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Information on EC 2.1.1.77 - protein-L-isoaspartate(D-aspartate) O-methyltransferase and Organism(s) Homo sapiens and UniProt Accession P22061
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EC Tree
2.1.1.77 protein-L-isoaspartate(D-aspartate) O-methyltransferaseIUBMB Comments
D-Aspartate (but not L-aspartate) residues in proteins can also act as acceptors. Previously also listed as EC 2.1.1.24.
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Word Map
- 2.1.1.77
-
deamidation
- centrosome
-
isomerized
-
age-damaged
- s-adenosylhomocysteine
- adomet
-
pericentriolar
-
l-asparaginyl
-
methyl-accepting
-
adohcy
-
centriolar
- s-adenosyl-l-homocysteine
-
3h-methylated
- succinimide
-
s-adenosyl-l-methyl-3hmethionine
-
dauers
- pericentrin
- medicine
-
dynactin
- biotechnology
- molecular biology
- nutrition
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
pcm-1, pcmt1, protein l-isoaspartyl methyltransferase, l-isoaspartyl methyltransferase, pimt1, protein-l-isoaspartate (d-aspartate) o-methyltransferase, protein l-isoaspartate (d-aspartate) o-methyltransferase, protein-l-isoaspartyl methyltransferase, protein isoaspartyl methyltransferase, pimt2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D-aspartyl/L-isoaspartyl methyltransferase
-
-
-
-
L-aspartyl/L-isoaspartyl protein methyltransferase
-
-
-
-
L-isoaspartyl/D-aspartyl protein carboxyl methyltransferase
-
-
-
-
methyltransferase, protein (D-aspartate)
-
-
-
-
PIMT
-
-
protein (L-isoaspartate) O-methyltransferase
-
-
-
-
protein D-aspartate methyltransferase
-
-
-
-
protein L-isoaspartate (D-aspartate) O-methyltransferase
-
-
protein L-isoaspartate methyltransferase
-
-
-
-
protein L-isoaspartyl methyltransferase
protein-beta-aspartate O-methyltransferase
-
-
-
-
protein-L-isoaspartate O-methyltransferase
-
-
-
-
protein L-isoaspartyl methyltransferase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:protein-L-isoaspartate O-methyltransferase
D-Aspartate (but not L-aspartate) residues in proteins can also act as acceptors. Previously also listed as EC 2.1.1.24.
CAS REGISTRY NUMBER
COMMENTARY
105638-50-4
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + protein D-aspartate
S-adenosyl-L-homocysteine + protein D-aspartate methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
S-adenosyl-L-methionine + 7-nitro-2,1,3-benzoxadiazole-delta sleep-inducing peptide-L-isoaspartate
S-adenosyl-L-homocysteine + 7-nitro-2,1,3-benzoxadiazole-delta sleep-inducing peptide-L-isoaspartate alpha-methyl ester
-
-
-
-
?
S-adenosyl-L-methionine + 7-nitro-2,1,3-benzoxadiazole-labeled delta sleep-inducing peptide L-isoaspartate
S-adenosyl-L-homocysteine + 7-nitro-2,1,3-benzoxadiazole-labeled delta sleep-inducing peptide L-isoaspartate methyl ester
-
-
-
-
?
S-adenosyl-L-methionine + acid trehalase D-aspartate
S-adenosyl-L-homocysteine + acid trehalase D-aspartate methyl ester
-
-
-
-
?
S-adenosyl-L-methionine + actin L-isoaspartate
S-adenosyl-L-homocysteine + actin L-isoaspartate alpha-methyl ester
-
-
-
-
?
S-adenosyl-L-methionine + Bcl-xL L-isoaspartate
S-adenosyl-L-homocysteine + Bcl-xL L-isoaspartate alpha-methyl ester
-
-
-
-
?
S-adenosyl-L-methionine + beta-101-lysozyme
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + calmodulin
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + delta-sleep-inducing peptide L-isoaspartate
S-adenosyl-L-homocysteine + delta-sleep-inducing peptide L-aspartate alpha-methyl ester
-
-
-
-
?
S-adenosyl-L-methionine + DR-Oct-VYPisoDHA
S-adenosyl-L-homocysteine + DR-Oct-VYPisoD(Me)HA
-
-
-
-
-
S-adenosyl-L-methionine + GFDL-isoD-GGGVG
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + histidine phosphocarrier protein (isoAsp-38)
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + histidine phosphocarrier protein-1 (isoAsp-38)
?
