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UniProtKB - Q01196 (RUNX1_HUMAN)

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Protein

Runt-related transcription factor 1

Gene

RUNX1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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
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
  • DNA binding Source: UniProtKB
  • DNA binding transcription factor activity Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • RNA polymerase II proximal promoter sequence-specific DNA binding Source: UniProtKB
  • RNA polymerase II regulatory region sequence-specific DNA binding Source: NTNU_SB
  • RNA polymerase II transcription factor activity, sequence-specific DNA binding Source: NTNU_SB
  • transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific DNA binding Source: NTNU_SB
  • transcription factor binding Source: UniProtKB
  • transcription regulatory region DNA binding Source: UniProtKB
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

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

Enzyme and pathway databases

ReactomeiR-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
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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 21

Organism-specific databases

EuPathDBiHostDB:ENSG00000159216.18
HGNCiHGNC:10471 RUNX1
MIMi151385 gene
neXtProtiNX_Q01196

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; Source: COMPARTMENTS

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 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
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
ProteomicsDBi57927
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

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. Interacts with TBX21 (By similarity).By similarity15 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • transcription factor binding Source: UniProtKB
View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi107309, 81 interactors
CORUMiQ01196
DIPiDIP-36773N
ELMiQ01196
IntActiQ01196, 35 interactors
MINTiQ01196
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

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.

Phylogenomic databases

eggNOGiKOG3982 Eukaryota
ENOG4111J4Y LUCA
GeneTreeiENSGT00390000016964
HOVERGENiHBG060268
InParanoidiQ01196
KOiK08367
OMAiQSYPYLG
OrthoDBiEOG091G0CXB
PhylomeDBiQ01196
TreeFamiTF321496

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

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 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
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

Similar proteinsi

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 historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: November 25, 2008
Last modified: July 18, 2018
This is version 223 of the entry and version 3 of the sequence. See 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

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

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