Q03347 (RUNX1_MOUSE) 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, Pebp2ab

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	451 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. Essential for the development of normal hematopoiesis. Isoform 4 shows higher binding activities for target genes and binds TCR-beta-E2 and RAG-1 target site with threefold higher affinity than other isoforms. It is less effective in the context of neutrophil terminal differentiation. Acts synergistically with ELF4 to transactivate the IL-3 promoter and with ELF2 to transactivate the BLK promoter. Inhibits KAT6B-dependent transcriptional activation By similarity. Ref.7 Ref.9
Subunit structure	Heterodimer with CBFB. RUNX1 binds DNA as a monomer and through the Runt domain. DNA-binding is increased by heterodimerization. Interacts with TLE1 and ALYREF/THOC4. Interacts with HIPK2, ELF1, ELF2 and SPI1. Interacts via its Runt domain with the ELF4 N-terminal region. Interaction with ELF2 isoform 2 (NERF-1a) may act to repress RUNX1-mediated transactivation. Interacts with KAT6A and KAT6B. Interacts with SUV39H1, leading to abrogation of transactivating and DNA-binding properties of RUNX1 By similarity. Interacts with YAP1. Interaction with CDK6 prevents myeloid differentiation, reducing its transcription transactivation activity By similarity. Found in a complex with PRMT5, RUNX1 and CBFB. Ref.8 Ref.10
Subcellular location	Nucleus.
Tissue specificity	Isoform 4 is expressed at high levels in thymus, spleen and T-cell lines and at lower levels in myeloid cell lines and nonhematopoietic cells. Isoform 5 is expressed ubiquitously in lumbar vertebrae, brain, kidney, heart, muscle, ovary and osteoblast-like cell line MC3T3-E1.
Developmental stage	Differentially expressed during hematopoietic differentiation. Isoform AML1-B is readily detectable in undifferentiated embryonic stem (es) cells and peak expression is seen on day 6 of differentiation, followed by a gradual decline thereafter. Isoform AML1-C is undetectable in undifferentiated es cells, but is gradually up-regulated along with differentiation and reaches its highest levels on day 8 and this expression is maintained through day 12. Isoform 5 is expressed at high levels at 6-8 dpc and then levels decrease on 12 dpc. Isoform 4 expression is high throughout T-cell development, declines with natural killer cell maturation, and appears to be transiently reduced and then restored during B-cell development.
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 By similarity. Ref.10 Methylated By similarity. Phosphorylated in Ser-249 Thr-273 and Ser-276 by HIPK2 when associated with CBFB and DNA. This phosphorylation promotes subsequent EP300 phosphorylation. Ref.10
Involvement in disease	Mice with an Runx1 lacking the DNA-binding region are found to die between embryonic days 11.5 to 12.5 due to hemorrhaging in the central nervous system. This hemorrhaging is preceded by necrosis and hematopoiesis is blocked.
Sequence similarities	Contains 1 Runt domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Ligand	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 mutant phenotype PubMed 16446141. Source: MGI central nervous system development Inferred from mutant phenotype PubMed 16174759. Source: MGI definitive hemopoiesis Inferred from mutant phenotype PubMed 10207104. Source: MGI embryonic hemopoiesis Inferred from mutant phenotype PubMed 16174759. Source: MGI hair follicle morphogenesis Inferred from mutant phenotype PubMed 17011173. Source: MGI in utero embryonic development Inferred from mutant phenotype PubMed 16174759. Source: MGI liver development Inferred from mutant phenotype PubMed 16174759. Source: MGI myeloid progenitor cell differentiation Inferred from mutant phenotype PubMed 19182774. Source: MGI neuron development Inferred from mutant phenotype PubMed 16446141. Source: MGI positive regulation of angiogenesis Inferred from mutant phenotype PubMed 10943840. Source: UniProtKB positive regulation of granulocyte differentiation Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: UniProtKB regulation of hair follicle cell proliferation Inferred from mutant phenotype PubMed 21464233. Source: MGI regulation of signal transduction Inferred from mutant phenotype PubMed 21464233. Source: MGI response to retinoic acid Inferred from direct assay PubMed 18439490. Source: BHF-UCL skeletal system development Inferred from mutant phenotype PubMed 15389629. Source: MGI transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	basement membrane Inferred from direct assay PubMed 17011173. Source: MGI nucleus Inferred from direct assay PubMed 21464233. Source: MGI
Molecular_function	ATP binding Inferred from electronic annotation. Source: InterPro DNA binding Inferred from direct assay PubMed 7774816. Source: UniProtKB sequence-specific DNA binding transcription factor activity Inferred from direct assay PubMed 12807883. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Tbx21	Q9JKD8	3	EBI-3863873,EBI-3863870