-
-
-
-
?
S-adenosyl-L-methionine + histidine phosphocarrier protein-2 (isoAsp-12,-38)
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + histone H2B L-isoaspartate
S-adenosyl-L-homocysteine + histone H2B L-isoaspartate alpha-methyl ester
-
-
-
-
?
S-adenosyl-L-methionine + histone H4 D-aspartate
S-adenosyl-L-homocysteine + histone H4 D-aspartate methyl ester
-
-
-
-
?
S-adenosyl-L-methionine + Hsp70 L-isoaspartate
S-adenosyl-L-homocysteine + Hsp70 L-isoaspartate alpha-methyl ester
-
-
-
-
?
S-adenosyl-L-methionine + Hsp90 L-isoaspartate
S-adenosyl-L-homocysteine + Hsp90 L-isoaspartate alpha-methyl ester
-
-
-
-
?
S-adenosyl-L-methionine + isoAsp-DSIP
S-adenosyl-L-homocysteine + isoAsp-alpha-methyl ester-DSIP
-
-
-
-
?
S-adenosyl-L-methionine + KASA (D-Asp) LAKY
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + KASA-L-isoAsp-LAKY
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + KMK-isoD-TDSEEEIR
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + KQVV-isoD-SAYEVIK
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + LSH-isoD-GY-Cya-L
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + N-succinyl-AAVA-p-nitroanilide
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + native lysozyme
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + ovalbumin
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + ovalbumin L-isoaspartate
S-adenosyl-L-homocysteine + ovalbumin L-isoaspartate alpha-methyl ester
-
-
-
-
?
S-adenosyl-L-methionine + protein D-aspartate
S-adenosyl-L-homocysteine + protein D-aspartate beta-methyl ester
S-adenosyl-L-methionine + protein D-aspartate
S-adenosyl-L-homocysteine + protein D-aspartate methyl ester
-
-
-
-
?
S-adenosyl-L-methionine + protein D-isoaspartate
S-adenosyl-L-homocysteine + protein D-isoaspartate alpha-methyl ester
-
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate methyl ester
-
-
-
-
?
S-adenosyl-L-methionine + protein p53
S-adenosyl-L-homocysteine + ?
-
the enzyme mediates methylation of protein p53 at isoaspartate residues 29 and 30
-
-
?
S-adenosyl-L-methionine + VYP-isoD-Cya-G
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + VYP-L-isoAsp-GA
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + VYP-L-isoAsp-HA
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + YVS-isoAsp-GHG
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + YVS-isoD-G-Cya-G
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
-
-
?
S-adenosyl-L-methionine + KASA (isoD) LAKY
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + KASA (isoD) LAKY
S-adenosyl-L-homocysteine + ?
-
synthetic methyl acceptor
-
-
?
S-adenosyl-L-methionine + protein D-aspartate
S-adenosyl-L-homocysteine + protein D-aspartate beta-methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein D-aspartate
S-adenosyl-L-homocysteine + protein D-aspartate beta-methyl ester
-
-
-
-
?
S-adenosyl-L-methionine + protein D-aspartate
S-adenosyl-L-homocysteine + protein D-aspartate beta-methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein D-aspartate
S-adenosyl-L-homocysteine + protein D-aspartate beta-methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein D-aspartate
S-adenosyl-L-homocysteine + protein D-aspartate beta-methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein D-aspartate
S-adenosyl-L-homocysteine + protein D-aspartate beta-methyl ester
-
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
701664, 701684, 702014, 702015, 703773, 706709, 733125, 733251, 733992, 735263, 755789, 756673, 756674, 756902, 757656, 757812, 758169
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
involved in the repair of age-damaged proteins, aspartyl and asparginyl residues that are susceptible to deamidation, isomerization and racemization
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
repair enzyme that acts upon damaged proteins bearing abnormal aspartyl residues
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
PCMT catalyzes methyl esterification of the free alpha-carboxyl group at the isoaspartyl site, thus initiating the repair of the abnormal protein through the conversion of the isopeptide bond into a normal alpha-peptide bond
-
-
?
additional information
?
-
protein L-Asp and protein D-isoaspartate are no substrates
-
-
?
additional information
?
-
-
protein L-Asp and protein D-isoaspartate are no substrates
-
-
?
additional information
?
