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Protein Page:
SMYD3 (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
SMYD3 Histone methyltransferase. Specifically methylates 'Lys- 4' of histone H3, inducing di- and tri-methylation, but not monomethylation. Plays an important role in transcriptional activation as a member of an RNA polymerase complex. Binds DNA containing 5'-CCCTCC-3' or 5'-GAGGGG-3' sequences. Belongs to the histone-lysine methyltransferase family. 3 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Methyltransferase; EC 2.1.1.43; Methyltransferase, protein lysine
Chromosomal Location of Human Ortholog: 1q44
Cellular Component: cytoplasm; nucleus
Molecular Function: metal ion binding; histone-lysine N-methyltransferase activity
Reference #:  Q9H7B4 (UniProtKB)
Alt. Names/Synonyms: bA74P14.1; bA74P14.1 (novel protein); FLJ21080; KMT3E; MGC104324; SET and MYND domain containing 3; SET and MYND domain-containing protein 3; SMYD3; Zinc finger MYND domain-containing protein 1; zinc finger protein, subfamily 3A (MYND domain containing), 1; zinc finger, MYND domain containing 1; ZMYND1; ZNFN3A1
Gene Symbols: SMYD3
Molecular weight: 49,097 Da
Basal Isoelectric point: 7.05  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

SMYD3

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 4 T22-p GNGLRAVtPLRPGEL
0 1 K122-ub GAPSESEkLySFYDL
0 12 Y124-p PSESEkLySFYDLES
0 11 Y127 SEkLySFYDLESNIN
1 0 Y239-p GEELTICyLDMLMTS
0 2 K378-ub VQVMKVGkLQLHQGM
0 1 K391-ub GMFPQAMkNLRLAFD
  mouse

 
A22 GNGLRAVAPLRPGEL
K122 EKPSESEKLYSFYDL
Y124 PSESEKLYSFYDLES
Y127 SEKLYSFYDLESNIS
Y239 GEELTICYLDMLMTS
K378-ub VQVMKVGkLQLHQGM
K391 GMFPQAMKNLRLAFD
  rat

 
A22 GNGLRAVAPLRPGEL
K122 GKPSESEKLySFyDL
Y124-p PSESEKLySFyDLES
Y127-p SEKLySFyDLESNIS
Y239 GEELTICYLDMLMTS
K378 VQVMKVGKLQLHQGM
K391 GMFPQAMKNLRLAFD
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