ID SYDC_HUMAN Reviewed; 501 AA. AC P14868; A8K3J2; D3DP77; Q2TNI3; Q32Q69; Q53HV4; Q53YC5; Q68CR9; Q9BW52; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 16-APR-2002, sequence version 2. DT 27-MAR-2024, entry version 229. DE RecName: Full=Aspartate--tRNA ligase, cytoplasmic {ECO:0000305}; DE EC=6.1.1.12 {ECO:0000250|UniProtKB:P15178}; DE AltName: Full=Aspartyl-tRNA synthetase; DE Short=AspRS; DE AltName: Full=Cell proliferation-inducing gene 40 protein; GN Name=DARS1 {ECO:0000312|HGNC:HGNC:2678}; Synonyms=DARS; GN ORFNames=PIG40; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=2674137; DOI=10.1016/s0021-9258(19)84749-x; RA Jacobo-Molina A., Peterson R., Yang D.C.H.; RT "cDNA sequence, predicted primary structure, and evolving amphiphilic helix RT of human aspartyl-tRNA synthetase."; RL J. Biol. Chem. 264:16608-16612(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kim J.W.; RT "Identification of a cell proliferation-inducing gene."; RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Heart; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Adipose tissue; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Embryo; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Eye; 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 [10] RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [11] RP INTERACTION WITH KARS1. RX PubMed=18029264; DOI=10.1016/j.bbrc.2007.11.028; RA Guzzo C.M., Yang D.C.H.; RT "Lysyl-tRNA synthetase interacts with EF1alpha, aspartyl-tRNA synthetase RT and p38 in vitro."; RL Biochem. Biophys. Res. Commun. 365:718-723(2008). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [13] RP SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=19131329; DOI=10.1074/jbc.m809636200; RA Kaminska M., Havrylenko S., Decottignies P., Gillet S., Le Marechal P., RA Negrutskii B., Mirande M.; RT "Dissection of the structural organization of the aminoacyl-tRNA synthetase RT complex."; RL J. Biol. Chem. 284:6053-6060(2009). RN [14] RP SUBCELLULAR LOCATION, AND SUBUNIT. RX PubMed=19289464; DOI=10.1074/jbc.m900480200; RA Kaminska M., Havrylenko S., Decottignies P., Le Marechal P., Negrutskii B., RA Mirande M.; RT "Dynamic Organization of Aminoacyl-tRNA Synthetase Complexes in the RT Cytoplasm of Human Cells."; RL J. Biol. Chem. 284:13746-13754(2009). RN [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-74 AND LYS-374, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [18] RP TISSUE SPECIFICITY, AND VARIANTS HBSL LEU-256; VAL-274; TYR-367; HIS-460; RP LEU-464; CYS-487; CYS-494 AND GLY-494. RX PubMed=23643384; DOI=10.1016/j.ajhg.2013.04.006; RA Taft R.J., Vanderver A., Leventer R.J., Damiani S.A., Simons C., RA Grimmond S.M., Miller D., Schmidt J., Lockhart P.J., Pope K., Ru K., RA Crawford J., Rosser T., de Coo I.F., Juneja M., Verma I.C., Prabhakar P., RA Blaser S., Raiman J., Pouwels P.J., Bevova M.R., Abbink T.E., RA van der Knaap M.S., Wolf N.I.; RT "Mutations in DARS cause hypomyelination with brain stem and spinal cord RT involvement and leg spasticity."; RL Am. J. Hum. Genet. 92:774-780(2013). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-52 AND SER-249, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [20] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [21] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [22] {ECO:0007744|PDB:4J15} RP X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS), AND SUBUNIT. RX PubMed=23609930; DOI=10.1002/prot.24306; RA Kim K.R., Park S.H., Kim H.S., Rhee K.H., Kim B.G., Kim D.G., Park M.S., RA Kim H.J., Kim S., Han B.W.; RT "Crystal structure of human cytosolic aspartyl-tRNA synthetase, a component RT of multi-tRNA synthetase complex."; RL Proteins 81:1840-1846(2013). 