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q03347-1)

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

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

Isoform 2 (identifier: Q03347-2)

Also known as: PEB2-alpha B2;

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

Isoform 3 (identifier: Q03347-3)

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

Isoform 4 (identifier: Q03347-4)

Also known as: AML1-C;

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

Isoform 5 (identifier: Q03347-5)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 451

451

Runt-related transcription factor 1

PRO_0000174656

Regions

Domain

50 – 178

129

Runt

Region

80 – 84

5

Interaction with DNA By similarity

Region

135 – 143

9

Interaction with DNA By similarity

Region

168 – 177

10

Interaction with DNA By similarity

Region

291 – 370

80

Interaction with KAT6A By similarity

Region

307 – 399

93

Interaction with KAT6B By similarity

Compositional bias

187 – 451

265

Pro/Ser/Thr-rich

Sites

Binding site

112

1

Chloride 1 By similarity

Binding site

116

1

Chloride 1; via amide nitrogen By similarity

Binding site

139

1

Chloride 2 By similarity

Binding site

170

1

Chloride 2; via amide nitrogen By similarity

Amino acid modifications

Modified residue

14

1

Phosphothreonine By similarity

Modified residue

21

1

Phosphoserine By similarity

Modified residue

24

1

N6-acetyllysine By similarity

Modified residue

43

1

N6-acetyllysine By similarity

Modified residue

249

1

Phosphoserine; by HIPK2 Ref.10

Modified residue

266

1

Phosphoserine By similarity

Modified residue

268

1

Phosphoserine By similarity

Modified residue

273

1

Phosphothreonine; by HIPK2 By similarity

Modified residue

276

1

Phosphoserine; by HIPK2 Ref.10

Natural variations

Alternative sequence

1 – 5

5

MRIPV → MASDSIFESFPSYPQCFMR in isoform 4.

VSP_005930

Alternative sequence

92 – 182

91

VALGD…RHRQK → LLPEEGGGRSRWRSADGQSE PRGQRLRRLLKGAACSRSLW SFSLSLGWGGDAALPWRPSG GSASEVSKREFF in isoform 3.

VSP_005931

Alternative sequence

178

1

R → N in isoform 2.

VSP_005932

Alternative sequence

179 – 242

64

Missing in isoform 2.

VSP_005933

Alternative sequence

183 – 451

269

Missing in isoform 3.

VSP_005934

Alternative sequence

242 – 303

62

DARQI…DLTAF → KNPTEPTTLCLCWSPRRRKH RGCQAFLGALRELLKPRSIS WEPNEENAVPSAEYLYSEKC GC in isoform 5.

VSP_005935

Alternative sequence

304 – 451

148

Missing in isoform 5.

VSP_005936

Experimental info

Mutagenesis

80

1

R → A: Interferes with DNA-binding. Ref.12

Mutagenesis

109

1

N → A: Interferes with heterodimerization. Ref.12

Mutagenesis

113

1

Y → A: Interferes with heterodimerization. Ref.12

Mutagenesis

142

1

R → A: Interferes with DNA-binding. Ref.12

Mutagenesis

144

1

K → M: Interferes with DNA-binding. Ref.12

Mutagenesis

149

1

T → A: Interferes with heterodimerization. Ref.12

Mutagenesis

170

1

V → A: No effect. Ref.12

Mutagenesis

171

1

D → A: Interferes with DNA-binding. Ref.12

Mutagenesis

174

1

R → A: Interferes with DNA-binding. Ref.12

Mutagenesis

177

1

R → A: Interferes with DNA-binding. Ref.12

Mutagenesis

249

1

S → A: Reduced phosphorylation. Ref.10

Mutagenesis

276

1

S → A: Reduced phosphorylation. Ref.10

Sequence conflict

37 – 38

2

GP → A in CAA65976. Ref.3

Secondary structure

1

.