-
no activity with VYP-D-beta-Asp-GA and VYP-L-alpha-Asp-GA
-
-
?
additional information
?
-
-
no activity with VYP-D-beta-Asp-GA and VYP-L-alpha-Asp-GA
-
-
?
additional information
?
-
-
native E. coli histidine phosphocarrier protein is no substrate
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + protein D-aspartate
S-adenosyl-L-homocysteine + protein D-aspartate methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
S-adenosyl-L-methionine + acid trehalase D-aspartate
S-adenosyl-L-homocysteine + acid trehalase D-aspartate methyl ester
-
-
-
-
?
S-adenosyl-L-methionine + histone H4 D-aspartate
S-adenosyl-L-homocysteine + histone H4 D-aspartate methyl ester
-
-
-
-
?
S-adenosyl-L-methionine + protein D-aspartate
S-adenosyl-L-homocysteine + protein D-aspartate methyl ester
-
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate methyl ester
-
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
involved in the repair of age-damaged proteins, aspartyl and asparginyl residues that are susceptible to deamidation, isomerization and racemization
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
repair enzyme that acts upon damaged proteins bearing abnormal aspartyl residues
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
PCMT catalyzes methyl esterification of the free alpha-carboxyl group at the isoaspartyl site, thus initiating the repair of the abnormal protein through the conversion of the isopeptide bond into a normal alpha-peptide bond
-
-
?
additional information
?
-
protein L-Asp and protein D-isoaspartate are no substrates
-
-
?
additional information
?
-
-
protein L-Asp and protein D-isoaspartate are no substrates
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.055
7-nitro-2,1,3-benzoxadiazole-delta sleep-inducing peptide -L-isoaspartate
-
in 0.1 M sodium phosphate (pH 6.8), 1 mM EGTA, 0.004% (w/v) sodium azide, and 0.16% (v/v) Triton X-100, at 37°C
0.055
7-nitro-2,1,3-benzoxadiazole-labeled delta sleep-inducing peptide L-isoaspartate
-
pH not specified in the publication, at 37°C
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0026
Nalpha-benzyloxycarbonyl-O-benzyl-L-Asp-Nepsilon-L-Lys-L-Tyr-L-Ala-amide
Homo sapiens
-
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
69% reduced PIMT expression as compared to normal brains
-
treatment of astrocytoma cells (U-87) with direct pharmacological GSK-3 inhibitors stimulate PIMT expression (2fold). Results demonstrate regulation of PIMT expression by GSK-3 inhibitor lithium at both the transcriptional and the translational levels. Inhibition by siRNA of GSK-3 and beta-catenin modulates expression of the PIMT in accordance with GSK-3 pharmacological inhibition. Valproic acid up-regulates phospho-GSK-3b (Ser9), beta-catenin and PIMT levels similarly to lithium
-
-
485591, 485593, 485594, 485595, 485596, 485597, 485598, 485600, 485605, 485611, 485613, 485614, 485615, 485617, 659913
-
-
485591, 485593, 485594, 485595, 485596, 485597, 485598, 485600, 485605, 485610, 485613, 485615, 485617
-
76% reduced PIMT expression as compared to normal brain
-
enzyme expression and enzyme activity are significantly decreased in all grades of tumors, 76% reduced PIMT expression in pilocytic astrocytomas (grade I), 46% reduced PIMT expression in astrocytomas (grade II), 69% reduced PIMT expression in anaplastic astrocytomas (grade III), 80% reduced PIMT expression in glioblastomas (grade IV) as compared to normal brains
-
enzyme expression and enzyme activity are significantly decreased in all grades of tumors, 76% reduced PIMT expression in pilocytic astrocytomas (grade I), 46% reduced PIMT expression in astrocytomas (grade II), 69% reduced PIMT expression in anaplastic astrocytomas (grade III)
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
PIMT-knockdown cells show significant accumulation of proteins with isomerized residues, compared to control cells
malfunction
-
enzyme depletion upregulates the proapoptotic and checkpoint activation functions of p53
malfunction
-
silencing enzym expression results in the accumulation of proteins with racemized or isomerized Asp residues. Suppression of enzyme expression leads to epidermal growth factor-stimulated hyperactivation of the MAP-kinase
malfunction
-
dopamine-associated enzyme downregulation leads to neuronal cell apoptosis
malfunction
-
enzyme down-regulation in HUVEC cells inhibits both cell migration and tube formation in vitro when stimulated by vascular endothelial growth factor
physiological function
-
PCMT maintains the functional stability of antiapoptotic proteins, PCMT when overexpressed in endothelial cells is able to prevent apoptosis induced by H2O2 treatment
physiological function
-
PCMT1 repairs proteins that have been damaged by deamidation of asparagine or isomerization of aspartate, resulting in the spontaneous generation of L-isoaspartyl residues within peptides and proteins during aging
physiological function
