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UniProtKB - P00966 (ASSY_HUMAN)

Entry version 226 (02 Dec 2020)
Sequence version 2 (03 Apr 2002)
Previous versions | rss
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Protein

Argininosuccinate synthase

Gene

ASS1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

One of the enzymes of the urea cycle, the metabolic pathway transforming neurotoxic amonia produced by protein catabolism into inocuous urea in the liver of ureotelic animals. Catalyzes the formation of arginosuccinate from aspartate, citrulline and ATP and together with ASL it is responsible for the biosynthesis of arginine in most body tissues.3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=112 µM for citrulline (at pH 7.0 and 37 degrees Celsius)1 Publication
  2. KM=68 µM for aspartate (at pH 7.0 and 37 degrees Celsius)1 Publication
  1. Vmax=143 nmol/min/mg enzyme toward citrulline (at pH 7.0 and 37 degrees Celsius)1 Publication
  2. Vmax=116 nmol/min/mg enzyme toward aspartate (at pH 7.0 and 37 degrees1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-arginine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-arginine from L-ornithine and carbamoyl phosphate.3 Publications
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Citrulline--aspartate ligase, Argininosuccinate synthase (ASS), Citrulline--aspartate ligase (ASS1), Citrulline--aspartate ligase (ASS1), Argininosuccinate synthase, Argininosuccinate synthase (ASS1), Citrulline--aspartate ligase (ASS1), Citrulline--aspartate ligase (LOC402295), Citrulline--aspartate ligase (ASS1)
  3. Argininosuccinate lyase (ASL)
This subpathway is part of the pathway L-arginine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-arginine from L-ornithine and carbamoyl phosphate, the pathway L-arginine biosynthesis and in Amino-acid biosynthesis.

Pathwayi: urea cycle

This protein is involved in step 1 of the subpathway that synthesizes (N(omega)-L-arginino)succinate from L-aspartate and L-citrulline.3 Publications
Proteins known to be involved in this subpathway in this organism are:
  1. Argininosuccinate synthase (ASS), Citrulline--aspartate ligase (ASS1), Argininosuccinate synthase 1 isoform 2 (ASS1), Citrulline--aspartate ligase (ASS1), Argininosuccinate synthase, Argininosuccinate synthase (ASS1), Citrulline--aspartate ligase (ASS1), Citrulline--aspartate ligase (ASS1)
This subpathway is part of the pathway urea cycle, which is itself part of Nitrogen metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (N(omega)-L-arginino)succinate from L-aspartate and L-citrulline, the pathway urea cycle and in Nitrogen metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei36ATP; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei87Citrulline1 Publication1
Binding sitei92Citrulline1 Publication1
Binding sitei119Aspartate1 Publication1
Binding sitei123Aspartate1 Publication1
Binding sitei123Citrulline1 Publication1
Binding sitei124Aspartate1 Publication1
Binding sitei127Citrulline1 Publication1
Binding sitei180Citrulline1 Publication1
Binding sitei189Citrulline1 Publication1
Binding sitei270Citrulline1 Publication1
Binding sitei282Citrulline1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi10 – 18ATPBy similarity9
Nucleotide bindingi115 – 123ATPBy similarity9

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionLigase
Biological processAmino-acid biosynthesis, Arginine biosynthesis, Urea cycle
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		MetaCyc:HS05425-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		6.3.4.5, 2681

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		P00966

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-70635, Urea cycle

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P00966

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi		UPA00068;UER00113
UPA00158;UER00272

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Argininosuccinate synthaseCurated (EC:6.3.4.53 Publications)
Alternative name(s):
Citrulline--aspartate ligase
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ASS1Imported
Synonyms:ASSImported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 9

Organism-specific databases

Eukaryotic Pathogen and Host Database Resources

More...EuPathDBi		HostDB:ENSG00000130707.17

Human Gene Nomenclature Database

More...HGNCi		HGNC:758, ASS1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		603470, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P00966

