Q01196 (RUNX1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	RUNX1
Synonyms:	AML1, CBFA2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	453 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Disease	Disease mutation Proto-oncogene
Ligand	Chloride DNA-binding
PTM	Acetylation Methylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	behavioral response to pain Inferred from electronic annotation. Source: Compara central nervous system development Inferred from electronic annotation. Source: Compara definitive hemopoiesis Inferred from electronic annotation. Source: Compara embryonic hemopoiesis Inferred from electronic annotation. Source: Compara hair follicle morphogenesis Inferred from electronic annotation. Source: Compara hematopoietic stem cell proliferation Traceable author statement PubMed 21873977. Source: UniProtKB in utero embryonic development Inferred from electronic annotation. Source: Compara liver development Inferred from electronic annotation. Source: Compara myeloid cell differentiation Inferred from direct assay Ref.22. Source: UniProtKB myeloid progenitor cell differentiation Inferred from electronic annotation. Source: Compara 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: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.21Ref.25PubMed 21873977. Source: UniProtKB positive regulation of transcription, DNA-dependent Inferred from direct assay Ref.22Ref.8. Source: UniProtKB regulation of hair follicle cell proliferation Inferred from electronic annotation. Source: Compara regulation of signal transduction Inferred from electronic annotation. Source: Compara skeletal system development Inferred from electronic annotation. Source: Compara transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	basement membrane Inferred from electronic annotation. Source: Compara nucleus Inferred from direct assay PubMed 7862156. Source: UniProtKB
Molecular_function	ATP binding Non-traceable author statement. Source: UniProtKB 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...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ELF2	Q15723	2	EBI-925904,EBI-956941
gro	P16371	4	EBI-925940,EBI-153866	From a different organism.
TLE1	Q04724	4	EBI-925940,EBI-711424

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 453

453

Runt-related transcription factor 1

PRO_0000174655

Regions

Domain

50 – 178

129

Runt

Region

80 – 84

5

Interaction with DNA

Region

135 – 143

9

Interaction with DNA

Region

168 – 177

10

Interaction with DNA

Region

291 – 371

81

Interaction with KAT6A

Region

307 – 400

94

Interaction with KAT6B By similarity

Compositional bias

187 – 453

267

Pro/Ser/Thr-rich

Sites

Binding site

112

1

Chloride 1

Binding site

116

1

Chloride 1; via amide nitrogen

Binding site

139

1

Chloride 2

Binding site

170

1

Chloride 2; via amide nitrogen

Site

177 – 178

2

Breakpoint 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

Site

241 – 242

2

Breakpoint for translocation to form AML1-EAP in T-MDS and CML and to form type II MACROD1-RUNX1 fusion protein

Amino acid modifications

Modified residue

14

1

Phosphothreonine Ref.31 Ref.32

Modified residue

21

1

Phosphoserine Ref.31

Modified residue

24

1

N6-acetyllysine Ref.33

Modified residue

43

1

N6-acetyllysine Ref.33

Modified residue

249

1

Phosphoserine; by HIPK2 Ref.29 Ref.32

Modified residue

266

1

Phosphoserine Ref.32

Modified residue

268

1

Phosphoserine Ref.32

Modified residue

273

1

Phosphothreonine; by HIPK2 Ref.29

Modified residue

276

1

Phosphoserine; by HIPK2 Ref.29 Ref.32

Natural variations

Alternative sequence

1 – 105

105

Missing in isoform AML-1L.

VSP_005919

Alternative sequence

1 – 5

5

MRIPV → MASDSIFESFPSYPQCFMRE CILGMNPSRDVH in isoform AML-1G.

VSP_005917

Alternative sequence

1 – 5

5

MRIPV → MNPSRDVH in isoform AML-1H.

VSP_005916

Alternative sequence

1 – 5

5

MRIPV → MPAAPRGPAQGEAAARTRSR in isoform AML-1I.

VSP_005918

Alternative sequence

137 – 242

106

VGRSG…SQMQD → VDGPREPRRHRQKLDDQTKP GSLSFSERLSELEQLRRTAM RVSPHHPAPTPNPRASLNHS TAFNPQPQSQMQDTRQIQPS PPWSYDQSYQYLGSIASPSV HPATPI in isoform AML-1FC.

VSP_005920

Alternative sequence

178 – 224

47

RHRQK…PNPRA → SKCIHLGLVHPPGWYTLQAG ILRDHVSDSLGSTFPPGGWQ APVKPKS in isoform AML-1FA.

VSP_005923

Alternative sequence

178 – 188

11

RHRQKLDDQTK → NSLTWPRYPHI in isoform AML-1FB.

VSP_005921

Alternative sequence

189 – 453

265

Missing in isoform AML-1FB.

