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Protein Page:
AML2 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
AML2 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. Heterodimer of an alpha and a beta subunit. The alpha subunit binds DNA as a monomer and through the Runt domain. DNA- binding is increased by heterodimerization. Interacts with TLE1 and SUV39H1. The tyrosine phosphorylated form (via runt domain) interacts with SRC (via protein kinase domain). Interacts with FYN and LCK. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: DNA binding protein; Transcription factor
Chromosomal Location of Human Ortholog: 1p36
Cellular Component: nuclear chromatin; cytoplasm; nucleus
Molecular Function: protein binding; transcription factor activity; ATP binding
Biological Process: transcription from RNA polymerase II promoter; peripheral nervous system neuron development; axon guidance; hair follicle morphogenesis; regulation of transcription, DNA-dependent; cell maturation; interferon-gamma production; chondrocyte differentiation; negative regulation of transcription from RNA polymerase II promoter; protein amino acid phosphorylation; negative regulation of epithelial cell proliferation; negative regulation of cell cycle
Reference #:  Q13761 (UniProtKB)
Alt. Names/Synonyms: Acute myeloid leukemia 2 protein; acute myeloid leukemia gene 2; AML2; CBF-alpha-3; CBFA3; Core-binding factor subunit alpha-3; core-binding factor, runt domain, alpha subunit 3; FLJ34510; MGC16070; Oncogene AML-2; PEA2 alpha C; PEA2-alpha C; PEBP2 alpha C; PEBP2-alpha C; PEBP2A3; PEBP2aC; Polyomavirus enhancer-binding protein 2 alpha C subunit; Runt-related transcription factor 3; RUNX3; SL3-3 enhancer factor 1 alpha C subunit; SL3/AKV core-binding factor alpha C subunit; transcription factor AML2
Gene Symbols: RUNX3
Molecular weight: 44,356 Da
Basal Isoelectric point: 9.53  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

AML2

Protein Structure Not Found.


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Sites Implicated In
cell cycle regulation: S149‑p, T151‑p, T153‑p, T155‑p
transcription, altered: S149‑p, T151‑p, T153‑p, T155‑p, S356‑p
intracellular localization: S149‑p, T151‑p, T153‑p, T155‑p
protein degradation: S356‑p
protein stabilization: S149‑p, T151‑p, T153‑p, T155‑p
ubiquitination: S356‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 T14-p PSTSRRFtPPsPAFP
0 8 S17-p SRRFtPPsPAFPCGG
1 0 K94-ub KTLPVAFkVVALGDV
0 8 K129-ub RNASAVMkNQVARFN
1 0 K148-ub VGRSGRGksFtLtIt
1 2 S149-p GRSGRGksFtLtItV
1 1 T151-p SGRGksFtLtItVFT
1 1 T153-p RGksFtLtItVFTNP
1 1 T155-p ksFtLtItVFTNPTQ
1 1 T209-p ERLRMRVtPstPsPR
0 4 S211-p LRMRVtPstPsPRGS
1 3 T212-p RMRVtPstPsPRGSL
1 8 S214-p RVtPstPsPRGSLsT
0 1 S220-p PsPRGSLsTtSHFSs
0 1 T222-p PRGSLsTtSHFSsQP
0 2 S227-p sTtSHFSsQPQtPIQ
1 18 T231-p HFSsQPQtPIQGTSE
0 2 S243-p TSELNPFsDPRQFDR
0 1 T254-p QFDRSFPtLPTLTEs
0 1 S261-p tLPTLTEsRFPDPRM
1 0 S356-p SSSGGDRsPTRMLAS
  mouse

 
T14-p PSTSRRFtPPSTAFP
S17 SRRFtPPSTAFPCGG
K95 KTLPVAFKVVALGDV
K130 RNASAVMKNQVARFN
K149 VGRSGRGKSFTLTIT
S150 GRSGRGKSFTLTITV
T152 SGRGKSFTLTITVFT
T154 RGKSFTLTITVFTNP
T156 KSFTLTITVFTNPTQ
T207 GDLRMRVTPStPsPR
S209 LRMRVTPStPsPRGS
T210-p RMRVTPStPsPRGSL
S212-p RVTPStPsPRGSLST
S218 PsPRGSLSTTSHFSS
T220 PRGSLSTTSHFSSQA
S225 STTSHFSSQAQTPIQ
T229 HFSSQAQTPIQGSSD
S241 SSDLNPFSDPRQFDR
T252 QFDRSFPTLQSLTES
S259 TLQSLTESRFPDPRM
S352 AAGGGERSPTRMLTS
  rat

 
T14 PSTSRRFTPPSTAFP
S17 SRRFTPPSTAFPCGG
K95 KTLPVAFKVVALGDV
K130 RNASAVMKNQVARFN
K149 VGRSGRGKSFTLTIT
S150 GRSGRGKSFTLTITV
T152 SGRGKSFTLTITVFT
T154 RGKSFTLTITVFTNP
T156 KSFTLTITVFTNPTQ
T207 GDLRMRVTPSTPSPR
S209 LRMRVTPSTPSPRGS
T210 RMRVTPSTPSPRGSL
S212 RVTPSTPSPRGSLST
S218 PSPRGSLSTTSHFSS
T220 PRGSLSTTSHFSSQA
S225 STTSHFSSQAQTPIQ
T229 HFSSQAQTPIQGSSD
S241 SSDLNPFSDPRQFDR
T252 QFDRSFPTLQSLTES
S259 TLQSLTESRFPEGRM
S352 AAGGGERSPTRMLTS
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