6 blocks myeloid differentiation by interfering with Runx1 DNA binding and Runx1-C/EBPalpha interaction."
      Fujimoto T., Anderson K., Jacobsen S.E., Nishikawa S.I., Nerlov C.
      EMBO J. 26:2361-2370(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MYELOID DIFFERENTIATION, INTERACTION WITH CDK6.
    28. "LRP16 is fused to RUNX1 in monocytic leukemia cell line with t(11;21)(q13;q22)."
      Imagama S., Abe A., Suzuki M., Hayakawa F., Katsumi A., Emi N., Kiyoi H., Naoe T.
      Eur. J. Haematol. 79:25-31(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL TRANSLOCATION WITH MACROD1.
    29. "PEBP2-beta/CBF-beta-dependent phosphorylation of RUNX1 and p300 by HIPK2: implications for leukemogenesis."
      Wee H.-J., Voon D.C.-C., Bae S.-C., Ito Y.
      Blood 112:3777-3787(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-249; THR-273 AND SER-276 BY HIPK2, VARIANT GLN-174, MUTAGENESIS OF SER-67; LYS-83; GLY-108; SER-249; THR-273 AND SER-276.
    30. "Yap1 phosphorylation by c-Abl is a critical step in selective activation of proapoptotic genes in response to DNA damage."
      Levy D., Adamovich Y., Reuven N., Shaul Y.
      Mol. Cell 29:350-361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH YAP1.
    31. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14 AND SER-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    32. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14; SER-249; SER-266; SER-268 AND SER-276, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    33. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-24 AND LYS-43, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    34. "Structural basis for the heterodimeric interaction between the acute leukaemia-associated transcription factors AML1 and CBFbeta."
      Warren A.J., Bravo J., Williams R.L., Rabbitts T.H.
      EMBO J. 19:3004-3015(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 59-173 IN COMPLEX WITH CBFB.
    35. "The leukemia-associated AML1 (Runx1) -- CBF beta complex functions as a DNA-induced molecular clamp."
      Bravo J., Li Z., Speck N.A., Warren A.J.
      Nat. Struct. Biol. 8:371-378(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 54-243 IN COMPLEX WITH CBFB AND DNA, MUTAGENESIS OF ARG-80; LYS-83; THR-84; ARG-135; ARG-139; ARG-142; LYS-167; THR-169; ASP-171; ARG-174 AND ARG-177.
    36. "DNA recognition by the RUNX1 transcription factor is mediated by an allosteric transition in the RUNT domain and by DNA bending."
      Bartfeld D., Shimon L., Couture G.C., Rabinovich D., Frolow F., Levanon D., Groner Y., Shakked Z.
      Structure 10:1395-1407(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 61-174 IN COMPLEX WITH DNA.
    37. "Immunoglobulin motif DNA recognition and heterodimerization of the PEBP2/CBF Runt domain."
      Nagata T., Gupta V., Sorce D., Kim W.-Y., Sali A., Chait B.T., Shigesada K., Ito Y., Werner M.H.
      Nat. Struct. Biol. 6:615-619(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 53-178, MUTAGENESIS OF ALA-107 AND GLY-108.
    38. "The Ig fold of the core binding factor alpha Runt domain is a member of a family of structurally and functionally related Ig-fold DNA-binding domains."
      Berardi M.J., Sun C., Zehr M., Abildgaard F., Peng J., Speck N.A., Bushweller J.H.
      Structure 7:1247-1256(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 61-175 IN COMPLEX WITH DNA.
    39. "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 46-185, CHLORIDE-BINDING.
    40. "AML1 and the 8;21 and 3;21 translocations in acute and chronic myeloid leukemia."
      Nucifora G., Rowley J.D.
      Blood 86:1-14(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON AML1 TRANSLOCATIONS.
    41. "Transcriptionally active chimeric gene derived from the fusion of the AML1 gene and a novel gene on chromosome 8 in t(8;21) leukemic cells."
      Nisson P.E., Watkins P.C., Sacchi N.
      Cancer Genet. Cytogenet. 63:81-88(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL TRANSLOCATION WITH MTG8/ETO IN AML-M2.
    42. "Junctions of the AML1/MTG8(ETO) fusion are constant in t(8;21) acute myeloid leukemia detected by reverse transcription polymerase chain reaction."
      Kozu T., Miyoshi H., Shimizu K., Maseki N., Kaneko Y., Asou H., Kamada N., Ohki M.
      Blood 82:1270-1276(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL TRANSLOCATION WITH MTG8/ETO IN AML-M2.
    43. "The t(8;21) translocation in acute myeloid leukemia results in production of an AML1-MTG8 fusion transcript."
      Miyoshi H., Kozu T., Shimizu K., Enomoto K., Maseki N., Kaneko Y., Kamada N., Ohki M.
      EMBO J. 12:2715-2721(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL TRANSLOCATION WITH MTG8/ETO IN AML-M2.
    44. "The 3;21 translocation in myelodysplasia results in a fusion transcript between the AML1 gene and the gene for EAP, a highly conserved protein associated with the Epstein-Barr virus small RNA EBER 1."
      Nucifora G., Begy C.R., Erickson P., Drabkin H.A., Rowley J.D.
      Proc. Natl. Acad. Sci. U.S.A. 90:7784-7788(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL TRANSLOCATION WITH EAP IN MYELODYSPLASIA.
      Tissue: Peripheral blood.
    45. "Alternative, out-of-frame runt/MTG8 transcripts are encoded by the derivative (8) chromosome in the t(8;21) of acute myeloid leukemia M2."
      Tighe J.E., Calabi F.
      Blood 84:2115-2121(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL TRANSLOCATION WITH MTG8/ETO IN AML-M2.
    46. "The t(12;21) of acute lymphoblastic leukemia results in a tel-AML1 gene fusion."
      Romana S.P., Mauchauffe M., le Coniat M., Chumakov I., le Paslier D., Berger R., Bernard O.A.
      Blood 85:3662-3670(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL TRANSLOCATION WITH TEL IN ACUTE LYMPHOBLASTIC LEUKEMIA (ALL).
    47. "Identification of two transcripts of AML1/ETO-fused gene in t(8;21) leukemic cells and expression of wild-type ETO gene in hematopoietic cells."
      Era T., Asou N., Kunisada T., Yamasaki H., Asou H., Kamada N., Nishikawa S., Yamaguchi K., Takatsuki K.
      Genes Chromosomes Cancer 13:25-33(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL TRANSLOCATION WITH MTG8/ETO IN AML-M2.
    48. Cited for: CHROMOSOMAL TRANSLOCATION WITH TEL IN ACUTE LYMPHOBLASTIC LEUKEMIA (ALL).
    49. Cited for: VARIANTS FPDMM GLN-139 AND GLN-174.
    50. Cited for: CHROMOSOMAL REARRANGEMENT.

    Entry informationi

    Entry nameiRUNX1_HUMAN
    AccessioniPrimary (citable) accession number: Q01196
    Secondary accession number(s): A8MV94
    , B2RMS4, D3DSG1, O60472, O60473, O76047, O76089, Q13081, Q13755, Q13756, Q13757, Q13758, Q13759, Q15341, Q15343, Q16122, Q16284, Q16285, Q16286, Q16346, Q16347, Q92479
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 184 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Caution

    The fusion of AML1 with EAP in T-MDS induces a change of reading frame in the latter resulting in 17 AA unrelated to those of EAP.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 21
      Human chromosome 21: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3