.

.

.

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.

.

.

.

.

.

.

.

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.

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.

.

.

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.

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.

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.

.

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.

.

451

Helix Strand Turn

Details...

Helix

51 – 57

7

Turn

59 – 61

3

Beta strand

63 – 67

5

Beta strand

70 – 72

3

Beta strand

77 – 80

4

Beta strand

90 – 95

6

Beta strand

102 – 109

8

Beta strand

112 – 115

4

Beta strand

117 – 119

3

Beta strand

121 – 125

5

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

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (AML1-B) (PEB2-alpha B1) [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 06B9E9BA01A6469C	FASTA	451	48,610
	10 20 30 40 50 60 MRIPVDASTS RRFTPPSTAL SPGKMSEALP LGAPDGGPAL ASKLRSGDRS 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 QDARQIQPSP PWSYDQSYQY LGSITSSSVH PATPISPGRA SGMTSLSAEL SSRLSTAPDL 310 320 330 340 350 360 TAFGDPRQFP TLPSISDPRM HYPGAFTYSP PVTSGIGIGM SAMSSASRYH TYLPPPYPGS 370 380 390 400 410 420 SQAQAGPFQT GSPSYHLYYG ASAGSYQFSM VGGERSPPRI LPPCTNASTG AALLNPSLPS 430 440 450 QSDVVETEGS HSNSPTNMPP ARLEEAVWRP Y
	Isoform 2 (PEB2-alpha B2) [UniParc]. Checksum: CB505325F9D4ED81	FASTA	387	41,299
	10 20 30 40 50 60 MRIPVDASTS RRFTPPSTAL SPGKMSEALP LGAPDGGPAL ASKLRSGDRS MVEVLADHPG 70 80 90 100 110 120 ELVRTDSPNF LCSVLPTHWR CNKTLPIAFK VVALGDVPDG TLVTVMAGND ENYSAELRNA 130 140 150 160 170 180 TAAMKNQVAR FNDLRFVGRS GRGKSFTLTI TVFTNPPQVA TYHRAIKITV DGPREPRNAR 190 200 210 220 230 240 QIQPSPPWSY DQSYQYLGSI TSSSVHPATP ISPGRASGMT SLSAELSSRL STAPDLTAFG 250 260 270 280 290 300 DPRQFPTLPS ISDPRMHYPG AFTYSPPVTS GIGIGMSAMS SASRYHTYLP PPYPGSSQAQ 310 320 330 340 350 360 AGPFQTGSPS YHLYYGASAG SYQFSMVGGE RSPPRILPPC TNASTGAALL NPSLPSQSDV 370 380 VETEGSHSNS PTNMPPARLE EAVWRPY
	Isoform 3 [UniParc]. Checksum: AE48F53C5FF9A096	FASTA	163	17,571
	10 20 30 40 50 60 MRIPVDASTS RRFTPPSTAL SPGKMSEALP LGAPDGGPAL ASKLRSGDRS MVEVLADHPG 70 80 90 100 110 120 ELVRTDSPNF LCSVLPTHWR CNKTLPIAFK VLLPEEGGGR SRWRSADGQS EPRGQRLRRL 130 140 150 160 LKGAACSRSL WSFSLSLGWG GDAALPWRPS GGSASEVSKR EFF
	Isoform 4 (AML1-C) [UniParc]. Checksum: 8C7E357BAA92E2E5	FASTA	465	50,238
	10 20 30 40 50 60 MASDSIFESF PSYPQCFMRD ASTSRRFTPP STALSPGKMS EALPLGAPDG GPALASKLRS 70 80 90 100 110 120 GDRSMVEVLA DHPGELVRTD SPNFLCSVLP THWRCNKTLP IAFKVVALGD VPDGTLVTVM 130 140 150 160 170 180 AGNDENYSAE LRNATAAMKN QVARFNDLRF VGRSGRGKSF TLTITVFTNP PQVATYHRAI 190 200 210 220 230 240 KITVDGPREP RRHRQKLDDQ TKPGSLSFSE RLSELEQLRR TAMRVSPHHP APTPNPRASL 250 260 270 280 290 300 NHSTAFNPQP QSQMQDARQI QPSPPWSYDQ SYQYLGSITS SSVHPATPIS PGRASGMTSL 310 320 330 340 350 360 SAELSSRLST APDLTAFGDP RQFPTLPSIS DPRMHYPGAF TYSPPVTSGI GIGMSAMSSA 370 380 390 400 410 420 SRYHTYLPPP YPGSSQAQAG PFQTGSPSYH LYYGASAGSY QFSMVGGERS PPRILPPCTN 430 440 450 460 ASTGAALLNP SLPSQSDVVE TEGSHSNSPT NMPPARLEEA VWRPY
	Isoform 5 [UniParc]. Checksum: ED89962B59A0EC94	FASTA	303	33,485
	10 20 30 40 50 60 MRIPVDASTS RRFTPPSTAL SPGKMSEALP LGAPDGGPAL ASKLRSGDRS 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 QKNPTEPTTL CLCWSPRRRK HRGCQAFLGA LRELLKPRSI SWEPNEENAV PSAEYLYSEK CGC

