SYDC_MOUSE
ID SYDC_MOUSE Reviewed; 501 AA.
AC Q922B2; Q3U987;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Aspartate--tRNA ligase, cytoplasmic;
DE EC=6.1.1.12 {ECO:0000250|UniProtKB:P15178};
DE AltName: Full=Aspartyl-tRNA synthetase;
DE Short=AspRS;
GN Name=Dars1; Synonyms=Dars;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP SUBUNIT.
RX PubMed=12060739; DOI=10.1073/pnas.122110199;
RA Kim J.Y., Kang Y.-S., Lee J.-W., Kim H.J., Ahn Y.H., Park H., Ko Y.-G.,
RA Kim S.;
RT "p38 is essential for the assembly and stability of macromolecular tRNA
RT synthetase complex: implications for its physiological significance.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:7912-7916(2002).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the specific attachment of an amino acid to its
CC cognate tRNA in a 2 step reaction: the amino acid (AA) is first
CC activated by ATP to form AA-AMP and then transferred to the acceptor
CC end of the tRNA. {ECO:0000250|UniProtKB:P15178}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-
CC aspartyl-tRNA(Asp); Xref=Rhea:RHEA:19649, Rhea:RHEA-COMP:9660,
CC Rhea:RHEA-COMP:9678, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78516,
CC ChEBI:CHEBI:456215; EC=6.1.1.12;
CC Evidence={ECO:0000250|UniProtKB:P15178};
CC -!- SUBUNIT: Homodimer (By similarity). Part of a multisubunit complex that
CC groups tRNA ligases for Arg (RARS1), Asp (DARS1), Gln (QARS1), Ile
CC (IARS1), Leu (LARS1), Lys (KARS1), Met (MARS1) the bifunctional ligase
CC for Glu and Pro (EPRS1) and the auxiliary subunits AIMP1/p43, AIMP2/p38
CC and EEF1E1/p18 (PubMed:12060739). {ECO:0000250|UniProtKB:P14868,
CC ECO:0000269|PubMed:12060739}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type 2 subfamily. {ECO:0000305}.
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DR EMBL; AK151027; BAE30045.1; -; mRNA.
DR EMBL; AK151897; BAE30780.1; -; mRNA.
DR EMBL; AK152304; BAE31110.1; -; mRNA.
DR EMBL; AK152562; BAE31315.1; -; mRNA.
DR EMBL; AK153256; BAE31847.1; -; mRNA.
DR EMBL; AK153299; BAE31881.1; -; mRNA.
DR EMBL; AK169716; BAE41327.1; -; mRNA.
DR EMBL; BC008638; AAH08638.1; -; mRNA.
DR CCDS; CCDS15253.1; -.
DR RefSeq; NP_803228.2; NM_177445.5.
DR AlphaFoldDB; Q922B2; -.
DR SMR; Q922B2; -.
DR BioGRID; 230508; 18.
DR IntAct; Q922B2; 4.
DR STRING; 10090.ENSMUSP00000027602; -.
DR iPTMnet; Q922B2; -.
DR PhosphoSitePlus; Q922B2; -.
DR SwissPalm; Q922B2; -.
DR EPD; Q922B2; -.
DR jPOST; Q922B2; -.
DR MaxQB; Q922B2; -.
DR PaxDb; Q922B2; -.
DR PeptideAtlas; Q922B2; -.
DR PRIDE; Q922B2; -.
DR ProteomicsDB; 257515; -.
DR Antibodypedia; 18737; 211 antibodies from 31 providers.
DR DNASU; 226414; -.
DR Ensembl; ENSMUST00000027602; ENSMUSP00000027602; ENSMUSG00000026356.
DR GeneID; 226414; -.
DR KEGG; mmu:226414; -.
DR UCSC; uc007clp.2; mouse.
DR CTD; 226414; -.
DR MGI; MGI:2442544; Dars.
DR VEuPathDB; HostDB:ENSMUSG00000026356; -.
DR eggNOG; KOG0556; Eukaryota.
DR GeneTree; ENSGT01030000234618; -.
DR HOGENOM; CLU_004553_2_1_1; -.
DR InParanoid; Q922B2; -.
DR OMA; WVHEIRD; -.
DR OrthoDB; 677307at2759; -.
DR PhylomeDB; Q922B2; -.
DR TreeFam; TF105676; -.
DR BRENDA; 6.1.1.12; 3474.
DR BioGRID-ORCS; 226414; 27 hits in 75 CRISPR screens.
DR ChiTaRS; Dars; mouse.
DR PRO; PR:Q922B2; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q922B2; protein.
DR Bgee; ENSMUSG00000026356; Expressed in yolk sac and 266 other tissues.
DR ExpressionAtlas; Q922B2; baseline and differential.
DR Genevisible; Q922B2; MM.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IDA:CAFA.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0004815; F:aspartate-tRNA ligase activity; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006422; P:aspartyl-tRNA aminoacylation; ISO:MGI.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_02075; Asp_tRNA_synth_type2; 1.
DR InterPro; IPR004364; Aa-tRNA-synt_II.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004523; Asp-tRNA_synthase_2.
DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR PANTHER; PTHR43450; PTHR43450; 1.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR PRINTS; PR01042; TRNASYNTHASP.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00458; aspS_nondisc; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 1: Evidence at protein level;
KW Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..501
FT /note="Aspartate--tRNA ligase, cytoplasmic"
FT /id="PRO_0000111011"
FT REGION 251..254
FT /note="Aspartate"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 273..275
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 273
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 281..283
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 424
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 427
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 431
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 472..475
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 52
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P14868"
FT MOD_RES 74
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P14868"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14868"
FT MOD_RES 374
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P14868"
FT CONFLICT 4
FT /note="T -> A (in Ref. 2; AAH08638)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 501 AA; 57147 MW; FC309A0CE55D36E6 CRC64;
MPSTNASRKG QEKPREIVDA AEDYAKERYG ISSMIQSQEK PDRVLVRVKD LTVQKADDVV
WVRARVHTSR AKGKQCFLVL RQQQFNVQAL VAVGDHASKQ MVKFAANINK ESIIDVEGVV
RKVNQKIGSC TQQDVELHVQ KIYVISLAEP RLPLQLDDAI RPEVEGEEDG RATVNQDTRL
DNRVIDLRTS TSQAIFRLQS GICHLFRETL INKGFVEIQT PKIISAASEG GANVFTVSYF
KNNAYLAQSP QLYKQMCICA DFEKVFCIGP VFRAEDSNTH RHLTEFVGLD IEMAFNYHYH
EVVEEIADTL VQIFKGLQER FQTEIQTVSK QFPCEPFKFL EPTLRLEYCE ALAMLREAGV
EMDDEEDLST PNEKLLGRLV KEKYDTDFYV LDKYPLAVRP FYTMPDPRNP KQSNSYDMFM
RGEEILSGAQ RIHDPQLLTE RALHHGIDLE KIKAYIDSFR FGAPPHAGGG IGLERVTMLF
LGLHNVRQTS MFPRDPKRLT P
