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Q01196 (RUNX1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 180. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:RUNX1
Synonyms:AML1, CBFA2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length453 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.21 Ref.23 Ref.25 Ref.27

Subunit structure

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. Ref.18 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.30

Subcellular location

Nucleus.

Tissue specificity

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

Domain

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

Post-translational modification

Phosphorylated in its C-terminus upon IL-6 treatment. Phosphorylation enhances interaction with KAT6A. Ref.22 Ref.29

Methylated. Ref.24

Phosphorylated in Ser-249 Thr-273 and Ser-276 by HIPK2 when associated with CBFB and DNA. This phosphorylation promotes subsequent EP300 phosphorylation. Ref.22 Ref.29

Involvement in disease

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. Ref.41 Ref.42 Ref.43 Ref.45 Ref.47

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.49

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 inv21(q21;q22) with USP16.

Sequence similarities

Contains 1 Runt domain.

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.

Sequence caution

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.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DiseaseDisease mutation
Proto-oncogene
   LigandChloride
DNA-binding
   PTMAcetylation
Methylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbehavioral response to pain

Inferred from electronic annotation. Source: Ensembl

central nervous system development

Inferred from electronic annotation. Source: Ensembl

definitive hemopoiesis

Inferred from electronic annotation. Source: Ensembl

embryonic hemopoiesis

Inferred from electronic annotation. Source: Ensembl

hair follicle morphogenesis

Inferred from electronic annotation. Source: Ensembl

hematopoietic stem cell proliferation

Traceable author statement PubMed 21873977. Source: UniProtKB

hemopoiesis

Inferred from direct assay PubMed 21873977. Source: UniProtKB

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

liver development

Inferred from electronic annotation. Source: Ensembl

myeloid cell differentiation

Inferred from direct assay Ref.22. Source: UniProtKB

myeloid progenitor cell differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of granulocyte differentiation

Inferred from mutant phenotype Ref.8. Source: UniProtKB

peripheral nervous system neuron development

Traceable author statement PubMed 20096094. Source: BHF-UCL

positive regulation of angiogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of granulocyte differentiation

Inferred from mutant phenotype Ref.8. Source: UniProtKB

positive regulation of progesterone secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.21Ref.25PubMed 21873977. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.21Ref.25Ref.22Ref.8. Source: UniProtKB

regulation of hair follicle cell proliferation

Inferred from electronic annotation. Source: Ensembl

regulation of signal transduction

Inferred from electronic annotation. Source: Ensembl

skeletal system development

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentbasement membrane

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 7862156. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: InterPro

DNA binding

Inferred from direct assay Ref.39Ref.8Ref.17. Source: UniProtKB

calcium ion binding

Inferred from direct assay Ref.39. Source: UniProtKB

protein heterodimerization activity

Inferred from direct assay Ref.17. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay Ref.34. Source: UniProtKB

regulatory region DNA binding

Inferred from direct assay PubMed 21873977. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from direct assay Ref.8Ref.25. Source: UniProtKB

transcription factor binding

Inferred from direct assay Ref.8. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 11 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform AML-1B (identifier: Q01196-1)

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.
Isoform AML-1A (identifier: Q01196-2)

The sequence of this isoform differs from the canonical sequence as follows:
     440-453: APSARLEEAVWRPY → GGASCSRQARRDPGPWARTPSWGRGRPTDRISL
Isoform AML-1C (identifier: Q01196-3)

The sequence of this isoform differs from the canonical sequence as follows:
     242-250: DTRQIQPSP → EEDTAPWRC
     251-453: Missing.
Isoform AML-1E (identifier: Q01196-4)

The sequence of this isoform differs from the canonical sequence as follows:
     258-453: Missing.
Isoform AML-1FA (identifier: Q01196-5)

