Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - Q01196 (RUNX1_HUMAN)

Entry version 236 (11 Dec 2019)
Sequence version 3 (25 Nov 2008)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Runt-related transcription factor 1

Gene

RUNX1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Forms the heterodimeric complex core-binding factor (CBF) with CBFB. RUNX members modulate the transcription of their target genes through recognizing the core consensus binding sequence 5'-TGTGGT-3', or very rarely, 5'-TGCGGT-3', within their regulatory regions via their runt domain, while CBFB is a non-DNA-binding regulatory subunit that allosterically enhances the sequence-specific DNA-binding capacity of RUNX. The heterodimers bind to the core site of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, LCK, IL3 and GM-CSF promoters (Probable). Essential for the development of normal hematopoiesis (PubMed:17431401). Acts synergistically with ELF4 to transactivate the IL-3 promoter and with ELF2 to transactivate the BLK promoter (PubMed:10207087, PubMed:14970218). Inhibits KAT6B-dependent transcriptional activation (By similarity). Involved in lineage commitment of immature T cell precursors. CBF complexes repress ZBTB7B transcription factor during cytotoxic (CD8+) T cell development. They bind to RUNX-binding sequence within the ZBTB7B locus acting as transcriptional silencer and allowing for cytotoxic T cell differentiation. CBF complexes binding to the transcriptional silencer is essential for recruitment of nuclear protein complexes that catalyze epigenetic modifications to establish epigenetic ZBTB7B silencing (By similarity). Controls the anergy and suppressive function of regulatory T-cells (Treg) by associating with FOXP3. Activates the expression of IL2 and IFNG and down-regulates the expression of TNFRSF18, IL2RA and CTLA4, in conventional T-cells (PubMed:17377532). Positively regulates the expression of RORC in T-helper 17 cells (By similarity).By similarityCurated5 Publications
Isoform AML-1G 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.By similarity
Isoform AML-1L interferes with the transactivation activity of RUNX1.1 Publication

Caution

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei112Chloride 11
Binding sitei116Chloride 1; via amide nitrogen1
Binding sitei139Chloride 21
Binding sitei170Chloride 2; via amide nitrogen1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActivator, DNA-binding, Repressor
Biological processTranscription, Transcription regulation
LigandChloride

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-1912408 Pre-NOTCH Transcription and Translation
R-HSA-549127 Organic cation transport
R-HSA-8877330 RUNX1 and FOXP3 control the development of regulatory T lymphocytes (Tregs)
R-HSA-8931987 RUNX1 regulates estrogen receptor mediated transcription
R-HSA-8934593 Regulation of RUNX1 Expression and Activity
R-HSA-8935964 RUNX1 regulates expression of components of tight junctions
R-HSA-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function
R-HSA-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-HSA-8939242 RUNX1 regulates transcription of genes involved in differentiation of keratinocytes
R-HSA-8939243 RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known
R-HSA-8939245 RUNX1 regulates transcription of genes involved in BCR signaling
R-HSA-8939246 RUNX1 regulates transcription of genes involved in differentiation of myeloid cells
R-HSA-8939247 RUNX1 regulates transcription of genes involved in interleukin signaling
R-HSA-8939256 RUNX1 regulates transcription of genes involved in WNT signaling
R-HSA-8941333 RUNX2 regulates genes involved in differentiation of myeloid cells
R-HSA-8951936 RUNX3 regulates p14-ARF
R-HSA-9018519 Estrogen-dependent gene expression
R-HSA-9616222 Transcriptional regulation of granulopoiesis

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		Q01196

SIGNOR Signaling Network Open Resource

More...SIGNORi		Q01196

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:RUNX1
Synonyms:AML1, CBFA2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 21

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000159216.18

Human Gene Nomenclature Database

More...HGNCi		HGNC:10471 RUNX1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		151385 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q01196

