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Search term: nucleus

Results 1 - 100 of 1116 > >>
EC Number
Localization
Commentary
GeneOntology No.
Reference
alcohol dehydrogenase
-
IMP dehydrogenase
strong association of subunit Imd2 with actively transcribed genes, it is not recruited to nontranscribed regions. Serine 2 C-terminal domain phosphorylation of the elongating RNA polymerase II by Ctk1 kinase is required to recruit Imd2 to actively transcribed genes in vivo
3alpha-hydroxysteroid 3-dehydrogenase (Re-specific)
-
mannose-6-phosphate 6-reductase
by immunocytochemistry
3alpha(17beta)-hydroxysteroid dehydrogenase (NAD+)
-
mannitol dehydrogenase
-
L-lactate dehydrogenase
-
S-(hydroxymethyl)glutathione dehydrogenase
-
isocitrate dehydrogenase (NADP+)
isozyme ICD1, minor appearance
3alpha-hydroxysteroid 3-dehydrogenase (Si-specific)
-
phospholipid-hydroperoxide glutathione peroxidase
-
phospholipid-hydroperoxide glutathione peroxidase
only in testicle
thioredoxin-dependent peroxiredoxin
NLS-Prx1
glutathione peroxidase
GPX4
quercetin 2,3-dioxygenase
-
arachidonate 15-lipoxygenase
-
arachidonate 15-lipoxygenase
15-LOX-2 is expressed in both the cytoplasm and the nucleus
arachidonate 15-lipoxygenase
the 15-LOX2 clones express 15-LOX2 in the nuclei and possess robust enzymatic activity, whereas 15-LOX2sc-b clones show neither nuclear protein localization nor arachidonic acid-metabolizing activity
arachidonate 5-lipoxygenase
5-LO associates with a nuclear fraction only when differentiated cells are primed with phorbol ester and stimulated with ionophore
arachidonate 5-lipoxygenase
alvelolar macrophages nuclear soluble enzyme moves to the nucear envelope where it interacts with 5-lipoxygenase-activating protein; in basophilic leukemia cells translocation of cytosolic enzyme and the soluble nuclear enzyme to the nuclear envelope where it interacts with 5-lipoxygenase-activating protein
arachidonate 5-lipoxygenase
Ca2+ induces the translocation of 5-LO from a soluble compartment to nuclear structures, where 5-LO co-localizes with 5-LO activating protein, FLAP
arachidonate 5-lipoxygenase
in activated cells
arachidonate 5-lipoxygenase
in stimulated HEK293/T and COS-7 cells the activated 5-lipoxygenase appears mainly at the nuclear envelope
arachidonate 5-lipoxygenase
resides in a nuclear soluble compartment associated with chromatin
arachidonate 5-lipoxygenase
resides in a nuclear soluble compartment associated with chromatin. In male neutrophils, a substantial part of 5-lipoxygenase is located at the perinuclear region already in resting cells, only marginally redistributes upon stimulation
arachidonate 5-lipoxygenase
soluble fraction, translocation to the nuclear envelope upon cell activation by Ca2+
arachidonate 5-lipoxygenase
tonsillar polymorphonuclear granulocytes
arachidonate 5-lipoxygenase
wild-type enzyme
acireductone dioxygenase (Ni2+-requiring)
-
firefly luciferase
associated to
gibberellin 2beta-dioxygenase
-
gibberellin 3beta-dioxygenase
dual localization to the nucleus and cytosol
[histone H3]-dimethyl-L-lysine36 demethylase
-
DNA oxidative demethylase
;
DNA oxidative demethylase
diffuse presence of YFP-ABH3 construct
procollagen-lysine 5-dioxygenase
-
mRNA N6-methyladenine demethylase
-
mRNA N6-methyladenine demethylase
localised in nuclear speckles, which are subnuclear structures that are enriched in pre-messenger RNA splicing factors
mRNA N1-methyladenine demethylase
-
peptidyl-lysine (3S)-dioxygenase
-
[histone H3]-dimethyl-L-lysine9 demethylase
;
-
[histone H3]-dimethyl-L-lysine9 demethylase
JMJ27 is a nuclear protein containing a zinc-finger motif
[histone H3]-dimethyl-L-lysine9 demethylase
KDM4A predominantly localizes to heterochromatin and regulates heterochromatin position-effect variegation, organization of repetitive DNAs, and DNA repair
[histone H3]-dimethyl-L-lysine9 demethylase
LSD1 is associated with folate
[histone H3]-dimethyl-L-lysine9 demethylase
the expression of PHF8 is restricted to the nucleus
[histone H3]-trimethyl-L-lysine9 demethylase
;
[histone H3]-trimethyl-L-lysine9 demethylase
heterochromatin-associated
[histone H3]-trimethyl-L-lysine4 demethylase
;
[histone H3]-trimethyl-L-lysine4 demethylase
Lid-containing protein complex, which is composed of proteins Lid, Rpd3, CG3815/Drosophila Pf1, CG13367, and Mrg15
[histone H3]-trimethyl-L-lysine27 demethylase
-
[histone H3]-trimethyl-L-lysine27 demethylase
;
[histone H3]-trimethyl-L-lysine27 demethylase
embryonic fibroblasts display a dynamic nucleocytoplasmic shuttling of endogenous Jmjd3. Jmjd3 is localized both into the cytoplasm and the nucleus, and its nuclear export is dependent on exportin-1
[histone H3]-trimethyl-L-lysine27 demethylase
exclusivley nuclear localization
[histone H3]-trimethyl-L-lysine27 demethylase
