P16460 (ASSY_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 117.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Argininosuccinate synthase EC=6.3.4.5 Alternative name(s): Citrulline--aspartate ligase | ||||
| Gene names |
| ||||
| Organism | Mus musculus (Mouse) [Reference proteome] | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus![]() |
Protein attributes
| Sequence length | 412 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Is indirectly involved in the control of blood pressure By similarity. |
| Catalytic activity | ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)-(L-arginino)succinate. |
| Pathway | |
| Subunit structure | Homotetramer. Interacts with NMRAL1 By similarity. |
| Sequence similarities | Belongs to the argininosuccinate synthase family. Type 1 subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Arginine biosynthesis Urea cycle |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Ligase |
| PTM | Phosphoprotein |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | arginine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway urea cycleInferred from electronic annotation. Source: UniProtKB-UniPathway |
| Cellular_component | mitochondrion Inferred from direct assay PubMed 14701727. Source: MGI |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW argininosuccinate synthase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 412 | 412 | Argininosuccinate synthase | PRO_0000148555 | |||||
Regions | |||||||||
| Nucleotide binding | 10 – 18 | 9 | ATP By similarity | ||||||
| Nucleotide binding | 115 – 123 | 9 | ATP By similarity | ||||||
Sites | |||||||||
| Binding site | 36 | 1 | ATP; via amide nitrogen and carbonyl oxygen By similarity | ||||||
| Binding site | 87 | 1 | Citrulline By similarity | ||||||
| Binding site | 92 | 1 | Citrulline By similarity | ||||||
| Binding site | 119 | 1 | Aspartate By similarity | ||||||
| Binding site | 123 | 1 | Aspartate By similarity | ||||||
| Binding site | 123 | 1 | Citrulline By similarity | ||||||
| Binding site | 124 | 1 | Aspartate By similarity | ||||||
| Binding site | 127 | 1 | Citrulline By similarity | ||||||
| Binding site | 180 | 1 | Citrulline By similarity | ||||||
| Binding site | 189 | 1 | Citrulline By similarity | ||||||
| Binding site | 270 | 1 | Citrulline By similarity | ||||||
| Binding site | 282 | 1 | Citrulline By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 180 | 1 | Phosphoserine By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Molecular characterization of the murine argininosuccinate synthetase locus." Surh L.C., Beaudet A.L., O'Brien W.E. Gene 99:181-189(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Strain: DBA/2J. Tissue: Liver. |
| [2] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Czech II and FVB/N. Tissue: Colon and Mammary gland. |
| [3] | Lubec G., Yang J.W., Zigmond M. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 128-140. Tissue: Brain. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M31690 mRNA. Translation: AAA37266.1. M31692 Genomic DNA. Translation: AAB60707.1. M31694, M31693, M31695 Genomic DNA. Translation: AAB60708.1. M31702 Genomic DNA. Translation: AAB60706.1. BC002074 mRNA. Translation: AAH02074.1. BC087556 mRNA. Translation: AAH87556.1. |
| IPI | IPI00134746. |
| PIR | AJMSRS. JU0463. |
| RefSeq | NP_031520.1. NM_007494.3. |
| UniGene | Mm.3217. |
3D structure databases | |
| ProteinModelPortal | P16460. |
| SMR | P16460. Positions 4-407. |
| ModBase | Search... |
PTM databases | |
| PhosphoSite | P16460. |
2D gel databases | |
| REPRODUCTION-2DPAGE | P16460. |
Proteomic databases | |
| PaxDb | P16460. |
| PRIDE | P16460. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000102840; ENSMUSP00000099904; ENSMUSG00000076441. |
| GeneID | 11898. |
| KEGG | mmu:11898. |
Organism-specific databases | |
| CTD | 445. |
| MGI | MGI:88090. Ass1. |
Phylogenomic databases | |
| eggNOG | COG0137. |
| HOGENOM | HOG000230093. |
| HOVERGEN | HBG001717. |
| InParanoid | P16460. |
| KO | K01940. |
| OMA | NDQFRFE. |
| OrthoDB | EOG45B1FK. |
Enzyme and pathway databases | |
| UniPathway | UPA00068; UER00113. UPA00158; UER00272. |
Gene expression databases | |
| ArrayExpress | P16460. |
| Bgee | P16460. |
| CleanEx | MM_ASS1. |
| Genevestigator | P16460. |
| GermOnline | ENSMUSG00000046687. Mus musculus. |
Family and domain databases | |
| Gene3D | 3.40.50.620. 1 hit. 3.90.1260.10. 1 hit. |
| 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. [Graphical view] |
| PANTHER | PTHR11587. PTHR11587. 1 hit. |
| Pfam | PF00764. Arginosuc_synth. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00032. argG. 1 hit. |
| PROSITE | PS00564. ARGININOSUCCIN_SYN_1. 1 hit. PS00565. ARGININOSUCCIN_SYN_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 279943. |
| SOURCE | Search... |
Entry information
| Entry name | ASSY_MOUSE | ||||||||
| Accession | Primary (citable) accession number: P16460 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
