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Protein Page:
AML1 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
AML1 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. 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. Interaction with CDK6 prevents myeloid differentiation, reducing its transcription transactivation activity. Expressed in all tissues examined except brain and heart. Highest levels in thymus, bone marrow and peripheral blood. 11 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Transcription factor; DNA binding protein
Cellular Component: basement membrane; nucleus
Molecular Function: protein binding; protein homodimerization activity; DNA binding; protein heterodimerization activity; calcium ion binding; transcription factor activity; transcription factor binding; ATP binding
Biological Process: central nervous system development; hair follicle morphogenesis; transcription, DNA-dependent; embryonic hemopoiesis; in utero embryonic development; positive regulation of transcription, DNA-dependent; positive regulation of granulocyte differentiation; regulation of signal transduction; liver development; negative regulation of granulocyte differentiation; peripheral nervous system neuron development; behavioral response to pain; positive regulation of angiogenesis; myeloid progenitor cell differentiation; hemopoiesis; myeloid cell differentiation; positive regulation of transcription from RNA polymerase II promoter; skeletal development
Reference #:  Q01196 (UniProtKB)
Alt. Names/Synonyms: Acute myeloid leukemia 1 protein; AML1; aml1 oncogene; AML1-EVI-1 fusion partner; AMLCR1; CBF-alpha-2; CBFA2; Core-binding factor subunit alpha-2; core-binding factor, runt domain, alpha subunit 2; EVI-1; Oncogene AML-1; PEA2-alpha B; PEBP2-alpha B; PEBP2aB; Polyomavirus enhancer-binding protein 2 alpha B subunit; Runt-related transcription factor 1; RUNX1; SL3-3 enhancer factor 1 alpha B subunit; SL3/AKV core-binding factor alpha B subunit
Gene Symbols: RUNX1
Molecular weight: 48,737 Da
Basal Isoelectric point: 9.4  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

AML1

Protein Structure Not Found.


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Sites Implicated In
cell growth, altered: S249‑p, S266‑p
transcription, altered: S249‑p, S266‑p
activity, induced: S249‑p, S266‑p
molecular association, regulation: S249‑p, S266‑p, T273‑p
phosphorylation: S249‑p, S266‑p, T273‑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

► Hide Isoforms
 
0 23 T14-p ASTSRRFtPPstALs
0 2 S17-p SRRFtPPstALsPGk
0 5 T18-p RRFtPPstALsPGkM
2 23 S21-p tPPstALsPGkMSEA
1 5 K24-a stALsPGkMSEALPL
1 5 K43-a AGAALAGkLRSGDRS
0 1 K43-u AGAALAGkLRSGDRS
0 2 K125-u RNATAAMkNQVARFN
0 7 K188-u QKLDDQTkPGsLsFS
0 3 S191-p DDQTkPGsLsFSERL
0 1 S193-p QTkPGsLsFSERLsE
0 2 S199-p LsFSERLsELEQLRr
1 0 R206-m sELEQLRrTAMrVsP
1 0 R210-m QLRrTAMrVsPHHPA
0 9 S212-p RrTAMrVsPHHPAPt
0 2 T219-p sPHHPAPtPNPRASL
0 16 S238-p AFNPQPQsQMQDTRQ
9 47 S249-p DTRQIQPsPPWsyDQ
0 5 S253-p IQPsPPWsyDQsYQY
0 2 Y254-p QPsPPWsyDQsYQYL
0 3 S257-p PPWsyDQsYQYLGsI
0 3 S263-p QsYQYLGsIAsPsVH
7 26 S266-p QYLGsIAsPsVHPAt
0 4 S268-p LGsIAsPsVHPAtPI
6 5 T273-p sPsVHPAtPIsPGRA
11 67 S276-p VHPAtPIsPGRASGM
0 7 T296-p ELSSRLStAPDLTAF
0 1 R319-m2 LPSISDPrMHYPGAF
2 2 S397-p SMVGGERsPPRILPP
3 0 S435 AEGSHSNSPTNMAPS
0 1 - gap
0 17 Y453-p EEAVWRPy_______
4327 : Phospho-AML1 (Ser249) Antibody
  AML1 iso2  
T14 ASTSRRFTPPSTALS
S17 SRRFTPPSTALSPGK
T18 RRFTPPSTALSPGKM
S21 TPPSTALSPGKMSEA
K24 STALSPGKMSEALPL
K43 AGAALAGKLRSGDRS
K43 AGAALAGKLRSGDRS
K125 RNATAAMKNQVARFN
K188 QKLDDQTKPGSLSFS
S191 DDQTKPGSLSFSERL
S193 QTKPGSLSFSERLSE
S199 LSFSERLSELEQLRR
R206 SELEQLRRTAMRVSP
R210 QLRRTAMRVSPHHPA
S212 RRTAMRVSPHHPAPT
T219 SPHHPAPTPNPRASL
S238 AFNPQPQSQMQDTRQ
S249 DTRQIQPSPPWSYDQ
S253 IQPSPPWSYDQSYQY
Y254 QPSPPWSYDQSYQYL
S257 PPWSYDQSYQYLGSI
S263 QSYQYLGSIASPSVH
S266 QYLGSIASPSVHPAT
S268 LGSIASPSVHPATPI
T273 SPSVHPATPISPGRA
S276 VHPATPISPGRASGM
T296 ELSSRLSTAPDLTAF
R319 LPSISDPRMHYPGAF
S397 SMVGGERSPPRILPP
S435 AEGSHSNSPTNMGGA
T458-p DPGPWARtPSWGRGR
- gap
  AML1 iso8  
T41 ASTSRRFTPPSTALs
S44 SRRFTPPSTALsPGK
T45 RRFTPPSTALsPGKM
S48-p TPPSTALsPGKMSEA
K51 STALsPGKMSEALPL
K70 AGAALAGKLRSGDRS
K70 AGAALAGKLRSGDRS
K152 RNATAAMKNQVARFN
K215 QKLDDQTKPGSLSFS
S218 DDQTKPGSLSFSERL
S220 QTKPGSLSFSERLSE
S226 LSFSERLSELEQLRR
R233 SELEQLRRTAMRVSP
R237 QLRRTAMRVSPHHPA
S239 RRTAMRVSPHHPAPT
T246 SPHHPAPTPNPRASL
S265 AFNPQPQSQMQDTRQ
S276-p DTRQIQPsPPWSYDQ
S280 IQPsPPWSYDQSYQY
Y281 QPsPPWSYDQSYQYL
S284 PPWSYDQSYQYLGSI
S290 QSYQYLGSIAsPSVH
S293-p QYLGSIAsPSVHPAt
S295 LGSIAsPSVHPAtPI
T300-p sPSVHPAtPIsPGRA
S303-p VHPAtPIsPGRASGM
T323-p ELSSRLStAPDLTAF
R346 LPSISDPRMHYPGAF
S424-p SMVGGERsPPRILPP
S462-p AEGSHSNsPTNMAPS
- gap
Y480 EEAVWRPY_______
  mouse