-
PIMT repair of abnormal proteins is necessary to maintain normal mitogen-activated protein kinase signaling
physiological function
-
protein L-isoaspartyl/D-aspartyl O-methyltransferase is a repair enzyme that initiates the conversion of L-isoaspartyl (or D-Asp) residues to L-aspartyl residues. Isomerization of Asn or Asp residues, and the repair of atypical residues by PIMT plays a role in the posttranslational regulation of protein activity. The repair of abnormal residues by the enzyme is essential for maintenance of the central nervous system
physiological function
-
the enzyme negatively regulates the tumour suppressor protein p53 by reducing p53 protein levels, thereby suppressing the p53-mediated transcription of target genes. The enzyme destabilizes p53 by enhancing the p53-HDM2 interaction
physiological function
-
the enzyme acts as a co-activator for estrogen receptor alpha-mediated transcription. Over-expression of the enzyme significantly increases the levels of trefoil factor 1 mRNA in the presence or absence of beta-estradiol
physiological function
-
the enzyme is an inhibitor of hypoxia/reoxygenation-induced activation of mammalian sterile 20-like kinase 1 and cell apoptosis in cardiomyocytes
physiological function
-
enzyme overexpression protects SH-SY5Y cells from cell death and caspase 3 activation upon dopamine treatments. Cells overexpressing enzyme produce significantly less reactive oxygen species despite dopamine treatment
physiological function
-
the enzyme has a protective role for maintenance of mitochondrial morphology in A-549 cells
physiological function
-
the enzyme is required for vascular endothelial growth factor-dependent endothelial cell migration and tubulogenesis. Enzyme overexpression promotes angiogenic properties in HUVEC cells
physiological function
-
the enzyme plays a critical role in repairing isomerized Asp residues in the cortex of lenses
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PIMT_HUMAN
227
0
24636
Swiss-Prot
other Location (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25000
27000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
V119I
the variant enzyme has lower activity and thermal stability but about 30% increased affinity for endogenous substrates compared to the I119I variant
A150V
-
the mutant shows 64% loss of activity compared to the wild type activity
D83V
L191S
-
the mutant shows 72% loss of activity compared to the wild type activity
P174H
-
the mutant shows 61% loss of activity compared to the wild type activity
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the Ile isoform of PCMT is more stable, but the Val isoform has a 30% higher affinity for protein substrates
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
southern blot analysis of PCR amplified genomic DNA, human chromosome contains a single gene encoding the enzyme, PCMT1, mapped to the q24-25 region of chromosome 6
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
5 mM valproic acid enhances protein L-isoaspartyl methyltransferase expression about 2fold through glycogen synthase kinase-3/beta-catenin requires 90 kDa ribosomal S6 kinase. Src, c-Raf, MEK1/2 and extracellular-regulated kinase 1/2 abolish the extracellular-regulated kinase 1/2 phosphorylation stimulated by valproic acid, thus preventing PIMT induction by valproic acid
-
down-regulation of PIMT by siRNA strikingly enhances phenylarsine oxide-induced reactive oxygen species
-
enzyme activity and expression are 50% lower in the hippocampus of epileptic patients
-
enzyme expression is down-regulated at both gene and protein levels by cytosolic dopamine in SH-SY5Y cells
-
PIMT is about 2fold up-regulated by 0.005 mM phenylarsine oxide in U-87 human astroglioma cells, PIMT up-regulation by phenylarsine oxide is mediated by the reaction with vicinal cysteines, PIMT induction by phenylarsine oxide is dependent on formation of reactive oxygen species, PIMT induction by phenylarsine oxide is inhibited by N-acetyl-L-cysteine and diphenyleneiodonium chloride
-
the enzyme expression is increased in patients with advanced stages of lung adenocarcinoma
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
aging research, accumulation of damaged proteins have detrimental effects over the human lifespan
medicine
-
results show that PIMT expression is up-regulated by GSK-3 inhibition and beta-catenin stabilization upon treatments with lithium and valproic acid suggesting a possible therapeutic role for PIMT in certain brain diseases including epilepsy
medicine
-
mutations in the PCMT1 gene are associated with premature ovarian failure
medicine
-
PCMT1 is associated with the type 1 diabetes in groups defined by other risk genes (SUMO4 and HLA)
medicine
-
strong enzyme expression is a predictive marker of poor prognosis for surgically resected lung adenocarcinoma
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Johnson, B.A.; Aswad, D.W.