The sequence of this isoform differs from the canonical sequence as follows:
     178-224: RHRQKLDDQT...HPAPTPNPRA → SKCIHLGLVH...GWQAPVKPKS
     225-453: Missing.
Isoform AML-1FB (identifier: Q01196-6)

The sequence of this isoform differs from the canonical sequence as follows:
     178-188: RHRQKLDDQTK → NSLTWPRYPHI
     189-453: Missing.
Isoform AML-1FC (identifier: Q01196-7)

The sequence of this isoform differs from the canonical sequence as follows:
     137-242: VGRSGRGKSF...NPQPQSQMQD → VDGPREPRRH...SPSVHPATPI
     243-453: Missing.
Isoform AML-1G (identifier: Q01196-8)

The sequence of this isoform differs from the canonical sequence as follows:
     1-5: MRIPV → MASDSIFESFPSYPQCFMRECILGMNPSRDVH
Isoform AML-1H (identifier: Q01196-9)

The sequence of this isoform differs from the canonical sequence as follows:
     1-5: MRIPV → MNPSRDVH
Isoform AML-1I (identifier: Q01196-10)

The sequence of this isoform differs from the canonical sequence as follows:
     1-5: MRIPV → MPAAPRGPAQGEAAARTRSR
Isoform AML-1L (identifier: Q01196-11)

Also known as: AML1-delta N;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 453453Runt-related transcription factor 1
PRO_0000174655

Regions

Domain50 – 178129Runt
Region80 – 845Interaction with DNA
Region135 – 1439Interaction with DNA
Region168 – 17710Interaction with DNA
Region291 – 37181Interaction with KAT6A
Region307 – 40094Interaction with KAT6B By similarity
Compositional bias187 – 453267Pro/Ser/Thr-rich

Sites

Binding site1121Chloride 1
Binding site1161Chloride 1; via amide nitrogen
Binding site1391Chloride 2
Binding site1701Chloride 2; via amide nitrogen
Site177 – 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
Site241 – 2422Breakpoint for translocation to form AML1-EAP in T-MDS and CML and to form type II MACROD1-RUNX1 fusion protein

Amino acid modifications

Modified residue141Phosphothreonine Ref.31 Ref.32
Modified residue211Phosphoserine Ref.31
Modified residue241N6-acetyllysine Ref.33
Modified residue431N6-acetyllysine Ref.33
Modified residue2491Phosphoserine; by HIPK2 Ref.29 Ref.32
Modified residue2661Phosphoserine Ref.32
Modified residue2681Phosphoserine Ref.32
Modified residue2731Phosphothreonine; by HIPK2 Ref.29
Modified residue2761Phosphoserine; by HIPK2 Ref.29 Ref.32

Natural variations

Alternative sequence1 – 105105Missing in isoform AML-1L.
VSP_005919
Alternative sequence1 – 55MRIPV → MASDSIFESFPSYPQCFMRE CILGMNPSRDVH in isoform AML-1G.
VSP_005917
Alternative sequence1 – 55MRIPV → MNPSRDVH in isoform AML-1H.
VSP_005916
Alternative sequence1 – 55MRIPV → MPAAPRGPAQGEAAARTRSR in isoform AML-1I.
VSP_005918
Alternative sequence137 – 242106VGRSG…SQMQD → VDGPREPRRHRQKLDDQTKP GSLSFSERLSELEQLRRTAM RVSPHHPAPTPNPRASLNHS TAFNPQPQSQMQDTRQIQPS PPWSYDQSYQYLGSIASPSV HPATPI in isoform AML-1FC.
VSP_005920
Alternative sequence178 – 22447RHRQK…PNPRA → SKCIHLGLVHPPGWYTLQAG ILRDHVSDSLGSTFPPGGWQ APVKPKS in isoform AML-1FA.
VSP_005923
Alternative sequence178 – 18811RHRQKLDDQTK → NSLTWPRYPHI in isoform AML-1FB.
VSP_005921
Alternative sequence189 – 453265Missing in isoform AML-1FB.
VSP_005922
Alternative sequence225 – 453229Missing in isoform AML-1FA.
VSP_005924
Alternative sequence242 – 2509DTRQIQPSP → EEDTAPWRC in isoform AML-1C.
VSP_005926
Alternative sequence243 – 453211Missing in isoform AML-1FC.
VSP_005925
Alternative sequence251 – 453203Missing in isoform AML-1C.
VSP_005927
Alternative sequence258 – 453196Missing in isoform AML-1E.
VSP_005928
Alternative sequence440 – 45314APSAR…VWRPY → GGASCSRQARRDPGPWARTP SWGRGRPTDRISL in isoform AML-1A.
VSP_005929
Natural variant1391R → Q in FPDMM. Ref.49
VAR_012128
Natural variant1741R → Q in FPDMM; impaired phosphorylation. Ref.29 Ref.49
VAR_012129
Natural variant4311S → R.
Corresponds to variant rs1055308 [ dbSNP | Ensembl ].
VAR_013177
Natural variant4331S → R.
Corresponds to variant rs1055309 [ dbSNP | Ensembl ].
VAR_013178

