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Protein

Runt-related transcription factor 1

Gene

RUNX1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. The alpha subunit binds DNA and appears to have a role in the development of normal hematopoiesis. Isoform AML-1L interferes with the transactivation activity of RUNX1. Acts synergistically with ELF4 to transactivate the IL-3 promoter and with ELF2 to transactivate the mouse BLK promoter. Inhibits KAT6B-dependent transcriptional activation. 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).5 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei112Chloride 11
Binding sitei116Chloride 1; via amide nitrogen1
Binding sitei139Chloride 21
Binding sitei170Chloride 2; via amide nitrogen1

GO - Molecular functioni

  • ATP binding Source: InterPro
  • calcium ion binding Source: UniProtKB
  • core promoter binding Source: UniProtKB
  • DNA binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • regulatory region DNA binding Source: UniProtKB
  • RNA polymerase II regulatory region sequence-specific DNA binding Source: NTNU_SB
  • transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding Source: NTNU_SB
  • transcription factor activity, sequence-specific DNA binding Source: UniProtKB
  • transcription factor binding Source: UniProtKB

GO - Biological processi

  • chondrocyte differentiation Source: GO_Central
  • hematopoietic stem cell proliferation Source: UniProtKB
  • hemopoiesis Source: UniProtKB
  • myeloid cell differentiation Source: UniProtKB
  • negative regulation of granulocyte differentiation Source: UniProtKB
  • ossification Source: GO_Central
  • peripheral nervous system neuron development Source: BHF-UCL
  • positive regulation of angiogenesis Source: UniProtKB
  • positive regulation of granulocyte differentiation Source: UniProtKB
  • positive regulation of interleukin-2 production Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Chloride, DNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000159216-MONOMER.
ReactomeiR-HSA-549127. Organic cation transport.
SignaLinkiQ01196.
SIGNORiQ01196.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 21

Organism-specific databases

HGNCiHGNC:10471. RUNX1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • intracellular membrane-bounded organelle Source: HPA
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

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.
See also OMIM:601399
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_012128139R → Q in FPDMM. 1 Publication1
Natural variantiVAR_012129174R → Q in FPDMM; impaired phosphorylation. 2 PublicationsCorresponds to variant rs74315450dbSNPEnsembl.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.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
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

DisGeNETi861.
MalaCardsiRUNX1.
MIMi601399. phenotype.
OpenTargetsiENSG00000159216.
Orphaneti102724. 'Acute myeloid leukemia with t(8;21)(q22;q22) translocation'.
521. Chronic myeloid leukemia.
71290. Familial platelet syndrome with predisposition to acute myelogenous leukemia.
248340. Isolated delta-storage pool disease.
99860. Precursor B-cell acute lymphoblastic leukemia.
PharmGKBiPA34884.

Polymorphism and mutation databases

BioMutaiRUNX1.
DMDMi215274205.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001746551 – 453Runt-related transcription factor 1Add BLAST453

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

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

EPDiQ01196.
MaxQBiQ01196.
PaxDbiQ01196.
PeptideAtlasiQ01196.
PRIDEiQ01196.

PTM databases

iPTMnetiQ01196.
PhosphoSitePlusiQ01196.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000159216.
ExpressionAtlasiQ01196. baseline and differential.
GenevisibleiQ01196. HS.

Organism-specific databases

HPAiHPA004176.
HPA037912.

Interactioni

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. Interacts with ELF1, ELF2 and SPI1. Interacts via its Runt domain with the ELF4 N-terminal region. Interaction with ELF2 isoform 2 (NERF-1a) may act to repress RUNX1-mediated transactivation. Interacts with KAT6A and KAT6B. Interacts with SUV39H1, leading to abrogation of transactivating and DNA-binding properties of RUNX1. Interacts with YAP1. Interacts with HIPK2 (By similarity). Interaction with CDK6 prevents myeloid differentiation, reducing its transcription transactivation activity. Found in a complex with PRMT5, RUNX1 AND CBFB. Interacts with FOXP3.By similarity15 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CBFBQ139512EBI-925904,EBI-718750
CDK6Q005345EBI-925904,EBI-295663
ELF2Q157232EBI-925904,EBI-956941
groP163714EBI-925940,EBI-153866From a different organism.
HIPK2Q9H2X64EBI-925904,EBI-348345
TAL1P175422EBI-925904,EBI-1753878
TLE1Q047244EBI-925940,EBI-711424
YAP1P469373EBI-925904,EBI-1044059

GO - Molecular functioni

  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107309. 72 interactors.
DIPiDIP-36773N.
IntActiQ01196. 28 interactors.
MINTiMINT-153610.
STRINGi9606.ENSP00000300305.