Enzymatic protein carboxyl methylation at physiological pH: cyclic imide formation explains rapid methyl turnover
Biochemistry
24
2581-2586
1985
Bos taurus, Homo sapiens
Ota, I.M.; Ding, L.; Clarke, S.
Methylation at specific altered aspartyl and asparaginyl residues in glucagon by the erythrocyte protein carboxyl methyltransferase
J. Biol. Chem.
262
8522-8531
1987
Homo sapiens
Gilbert, J.M.; Fowler, A.; Bleibaum, J.; Clarke, S.
Purification of homologous protein carboxyl methyltransferase isozymes from human and bovine erythrocytes
Biochemistry
27
5227-5233
1988
Bos taurus, Escherichia coli, Homo sapiens, Salmonella enterica subsp. enterica serovar Typhimurium
Ota, I.M.; Gilbert, J.M.; Clarke, S.
Two major isozymes of the protein D-aspartyl/L-isoaspartyl methyltransferase from human erythrocytes
Biochem. Biophys. Res. Commun.
151
1136-1143
1988
Bos taurus, Oryctolagus cuniculus, Equus sp., Homo sapiens, Rattus norvegicus, Torpedo ocellata, Xenopus laevis
Ingrosso, D.; Fowler, A.V.; Bleibaum, J.; Clarke, S.
Sequence of the D-aspartyl/L-isoaspartyl protein methyltransferase from human erythrocytes. Common sequence motifs for protein, DNA, RNA, and small molecule S-adenosylmethionine-dependent methyltransferases
J. Biol. Chem.
264
20131-20139
1989
Bos taurus, Escherichia coli, Homo sapiens, Rattus norvegicus, Salmonella enterica subsp. enterica serovar Typhimurium
Lowenson, J.D.; Clarke, S.
Identification of isoaspartyl-containing sequences in peptides and proteins that are usually poor substrates for the class II protein carboxyl methyltransferase
J. Biol. Chem.
265
3106-3110
1990
Bos taurus, Homo sapiens
Fu, J.C.; Ding, L.; Clarke, S.
Purification, gene cloning, and sequence analysis of an L-isoaspartyl protein carboxyl methyltransferase from Escherichia coli [published erratum appears in J Biol Chem 1992 Jun 5;267(16):11660]
J. Biol. Chem.
266
14562-14572
1991
Bos taurus, Escherichia coli, Homo sapiens, Salmonella enterica subsp. enterica serovar Typhimurium
Ingrosso, D.; Kagan, R.M.; Clarke, S.
Distinct C-terminal sequences of isozymes I and II of the human erythrocyte L-isoaspartyl/D-aspartyl protein methyltransferase [published erratum appears in Biochem Biophys Res Commun 1991 Apr 15;176(1):549]
Biochem. Biophys. Res. Commun.
175
351-358
1991
Bos taurus, Oryctolagus cuniculus, Drosophila melanogaster, Escherichia coli, Homo sapiens, Mus musculus, Rattus norvegicus, Salmonella enterica subsp. enterica serovar Typhimurium
Brennan, T.V.; Anderson, J.W.; Jia, Z.; Waygood, E.B.; Clarke, S.
Repair of spontaneously deamidated HPr phosphocarrier protein catalyzed by the L-isoaspartate-(D-aspartate) O-methyltransferase
J. Biol. Chem.
269
24586-24595
1994
Homo sapiens
Boivin, D.; Bilodeau, D.; Beliveau, R.
Immunochemical characterization of L-isoaspartyl-protein carboxyl methyltransferase from mammalian tissues
Biochem. J.
309
993-998
1995
Bos taurus, Gallus gallus, Homo sapiens, Oryctolagus cuniculus, Rattus norvegicus, Rattus norvegicus Sprague-Dawley, Torpedo ocellata, Triticum aestivum, Xenopus laevis
-
Mudgett, M.B.; Clarke, S.
A distinctly regulated protein repair L-isoaspartylmethyltransferase from Arabidopsis thaliana
Plant Mol. Biol.