Experimental info

Mutagenesis671S → R: Loss of heterodimerization and reduced EP300 phosphorylation induction. Ref.29
Mutagenesis801R → A: Strongly reduces DNA-binding. Ref.35
Mutagenesis831K → A: Strongly reduces DNA-binding. Ref.29 Ref.35
Mutagenesis831K → E: Strongly reduces DNA-binding, impaired phosphorylation and reduced EP300 phosphorylation induction. Ref.29 Ref.35
Mutagenesis841T → A: No effect on DNA binding. Ref.35
Mutagenesis1071A → T: Loss of heterodimerization. Ref.37
Mutagenesis1081G → R: Loss of heterodimerization and impaired phosphorylation. Ref.29 Ref.37
Mutagenesis1351R → A: Strongly reduces DNA-binding. Ref.35
Mutagenesis1391R → A: Strongly reduces DNA-binding. Ref.35
Mutagenesis1421R → A: Strongly reduces DNA-binding. Ref.35
Mutagenesis145 – 453309Missing: No DNA-binding.
Mutagenesis1671K → A: Reduces DNA-binding. Ref.35
Mutagenesis1691T → A: Strongly reduces DNA-binding. Ref.35
Mutagenesis1711D → A: Strongly reduces DNA-binding. Ref.35
Mutagenesis1741R → A: Strongly reduces DNA-binding. Ref.35
Mutagenesis1771R → A: Strongly reduces DNA-binding. Ref.35
Mutagenesis2491S → A: Reduced phosphorylation. Ref.29
Mutagenesis2731T → A: Reduced phosphorylation; when associated with A-276. Ref.29
Mutagenesis2761S → A: Reduced phosphorylation; when associated with A-273. Ref.29
Sequence conflict4121S → F in AAA51720. Ref.1

Secondary structure

................................. 453
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform AML-1B [UniParc].

Last modified November 25, 2008. Version 3.
Checksum: 4F1F193A7CADDBAB

FASTA45348,737
        10         20         30         40         50         60 
MRIPVDASTS RRFTPPSTAL SPGKMSEALP LGAPDAGAAL AGKLRSGDRS MVEVLADHPG 

        70         80         90        100        110        120 
ELVRTDSPNF LCSVLPTHWR CNKTLPIAFK VVALGDVPDG TLVTVMAGND ENYSAELRNA 

       130        140        150        160        170        180 
TAAMKNQVAR FNDLRFVGRS GRGKSFTLTI TVFTNPPQVA TYHRAIKITV DGPREPRRHR 

       190        200        210        220        230        240 
QKLDDQTKPG SLSFSERLSE LEQLRRTAMR VSPHHPAPTP NPRASLNHST AFNPQPQSQM 