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Citrullinemia 1 (CTLN1)16 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionThe classic form of citrullinemia, an autosomal recessive disease characterized primarily by elevated serum and urine citrulline levels. Ammonia intoxication is another manifestation. It is a disorder of the urea cycle, usually manifesting in the first few days of life. Affected infants appear normal at birth, but as ammonia builds up in the body they present symptoms such as lethargy, poor feeding, vomiting, seizures and loss of consciousness. Less commonly, a milder form can develop later in childhood or adulthood.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_00068114G → S in CTLN1. 2 PublicationsCorresponds to variant dbSNP:rs121908636EnsemblClinVar.1
Natural variantiVAR_00068218S → L in CTLN1. 1 PublicationCorresponds to variant dbSNP:rs121908643EnsemblClinVar.1
Natural variantiVAR_01589119C → R in CTLN1. 1 Publication1
Natural variantiVAR_07838727 – 412Missing in CTLN1. 1 PublicationAdd BLAST386
Natural variantiVAR_05833740Q → L in CTLN1. 1 Publication1
Natural variantiVAR_07838864V → I in CTLN1; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs556297791EnsemblClinVar.1
Natural variantiVAR_01601369V → A in CTLN1. 1 PublicationCorresponds to variant dbSNP:rs771594651Ensembl.1
Natural variantiVAR_05833879S → P in CTLN1. 2 Publications1
Natural variantiVAR_00068386R → C in CTLN1. 1 PublicationCorresponds to variant dbSNP:rs121908644EnsemblClinVar.1
Natural variantiVAR_01589286R → H in CTLN1. 1 PublicationCorresponds to variant dbSNP:rs575001023EnsemblClinVar.1
Natural variantiVAR_07838991T → P in CTLN1; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity. 2 PublicationsCorresponds to variant dbSNP:rs769018733Ensembl.1
Natural variantiVAR_01589395R → S in CTLN1; increased thermal stability; loss of argininosuccinate synthase activity. 2 Publications1
Natural variantiVAR_05833996P → H in CTLN1; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity. 2 Publications1
Natural variantiVAR_07839096P → L in CTLN1; decreased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; loss of argininosuccinate synthase activity. 1 Publication1
Natural variantiVAR_01589496P → S in CTLN1; no effect on thermal stability; decreased argininosuccinate synthase activity. 2 Publications1
Natural variantiVAR_07839197 – 412Missing in CTLN1. 1 PublicationAdd BLAST316
Natural variantiVAR_078392100R → C in CTLN1. 1 PublicationCorresponds to variant dbSNP:rs370695114EnsemblClinVar.1
Natural variantiVAR_078393100R → H in CTLN1. 1 PublicationCorresponds to variant dbSNP:rs138279074EnsemblClinVar.1
Natural variantiVAR_016014108R → L in CTLN1. 2 PublicationsCorresponds to variant dbSNP:rs35269064EnsemblClinVar.1
Natural variantiVAR_078394111A → D in CTLN1. 1 Publication1
Natural variantiVAR_078395117G → C in CTLN1. 1 Publication1
Natural variantiVAR_015896117G → D in CTLN1. 2 Publications1
Natural variantiVAR_015895117G → S in CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity. 2 PublicationsCorresponds to variant dbSNP:rs770944877EnsemblClinVar.1
Natural variantiVAR_000684118A → T in CTLN1; decreased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity. 3 PublicationsCorresponds to variant dbSNP:rs775305020EnsemblClinVar.1
Natural variantiVAR_016015119T → I in CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity. 2 Publications1
Natural variantiVAR_058340124D → N in CTLN1; loss of argininosuccinate synthase activity. 2 PublicationsCorresponds to variant dbSNP:rs936192871EnsemblClinVar.1
Natural variantiVAR_058341127R → Q in CTLN1; increased thermal stability; loss of argininosuccinate synthase activity. 3 PublicationsCorresponds to variant dbSNP:rs201623252EnsemblClinVar.1
Natural variantiVAR_058342127R → W in CTLN1; severe clinical course; loss of argininosuccinate synthase activity. 2 PublicationsCorresponds to variant dbSNP:rs771794639EnsemblClinVar.1