30
723-737
1996
Arabidopsis thaliana, Escherichia coli, Homo sapiens, Mus musculus, Triticum aestivum
Ichikawa, J.K.; Clarke, S.
A highly active protein repair enzyme from an extreme thermophile: the L-isoaspartyl methyltransferase from Thermotoga maritima
Arch. Biochem. Biophys.
358
222-231
1998
Archaeoglobus fulgidus, Caenorhabditis elegans, Escherichia coli, Homo sapiens, Methanocaldococcus jannaschii, Methanothermobacter thermautotrophicus, Mus musculus, no activity in Aquifex aeolicus, no activity in Bacillus subtilis, no activity in Borrelia burgdorferi, no activity in Haemophilus influenzae, no activity in Mycoplasma genitalium, no activity in Mycoplasma pneumoniae, no activity in Sinorhizobium meliloti, no activity in Treponema pallidum, Rattus norvegicus, Thermotoga maritima, Triticum aestivum
O'Connor, M.B.; O'Connor, C.M.
Complex interactions of the protein L-isoaspartyl methyltransferase and calmodulin revealed with the yeast two-hybrid system
J. Biol. Chem.
273
12909-12913
1998
Escherichia coli, Homo sapiens
DeVry, C.G.; Clarke, S.
Polymorphic forms of the protein L-isoaspartate (D-aspartate) O-methyltransferase involved in the repair of age-damaged proteins
J. Hum. Genet.
44
275-288
1999
Homo sapiens, Mus musculus
Niewmierzycka, A.; Clarke, S.
Do damaged proteins accumulate in Caenorhabditis elegans L-isoaspartate methyltransferase (pcm-1) deletion mutants?
Arch. Biochem. Biophys.
364
209-218
1999
Caenorhabditis elegans, Escherichia coli, Homo sapiens, Mus musculus
Thapar, N.; Clarke, S.
Expression, Purification, and Characterization of the Protein Repair L-Isoaspartyl Methyltransferase from Arabidopsis thaliana
Protein Expr. Purif.
20
237-251
2000
Arabidopsis thaliana, Caenorhabditis elegans, Drosophila melanogaster, Escherichia coli, Homo sapiens, Oryza sativa, Rattus norvegicus, Solanum lycopersicum, Thermotoga maritima, Triticum aestivum, Xenopus laevis, Zea mays
Lowenson, J.D.; Kim, E.; Young, S.G.; Clarke, S.
Limited accumulation of damaged proteins in L-isoaspartyl (D-aspartyl) O-methyltransferase-deficient mice
J. Biol. Chem.
276
20695-20702
2001
Homo sapiens, Mus musculus, Xenopus laevis
Thapar, N.; Kim, A.K.; Clarke, S.
Distinct patterns of expression but similar biochemical properties of protein L-isoaspartyl methyltransferase in higher plants
Plant Physiol.
125
1023-1035
2001
Arabidopsis thaliana, Caenorhabditis elegans, Caenorhabditis elegans N2, Daucus carota, Escherichia coli, Homo sapiens, Oryza sativa, Oryza sativa M-101, Triticum aestivum, Zea mays
Ryttersgaard, C.; Griffith, S.C.; Sawaya, M.R.; MacLaren, D.C.; Clarke, S.; Yeates, T.O.
Crystal structure of human L-isoaspartyl methyltransferase
J. Biol. Chem.
277
10642-10646
2002
Homo sapiens
Smith, C.D.; Carson, M.; Friedman, A.M.; Skinner, M.M.; Delucas, L.; Chantalat, L.; Weise, L.; Shirasawa, T.; Chattopadhyay, D.
Crystal structure of human L-isoaspartyl-O-methyltransferase with S-adenosyl homocysteine at 1.6-.ANG. resolution and modeling of an isoaspartyl-containing peptide at the active site
Protein Sci.
11
625-635
2002
Homo sapiens, Thermotoga maritima
Thapar, N.; Griffith, S.C.; Yeates, T.O.; Clarke, S.
Protein repair methyltransferase from the hyperthermophilic archaeon Pyrococcus furiosus: unusual methyl-accepting affinity for D-aspartyl and N-succinyl-containing peptides
J. Biol. Chem.
277
1058-1065
2002
Arabidopsis thaliana, Caenorhabditis elegans, Escherichia coli, Homo sapiens, Mus musculus, Pyrococcus furiosus, Thermotoga maritima
Lapointe, M.; Lanthier, J.; Moumdjian, R.; Regina, A.; Desrosiers, R.R.
