Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Combined Automated Annotation using Multiple IEA Methods
Novel raf kinase protein-protein interactions found by an exhaustive yeast two-hybrid analysis.
Towards a proteome-scale map of the human protein-protein interaction network.
Restructuring of the dinucleotide-binding fold in an NADP(H) sensor protein.
Investigation of citrullinemia type I variants by in vitro expression studies.
Large-scale proteomics and phosphoproteomics of urinary exosomes.
Endothelial argininosuccinate synthetase 1 regulates nitric oxide production and monocyte adhesion under static and laminar shear stress conditions.
-
Increasing ASS1 expression in human endothelial cells increases NO production and reduces TNF-induced monocyte adhesion.
"Exogenous
expression of either NOS3 or ASS1 in human umbilical vein endothelial cells
increased NO production and decreased monocyte adhesion stimulated by tumor
necrosis factor-α (TNF-α)."
Toward an understanding of the protein interaction network of the human liver.
Insights into RNA biology from an atlas of mammalian mRNA-binding proteins.
In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine.
A proteome-scale map of the human interactome network.
Kinetic mutations in argininosuccinate synthetase deficiency: characterisation and in vitro correction by substrate supplementation.
-
Eight kinetic ASS1 variants retained activity that increased in vitro at high L-aspartate concentrations; clinical efficacy was not established.
"RESULTS: Of the characterised mutants, 13 were totally inactive while 8
exhibited decreased affinity for aspartate and citrulline. The activity of these
eight kinetic mutations could be rescued to ∼10-99% of the wild-type using high
l-aspartate concentrations."
PRMT7 Interacts with ASS1 and Citrullinemia Mutations Disrupt the Interaction.
-
ASS1 associates directly with PRMT7 in the reported pull-down assay; this does not establish that ASS1 methylates proteins.
"We confirmed that PRMT7 directly
interacts with ASS1 using pull-down studies."
CLOCK Acetylates ASS1 to Drive Circadian Rhythm of Ureagenesis.
-
CLOCK acetylates ASS1 at K165 and K176 and inhibits its activity; CLOCK performs the acetyl-transfer reaction.
"Facilitated by BMAL1 (brain and muscle
Arnt-like protein), CLOCK directly acetylates K165 and K176 of argininosuccinate
synthase (ASS1) to inactivate ASS1"
Sequence for human argininosuccinate synthetase cDNA.
Mutations in argininosuccinate synthetase mRNA of Japanese patients, causing classical citrullinemia.
Characterization of human wild-type and mutant argininosuccinate synthetase proteins expressed in bacterial cells.
-
Human ASS1 is a homotetramer; recombinant wild-type enzyme agrees with native human liver enzyme.
"Argininosuccinate synthetase (ASS) is a urea cycle enzyme with a tetrameric
structure composed of identical subunits."
-
Recombinant wild-type human ASS1 reproduces the properties of native human liver enzyme.
"The
properties of the purified recombinant protein with wild-type human ASS showed
good agreement with native enzyme purified from human liver."
ASS1 tetramer:NMRAL1 dimer:NADPH transforms L-Asp and L-Cit to ARSUA
-
Curated human ASS1 catalysis joins aspartate and citrulline using ATP in the cytosol.
"Cytosolic argininosuccinate synthase (ASS1 tetramer) catalyzes the reaction of aspartate (L-Asp), citrulline (L-Cit), and ATP to form argininosuccinate (ARSUA), AMP, and pyrophosphate (PPi)."
ASS1 variants don't synthesize arginosuccinate
-
Some ASS1 deficiency variants retain partial enzyme activity.
"Milder, later-onset forms may present with episodic symptoms due to partial enzyme activity"
Demonstration of argininosuccinate synthetase activity associated with mitochondrial membrane: characterization and hormonal regulation.
Argininosuccinate synthetase and argininosuccinate lyase are localized around mitochondria: an immunocytochemical study.
Structure of human argininosuccinate synthetase.
-
The human ASS1 structure contains bound citrulline and aspartate.
"the first crystal structure of human
argininosuccinate synthetase in complex with the substrates citrulline and
aspartate is presented."
Identification of fumonisin B1 as an inhibitor of argininosuccinate synthetase using fumonisin affinity chromatography and in vitro kinetic studies.
-
Fumonisin inhibits recombinant human ASS1 in vitro, without establishing its cellular toxicological importance.
"approximately 6 mM with the recombinant human argininosuccinate synthase"
An NADPH sensor protein (HSCARG) down-regulates nitric oxide synthesis by association with argininosuccinate synthetase and is essential for epithelial cell viability.
ASS1 metabolically contributes to the nuclear and cytosolic p53-mediated DNA damage response.
-
Endogenous ASS1 occurs in human HCT116 nuclei and increases after doxorubicin treatment.
"we unexpectedly observed nuclear expression of ASS1 in untreated HCT116 colon cancer cells, with a robust increase following Dox treatment"