VSP_005922

Alternative sequence

225 – 453

229

Missing in isoform AML-1FA.

VSP_005924

Alternative sequence

242 – 250

9

DTRQIQPSP → EEDTAPWRC in isoform AML-1C.

VSP_005926

Alternative sequence

243 – 453

211

Missing in isoform AML-1FC.

VSP_005925

Alternative sequence

251 – 453

203

Missing in isoform AML-1C.

VSP_005927

Alternative sequence

258 – 453

196

Missing in isoform AML-1E.

VSP_005928

Alternative sequence

440 – 453

14

APSAR…VWRPY → GGASCSRQARRDPGPWARTP SWGRGRPTDRISL in isoform AML-1A.

VSP_005929

Natural variant

139

1

R → Q in FPDMM. Ref.49

VAR_012128

Natural variant

174

1

R → Q in FPDMM; impaired phosphorylation. Ref.29 Ref.49

VAR_012129

Natural variant

431

1

S → R.
Corresponds to variant rs1055308 [ dbSNP | Ensembl ].

VAR_013177

Natural variant

433

1

S → R.
Corresponds to variant rs1055309 [ dbSNP | Ensembl ].

VAR_013178

Experimental info

Mutagenesis

67

1

S → R: Loss of heterodimerization and reduced EP300 phosphorylation induction. Ref.29

Mutagenesis

80

1

R → A: Strongly reduces DNA-binding. Ref.35

Mutagenesis

83

1

K → A: Strongly reduces DNA-binding. Ref.29 Ref.35

Mutagenesis

83

1

K → E: Strongly reduces DNA-binding, impaired phosphorylation and reduced EP300 phosphorylation induction. Ref.29 Ref.35

Mutagenesis

84

1

T → A: No effect on DNA binding. Ref.35

Mutagenesis

107

1

A → T: Loss of heterodimerization. Ref.37

Mutagenesis

108

1

G → R: Loss of heterodimerization and impaired phosphorylation. Ref.29 Ref.37

Mutagenesis

135

1

R → A: Strongly reduces DNA-binding. Ref.35

Mutagenesis

139

1

R → A: Strongly reduces DNA-binding. Ref.35

Mutagenesis

142

1

R → A: Strongly reduces DNA-binding. Ref.35

Mutagenesis

145 – 453

309

Missing: No DNA-binding.

Mutagenesis

167

1

K → A: Reduces DNA-binding. Ref.35

Mutagenesis

169

1

T → A: Strongly reduces DNA-binding. Ref.35

Mutagenesis

171

1

D → A: Strongly reduces DNA-binding. Ref.35

Mutagenesis

174

1

R → A: Strongly reduces DNA-binding. Ref.35

Mutagenesis

177

1

R → A: Strongly reduces DNA-binding. Ref.35

Mutagenesis

249

1

S → A: Reduced phosphorylation. Ref.29

Mutagenesis

273

1

T → A: Reduced phosphorylation; when associated with A-276. Ref.29

Mutagenesis

276

1

S → A: Reduced phosphorylation; when associated with A-273. Ref.29

Sequence conflict

412

1

S → F in AAA51720. Ref.1

Secondary structure

1

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453

Helix Strand Turn

Details...