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

A chromosomal aberration involving RUNX1/AML1 is a cause of M2 type acute myeloid leukemia (AML-M2). Translocation t(8;21)(q22;q22) with RUNX1T1.
A chromosomal aberration involving RUNX1/AML1 is a cause of therapy-related myelodysplastic syndrome (T-MDS). Translocation t(3;21)(q26;q22) with EAP or MECOM.
A chromosomal aberration involving RUNX1/AML1 is a cause of chronic myelogenous leukemia (CML). Translocation t(3;21)(q26;q22) with EAP or MECOM.
A chromosomal aberration involving RUNX1/AML1 is found in childhood acute lymphoblastic leukemia (ALL). Translocation t(12;21)(p13;q22) with TEL. The translocation fuses the 3'-end of TEL to the alternate 5'-exon of AML-1H.
A chromosomal aberration involving RUNX1 is found in acute leukemia. Translocation t(11,21)(q13;q22) that forms a MACROD1-RUNX1 fusion protein.
Familial platelet disorder with associated myeloid malignancy (FPDMM)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAutosomal dominant disease characterized by qualitative and quantitative platelet defects, and propensity to develop acute myelogenous leukemia.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_012128139R → Q in FPDMM. 1 PublicationCorresponds to variant dbSNP:rs1060499616Ensembl.1
Natural variantiVAR_012129174R → Q in FPDMM; impaired phosphorylation. 2 PublicationsCorresponds to variant dbSNP:rs74315450Ensembl.1
A chromosomal aberration involving RUNX1/AML1 is found in therapy-related myeloid malignancies. Translocation t(16;21)(q24;q22) that forms a RUNX1-CBFA2T3 fusion protein.
A chromosomal aberration involving RUNX1/AML1 is a cause of chronic myelomonocytic leukemia. Inversion inv(21)(q21;q22) with USP16.
A chromosomal aberration involving RUNX1/AML1 is found in acute myeloid leukemia. Translocation t(20;21)(q11;q22) with CBFA2T2.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi67S → R: Loss of heterodimerization and reduced EP300 phosphorylation induction. 1 Publication1
Mutagenesisi80R → A: Strongly reduces DNA-binding. 1 Publication1
Mutagenesisi83K → A: Strongly reduces DNA-binding. 2 Publications1
Mutagenesisi83K → E: Strongly reduces DNA-binding, impaired phosphorylation and reduced EP300 phosphorylation induction. 2 Publications1
Mutagenesisi84T → A: No effect on DNA binding. 1 Publication1
Mutagenesisi106M → V: Disrupts interaction of AML1-MTG8/ETO with CBFB, no effect on AML1-MTG8/ETO-mediated transformation activity. 1 Publication1
Mutagenesisi107A → T: Loss of heterodimerization. Disrupts interactionof AML1-MTG8/ETO with CBFB, no effect on AML1-MTG8/ETO-mediated transformation activity. 2 Publications1
Mutagenesisi108G → R: Loss of heterodimerization and impaired phosphorylation. 2 Publications1
Mutagenesisi135R → A: Strongly reduces DNA-binding. 1 Publication1
Mutagenesisi139R → A: Strongly reduces DNA-binding. 1 Publication1
Mutagenesisi140S → G: Disrupts AML1-MTG8/ETO DNA-binding, decreases AML1-MTG8/ETO transforming activity. 1 Publication1
Mutagenesisi142R → A: Strongly reduces DNA-binding. 1 Publication1
Mutagenesisi145 – 453Missing : No DNA-binding. Add BLAST309
Mutagenesisi167K → A: Reduces DNA-binding. 1 Publication1
Mutagenesisi169T → A: Strongly reduces DNA-binding. 1 Publication1
Mutagenesisi171D → A: Strongly reduces DNA-binding. 1 Publication1
Mutagenesisi174R → A: Strongly reduces DNA-binding. 1 Publication1
Mutagenesisi177R → A: Strongly reduces DNA-binding. 1 Publication1
Mutagenesisi249S → A: Reduced phosphorylation. 1 Publication1
Mutagenesisi273T → A: Reduced phosphorylation; when associated with A-276. 1 Publication1
Mutagenesisi276S → A: Reduced phosphorylation; when associated with A-273. 1 Publication1

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei177 – 178Breakpoint 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 protein2
Sitei241 – 242Breakpoint for translocation to form AML1-EAP in T-MDS and CML, to form type II MACROD1-RUNX1 fusion protein and to form RUNX1-CBFA2T2 in acute myeloid leukemia1 Publication2

