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Q03347

- RUNX1_MOUSE

UniProt

Q03347 - RUNX1_MOUSE

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Protein

Runt-related transcription factor 1

Gene

Runx1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

Sites

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

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

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

Organism-specific databases

MGIiMGI:99852. Runx1.

Subcellular locationi

GO - Cellular componenti

  1. basement membrane Source: MGI
  2. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

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

Mutagenesis

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

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

MaxQBiQ03347.
PaxDbiQ03347.
PRIDEiQ03347.

PTM databases

PhosphoSiteiQ03347.

Expressioni

Tissue specificityi

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

Developmental stagei

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

Gene expression databases

CleanExiMM_RUNX1.
GenevestigatoriQ03347.

Interactioni

Subunit structurei

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

Binary interactionsi

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

Protein-protein interaction databases

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

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EANX-ray1.70A46-185[»]
1EAOX-ray1.40A/B46-185[»]
1EAQX-ray1.25A/B46-185[»]
1HJBX-ray3.00C/F60-182[»]
1HJCX-ray2.65A/D60-182[»]
1IO4X-ray3.00C60-182[»]
2J6WX-ray2.60A/B46-185[»]
3WTSX-ray2.35A/F60-263[»]
3WTTX-ray2.35A/F60-263[»]
3WTUX-ray2.70A/F60-263[»]
3WTVX-ray2.70A/F60-263[»]
3WTWX-ray2.90A/F60-263[»]
3WTXX-ray2.80A/F60-263[»]
3WTYX-ray2.70A/F60-263[»]
3WU1X-ray2.40A55-177[»]
4L0YX-ray2.50A1-242[»]
4L0ZX-ray2.70A1-242[»]
4L18X-ray2.30A/E48-214[»]
ProteinModelPortaliQ03347.
SMRiQ03347. Positions 50-212, 319-345.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ03347.

Family & Domainsi

Domains and Repeats

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

Region

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

Compositional bias

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

Domaini

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

Sequence similaritiesi

Contains 1 Runt domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG123889.
HOGENOMiHOG000045616.
HOVERGENiHBG060268.
InParanoidiQ03347.
PhylomeDBiQ03347.

Family and domain databases

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

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

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

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

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

« Hide

        10         20         30         40         50
MRIPVDASTS RRFTPPSTAL SPGKMSEALP LGAPDGGPAL ASKLRSGDRS
60 70 80 90 100
MVEVLADHPG ELVRTDSPNF LCSVLPTHWR CNKTLPIAFK VVALGDVPDG
110 120 130 140 150
TLVTVMAGND ENYSAELRNA TAAMKNQVAR FNDLRFVGRS GRGKSFTLTI
160 170 180 190 200
TVFTNPPQVA TYHRAIKITV DGPREPRRHR QKLDDQTKPG SLSFSERLSE
210 220 230 240 250
LEQLRRTAMR VSPHHPAPTP NPRASLNHST AFNPQPQSQM QDARQIQPSP
260 270 280 290 300
PWSYDQSYQY LGSITSSSVH PATPISPGRA SGMTSLSAEL SSRLSTAPDL
310 320 330 340 350
TAFGDPRQFP TLPSISDPRM HYPGAFTYSP PVTSGIGIGM SAMSSASRYH
360 370 380 390 400
TYLPPPYPGS SQAQAGPFQT GSPSYHLYYG ASAGSYQFSM VGGERSPPRI
410 420 430 440 450
LPPCTNASTG AALLNPSLPS QSDVVETEGS HSNSPTNMPP ARLEEAVWRP

Y
Length:451
Mass (Da):48,610
Last modified:November 1, 1996 - v1
Checksum:i06B9E9BA01A6469C
GO
Isoform 2 (identifier: Q03347-2) [UniParc]FASTAAdd to Basket

Also known as: PEB2-alpha B2

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

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

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

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

Also known as: AML1-C

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

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

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

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

Experimental Info

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

Alternative sequence

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

Sequence databases

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

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EAN X-ray 1.70 A 46-185 [» ]
1EAO X-ray 1.40 A/B 46-185 [» ]
1EAQ X-ray 1.25 A/B 46-185 [» ]
1HJB X-ray 3.00 C/F 60-182 [» ]
1HJC X-ray 2.65 A/D 60-182 [» ]
1IO4 X-ray 3.00 C 60-182 [» ]
2J6W X-ray 2.60 A/B 46-185 [» ]
3WTS X-ray 2.35 A/F 60-263 [» ]
3WTT X-ray 2.35 A/F 60-263 [» ]
3WTU X-ray 2.70 A/F 60-263 [» ]
3WTV X-ray 2.70 A/F 60-263 [» ]
3WTW X-ray 2.90 A/F 60-263 [» ]
3WTX X-ray 2.80 A/F 60-263 [» ]
3WTY X-ray 2.70 A/F 60-263 [» ]
3WU1 X-ray 2.40 A 55-177 [» ]
4L0Y X-ray 2.50 A 1-242 [» ]
4L0Z X-ray 2.70 A 1-242 [» ]
4L18 X-ray 2.30 A/E 48-214 [» ]
ProteinModelPortali Q03347.
SMRi Q03347. Positions 50-212, 319-345.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

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

PTM databases

PhosphoSitei Q03347.

Proteomic databases

MaxQBi Q03347.
PaxDbi Q03347.
PRIDEi Q03347.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

MGIi MGI:99852. Runx1.

Phylogenomic databases

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

Miscellaneous databases

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

Gene expression databases

CleanExi MM_RUNX1.
Genevestigatori Q03347.

Family and domain databases

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

Publicationsi

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

Entry informationi

Entry nameiRUNX1_MOUSE
AccessioniPrimary (citable) accession number: Q03347
Secondary accession number(s): O08598
, Q62049, Q9ESB9, Q9ET65
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 147 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3