Helix

54 – 57

4

Beta strand

62 – 64

3

Beta strand

70 – 73

4

Beta strand

77 – 80

4

Beta strand

82 – 84

3

Beta strand

90 – 93

4

Beta strand

102 – 108

7

Beta strand

110 – 114

5

Beta strand

117 – 119

3

Beta strand

121 – 123

3

Beta strand

128 – 130

3

Beta strand

146 – 152

7

Beta strand

154 – 156

3

Beta strand

158 – 161

4

Beta strand

166 – 171

6

Helix

175 – 177

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform AML-1B [UniParc]. Last modified November 25, 2008. Version 3. Checksum: 4F1F193A7CADDBAB	FASTA	453	48,737
	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
	Isoform AML-1A [UniParc]. Checksum: 13349A060DC3B793	FASTA	472	50,701
	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 430 440 450 460 470 NQSDVVEAEG SHSNSPTNMG GASCSRQARR DPGPWARTPS WGRGRPTDRI SL
	Isoform AML-1C [UniParc]. Checksum: FADB4980D9FCA9D5	FASTA	250	27,427
	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 QEEDTAPWRC
	Isoform AML-1E [UniParc]. Checksum: 10A5E857CB432487	FASTA	257	28,226
	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 QDTRQIQPSP PWSYDQS
	Isoform AML-1FA [UniParc]. Checksum: 08A3748CC9F566E5	FASTA	224	24,049
	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 DGPREPRSKC 190 200 210 220 IHLGLVHPPG WYTLQAGILR DHVSDSLGST FPPGGWQAPV KPKS
	Isoform AML-1FB [UniParc]. Checksum: D2B706A902D72B2A	FASTA	188	20,395
	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 DGPREPRNSL TWPRYPHI
	Isoform AML-1FC [UniParc]. Checksum: 7DB647BA4D4BF366	FASTA	242	26,509
	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 FNDLRFVDGP REPRRHRQKL DDQTKPGSLS FSERLSELEQ LRRTAMRVSP 190 200 210 220 230 240 HHPAPTPNPR ASLNHSTAFN PQPQSQMQDT RQIQPSPPWS YDQSYQYLGS IASPSVHPAT PI
	Isoform AML-1G [UniParc]. Checksum: 69582971F63E26D7	FASTA	480	51,818
	10 20 30 40 50 60 MASDSIFESF PSYPQCFMRE CILGMNPSRD VHDASTSRRF TPPSTALSPG KMSEALPLGA 70 80 90 100 110 120 PDAGAALAGK LRSGDRSMVE VLADHPGELV RTDSPNFLCS VLPTHWRCNK TLPIAFKVVA 130 140 150 160 170 180 LGDVPDGTLV TVMAGNDENY SAELRNATAA MKNQVARFND LRFVGRSGRG KSFTLTITVF 190 200 210 220 230 240 TNPPQVATYH RAIKITVDGP REPRRHRQKL DDQTKPGSLS FSERLSELEQ LRRTAMRVSP 250 260 270 280 290 300 HHPAPTPNPR ASLNHSTAFN PQPQSQMQDT RQIQPSPPWS YDQSYQYLGS IASPSVHPAT 310 320 330 340 350 360 PISPGRASGM TTLSAELSSR LSTAPDLTAF SDPRQFPALP SISDPRMHYP GAFTYSPTPV 370 380 390 400 410 420 TSGIGIGMSA MGSATRYHTY LPPPYPGSSQ AQGGPFQASS PSYHLYYGAS AGSYQFSMVG 430 440 450 460 470 480 GERSPPRILP PCTNASTGSA LLNPSLPNQS DVVEAEGSHS NSPTNMAPSA RLEEAVWRPY
	Isoform AML-1H [UniParc]. Checksum: 9DE001CA7E9BA81B	FASTA	456	49,077
	10 20 30 40 50 60 MNPSRDVHDA STSRRFTPPS TALSPGKMSE ALPLGAPDAG AALAGKLRSG DRSMVEVLAD 70 80 90 100 110 120 HPGELVRTDS PNFLCSVLPT HWRCNKTLPI AFKVVALGDV PDGTLVTVMA GNDENYSAEL 130 140 150 160 170 180 RNATAAMKNQ VARFNDLRFV GRSGRGKSFT LTITVFTNPP QVATYHRAIK ITVDGPREPR 190 200 210 220 230 240 RHRQKLDDQT KPGSLSFSER LSELEQLRRT AMRVSPHHPA PTPNPRASLN HSTAFNPQPQ 250 260 270 280 290 300 SQMQDTRQIQ PSPPWSYDQS YQYLGSIASP SVHPATPISP GRASGMTTLS AELSSRLSTA 310 320 330 340 350 360 PDLTAFSDPR QFPALPSISD PRMHYPGAFT YSPTPVTSGI GIGMSAMGSA TRYHTYLPPP 370 380 390 400 410 420 YPGSSQAQGG PFQASSPSYH LYYGASAGSY QFSMVGGERS PPRILPPCTN ASTGSALLNP 430 440 450 SLPNQSDVVE AEGSHSNSPT NMAPSARLEE AVWRPY
	Isoform AML-1I [UniParc]. Checksum: 07A186F5A0EEB6E4	FASTA	468	50,173
	10 20 30 40 50 60 MPAAPRGPAQ GEAAARTRSR DASTSRRFTP PSTALSPGKM SEALPLGAPD AGAALAGKLR 70 80 90 100 110 120 SGDRSMVEVL ADHPGELVRT DSPNFLCSVL PTHWRCNKTL PIAFKVVALG DVPDGTLVTV 130 140 150 160 170 180 MAGNDENYSA ELRNATAAMK NQVARFNDLR FVGRSGRGKS FTLTITVFTN PPQVATYHRA 190 200 210 220 230 240 IKITVDGPRE PRRHRQKLDD QTKPGSLSFS ERLSELEQLR RTAMRVSPHH PAPTPNPRAS 250 260 270 280 290 300 LNHSTAFNPQ PQSQMQDTRQ IQPSPPWSYD QSYQYLGSIA SPSVHPATPI SPGRASGMTT 310 320 330 340 350 360 LSAELSSRLS TAPDLTAFSD PRQFPALPSI SDPRMHYPGA FTYSPTPVTS GIGIGMSAMG 370 380 390 400 410 420 SATRYHTYLP PPYPGSSQAQ GGPFQASSPS YHLYYGASAG SYQFSMVGGE RSPPRILPPC 430 440 450 460 TNASTGSALL NPSLPNQSDV VEAEGSHSNS PTNMAPSARL EEAVWRPY
	Isoform AML-1L (AML1-delta N) [UniParc]. Checksum: D1E344B2E6586EC8	FASTA	348	37,733
	10 20 30 40 50 60 MAGNDENYSA ELRNATAAMK NQVARFNDLR FVGRSGRGKS FTLTITVFTN PPQVATYHRA 70 80 90 100 110 120 IKITVDGPRE PRRHRQKLDD QTKPGSLSFS ERLSELEQLR RTAMRVSPHH PAPTPNPRAS 130 140 150 160 170 180 LNHSTAFNPQ PQSQMQDTRQ IQPSPPWSYD QSYQYLGSIA SPSVHPATPI SPGRASGMTT 190 200 210 220 230 240 LSAELSSRLS TAPDLTAFSD PRQFPALPSI SDPRMHYPGA FTYSPTPVTS GIGIGMSAMG 250 260 270 280 290 300 SATRYHTYLP PPYPGSSQAQ GGPFQASSPS YHLYYGASAG SYQFSMVGGE RSPPRILPPC 310 320 330 340 TNASTGSALL NPSLPNQSDV VEAEGSHSNS PTNMAPSARL EEAVWRPY