       250        260        270        280        290        300 
QDTRQIQPSP PWSYDQSYQY LGSIASPSVH PATPISPGRA SGMTTLSAEL SSRLSTAPDL 

       310        320        330        340        350        360 
TAFSDPRQFP ALPSISDPRM HYPGAFTYSP TPVTSGIGIG MSAMGSATRY HTYLPPPYPG 

       370        380        390        400        410        420 
SSQAQGGPFQ ASSPSYHLYY GASAGSYQFS MVGGERSPPR ILPPCTNAST GSALLNPSLP 

       430        440        450 
NQSDVVEAEG SHSNSPTNMA PSARLEEAVW RPY 

« Hide

Isoform AML-1A [UniParc].

Checksum: 13349A060DC3B793
Show »

FASTA47250,701
Isoform AML-1C [UniParc].

Checksum: FADB4980D9FCA9D5
Show »

FASTA25027,427
Isoform AML-1E [UniParc].

Checksum: 10A5E857CB432487
Show »

FASTA25728,226
Isoform AML-1FA [UniParc].

Checksum: 08A3748CC9F566E5
Show »

FASTA22424,049
Isoform AML-1FB [UniParc].

Checksum: D2B706A902D72B2A
Show »

FASTA18820,395
Isoform AML-1FC [UniParc].

Checksum: 7DB647BA4D4BF366
Show »

FASTA24226,509
Isoform AML-1G [UniParc].

Checksum: 69582971F63E26D7
Show »

FASTA48051,818
Isoform AML-1H [UniParc].

Checksum: 9DE001CA7E9BA81B
Show »

FASTA45649,077
Isoform AML-1I [UniParc].

Checksum: 07A186F5A0EEB6E4
Show »

FASTA46850,173
Isoform AML-1L (AML1-delta N) [UniParc].

Checksum: D1E344B2E6586EC8
Show »

FASTA34837,733

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Leukaemia/Drosophila homology."
Daga A., Tighe J.E., Calabi F.
Nature 356:484-484(1992) [PubMed] [Europe PMC] [Abstract]
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]"RUNX1 associates with histone deacetylases and SUV39H1 to repress transcription."
Reed-Inderbitzin E., Moreno-Miralles I., Vanden-Eynden S.K., Xie J., Lutterbach B., Durst-Goodwin K.L., Luce K.S., Irvin B.J., Cleary M.L., Brandt S.J., Hiebert S.W.
Oncogene 25:5777-5786(2006) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Fusion of the TEL gene on 12p13 to the AML1 gene on 21q22 in acute lymphoblastic leukemia."
Golub T.R., Barker G.F., Bohlander S.K., Hiebert S.W., Ward D.C., Bray-Ward P., Morgan E., Raimondi S.C., Rowley J.D., Gilliland D.G.
Proc. Natl. Acad. Sci. U.S.A. 92:4917-4921(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH TEL IN ACUTE LYMPHOBLASTIC LEUKEMIA (ALL).
[49]"Haploinsufficiency of CBFA2 causes familial thrombocytopenia with propensity to develop acute myelogenous leukaemia."
Song W.-J., Sullivan M.G., Legare R.D., Hutchings S., Tan X., Kufrin D., Ratajczak J., Resende I.C., Haworth C., Hock R., Loh M., Felix C., Roy D.-C., Busque L., Kurnit D., Willman C., Gewirtz A.M., Speck N.A. expand/collapse author list , Bushweller J.H., Li F.P., Gardiner K., Poncz M., Maris J.M., Gilliland D.G.
Nat. Genet. 23:166-175(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FPDMM GLN-139 AND GLN-174.
[50]"Genome profiling of chronic myelomonocytic leukemia: frequent alterations of RAS and RUNX1 genes."
Gelsi-Boyer V., Trouplin V., Adelaide J., Aceto N., Remy V., Pinson S., Houdayer C., Arnoulet C., Sainty D., Bentires-Alj M., Olschwang S., Vey N., Mozziconacci M.-J., Birnbaum D., Chaffanet M.
BMC Cancer 8:299-299(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL REARRANGEMENT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRI39443.
S57842.
RefSeqNP_001001890.1. NM_001001890.2.
NP_001116079.1. NM_001122607.1.
NP_001745.2. NM_001754.4.
XP_005261125.1. XM_005261068.2.
UniGeneHs.149261.
Hs.612648.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ01196.
SMRQ01196. Positions 60-173, 319-346.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107309. 69 interactions.
DIPDIP-36773N.
IntActQ01196. 16 interactions.
MINTMINT-153610.

