Attention: World-2DPAGE is no longer maintained. It will be discontinued on 31-May-2024.
Swiss-2DPAGE data (text records and image files) will continue to be available from https://ftp.expasy.org/databases/swiss-2dpage/.
World-2DPAGE Repository no longer accepts submissions.
Mascot Search Results
Protein View
ID ASSY_MOUSE Reviewed; 412 AA. AC P16460; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1990, sequence version 1. DT 15-DEC-2009, entry version 91. DE RecName: Full=Argininosuccinate synthase; DE EC=6.3.4.5; DE AltName: Full=Citrulline--aspartate ligase; GN Name=Ass1; Synonyms=Ass; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RC STRAIN=DBA/2J; TISSUE=Liver; RX MEDLINE=91216457; PubMed=1708740; DOI=10.1016/0378-1119(91)90125-U; RA Surh L.C., Beaudet A.L., O'Brien W.E.; RT "Molecular characterization of the murine argininosuccinate synthetase RT locus."; RL Gene 99:181-189(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Czech II, and FVB/N; TISSUE=Colon, and Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PROTEIN SEQUENCE OF 128-140. RC TISSUE=Brain; RA Lubec G., Yang J.W., Zigmond M.; RL Submitted (JUL-2007) to UniProtKB. CC -!- CATALYTIC ACTIVITY: ATP + L-citrulline + L-aspartate = AMP + CC diphosphate + N(omega)-(L-arginino)succinate. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L- CC arginine from L-ornithine and carbamoyl phosphate: step 2/3. CC -!- PATHWAY: Nitrogen metabolism; urea cycle; (N(omega)-L- CC arginino)succinate from L-aspartate and L-citrulline: step 1/1. CC -!- SUBUNIT: Homotetramer. Interacts with NMRAL1 (By similarity). CC -!- SIMILARITY: Belongs to the argininosuccinate synthase family. Type CC 1 subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M31690; AAA37266.1; -; mRNA. DR EMBL; M31692; AAB60707.1; -; Genomic_DNA. DR EMBL; M31694; AAB60708.1; -; Genomic_DNA. DR EMBL; M31693; AAB60708.1; JOINED; Genomic_DNA. DR EMBL; M31695; AAB60708.1; JOINED; Genomic_DNA. DR EMBL; M31702; AAB60706.1; -; Genomic_DNA. DR EMBL; BC002074; AAH02074.1; -; mRNA. DR EMBL; BC087556; AAH87556.1; -; mRNA. DR IPI; IPI00134746; -. DR PIR; JU0463; AJMSRS. DR RefSeq; NP_031520.1; -. DR UniGene; Mm.3217; -. DR SMR; P16460; 4-407. DR STRING; P16460; -. DR PhosphoSite; P16460; -. DR REPRODUCTION-2DPAGE; P16460; -. DR PRIDE; P16460; -. DR Ensembl; ENSMUST00000102840; ENSMUSP00000099904; ENSMUSG00000076441; Mus musculus. DR GeneID; 11898; -. DR KEGG; mmu:11898; -. DR UCSC; uc008jdu.1; mouse. DR CTD; 11898; -. DR MGI; MGI:88090; Ass1. DR HOGENOM; HBG335267; -. DR HOVERGEN; P16460; -. DR InParanoid; P16460; -. DR OMA; IAPVREW; -. DR OrthoDB; EOG954CJT; -. DR BRENDA; 6.3.4.5; 244. DR NextBio; 279943; -. DR Bgee; P16460; -. DR CleanEx; MM_ASS1; -. DR Genevestigator; P16460; -. DR GermOnline; ENSMUSG00000046687; Mus musculus. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0004055; F:argininosuccinate synthase activity; IEA:EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0000050; P:urea cycle; IEA:UniProtKB-KW. DR InterPro; IPR001518; Arginosuc_synth. DR InterPro; IPR018223; Arginosuc_synth_CS. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1. DR PANTHER; PTHR11587; Arginosuc_synth; 1. DR Pfam; PF00764; Arginosuc_synth; 1. DR PROSITE; PS00564; ARGININOSUCCIN_SYN_1; 1. DR PROSITE; PS00565; ARGININOSUCCIN_SYN_2; 1. PE 1: Evidence at protein level; KW Acetylation; Amino-acid biosynthesis; Arginine biosynthesis; KW ATP-binding; Direct protein sequencing; Ligase; Nucleotide-binding; KW Phosphoprotein; Urea cycle. FT CHAIN 1 412 Argininosuccinate synthase. FT /FTId=PRO_0000148555. FT NP_BIND 10 18 ATP (By similarity). FT NP_BIND 115 123 ATP (By similarity). FT BINDING 36 36 ATP; via amide nitrogen and carbonyl FT oxygen (By similarity). FT BINDING 87 87 Citrulline (By similarity). FT BINDING 92 92 Citrulline (By similarity). FT BINDING 119 119 Aspartate (By similarity). FT BINDING 123 123 Aspartate (By similarity). FT BINDING 123 123 Citrulline (By similarity). FT BINDING 124 124 Aspartate (By similarity). FT BINDING 127 127 Citrulline (By similarity). FT BINDING 180 180 Citrulline (By similarity). FT BINDING 189 189 Citrulline (By similarity). FT BINDING 270 270 Citrulline (By similarity). FT BINDING 282 282 Citrulline (By similarity). FT MOD_RES 165 165 N6-acetyllysine (By similarity). FT MOD_RES 352 352 Phosphoserine (By similarity). SQ SEQUENCE 412 AA; 46584 MW; A8F3AFDDFBDAEF6A CRC64; MSSKGSVVLA YSGGLDTSCI LVWLKEQGYD VIAYLANIGQ KEDFEEARKK ALKLGAKKVF IEDVSKEFVE EFIWPAVQSS ALYEDRYLLG TSLARPCIAR RQVEIAQREG AKYVSHGATG KGNDQVRFEL TCYSLAPQIK VIAPWRMPEF YNRFKGRNDL MEYAKQHGIP IPVTPKSPWS MDENLMHISY EAGILENPKN QAPPGLYTKT QDPAKAPNSP DVLEIEFKKG VPVKVTNIKD GTTRTTSLEL FMYLNEVAGK HGVGRIDIVE NRFIGMKSRG IYETPAGTIL YHAHLDIEAF TMDREVRKIK QGLGLKFAEL VYTGFWHSPE CEFVRHCIQK SQERVEGKVQ VSVFKGQVYI LGRESPLSLY NEELVSMNVQ GDYEPIDATG FININSLRLK EYHRLQSKVT AK
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