Chemistry databases

BindingDBiQ01196.

Structurei

Secondary structure

1453
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi54 – 57Combined sources4
Beta strandi62 – 64Combined sources3
Beta strandi70 – 73Combined sources4
Beta strandi77 – 80Combined sources4
Beta strandi82 – 84Combined sources3
Beta strandi90 – 93Combined sources4
Beta strandi102 – 108Combined sources7
Beta strandi110 – 114Combined sources5
Beta strandi117 – 119Combined sources3
Beta strandi121 – 123Combined sources3
Beta strandi128 – 130Combined sources3
Beta strandi146 – 152Combined sources7
Beta strandi154 – 156Combined sources3
Beta strandi158 – 161Combined sources4
Beta strandi166 – 171Combined sources6
Helixi175 – 177Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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[»]
ProteinModelPortaliQ01196.
SMRiQ01196.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01196.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini50 – 178RuntPROSITE-ProRule annotationAdd BLAST129

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Compositional biasi187 – 453Pro/Ser/Thr-richAdd BLAST267

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

eggNOGiKOG3982. Eukaryota.
ENOG4111J4Y. LUCA.
GeneTreeiENSGT00390000016964.
HOVERGENiHBG060268.
InParanoidiQ01196.
KOiK08367.
OMAiFSMMAGG.
OrthoDBiEOG091G0CXB.
PhylomeDBiQ01196.
TreeFamiTF321496.

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 (11)i

Sequence statusi: Complete.

This entry describes 11 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.
Isoform AML-1B (identifier: Q01196-1) [UniParc]FASTAAdd to basket

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 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
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

Sequence cautioni

The sequence AAC05246 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAC05247 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti412S → F in AAA51720 (Ref. 1) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_012128139R → Q in FPDMM. 1 Publication1
Natural variantiVAR_012129174R → Q in FPDMM; impaired phosphorylation. 2 PublicationsCorresponds to variant rs74315450dbSNPEnsembl.1
Natural variantiVAR_013177431S → R.Corresponds to variant rs1055308dbSNPEnsembl.1
Natural variantiVAR_013178433S → R.Corresponds to variant rs1055309dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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:
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]
UniGeneiHs.149261.
Hs.612648.
Hs.705364.

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]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

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]
UniGeneiHs.149261.
Hs.612648.
Hs.705364.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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[»]
ProteinModelPortaliQ01196.
SMRiQ01196.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107309. 72 interactors.
DIPiDIP-36773N.
IntActiQ01196. 28 interactors.
MINTiMINT-153610.
STRINGi9606.ENSP00000300305.

Chemistry databases

BindingDBiQ01196.

PTM databases

iPTMnetiQ01196.
PhosphoSitePlusiQ01196.

Polymorphism and mutation databases

BioMutaiRUNX1.
DMDMi215274205.

Proteomic databases

EPDiQ01196.
MaxQBiQ01196.
PaxDbiQ01196.
PeptideAtlasiQ01196.
PRIDEiQ01196.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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

CTDi861.
DisGeNETi861.
GeneCardsiRUNX1.
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 syndrome with predisposition to acute myelogenous leukemia.
248340. Isolated delta-storage pool disease.
99860. Precursor B-cell acute lymphoblastic leukemia.
PharmGKBiPA34884.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3982. Eukaryota.
ENOG4111J4Y. LUCA.
GeneTreeiENSGT00390000016964.
HOVERGENiHBG060268.
InParanoidiQ01196.
KOiK08367.
OMAiFSMMAGG.
OrthoDBiEOG091G0CXB.
PhylomeDBiQ01196.
TreeFamiTF321496.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000159216-MONOMER.
ReactomeiR-HSA-549127. Organic cation transport.
SignaLinkiQ01196.
SIGNORiQ01196.

Miscellaneous databases

ChiTaRSiRUNX1. human.
EvolutionaryTraceiQ01196.
GeneWikiiRUNX1.
GenomeRNAii861.
PROiQ01196.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000159216.
ExpressionAtlasiQ01196. baseline and differential.
GenevisibleiQ01196. HS.

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]
ProtoNetiSearch...

Entry informationi

Entry nameiRUNX1_HUMAN
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
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: November 25, 2008
Last modified: November 30, 2016
This is version 209 of the entry and version 3 of the sequence. [Complete history]
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.

Miscellaneousi

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 21
    Human chromosome 21: entries, gene names and cross-references to MIM
  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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.