Keywords - Diseasei

Disease mutation, Proto-oncogene

Organism-specific databases

DisGeNET

More...DisGeNETi		861

MalaCards human disease database

More...MalaCardsi		RUNX1
MIMi601399 phenotype

Open Targets

More...OpenTargetsi		ENSG00000159216

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		102724 Acute myeloid leukemia with t(8;21)(q22;q22) translocation
521 Chronic myeloid leukemia
71290 Familial platelet disorder with associated myeloid malignancy
248340 Isolated delta-storage pool disease
99860 Precursor B-cell acute lymphoblastic leukemia

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA34884

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q01196 Tbio

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		RUNX1

Domain mapping of disease mutations (DMDM)

More...DMDMi		215274205

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001746551 – 453Runt-related transcription factor 1Add BLAST453

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei14PhosphothreonineCombined sources1
Modified residuei21PhosphoserineCombined sources1
Modified residuei24N6-acetyllysineCombined sources1
Modified residuei43N6-acetyllysineCombined sources1
Modified residuei193PhosphoserineCombined sources1
Modified residuei212PhosphoserineCombined sources1
Modified residuei249Phosphoserine; by HIPK2Combined sources1 Publication1
Modified residuei266PhosphoserineCombined sources1
Modified residuei268PhosphoserineCombined sources1
Modified residuei273Phosphothreonine; by HIPK21 Publication1
Modified residuei276Phosphoserine; by HIPK2Combined sources1 Publication1
Modified residuei296PhosphothreonineCombined sources1
Modified residuei435PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q01196

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q01196

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q01196

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q01196

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q01196

PeptideAtlas

More...PeptideAtlasi		Q01196

PRoteomics IDEntifications database

More...PRIDEi		Q01196

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		57927 [Q01196-1]
57928 [Q01196-10]
57929 [Q01196-11]
57930 [Q01196-2]
57931 [Q01196-3]
57932 [Q01196-4]
57933 [Q01196-5]
57934 [Q01196-6]
57935 [Q01196-7]
57936 [Q01196-8]
57937 [Q01196-9]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q01196

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		Q01196

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

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

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulated by phorbol myristate acetate (PMA).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000159216 Expressed in 194 organ(s), highest expression level in epithelium of mammary gland

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q01196 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q01196 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		HPA004176
HPA037912

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Heterodimer with CBFB. RUNX1 binds DNA as a monomer and through the Runt domain. DNA-binding is increased by heterodimerization. Isoform AML-1L can neither bind DNA nor heterodimerize.

Interacts with TLE1 and ALYREF/THOC4 (PubMed:9119228, PubMed:9751710).

Interacts with ELF1, ELF2 and SPI1 (PubMed:10207087).

Interacts via its Runt domain with the ELF4 N-terminal region (PubMed:10207087). Interaction with ELF2 isoform 2 (NERF-1a) may act to repress RUNX1-mediated transactivation (PubMed:14970218).

Interacts with KAT6A and KAT6B (PubMed:11742995, PubMed:11965546).

Interacts with SUV39H1, leading to abrogation of transactivating and DNA-binding properties of RUNX1 (PubMed:12917624, PubMed:16652147).

Interacts with YAP1 (PubMed:18280240).

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.

Interacts with FOXP3 (PubMed:17377532).

Interacts with TBX21 (By similarity).

Interacts with DPF2 (PubMed:28533407).

By similarity16 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Show more details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		107309, 217 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q01196

Database of interacting proteins

More...DIPi		DIP-36773N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		Q01196

Protein interaction database and analysis system

More...IntActi		Q01196, 36 interactors

Molecular INTeraction database

More...MINTi		Q01196

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000300305

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q01196

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q01196 protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1453
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q01196

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q01196

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini50 – 178RuntPROSITE-ProRule annotationAdd BLAST129

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni80 – 84Interaction with DNA5
Regioni135 – 143Interaction with DNA9
Regioni168 – 177Interaction with DNA10
Regioni291 – 371Interaction with KAT6A1 PublicationAdd BLAST81
Regioni307 – 400Interaction with KAT6BBy similarityAdd BLAST94
Regioni362 – 402Interaction with FOXP31 PublicationAdd BLAST41

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi187 – 453Pro/Ser/Thr-richAdd BLAST267

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3982 Eukaryota
ENOG4111J4Y LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000159255

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q01196

KEGG Orthology (KO)

More...KOi		K08367

Identification of Orthologs from Complete Genome Data

More...OMAi		PRVNHST

Database of Orthologous Groups

More...OrthoDBi		562214at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q01196