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 (PubMed:23609930). Part of a multisubunit complex CC that 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:19131329, PubMed:19289464). CC {ECO:0000269|PubMed:19131329, ECO:0000269|PubMed:19289464, CC ECO:0000269|PubMed:23609930}. CC -!- INTERACTION: CC P14868; Q13155: AIMP2; NbExp=10; IntAct=EBI-358730, EBI-745226; CC P14868; Q08050: FOXM1; NbExp=2; IntAct=EBI-358730, EBI-866480; CC P14868; P62993: GRB2; NbExp=2; IntAct=EBI-358730, EBI-401755; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:19289464}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P14868-1; Sequence=Displayed; CC Name=2; CC IsoId=P14868-2; Sequence=VSP_056192; CC -!- TISSUE SPECIFICITY: Expression in the developing and adult brain shows CC similar patterns. Highly expressed in the ventricular and CC subventricular zones, including hippocampal subfields, the midlateral CC temporal cortex and the frontal polar cortex. The cerebellum, cerebral CC cortex, hippocampus, and lateral ventricle show preferential neuronal CC expression. Expression in the peripheral neurons is evident in the CC colon. {ECO:0000269|PubMed:23643384}. CC -!- DISEASE: Hypomyelination with brainstem and spinal cord involvement and CC leg spasticity (HBSL) [MIM:615281]: An autosomal recessive CC leukoencephalopathy characterized by onset in the first year of life of CC severe spasticity, mainly affecting the lower limbs and resulting in an CC inability to achieve independent ambulation. Affected individuals show CC delayed motor development and nystagmus; some may have mild CC intellectual disability. Brain MRI shows hypomyelination and white CC matter lesions in the cerebrum, brainstem, cerebellum, and spinal cord. CC {ECO:0000269|PubMed:23643384}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. CC Type 2 subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J05032; AAA35567.1; -; mRNA. DR EMBL; AY762100; AAX07827.1; -; mRNA. DR EMBL; BT006710; AAP35356.1; -; mRNA. DR EMBL; AK290607; BAF83296.1; -; mRNA. DR EMBL; AK222476; BAD96196.1; -; mRNA. DR EMBL; CR749809; CAH18669.1; -; mRNA. DR EMBL; AC011999; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC093391; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471058; EAX11617.1; -; Genomic_DNA. DR EMBL; CH471058; EAX11620.1; -; Genomic_DNA. DR EMBL; BC000629; AAH00629.1; -; mRNA. DR EMBL; BC107749; AAI07750.1; -; mRNA. DR CCDS; CCDS2180.1; -. [P14868-1] DR PIR; A34393; SYHUDT. DR RefSeq; NP_001280241.1; NM_001293312.1. [P14868-2] DR RefSeq; NP_001340.2; NM_001349.3. [P14868-1] DR PDB; 4J15; X-ray; 2.24 A; A/B=1-501. DR PDB; 5Y6L; X-ray; 2.90 A; E=1-501. DR PDB; 6IY6; X-ray; 3.60 A; A/B/G/H=21-501. DR PDBsum; 4J15; -. DR PDBsum; 5Y6L; -. DR PDBsum; 6IY6; -. DR AlphaFoldDB; P14868; -. DR BMRB; P14868; -. DR SMR; P14868; -. DR BioGRID; 107984; 331. DR ComplexPortal; CPX-2469; Multiaminoacyl-tRNA synthetase complex. DR CORUM; P14868; -. DR IntAct; P14868; 64. DR MINT; P14868; -. DR STRING; 9606.ENSP00000264161; -. DR DrugBank; DB00128; Aspartic acid. DR DrugCentral; P14868; -. DR GlyGen; P14868; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P14868; -. DR MetOSite; P14868; -. DR PhosphoSitePlus; P14868; -. DR SwissPalm; P14868; -. DR BioMuta; DARS; -. DR DMDM; 20178330; -. DR OGP; P14868; -. DR REPRODUCTION-2DPAGE; IPI00216951; -. DR EPD; P14868; -. DR jPOST; P14868; -. DR MassIVE; P14868; -. DR MaxQB; P14868; -. DR PaxDb; 9606-ENSP00000264161; -. DR PeptideAtlas; P14868; -. DR ProteomicsDB; 53092; -. [P14868-1] DR ProteomicsDB; 66028; -. DR Pumba; P14868; -. DR ABCD; P14868; 1 sequenced antibody. DR Antibodypedia; 18737; 246 antibodies from 31 