Natural variantiVAR_078397138 – 412Missing in CTLN1. 1 PublicationAdd BLAST275
Natural variantiVAR_072792141V → G in CTLN1. 1 PublicationCorresponds to variant dbSNP:rs1184442048Ensembl.1
Natural variantiVAR_015897157R → C in CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity. 3 PublicationsCorresponds to variant dbSNP:rs770585183EnsemblClinVar.1
Natural variantiVAR_000685157R → H in CTLN1; loss of argininosuccinate synthase activity. 3 PublicationsCorresponds to variant dbSNP:rs121908637EnsemblClinVar.1
Natural variantiVAR_078398157R → S in CTLN1. 1 Publication1
Natural variantiVAR_058343160L → P in CTLN1. 2 PublicationsCorresponds to variant dbSNP:rs969835605Ensembl.1
Natural variantiVAR_078399163 – 412Missing in CTLN1. 1 PublicationAdd BLAST250
Natural variantiVAR_078400164A → P in CTLN1. 1 Publication1
Natural variantiVAR_015898179W → R in CTLN1; mild; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity. 4 PublicationsCorresponds to variant dbSNP:rs121908646EnsemblClinVar.1
Natural variantiVAR_078401180S → I in CTLN1; increased thermal stability; loss of argininosuccinate synthase activity. 2 PublicationsCorresponds to variant dbSNP:rs121908638EnsemblClinVar.1
Natural variantiVAR_000686180S → N in CTLN1; decreased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity. 2 PublicationsCorresponds to variant dbSNP:rs121908638EnsemblClinVar.1
Natural variantiVAR_078402184N → K in CTLN1. 1 PublicationCorresponds to variant dbSNP:rs368192467Ensembl.1
Natural variantiVAR_058344190Y → D in CTLN1. 2 Publications1
Natural variantiVAR_015899191E → K in CTLN1. 1 PublicationCorresponds to variant dbSNP:rs777828000EnsemblClinVar.1
Natural variantiVAR_058345191E → Q in CTLN1; loss of argininosuccinate synthase activity. 2 Publications1
Natural variantiVAR_000687192A → V in CTLN1; decreased protein abundance. 2 Publications1
Natural variantiVAR_058346202A → E in CTLN1. 1 PublicationCorresponds to variant dbSNP:rs376371866EnsemblClinVar.1
Natural variantiVAR_058347206L → P in CTLN1. 2 Publications1
Natural variantiVAR_078403230G → R in CTLN1. 1 Publication1
Natural variantiVAR_078404237N → I in CTLN1. 1 Publication1
Natural variantiVAR_078405258A → P in CTLN1. 1 Publication1
Natural variantiVAR_078406258A → V in CTLN1. 1 PublicationCorresponds to variant dbSNP:rs753078725EnsemblClinVar.1
Natural variantiVAR_058348263V → M in CTLN1; mild clinical course; no effect on affinity for aspartate; no effect on affinity for citrulline; decreased argininosuccinate synthase activity. 2 PublicationsCorresponds to variant dbSNP:rs192838388EnsemblClinVar.1
Natural variantiVAR_058349265R → C in CTLN1; severe clinical course; loss of argininosuccinate synthase activity. 4 PublicationsCorresponds to variant dbSNP:rs148918985EnsemblClinVar.1
Natural variantiVAR_015900265R → H in CTLN1. 1 PublicationCorresponds to variant dbSNP:rs398123131EnsemblClinVar.1
Natural variantiVAR_015901269V → M in CTLN1. 2 PublicationsCorresponds to variant dbSNP:rs370595480EnsemblClinVar.1
Natural variantiVAR_016007270E → Q in CTLN1; loss of argininosuccinate synthase activity. 3 PublicationsCorresponds to variant dbSNP:rs775163147EnsemblClinVar.1
Natural variantiVAR_000688272R → C in CTLN1; increased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity. 4 PublicationsCorresponds to variant dbSNP:rs762387914EnsemblClinVar.1
Natural variantiVAR_078407272R → H in CTLN1; increased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity. 1 PublicationCorresponds to variant dbSNP:rs768215008Ensembl.1
Natural variantiVAR_078408272R → L in CTLN1; increased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity. 1 PublicationCorresponds to variant dbSNP:rs768215008Ensembl.1
Natural variantiVAR_078409275 – 412Missing in CTLN1. 1 PublicationAdd BLAST138
Natural variantiVAR_058350277K → T in CTLN1. 2 Publications1
Natural variantiVAR_078410279 – 412Missing in CTLN1. 1 PublicationAdd BLAST134
