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Protein Page:
ELP3 (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
ELP3 a histone acetyltransferase. A subunit of the Elongator complex, which associates with the elongating, hyperphosphorylated form of RNA polymerase II. Note: This description may include information from UniProtKB.
Protein type: EC 2.3.1.48; Acetyltransferase
Chromosomal Location of Human Ortholog: 8p21.1
Cellular Component: transcription elongation factor complex; Elongator holoenzyme complex; cytoplasm; nucleolus; DNA-directed RNA polymerase II, holoenzyme
Molecular Function: protein binding; histone acetyltransferase activity; DNA binding; metal ion binding; iron-sulfur cluster binding; phosphorylase kinase regulator activity
Biological Process: regulation of transcription from RNA polymerase II promoter; establishment and/or maintenance of chromatin architecture; RNA elongation from RNA polymerase II promoter; histone acetylation; regulation of protein kinase activity; positive regulation of cell migration
Reference #:  Q9H9T3 (UniProtKB)
Alt. Names/Synonyms: elongation protein 3 homolog (S. cerevisiae); Elongator complex protein 3; ELP3; FLJ10422; hELP3; KAT9
Gene Symbols: ELP3
Molecular weight: 62,259 Da
Basal Isoelectric point: 9.04  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

ELP3

Protein Structure Not Found.


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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 5 K34-ub IEAHEQGkDIDLNkV
0 2 K40-ub GkDIDLNkVKTKTAA
0 3 K48-ub VKTKTAAkYGLSAQP
0 32 K77-ub KVLMPKLkAKPIRTA
0 1 K156-ub RHRIEQLkQLGHsVD
0 2 S161-p QLkQLGHsVDKVEFI
0 1 T197-p HDALSGHtSNNIyEA
0 347 Y202-p GHtSNNIyEAVkySE
0 2 K206-ub NNIyEAVkySERSLT
0 1 Y207-p NIyEAVkySERSLTK
0 1 K229-m1 TRPDYCMkRHLSDML
0 2 Y251-p EIGVQSVyEDVARDT
0 1 K280-ac LAKDSGFkVVAHMMP
0 1 K316-ub AFRPDGLkLyPTLVI
0 3 Y318-p RPDGLkLyPTLVIRG
0 114 Y329-p VIRGTGLyELWkSGR
0 3 K333-ub TGLyELWkSGRYkSY
0 2 K338-ub LWkSGRYkSYSPSDL
0 1 T360-p LALVPPWtRVYRVQR
0 2 K392-ub ELALARMkDLGIQCR
0 1 Y427-p VELVRRDyVANGGWE
0 1 S470 FELGGGVSIVRELHV
0 1 K491-ub VSSRDPTkFQHQGFG
0 1 K517-ub REEHGSGkIAVISGV
  mouse

 
K34-ub VEAHEQGkDVDLNkM
K40-ub GkDVDLNkMKTKTAA
K48-ub MKTKTAAkYGLASQP
K77 KILIPKLKAKPVRTA
K156 RHRIEQLKQLGHsVD
S161-p QLKQLGHsVDKVEFI
T197 HDALSGHTSNNIHEA
H202 GHTSNNIHEAIKYSE
K206 NNIHEAIKYSERSFT
Y207 NIHEAIKYSERSFTK
K229 TRPDYCMKRHLSDML
Y251 EIGVQSVYEDVARDT
K280-ac LAKDSGFkVVTHMMP
K316 AFRPDGLKLYPTLVI
Y318 RPDGLKLYPTLVIRG
Y329-p VIRGTGLyELWkSGR
K333-ub TGLyELWkSGRYRSY
R338 LWkSGRYRSYSPSDL
T360 LALVPPWTRVYRVQR
K392-ub ELAFARMkDLGIQCR
Y427 VELVRRDYVANGGWE
S470-p FELGGGVsIVRELHV
K491 VSSRDPTKFQHQGFG
K517 REEHGSGKMAVISGV
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