Chemistry

BindingDBQ01196.
ChEMBLCHEMBL2093862.

PTM databases

PhosphoSiteQ01196.

Polymorphism databases

DMDM215274205.

Proteomic databases

PaxDbQ01196.
PRIDEQ01196.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000300305; ENSP00000300305; ENSG00000159216. [Q01196-8]
ENST00000325074; ENSP00000319459; ENSG00000159216. [Q01196-10]
ENST00000344691; ENSP00000340690; ENSG00000159216. [Q01196-1]
ENST00000358356; ENSP00000351123; ENSG00000159216. [Q01196-3]
ENST00000416754; ENSP00000405158; ENSG00000159216.
ENST00000437180; ENSP00000409227; ENSG00000159216. [Q01196-8]
GeneID861.
KEGGhsa:861.
UCSCuc002yuh.3. human. [Q01196-1]
uc002yuk.4. human. [Q01196-8]
uc002yuo.1. human. [Q01196-3]
uc002yur.1. human. [Q01196-5]

Organism-specific databases

CTD861.
GeneCardsGC21M036160.
HGNCHGNC:10471. RUNX1.
HPAHPA004176.
MIM151385. gene.
601399. phenotype.
neXtProtNX_Q01196.
Orphanet102724. Acute myeloid leukemia with t(8;21)(q22;q22) translocation.
521. Chronic myeloid leukemia.
71290. Familial platelet syndrome with predisposition to acute myelogenous leukemia.
99860. Precursor B-cell acute lymphoblastic leukemia.
PharmGKBPA34884.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG123889.
HOVERGENHBG060268.
KOK08367.
OMAQSSPSWS.
PhylomeDBQ01196.
TreeFamTF321496.

Enzyme and pathway databases

SignaLinkQ01196.

Gene expression databases

ArrayExpressQ01196.
BgeeQ01196.
GenevestigatorQ01196.

Family and domain databases

Gene3D2.60.40.720. 1 hit.
4.10.770.10. 1 hit.
InterProIPR000040. 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]
PANTHERPTHR11950. PTHR11950. 1 hit.
PfamPF00853. Runt. 1 hit.
PF08504. RunxI. 1 hit.
[Graphical view]
PIRSFPIRSF009374. TF_Runt-rel_RUNX. 1 hit.
PRINTSPR00967. ONCOGENEAML1.
SUPFAMSSF49417. SSF49417. 1 hit.
PROSITEPS51062. RUNT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRUNX1. human.
EvolutionaryTraceQ01196.
GeneWikiRUNX1.
GenomeRNAi861.
NextBio3580.
PROQ01196.
SOURCESearch...

Entry information

Entry nameRUNX1_HUMAN
AccessionPrimary (citable) accession number: Q01196
Secondary accession number(s): A8MV94 expand/collapse secondary AC list , B2RMS4, D3DSG1, O60472, O60473, O76047, O76089, Q13081, Q13755, Q13756, Q13757, Q13758, Q13759, Q15341, Q15343, Q16122, Q16284, Q16285, Q16286, Q16346, Q16347, Q92479
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: November 25, 2008
Last modified: April 16, 2014
This is version 180 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 21

Human chromosome 21: entries, gene names and cross-references to MIM