Natural variantiVAR_016008279R → Q in CTLN1. 1 PublicationCorresponds to variant dbSNP:rs371265106EnsemblClinVar.1
Natural variantiVAR_000689280G → R in CTLN1; loss of argininosuccinate synthase activity. 2 Publications1
Natural variantiVAR_015902283E → K in CTLN1. 4 PublicationsCorresponds to variant dbSNP:rs765338121EnsemblClinVar.1
Natural variantiVAR_058351284T → I in CTLN1; mild clinical course. 2 PublicationsCorresponds to variant dbSNP:rs886039853EnsemblClinVar.1
Natural variantiVAR_078411290L → P in CTLN1. 1 Publication1
Natural variantiVAR_058352291Y → S in CTLN1. 2 Publications1
Natural variantiVAR_058353296D → G in CTLN1. 2 Publications1
Natural variantiVAR_078412299A → D in CTLN1. 1 PublicationCorresponds to variant dbSNP:rs768394647Ensembl.1
Natural variantiVAR_058354302M → V in CTLN1; no effect on affinity for aspartate; no effect on affinity for citrulline; decreased argininosuccinate synthase activity. 2 Publications1
Natural variantiVAR_000690304R → W in CTLN1; decreased protein abundance. 3 PublicationsCorresponds to variant dbSNP:rs121908642EnsemblClinVar.1
Natural variantiVAR_078413306V → G in CTLN1. 1 Publication1
Natural variantiVAR_058355307R → C in CTLN1. 1 PublicationCorresponds to variant dbSNP:rs183276875EnsemblClinVar.1
Natural variantiVAR_016009310K → Q in CTLN1. 1 PublicationCorresponds to variant dbSNP:rs121908648EnsemblClinVar.1
Natural variantiVAR_015903310K → R in CTLN1. 1 PublicationCorresponds to variant dbSNP:rs199751308EnsemblClinVar.1
Natural variantiVAR_078414311 – 412Missing in CTLN1. 1 PublicationAdd BLAST102
Natural variantiVAR_078415321V → M in CTLN1. 1 PublicationCorresponds to variant dbSNP:rs727503813EnsemblClinVar.1
Natural variantiVAR_000691324G → S in CTLN1; loss of argininosuccinate synthase activity. 6 PublicationsCorresponds to variant dbSNP:rs121908639EnsemblClinVar.1
Natural variantiVAR_058356324G → V in CTLN1. 2 Publications1
Natural variantiVAR_078416335R → H in CTLN1. 1 PublicationCorresponds to variant dbSNP:rs555388438EnsemblClinVar.1
Natural variantiVAR_078417337C → R in CTLN1. 1 Publication1
Natural variantiVAR_058357341S → F in CTLN1. 2 Publications1
Natural variantiVAR_078418344 – 412Missing in CTLN1. 1 PublicationAdd BLAST69
Natural variantiVAR_058358345V → G in CTLN1. 1 Publication1
Natural variantiVAR_058359347G → R in CTLN1; severe clinical course. 2 Publications1
Natural variantiVAR_078419356G → V in CTLN1. 1 Publication1
Natural variantiVAR_078420357 – 412Missing in CTLN1. 1 PublicationAdd BLAST56
Natural variantiVAR_058360359Y → D in CTLN1; mild clinical course. 2 Publications1
Natural variantiVAR_015904362G → V in CTLN1; mild; no effect on affinity for aspartate; no effect on affinity for citrulline; decreased argininosuccinate synthase activity. 4 PublicationsCorresponds to variant dbSNP:rs121908647EnsemblClinVar.1
Natural variantiVAR_016010363R → G in CTLN1. 1 Publication1
Natural variantiVAR_000692363R → L in CTLN1. 1 Publication1
Natural variantiVAR_016011363R → Q in CTLN1. 1 PublicationCorresponds to variant dbSNP:rs771937610EnsemblClinVar.1
Natural variantiVAR_000693363R → W in CTLN1. 2 PublicationsCorresponds to variant dbSNP:rs121908640EnsemblClinVar.1
Natural variantiVAR_078421380 – 412Missing in CTLN1. 1 PublicationAdd BLAST33
Natural variantiVAR_016012389T → I in CTLN1. 1 PublicationCorresponds to variant dbSNP:rs1474017319EnsemblClinVar.1
Natural variantiVAR_078422389T → P in CTLN1. 1 Publication1
Natural variantiVAR_000694390G → R in CTLN1; loss of argininosuccinate synthase activity. 7 PublicationsCorresponds to variant dbSNP:rs121908641EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi165K → Q or R: Significant loss of acetylation but no decrease in enzyme activity; when associated with Q-176 or R-176. 1 Publication1
Mutagenesisi176K → Q or R: Significant loss of acetylation but no decrease in enzyme activity; when associated with Q-165 or R-165. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...DisGeNETi		445