 
T14-p ASTSRRFtPPstALs
S17-p SRRFtPPstALsPGK
T18-p RRFtPPstALsPGKM
S21-p tPPstALsPGKMSEA
K24 stALsPGKMSEALPL
K43 GGPALASKLRSGDRS
K43 GGPALASKLRSGDRS
K125 RNATAAMKNQVARFN
K188 QKLDDQTKPGSLSFS
S191 DDQTKPGSLSFSERL
S193 QTKPGSLSFSERLsE
S199-p LSFSERLsELEQLRR
R206 sELEQLRRTAMRVsP
R210 QLRRTAMRVsPHHPA
S212-p RRTAMRVsPHHPAPT
T219 sPHHPAPTPNPRASL
S238 AFNPQPQSQMQDARQ
S249-p DARQIQPsPPWSYDQ
S253 IQPsPPWSYDQSYQY
Y254 QPsPPWSYDQSYQYL
S257 PPWSYDQSYQYLGSI
S263 QSYQYLGSITSSSVH
S266 QYLGSITSSSVHPAt
S268 LGSITSSSVHPAtPI
T273-p SSSVHPAtPIsPGRA
S276-p VHPAtPIsPGRASGM
T296 ELSSRLSTAPDLTAF
R319 LPSISDPRMHYPGAF
S396 SMVGGERSPPRILPP
S434-p TEGSHSNsPTNMPPA
- gap
Y451 EEAVWRPY_______
  rat

 
T14 ASTSRRFTPPSTALS
S17 SRRFTPPSTALSPGK
T18 RRFTPPSTALSPGKM
S21 TPPSTALSPGKMSEA
K24 STALSPGKMSEALPL
K43 GGAALASKLRSGDRS
K43 GGAALASKLRSGDRS
K125 RNATAAMKNQVARFN
K188 QKLDDQTKPGSLSFS
S191 DDQTKPGSLSFSERL
S193 QTKPGSLSFSERLSE
S199 LSFSERLSELEQLRR
R206 SELEQLRRTAMRVSP
R210 QLRRTAMRVSPHHPA
S212 RRTAMRVSPHHPAPT
T219 SPHHPAPTPNPRASL
S238 AFNPQPQSQMQDARQ
S249 DARQIQPSPPWSYDQ
S253 IQPSPPWSYDQSYQY
Y254 QPSPPWSYDQSYQYL
S257 PPWSYDQSYQYLGSI
S263 QSYQYLGSITSSVHP
S266 QYLGSITSSVHPATP
- gap
T272 TSSVHPATPISPGRA
S275 VHPATPISPGRASGM
T295 ELSSRLSTAPDLTAF
R318 LPSISDPRMHYPGAF
S395 SMVGGERSPPRILPP
S433 TEGSHSNSPTNMPPA
- gap
Y450 EEAVWRPY_______
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