TreeFam database of animal gene trees

More...TreeFami		TF321496

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.60.40.720, 1 hit
4.10.770.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR000040 AML1_Runt
IPR008967 p53-like_TF_DNA-bd
IPR012346 p53/RUNT-type_TF_DNA-bd_sf
IPR013524 Runt_dom
IPR027384 Runx_central_dom_sf
IPR013711 RunxI_C_dom
IPR016554 TF_Runt-rel_RUNX

The PANTHER Classification System

More...PANTHERi		PTHR11950 PTHR11950, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00853 Runt, 1 hit
PF08504 RunxI, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF009374 TF_Runt-rel_RUNX, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00967 ONCOGENEAML1

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF49417 SSF49417, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51062 RUNT, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (11+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 11 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Note: Additional isoforms seem to exist.

This entry has 11 described isoforms and 6 potential isoforms that are computationally mapped.Show allAlign All

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

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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 LGAPDAGAAL AGKLRSGDRS 
        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 QDTRQIQPSP 
       260        270        280        290        300
PWSYDQSYQY LGSIASPSVH PATPISPGRA SGMTTLSAEL SSRLSTAPDL 
       310        320        330        340        350
TAFSDPRQFP ALPSISDPRM HYPGAFTYSP TPVTSGIGIG MSAMGSATRY 
       360        370        380        390        400
HTYLPPPYPG SSQAQGGPFQ ASSPSYHLYY GASAGSYQFS MVGGERSPPR 
       410        420        430        440        450
ILPPCTNAST GSALLNPSLP NQSDVVEAEG SHSNSPTNMA PSARLEEAVW 

RPY
Length:453
Mass (Da):48,737
Last modified:November 25, 2008 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i4F1F193A7CADDBAB
GO
Isoform AML-1A (identifier: Q01196-2) [UniParc]FASTAAdd to basket

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

Show »
Length:468
Mass (Da):50,173
Checksum:i07A186F5A0EEB6E4
GO
Isoform AML-1L (identifier: Q01196-11) [UniParc]FASTAAdd to basket
Also known as: AML1-delta N

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

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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 6 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H9KVB1H9KVB1_HUMAN
Runt-related transcription factor
RUNX1
389Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A8MZI9A8MZI9_HUMAN
Runt-related transcription factor 1
RUNX1
256Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
C9JWM1C9JWM1_HUMAN
Runt-related transcription factor 1
RUNX1
140Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
V9GYT5V9GYT5_HUMAN
Runt-related transcription factor 1
RUNX1
49Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
V9GYT3V9GYT3_HUMAN
Runt-related transcription factor 1
RUNX1
38Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A0C4DG58A0A0C4DG58_HUMAN
Runt-related transcription factor 1
RUNX1
32Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAC05246 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated
The sequence AAC05247 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti412S → F in AAA51720 (Ref. 1) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_012128139R → Q in FPDMM. 1 PublicationCorresponds to variant dbSNP:rs1060499616Ensembl.1
Natural variantiVAR_012129174R → Q in FPDMM; impaired phosphorylation. 2 PublicationsCorresponds to variant dbSNP:rs74315450Ensembl.1
Natural variantiVAR_013177431S → R. Corresponds to variant dbSNP:rs1055308Ensembl.1
Natural variantiVAR_013178433S → R. Corresponds to variant dbSNP:rs1055309Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0059191 – 105Missing in isoform AML-1L. 2 PublicationsAdd BLAST105
Alternative sequenceiVSP_0059171 – 5MRIPV → MASDSIFESFPSYPQCFMRE CILGMNPSRDVH in isoform AML-1G. 3 Publications5
Alternative sequenceiVSP_0059161 – 5MRIPV → MNPSRDVH in isoform AML-1H. Curated5
Alternative sequenceiVSP_0059181 – 5MRIPV → MPAAPRGPAQGEAAARTRSR in isoform AML-1I. Curated5
Alternative sequenceiVSP_005920137 – 242VGRSG…SQMQD → VDGPREPRRHRQKLDDQTKP GSLSFSERLSELEQLRRTAM RVSPHHPAPTPNPRASLNHS TAFNPQPQSQMQDTRQIQPS PPWSYDQSYQYLGSIASPSV HPATPI in isoform AML-1FC. CuratedAdd BLAST106
Alternative sequenceiVSP_005923178 – 224RHRQK…PNPRA → SKCIHLGLVHPPGWYTLQAG ILRDHVSDSLGSTFPPGGWQ APVKPKS in isoform AML-1FA. CuratedAdd BLAST47
Alternative sequenceiVSP_005921178 – 188RHRQKLDDQTK → NSLTWPRYPHI in isoform AML-1FB. CuratedAdd BLAST11
Alternative sequenceiVSP_005922189 – 453Missing in isoform AML-1FB. CuratedAdd BLAST265
Alternative sequenceiVSP_005924225 – 453Missing in isoform AML-1FA. CuratedAdd BLAST229
Alternative sequenceiVSP_005926242 – 250DTRQIQPSP → EEDTAPWRC in isoform AML-1C. 1 Publication9
Alternative sequenceiVSP_005925243 – 453Missing in isoform AML-1FC. CuratedAdd BLAST211
Alternative sequenceiVSP_005927251 – 453Missing in isoform AML-1C. 1 PublicationAdd BLAST203
Alternative sequenceiVSP_005928258 – 453Missing in isoform AML-1E. 1 PublicationAdd BLAST196
Alternative sequenceiVSP_005929440 – 453APSAR…VWRPY → GGASCSRQARRDPGPWARTP SWGRGRPTDRISL in isoform AML-1A. 2 PublicationsAdd BLAST14