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

More...GeneReviewsi		ASS1

MalaCards human disease database

More...MalaCardsi		ASS1
MIMi215700, phenotype

Open Targets

More...OpenTargetsi		ENSG00000130707

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		247546, Acute neonatal citrullinemia type I
247573, Adult-onset citrullinemia type I

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA162376926

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P00966, Tbio

Chemistry databases

Drug and drug target database

More...DrugBanki		DB00125, Arginine
DB00128, Aspartic acid
DB00171, ATP
DB00155, Citrulline

DrugCentral

More...DrugCentrali		P00966

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		ASS1

Domain mapping of disease mutations (DMDM)

More...DMDMi		20141195

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001485541 – 412Argininosuccinate synthaseAdd BLAST412

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei87PhosphotyrosineBy similarity1
Modified residuei112N6-acetyllysineBy similarity1
Modified residuei113PhosphotyrosineCombined sources1
Modified residuei165N6-acetyllysine; by CLOCK1 Publication1
Modified residuei176N6-acetyllysine; by CLOCK1 Publication1
Modified residuei180PhosphoserineCombined sources1
Modified residuei219PhosphothreonineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Acetylated by CLOCK in a circadian manner which negatively regulates its enzyme activity. Deacetylated by histone deacetylases.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

The CPTAC Assay portal

More...CPTACi		CPTAC-169
CPTAC-170

Encyclopedia of Proteome Dynamics

More...EPDi		P00966

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P00966

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P00966

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P00966

PeptideAtlas

More...PeptideAtlasi		P00966

PRoteomics IDEntifications database

More...PRIDEi		P00966

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		51293

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P00966

MetOSite database of methionine sulfoxide sites

More...MetOSitei		P00966

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P00966

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in adult liver.1 Publication

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Expressed in fetal liver and kidney.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000130707, Expressed in nephron tubule and 242 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P00966, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P00966, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000130707, Group enriched (kidney, liver)

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotetramer (PubMed:18323623).

Interacts with NMRAL1 (PubMed:17496144).

Interacts with CLOCK; in a circadian manner (PubMed:28985504).

3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		106937, 105 interactors

Database of interacting proteins

More...DIPi		DIP-34055N

Protein interaction database and analysis system

More...IntActi		P00966, 31 interactors

Molecular INTeraction database

More...MINTi		P00966

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000361471

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P00966, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1412
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P00966

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P00966

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the argininosuccinate synthase family. Type 1 subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1706, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00390000004524

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_032784_4_2_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P00966

Identification of Orthologs from Complete Genome Data

More...OMAi		FHIRSGG

Database of Orthologous Groups

More...OrthoDBi		1459745at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P00966

TreeFam database of animal gene trees

More...TreeFami		TF300736

Family and domain databases

Conserved Domains Database

More...CDDi		cd01999, Argininosuccinate_Synthase, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.50.620, 1 hit
3.90.1260.10, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_00005, Arg_succ_synth_type1, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR001518, Arginosuc_synth
IPR018223, Arginosuc_synth_CS
IPR023434, Arginosuc_synth_type_1_subfam
IPR024074, AS_cat/multimer_dom_body
IPR014729, Rossmann-like_a/b/a_fold

The PANTHER Classification System

More...PANTHERi		PTHR11587, PTHR11587, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00764, Arginosuc_synth, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF69864, SSF69864, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00032, argG, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00564, ARGININOSUCCIN_SYN_1, 1 hit
PS00565, ARGININOSUCCIN_SYN_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

P00966-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSSKGSVVLA YSGGLDTSCI LVWLKEQGYD VIAYLANIGQ KEDFEEARKK 
        60         70         80         90        100
ALKLGAKKVF IEDVSREFVE EFIWPAIQSS ALYEDRYLLG TSLARPCIAR 
       110        120        130        140        150
KQVEIAQREG AKYVSHGATG KGNDQVRFEL SCYSLAPQIK VIAPWRMPEF 
       160        170        180        190        200
YNRFKGRNDL MEYAKQHGIP IPVTPKNPWS MDENLMHISY EAGILENPKN 
       210        220        230        240        250
QAPPGLYTKT QDPAKAPNTP DILEIEFKKG VPVKVTNVKD GTTHQTSLEL 
       260        270        280        290        300
FMYLNEVAGK HGVGRIDIVE NRFIGMKSRG IYETPAGTIL YHAHLDIEAF 
       310        320        330        340        350
TMDREVRKIK QGLGLKFAEL VYTGFWHSPE CEFVRHCIAK SQERVEGKVQ 
       360        370        380        390        400
VSVLKGQVYI LGRESPLSLY NEELVSMNVQ GDYEPTDATG FININSLRLK 
       410 
EYHRLQSKVT AK
Length:412
Mass (Da):46,530
Last modified:April 3, 2002 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i47CAD2373AE47E47
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q5T6L5Q5T6L5_HUMAN
Citrulline--aspartate ligase
ASS1
179Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
Q5T6L6Q5T6L6_HUMAN
Citrulline--aspartate ligase
ASS1
198Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti325 – 327FWH → LRP in CAA25771 (PubMed:6194510).Curated3
Sequence conflicti325 – 327FWH → LRP in AAA51783 (PubMed:6321498).Curated3

