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Protein Page:
ELP3 (human)
rdtyret
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
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: cytoplasm; Elongator holoenzyme complex; histone acetyltransferase complex; nucleolus; transcription elongation factor complex
Molecular Function: H3 histone acetyltransferase activity; H4 histone acetyltransferase activity; iron-sulfur cluster binding; metal ion binding; phosphorylase kinase regulator activity; protein binding
Biological Process: central nervous system development; establishment and/or maintenance of chromatin architecture; neuron migration; positive regulation of cell migration; regulation of protein kinase activity; regulation of transcription from RNA polymerase II promoter; RNA elongation from RNA polymerase II promoter; tRNA wobble uridine modification
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  
Click here to view other types of protein modifications

Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

Show Multiple Sequence Alignment


 LTP 

LTP: 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.


 HTP 

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


       human

 
0 6 K34‑ub IEAHEQGkDIDLNkV
0 2 K40‑ub GkDIDLNkVKTKTAA
0 4 K48‑ub VKTKTAAkYGLSAQP
0 1 A53 AAkYGLSAQPRLVDI
0 32 K77‑ub KVLMPKLkAKPIRTA
0 1 K156‑ub RHRIEQLkQLGHsVD
0 2 S161‑p QLkQLGHsVDKVEFI
0 1 T197‑p HDALSGHtSNNIyEA
0 349 Y202‑p GHtSNNIyEAVkySE
0 3 K206‑ub NNIyEAVkySERSLT
0 1 Y207‑p NIyEAVkySERSLTK
0 1 K229‑m1 TRPDYCMkRHLSDML
0 2 Y251‑p EIGVQSVyEDVARDT
0 1 K275‑ub CESFHLAkDSGFkVV
0 1 K280‑ac LAkDSGFkVVAHMMP
0 1 K316‑ub AFRPDGLkLyPTLVI
0 3 Y318‑p RPDGLkLyPTLVIRG
0 115 Y329‑p VIRGTGLyELWkSGR
0 4 K333‑ub TGLyELWkSGRYkSY
0 2 K338‑ub LWkSGRYkSYSPSDL
0 1 T360‑p LALVPPWtRVYRVQR
0 2 K392‑ub ELALARMkDLGIQCR
0 1 K414‑ub GIQEIHHkVRPYQVE
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
S53‑p AAkYGLAsQPRLVDI
K77 KILIPKLKAKPVRTA
K156 RHRIEQLKQLGHsVD
S161‑p QLKQLGHsVDKVEFI
T197 HDALSGHTSNNIHEA
H202 GHTSNNIHEAIKYSE
K206 NNIHEAIKYSERSFT
Y207 NIHEAIKYSERSFTK
K229 TRPDYCMKRHLSDML
Y251 EIGVQSVYEDVARDT
K275 CESFHLAKDSGFkVV
K280‑ac LAKDSGFkVVTHMMP
K316 AFRPDGLKLYPTLVI
Y318 RPDGLKLYPTLVIRG
Y329‑p VIRGTGLyELWkSGR
K333‑ub TGLyELWkSGRYRSY
R338 LWkSGRYRSYSPSDL
T360 LALVPPWTRVYRVQR
K392‑ub ELAFARMkDLGIQCR
R414 GIQEIHHRVRPYQVE
Y427 VELVRRDYVANGGWE
S470‑p FELGGGVsIVRELHV
K491 VSSRDPTKFQHQGFG
K517 REEHGSGKMAVISGV
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