Expression and activity of L-isoaspartyl methyltransferase decrease in stage progression of human astrocytic tumors
Mol. Brain Res.
135
93-103
2005
Homo sapiens
Lamarre, M.; Desrosiers, R.R.
Up-regulation of protein L-isoaspartyl methyltransferase expression by lithium is mediated by glycogen synthase kinase-3 inactivation and beta-catenin stabilization
Neuropharmacology
55
669-676
2008
Homo sapiens
Furuchi, T.; Kosugi, S.; Ohno, K.; Egawa, T.; Sekine, M.; Katane, M.; Homma, H.
High-performance liquid chromatographic method to measure protein L-isoaspartyl/D-aspartyl O-methyltransferase activity in cell lysates
Anal. Biochem.
384
207-212
2009
Homo sapiens
Alfaro, J.F.; Gillies, L.A.; Sun, H.G.; Dai, S.; Zang, T.; Klaene, J.J.; Kim, B.J.; Lowenson, J.D.; Clarke, S.G.; Karger, B.L.; Zhou, Z.S.
Chemo-enzymatic detection of protein isoaspartate using protein isoaspartate methyltransferase and hydrazine trapping
Anal. Chem.
80
3882-3889
2008
Homo sapiens
Fanelus, I.; Desrosiers, R.R.
Reactive oxygen species generated by thiol-modifying phenylarsine oxide stimulate the expression of protein L-isoaspartyl methyltransferase
Biochem. Biophys. Res. Commun.
371
203-208
2008
Homo sapiens
Kosugi, S.; Furuchi, T.; Katane, M.; Sekine, M.; Shirasawa, T.; Homma, H.
Suppression of protein L-isoaspartyl (D-aspartyl) methyltransferase results in hyperactivation of EGF-stimulated MEK-ERK signaling in cultured mammalian cells
Biochem. Biophys. Res. Commun.
371
22-27
2008
Homo sapiens
Pyun, J.A.; Kang, H.; Lee, S.K.; Kim, M.H.; Kwack, K.
Association between polymorphisms in the protein L-isoaspartate (D-aspartate) O-methyltransferase gene and premature ovarian failure
Fertil. Steril.
91
1362-1365
2009
Homo sapiens
Cournoyer, P.; Desrosiers, R.R.
Valproic acid enhances protein L-isoaspartyl methyltransferase expression by stimulating extracellular signal-regulated kinase signaling pathway
Neuropharmacology
56
839-848
2009
Homo sapiens
Cimmino, A.; Capasso, R.; Muller, F.; Sambri, I.; Masella, L.; Raimo, M.; De Bonis, M.L.; DAngelo, S.; Zappia, V.; Galletti, P.; Ingrosso, D.
Protein isoaspartate methyltransferase prevents apoptosis induced by oxidative stress in endothelial cells: role of Bcl-Xl deamidation and methylation
PLoS ONE
3
e3258
2008
Homo sapiens
Rutherford, K.; Daggett, V.
The V119I polymorphism in protein L-isoaspartate O-methyltransferase alters the substrate-binding interface
Protein Eng. Des. Sel.
22
713-721
2009
Homo sapiens (P22061)
Waegner, A.M.; Cloos, P.; Bergholdt, R.; Eising, S.; Brorsson, C.; Stalhut, M.; Christgau, S.; Nerup, J.; Pociot, F.
Posttranslational protein modifications in type 1 diabetes - Genetic studies with PCMT1, the repair enzyme protein isoaspartate methyltransferase (PIMT) encoding gene
Rev. Diabet. Stud.
5
225-231
2008
Homo sapiens
Liu, M.; Cheetham, J.; Cauchon, N.; Ostovic, J.; Ni, W.; Ren, D.; Zhou, Z.S.
Protein isoaspartate methyltransferase-mediated 18O-labeling of isoaspartic acid for mass spectrometry analysis
Anal. Chem.
84
1056-1062
2012
Homo sapiens
Furuchi, T.; Sakurako, K.; Katane, M.; Sekine, M.; Homma, H.
The role of protein L-isoaspartyl/D-aspartyl O-methyltransferase (PIMT) in intracellular signal transduction
Chem. Biodivers.
7
1337-1348
2010
Homo sapiens
Lee, J.C.; Kang, S.U.; Jeon, Y.; Park, J.W.; You, J.S.; Ha, S.W.; Bae, N.; Lubec, G.; Kwon, S.H.; Lee, J.S.; Cho, E.J.; Han, J.W.