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
L34598 mRNA Translation: AAA51720.1
D43967 mRNA Translation: BAA07902.1
D10570 mRNA Translation: BAA01426.1
S76345 mRNA Translation: AAB33729.1
S76346 mRNA Translation: AAB33730.1
S76350 mRNA Translation: AAB33731.1
S60998 mRNA No translation available.
X79549 mRNA Translation: CAA56092.1
D43968 mRNA Translation: BAA07903.1
D43969 mRNA Translation: BAA07904.1
U19601 mRNA Translation: AAB51691.1
L21756 mRNA Translation: AAA03086.1 Different termination.
S69002 mRNA Translation: AAB29907.1 Different termination.
D13979 mRNA Translation: BAA03089.1
D14822 mRNA Translation: BAA03559.1 Different termination.
D14823 mRNA Translation: BAA03560.1 Different termination.
S78158 mRNA Translation: AAB34819.2 Different termination.
S78159 mRNA Translation: AAB34820.2 Different termination.
S50186 Genomic DNA No translation available.
S78496 mRNA No translation available.
S74092 Genomic DNA No translation available.
X90979 mRNA Translation: CAA62466.1
X90976 mRNA Translation: CAA62464.1
D89790 mRNA Translation: BAA14022.1
D89788 mRNA Translation: BAA14020.1
D89789 mRNA Translation: BAA14021.1
AP000330 Genomic DNA No translation available.
AP000331 Genomic DNA No translation available.
AP000332 Genomic DNA No translation available.
AP000333 Genomic DNA No translation available.
AP000334 Genomic DNA No translation available.
AF015262 Genomic DNA No translation available.
CH471079 Genomic DNA Translation: EAX09769.1
CH471079 Genomic DNA Translation: EAX09770.1
BC136380 mRNA Translation: AAI36381.1
BC136381 mRNA Translation: AAI36382.1
BC144053 mRNA Translation: AAI44054.1
AF025841 Genomic DNA Translation: AAC05246.1 Different initiation.
AF025841 Genomic DNA Translation: AAC05247.1 Different initiation.
AJ229043 Genomic DNA Translation: CAA13070.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS13639.1 [Q01196-8]
CCDS42922.1 [Q01196-1]
CCDS46646.1 [Q01196-3]

Protein sequence database of the Protein Information Resource

More...PIRi		I39443
S57842

NCBI Reference Sequences

More...RefSeqi		NP_001001890.1, NM_001001890.2 [Q01196-1]
NP_001116079.1, NM_001122607.1 [Q01196-3]
NP_001745.2, NM_001754.4 [Q01196-8]
XP_005261125.1, XM_005261068.3 [Q01196-10]
XP_011528068.1, XM_011529766.2 [Q01196-8]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000300305; ENSP00000300305; ENSG00000159216 [Q01196-8]
ENST00000344691; ENSP00000340690; ENSG00000159216 [Q01196-1]
ENST00000358356; ENSP00000351123; ENSG00000159216 [Q01196-3]
ENST00000437180; ENSP00000409227; ENSG00000159216 [Q01196-8]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		861