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00068114G → S in CTLN1. 2 PublicationsCorresponds to variant dbSNP:rs121908636EnsemblClinVar.1
Natural variantiVAR_00068218S → L in CTLN1. 1 PublicationCorresponds to variant dbSNP:rs121908643EnsemblClinVar.1
Natural variantiVAR_01589119C → R in CTLN1. 1 Publication1
Natural variantiVAR_07838727 – 412Missing in CTLN1. 1 PublicationAdd BLAST386
Natural variantiVAR_05833740Q → L in CTLN1. 1 Publication1
Natural variantiVAR_07838864V → I in CTLN1; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs556297791EnsemblClinVar.1
Natural variantiVAR_01601369V → A in CTLN1. 1 PublicationCorresponds to variant dbSNP:rs771594651Ensembl.1
Natural variantiVAR_05833879S → P in CTLN1. 2 Publications1
Natural variantiVAR_00068386R → C in CTLN1. 1 PublicationCorresponds to variant dbSNP:rs121908644EnsemblClinVar.1
Natural variantiVAR_01589286R → H in CTLN1. 1 PublicationCorresponds to variant dbSNP:rs575001023EnsemblClinVar.1
Natural variantiVAR_07838991T → P in CTLN1; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity. 2 PublicationsCorresponds to variant dbSNP:rs769018733Ensembl.1
Natural variantiVAR_01589395R → S in CTLN1; increased thermal stability; loss of argininosuccinate synthase activity. 2 Publications1
Natural variantiVAR_05833996P → H in CTLN1; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity. 2 Publications1
Natural variantiVAR_07839096P → L in CTLN1; decreased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; loss of argininosuccinate synthase activity. 1 Publication1
Natural variantiVAR_01589496P → S in CTLN1; no effect on thermal stability; decreased argininosuccinate synthase activity. 2 Publications1
Natural variantiVAR_07839197 – 412Missing in CTLN1. 1 PublicationAdd BLAST316
Natural variantiVAR_078392100R → C in CTLN1. 1 PublicationCorresponds to variant dbSNP:rs370695114EnsemblClinVar.1
Natural variantiVAR_078393100R → H in CTLN1. 1 PublicationCorresponds to variant dbSNP:rs138279074EnsemblClinVar.1
Natural variantiVAR_016014108R → L in CTLN1. 2 PublicationsCorresponds to variant dbSNP:rs35269064EnsemblClinVar.1
Natural variantiVAR_078394111A → D in CTLN1. 1 Publication1
Natural variantiVAR_078395117G → C in CTLN1. 1 Publication1
Natural variantiVAR_015896117G → D in CTLN1. 2 Publications1
Natural variantiVAR_015895117G → S in CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity. 2 PublicationsCorresponds to variant dbSNP:rs770944877EnsemblClinVar.1
Natural variantiVAR_000684118A → T in CTLN1; decreased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity. 3 PublicationsCorresponds to variant dbSNP:rs775305020EnsemblClinVar.1
Natural variantiVAR_016015119T → I in CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity. 2 Publications1
Natural variantiVAR_058340124D → N in CTLN1; loss of argininosuccinate synthase activity. 2 PublicationsCorresponds to variant dbSNP:rs936192871EnsemblClinVar.1
Natural variantiVAR_078396127R → L Increased thermal stability; loss of argininosuccinate synthase activity. 2 PublicationsCorresponds to variant dbSNP:rs201623252EnsemblClinVar.1
Natural variantiVAR_058341127R → Q in CTLN1; increased thermal stability; loss of argininosuccinate synthase activity. 3 PublicationsCorresponds to variant dbSNP:rs201623252EnsemblClinVar.1
Natural variantiVAR_058342127R → W in CTLN1; severe clinical course; loss of argininosuccinate synthase activity. 2 Publications