References

	« Hide 'large scale' referencesShow '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 FORMS, 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]	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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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. , 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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

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.

IPI

IPI00218529.
IPI00218530.
IPI00218936.
IPI00218942.
IPI00218943.
IPI00477787.
IPI00797455.
IPI00936936.
IPI00939238.
IPI00952824.
IPI01018795.

PIR

I39443.
S57842.

RefSeq

NP_001001890.1. NM_001001890.2.
NP_001116079.1. NM_001122607.1.
NP_001745.2. NM_001754.4.

UniGene

Hs.149261.
Hs.612648.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q01196.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-36773N.

IntAct

Q01196. 8 interactions.

MINT

MINT-153610.

PTM databases

PhosphoSite

Q01196.

Polymorphism databases

DMDM

215274205.

Proteomic databases

PaxDb

Q01196.

PRIDE

Q01196.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000300305; ENSP00000300305; ENSG00000159216.
ENST00000325074; ENSP00000319459; ENSG00000159216.
ENST00000344691; ENSP00000340690; ENSG00000159216.
ENST00000358356; ENSP00000351123; ENSG00000159216.
ENST00000416754; ENSP00000405158; ENSG00000159216.
ENST00000437180; ENSP00000409227; ENSG00000159216.

GeneID

861.

KEGG

hsa:861.

UCSC

uc002yuh.3. human.
uc002yuk.4. human.
uc002yuo.1. human.
uc002yur.1. human.

Organism-specific databases

CTD

861.

GeneCards

GC21M036160.

HGNC

HGNC:10471. RUNX1.

HPA

HPA004176.

MIM

151385. gene.
601399. phenotype.

neXtProt

NX_Q01196.

Orphanet

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.
99860. Precursor B-cell acute lymphoblastic leukemia.

PharmGKB

PA34884.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG123889.

HOVERGEN

HBG060268.

KO

K08367.

OMA

FPTLPSI.

OrthoDB

EOG47M1XZ.

Enzyme and pathway databases

Pathway_Interaction_DB

smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.

SignaLink

Q01196.

Gene expression databases

ArrayExpress

Q01196.

Bgee

Q01196.

Genevestigator

Q01196.

GermOnline

ENSG00000159216. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.720. 1 hit.
4.10.770.10. 1 hit.

InterPro

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]

PANTHER

PTHR11950. PTHR11950. 1 hit.

Pfam

PF00853. Runt. 1 hit.
PF08504. RunxI. 1 hit.
[Graphical view]

PIRSF

PIRSF009374. TF_Runt-rel_RUNX. 1 hit.

PRINTS

PR00967. ONCOGENEAML1.

SUPFAM

SSF49417. P53_like_DNA_bnd. 1 hit.

PROSITE

PS51062. RUNT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q01196.

ChEMBL

CHEMBL1615385.

ChiTaRS

RUNX1. human.

EvolutionaryTrace

Q01196.

GenomeRNAi

861.

NextBio

3580.

SOURCE

Search...

Entry information

Entry name

RUNX1_HUMAN

Accession

Primary (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 history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	November 25, 2008
Last modified:	May 29, 2013
This is version 170 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.