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:861

UCSC genome browser

More...UCSCi		uc002yuh.3 human [Q01196-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L34598 mRNA Translation: AAA51720.1
D43967 mRNA Translation: BAA07902.1
D10570 mRNA Translation: BAA01426.1
S76345 mRNA Translation: AAB33729.1
S76346 mRNA Translation: AAB33730.1
S76350 mRNA Translation: AAB33731.1
S60998 mRNA No translation available.
X79549 mRNA Translation: CAA56092.1
D43968 mRNA Translation: BAA07903.1
D43969 mRNA Translation: BAA07904.1
U19601 mRNA Translation: AAB51691.1
L21756 mRNA Translation: AAA03086.1 Different termination.
S69002 mRNA Translation: AAB29907.1 Different termination.
D13979 mRNA Translation: BAA03089.1
D14822 mRNA Translation: BAA03559.1 Different termination.
D14823 mRNA Translation: BAA03560.1 Different termination.
S78158 mRNA Translation: AAB34819.2 Different termination.
S78159 mRNA Translation: AAB34820.2 Different termination.
S50186 Genomic DNA No translation available.
S78496 mRNA No translation available.
S74092 Genomic DNA No translation available.
X90979 mRNA Translation: CAA62466.1
X90976 mRNA Translation: CAA62464.1
D89790 mRNA Translation: BAA14022.1
D89788 mRNA Translation: BAA14020.1
D89789 mRNA Translation: BAA14021.1
AP000330 Genomic DNA No translation available.
AP000331 Genomic DNA No translation available.
AP000332 Genomic DNA No translation available.
AP000333 Genomic DNA No translation available.
AP000334 Genomic DNA No translation available.
AF015262 Genomic DNA No translation available.
CH471079 Genomic DNA Translation: EAX09769.1
CH471079 Genomic DNA Translation: EAX09770.1
BC136380 mRNA Translation: AAI36381.1
BC136381 mRNA Translation: AAI36382.1
BC144053 mRNA Translation: AAI44054.1
AF025841 Genomic DNA Translation: AAC05246.1 Different initiation.
AF025841 Genomic DNA Translation: AAC05247.1 Different initiation.
AJ229043 Genomic DNA Translation: CAA13070.1
CCDSiCCDS13639.1 [Q01196-8]
CCDS42922.1 [Q01196-1]
CCDS46646.1 [Q01196-3]
PIRiI39443
S57842
RefSeqiNP_001001890.1, NM_001001890.2 [Q01196-1]
NP_001116079.1, NM_001122607.1 [Q01196-3]
NP_001745.2, NM_001754.4 [Q01196-8]
XP_005261125.1, XM_005261068.3 [Q01196-10]
XP_011528068.1, XM_011529766.2 [Q01196-8]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB 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[»]
SMRiQ01196
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi107309, 217 interactors
CORUMiQ01196
DIPiDIP-36773N
ELMiQ01196
IntActiQ01196, 36 interactors
MINTiQ01196
STRINGi9606.ENSP00000300305

Chemistry databases

BindingDBiQ01196

PTM databases

iPTMnetiQ01196
PhosphoSitePlusiQ01196

Polymorphism and mutation databases

BioMutaiRUNX1
DMDMi215274205

Proteomic databases

EPDiQ01196
jPOSTiQ01196
MassIVEiQ01196
MaxQBiQ01196
PaxDbiQ01196
PeptideAtlasiQ01196
PRIDEiQ01196
ProteomicsDBi57927 [Q01196-1]
57928 [Q01196-10]
57929 [Q01196-11]
57930 [Q01196-2]
57931 [Q01196-3]
57932 [Q01196-4]
57933 [Q01196-5]
57934 [Q01196-6]
57935 [Q01196-7]
57936 [Q01196-8]
57937 [Q01196-9]

Genome annotation databases

EnsembliENST00000300305; ENSP00000300305; ENSG00000159216 [Q01196-8]
ENST00000344691; ENSP00000340690; ENSG00000159216 [Q01196-1]
ENST00000358356; ENSP00000351123; ENSG00000159216 [Q01196-3]
ENST00000437180; ENSP00000409227; ENSG00000159216 [Q01196-8]
GeneIDi861
KEGGihsa:861
UCSCiuc002yuh.3 human [Q01196-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		861
DisGeNETi861
EuPathDBiHostDB:ENSG00000159216.18