References

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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D26532 mRNA. Translation: BAA05535.1.
D13802 mRNA. Translation: BAA02960.1.
X97306 mRNA. Translation: CAA65976.1.
AB046930 mRNA. Translation: BAB08105.1.
AF345649 mRNA. Translation: AAK29784.1.
AF193030 Genomic DNA. Translation: AAG32957.1.

IPI

IPI00131214.
IPI00230038.
IPI00230039.
IPI00230040.
IPI00230041.

PIR

A56017.

RefSeq

NP_033951.2. NM_009821.2.

UniGene

Mm.4081.
Mm.470227.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EAN	X-ray	1.70	A	46-185	[»]
1EAO	X-ray	1.40	A/B	46-185	[»]
1EAQ	X-ray	1.25	A/B	46-185	[»]
1HJB	X-ray	3.00	C/F	60-182	[»]
1HJC	X-ray	2.65	A/D	60-182	[»]
1IO4	X-ray	3.00	C	60-182	[»]
2J6W	X-ray	2.60	A/B	46-185	[»]

ProteinModelPortal

Q03347.

SMR

Q03347. Positions 60-173, 319-345.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-40723N.

IntAct

Q03347. 2 interactions.

MINT

MINT-91306.

PTM databases

PhosphoSite

Q03347.

Proteomic databases

PaxDb

Q03347.

PRIDE

Q03347.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

12394.

KEGG

mmu:12394.

UCSC

uc007zzk.2. mouse.

Organism-specific databases

CTD

861.

MGI

MGI:99852. Runx1.

Phylogenomic databases

eggNOG

NOG123889.

HOGENOM

HOG000045616.

HOVERGEN

HBG060268.

InParanoid

Q03347.

KO

K08367.

Gene expression databases

CleanEx

MM_RUNX1.

Genevestigator

Q03347.

GermOnline

ENSMUSG00000022952. Mus musculus.

Family and domain databases

Gene3D

2.60.40.720. 1 hit.

InterPro

IPR000040. AML1_Runt.
IPR008967. p53-like_TF_DNA-bd.
IPR012346. p53/RUNT-type_TF_DNA-bd.
IPR013524. Runt_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

EvolutionaryTrace

Q03347.

NextBio

281140.

SOURCE

Search...

Entry information

Entry name

RUNX1_MOUSE

Accession

Primary (citable) accession number: Q03347
Secondary accession number(s): O08598 , Q62049, Q9ESB9, Q9ET65

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 135 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program