Protein L-isoaspartyl methyltransferase regulates p53 activity
Nat. Commun.
3
927
2012
Homo sapiens
Dutta, T.; Banerjee, S.; Soren, D.; Lahiri, S.; Sengupta, S.; Rasquinha, J.A.; Ghosh, A.K.
Regulation of enzymatic activity by deamidation and their subsequent repair by protein L-isoaspartyl methyl transferase
Appl. Biochem. Biotechnol.
168
2358-2375
2012
Homo sapiens
Park, J.W.; Lee, J.C.; Ha, S.W.; Bang, S.Y.; Park, E.K.; Yi, S.A.; Lee, M.G.; Kim, D.S.; Nam, K.H.; Yoo, J.H.; Kwon, S.H.; Han, J.W.
Requirement of protein L-isoaspartyl O-methyltransferase for transcriptional activation of trefoil factor 1 (TFF1) gene by estrogen receptor alpha
Biochem. Biophys. Res. Commun.
420
223-229
2012
Homo sapiens
Yan, G.; Qin, Q.; Yi, B.; Chuprun, K.; Sun, H.; Huang, S.; Sun, J.
Protein-L-isoaspartate (D-aspartate) O-methyltransferase protects cardiomyocytes against hypoxia induced apoptosis through inhibiting proapoptotic kinase Mst1
Int. J. Cardiol.
168
3291-3299
2013
Homo sapiens
Oda, A.; Noji, I.; Fukuyoshi, S.; Takahashi, O.
Prediction of binding modes between protein L-isoaspartyl (D-aspartyl) O-methyltransferase and peptide substrates including isomerized aspartic acid residues using in silico analytic methods for the substrate screening
J. Pharm. Biomed. Anal.
116
116-122
2015
Homo sapiens (P22061), Homo sapiens
Biterge, B.; Richter, F.; Mittler, G.; Schneider, R.
Methylation of histone H4 at aspartate 24 by protein L-isoaspartate O-methyltransferase (PCMT1) links histone modifications with protein homeostasis
Sci. Rep.
4
6674
2014
Homo sapiens
Kimura, Y.; Komatsu, T.; Yanagi, K.; Hanaoka, K.; Ueno, T.; Terai, T.; Kojima, H.; Okabe, T.; Nagano, T.; Urano, Y.
Development of chemical tools to monitor and control isoaspartyl peptide methyltransferase activity
Angew. Chem. Int. Ed. Engl.
56
153-157
2017
Homo sapiens
Lyon, Y.A.; Sabbah, G.M.; Julian, R.R.
Differences in alpha-crystallin isomerization reveal the activity of protein isoaspartyl methyltransferase (PIMT) in the nucleus and cortex of human lenses
Exp. Eye Res.
171
131-141
2018
Homo sapiens
Ogasawara, M.; Otani, M.; Takano, M.; Shudou, M.; Inaba, Y.; Nirasawa, S.; Takahashi, S.; Kiyoi, T.; Tanaka, Y.; Kameda, K.; Kunugita, N.; Maeyama, K.; Sano, K.; Yamashita, M.; Yamauchi, K.
The protective role of protein L-isoaspartyl (D-aspartate) O-methyltransferase for maintenance of mitochondrial morphology in A549 cell
Exp. Lung Res.
42
245-262
2016
Homo sapiens
Saito, H.; Yamashita, M.; Ogasawara, M.; Yamada, N.; Niisato, M.; Tomoyasu, M.; Deguchi, H.; Tanita, T.; Ishida, K.; Sugai, T.; Yamauchi, K.
Chaperone protein L-isoaspartate (D-aspartyl) O-methyltransferase as a novel predictor of poor prognosis in lung adenocarcinoma
Hum. Pathol.
50
1-10
2016
Homo sapiens
Ouanouki, A.; Desrosiers, R.R.
The enzyme L-isoaspartyl (D-aspartyl) methyltransferase is required for VEGF-dependent endothelial cell migration and tubulogenesis
Mol. Cell. Biochem.
413
37-46
2016
Homo sapiens
Ouazia, D.; Levros, L.C.; Rassart, E.; Desrosiers, R.R.
The protein L-isoaspartyl (D-aspartyl) methyltransferase protects against dopamine-induced apoptosis in neuroblastoma SH-SY5Y cells
Neuroscience
295
139-150
2015
Homo sapiens
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