nuclear localization of Jmjd3 is required for effective demethylation of H3K27me3. The N-terminal region of the protein is responsible for its nuclear placement
flavanone 3-dioxygenase
-
[histone H3]-trimethyl-L-lysine56 demethylase
KDM4A predominantly localizes to heterochromatin and regulates heterochromatin position-effect variegation, organization of repetitive DNAs, and DNA repair
salicylate 1-monooxygenase
-
nitric-oxide synthase (NADPH)
-
nitric-oxide synthase (NADPH)
isozyme iNOS
heme oxygenase (biliverdin-producing)
-
heme oxygenase (biliverdin-producing)
in response to different stimuli, e.g. hypoxia by 3% oxygen or incubation with hemin or heme-hemopexin, HO-1 can migrate to the nucleus. Nuclear translocation is associated with truncation of the C-terminus of HO-1
heme oxygenase (biliverdin-producing)
in response to different stimuli, e.g. hypoxia by 3% oxygen or incubation with hemin or heme-hemopexin, HO-1 can migrate to the nucleus. Nuclear translocation is associated with truncation of the C-terminus of HO-1 by 52 amino acids, the C-terminal region of HO-1 inhibits the nuclear import
vitamin D 25-hydroxylase
-
17alpha-hydroxyprogesterone deacetylase
perinucleus
heme oxygenase (biliverdin-producing, ferredoxin)
-
cholesterol monooxygenase (side-chain-cleaving)
truncated form
tyrosine 3-monooxygenase
molecules phosphorylated at Ser19 are found mainly in the nucleus
aminocyclopropanecarboxylate oxidase
-
5,6-dihydroxyindole-2-carboxylic acid oxidase
-
anthocyanidin synthase
in the mesocarp vascular bundle and leaf bud cells
[histone H3]-N6,N6-dimethyl-L-lysine4 FAD-dependent demethylase
association of LSD1 with sites of DNA damage, immunohistochemic localization, overview
[histone H3]-N6,N6-dimethyl-L-lysine4 FAD-dependent demethylase
LSD1 is associated with folate
[histone H3]-N6,N6-dimethyl-L-lysine4 FAD-dependent demethylase
nuclear localization signal at positions 517-534 of the LSD1 amino acid sequence
[histone H3]-N6,N6-dimethyl-L-lysine4 FAD-dependent demethylase
presence of FAD facilitates the nuclear localization of LSD1
ferric-chelate reductase (NADH)
;
ribonucleoside-diphosphate reductase
-
ribonucleoside-diphosphate reductase
during the normal cell cycle, the two small subunits Rnr2 and Rnr4 are predominantly localized to nucleus. Under genotoxic stress, Rnr2 and Rnr4 become redistributed to the cytoplasm in a checkpoint-dependent manner
ribonucleoside-triphosphate reductase (thioredoxin)
in response to DNA replication, subunit M2B redistributes from the cytoplasm to the nucleus
ribonucleoside-triphosphate reductase (thioredoxin)
the subcellular localization of RNR2 is primarily nuclear in meristematic regions, and cytoplasmic in adult cells. RNR2 is constitutively nuclear in csn7 mutant seedlings; the subcellular localization of RNR2 is primarily nuclear in meristematic regions, and cytoplasmic in adult cells. RNR2 is constitutively nuclear in csn7 mutant seedlings
glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)
-
glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)
; of protoplast, both isoforms GapC1 and GapC2; of protoplast, both isoforms GapC1 and GapC2
glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)
GAPDH colocalizes with viral RNA-dependentRNA polymerase in cells infected with Japanese encephalitis virus. GAPDH remains relatively constant in the cytosol, while increasing at 12 to 24 hours postinfection and decreasing at 36 hours postinfection in the nuclear fraction of infected cells. There is no direct protein-protein interaction; instead, GAPDH binds to the 3' termini of plus- and minus-strand RNAs of Japanese encephalitis virus. GAPDH binds to the minus-strand more efficiently than to the plus-strand of Japanese encephalitis virus RNAs
glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)
isozyme uracil-DNA glycosylase localizes in the nucleus as a monomer, UDG, or a dimer (RNA-binding form), but not in the native tetrameric form
glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)
minor amounts
glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)
non-native GAPDH is unevenly distributed within the nuclei
glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)
nuclear expression of GAPDH increases in apoptosis
glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)
O-GlcNAcylation at residue T227 interrupts the hydrophobic interfaces formed between the enzyme monomers in its terameric state and allows for nucleic translocation of the cytoplasmic enzyme
glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)
protein complex containing GAPDH and androgen receptor in the nucleus
glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)
relocalization of GAPC1 to the nucleus is induced by calcium stress
Results 1 - 100 of 1116 > >>