GeneCards: human genes, protein and diseases

More...GeneCardsi		RUNX1
HGNCiHGNC:10471 RUNX1
HPAiHPA004176
HPA037912
MalaCardsiRUNX1
MIMi151385 gene
601399 phenotype
neXtProtiNX_Q01196
OpenTargetsiENSG00000159216
Orphaneti102724 Acute myeloid leukemia with t(8;21)(q22;q22) translocation
521 Chronic myeloid leukemia
71290 Familial platelet disorder with associated myeloid malignancy
248340 Isolated delta-storage pool disease
99860 Precursor B-cell acute lymphoblastic leukemia
PharmGKBiPA34884

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG3982 Eukaryota
ENOG4111J4Y LUCA
GeneTreeiENSGT00940000159255
InParanoidiQ01196
KOiK08367
OMAiPRVNHST
OrthoDBi562214at2759
PhylomeDBiQ01196
TreeFamiTF321496

Enzyme and pathway databases

ReactomeiR-HSA-1912408 Pre-NOTCH Transcription and Translation
R-HSA-549127 Organic cation transport
R-HSA-8877330 RUNX1 and FOXP3 control the development of regulatory T lymphocytes (Tregs)
R-HSA-8931987 RUNX1 regulates estrogen receptor mediated transcription
R-HSA-8934593 Regulation of RUNX1 Expression and Activity
R-HSA-8935964 RUNX1 regulates expression of components of tight junctions
R-HSA-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function
R-HSA-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-HSA-8939242 RUNX1 regulates transcription of genes involved in differentiation of keratinocytes
R-HSA-8939243 RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known
R-HSA-8939245 RUNX1 regulates transcription of genes involved in BCR signaling
R-HSA-8939246 RUNX1 regulates transcription of genes involved in differentiation of myeloid cells
R-HSA-8939247 RUNX1 regulates transcription of genes involved in interleukin signaling
R-HSA-8939256 RUNX1 regulates transcription of genes involved in WNT signaling
R-HSA-8941333 RUNX2 regulates genes involved in differentiation of myeloid cells
R-HSA-8951936 RUNX3 regulates p14-ARF
R-HSA-9018519 Estrogen-dependent gene expression
R-HSA-9616222 Transcriptional regulation of granulopoiesis
SignaLinkiQ01196
SIGNORiQ01196

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		RUNX1 human
EvolutionaryTraceiQ01196

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		RUNX1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		861
PharosiQ01196 Tbio

Protein Ontology

More...PROi		PR:Q01196
RNActiQ01196 protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000159216 Expressed in 194 organ(s), highest expression level in epithelium of mammary gland
ExpressionAtlasiQ01196 baseline and differential
GenevisibleiQ01196 HS

Family and domain databases

Gene3Di2.60.40.720, 1 hit
4.10.770.10, 1 hit
InterProiView protein in InterPro
IPR000040 AML1_Runt
IPR008967 p53-like_TF_DNA-bd
IPR012346 p53/RUNT-type_TF_DNA-bd_sf
IPR013524 Runt_dom
IPR027384 Runx_central_dom_sf
IPR013711 RunxI_C_dom
IPR016554 TF_Runt-rel_RUNX
PANTHERiPTHR11950 PTHR11950, 1 hit
PfamiView protein in Pfam
PF00853 Runt, 1 hit
PF08504 RunxI, 1 hit
PIRSFiPIRSF009374 TF_Runt-rel_RUNX, 1 hit
PRINTSiPR00967 ONCOGENEAML1
SUPFAMiSSF49417 SSF49417, 1 hit
PROSITEiView protein in PROSITE
PS51062 RUNT, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRUNX1_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q01196
Secondary accession number(s): A8MV94
, B2RMS4, D3DSG1, O60472, O60473, O76047, O76089, Q13081, Q13755, Q13756, Q13757, Q13758, Q13759, Q15341, Q15343, Q16122, Q16284, Q16285, Q16286, Q16346, Q16347, Q92479
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: November 25, 2008
Last modified: December 11, 2019
This is version 236 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human chromosome 21
    Human chromosome 21: entries, gene names and cross-references to MIM
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again