providers. DR DNASU; 1615; -. DR Ensembl; ENST00000264161.9; ENSP00000264161.4; ENSG00000115866.11. [P14868-1] DR GeneID; 1615; -. DR KEGG; hsa:1615; -. DR MANE-Select; ENST00000264161.9; ENSP00000264161.4; NM_001349.4; NP_001340.2. DR UCSC; uc002tux.2; human. [P14868-1] DR AGR; HGNC:2678; -. DR CTD; 1615; -. DR DisGeNET; 1615; -. DR GeneCards; DARS1; -. DR HGNC; HGNC:2678; DARS1. DR HPA; ENSG00000115866; Low tissue specificity. DR MalaCards; DARS1; -. DR MIM; 603084; gene. DR MIM; 615281; phenotype. DR neXtProt; NX_P14868; -. DR OpenTargets; ENSG00000115866; -. DR Orphanet; 363412; Hypomyelination with brain stem and spinal cord involvement and leg spasticity. DR PharmGKB; PA27146; -. DR VEuPathDB; HostDB:ENSG00000115866; -. DR eggNOG; KOG0556; Eukaryota. DR GeneTree; ENSGT01030000234618; -. DR HOGENOM; CLU_004553_2_1_1; -. DR InParanoid; P14868; -. DR OMA; WVHEIRD; -. DR OrthoDB; 382728at2759; -. DR PhylomeDB; P14868; -. DR TreeFam; TF105676; -. DR BRENDA; 6.1.1.12; 2681. DR PathwayCommons; P14868; -. DR Reactome; R-HSA-2408522; Selenoamino acid metabolism. DR Reactome; R-HSA-379716; Cytosolic tRNA aminoacylation. DR SignaLink; P14868; -. DR SIGNOR; P14868; -. DR BioGRID-ORCS; 1615; 830 hits in 1143 CRISPR screens. DR ChiTaRS; DARS; human. DR GeneWiki; DARS_(gene); -. DR GenomeRNAi; 1615; -. DR Pharos; P14868; Tbio. DR PRO; PR:P14868; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; P14868; Protein. DR Bgee; ENSG00000115866; Expressed in oocyte and 215 other cell types or tissues. DR ExpressionAtlas; P14868; baseline and differential. DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0045202; C:synapse; IEA:Ensembl. DR GO; GO:0004046; F:aminoacylase activity; TAS:ProtInc. DR GO; GO:0004815; F:aspartate-tRNA ligase activity; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IBA:GO_Central. DR GO; GO:0065003; P:protein-containing complex assembly; TAS:ProtInc. DR GO; GO:0006412; P:translation; TAS:ProtInc. DR CDD; cd04320; AspRS_cyto_N; 1. DR CDD; cd00776; AsxRS_core; 1. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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 NCBIfam; TIGR00458; aspS_nondisc; 1. DR PANTHER; PTHR43450:SF1; ASPARTATE--TRNA LIGASE, CYTOPLASMIC; 1. DR PANTHER; PTHR43450; ASPARTYL-TRNA SYNTHETASE; 1. DR Pfam; PF00152; tRNA-synt_2; 1. DR Pfam; PF01336; tRNA_anti-codon; 1. DR PRINTS; PR01042; TRNASYNTHASP. DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. DR Genevisible; P14868; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Aminoacyl-tRNA synthetase; KW ATP-binding; Cytoplasm; Disease variant; Ligase; Nucleotide-binding; KW Phosphoprotein; Protein biosynthesis; Reference proteome. FT CHAIN 1..501 FT /note="Aspartate--tRNA ligase, cytoplasmic" FT /id="PRO_0000111010" FT REGION 251..254 FT /note="Aspartate" FT /evidence="ECO:0000250" FT REGION 411..415 FT /note="Binding site for the 3'-end of tRNA" FT /evidence="ECO:0000255" 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:0007744|PubMed:23186163" FT MOD_RES 74 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 249 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 374 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 500 FT /note="Phosphothreonine; by PKA" FT /evidence="ECO:0000255" FT VAR_SEQ 1..100 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_056192" FT VARIANT 256 FT /note="M -> L (in HBSL; dbSNP:rs886037635)" FT /evidence="ECO:0000269|PubMed:23643384" FT /id="VAR_070038" FT VARIANT 274 FT /note="A -> V (in HBSL; dbSNP:rs369152939)" FT /evidence="ECO:0000269|PubMed:23643384" FT /id="VAR_070039" FT VARIANT 367 FT /note="D -> Y (in HBSL; dbSNP:rs370064817)" FT /evidence="ECO:0000269|PubMed:23643384" FT /id="VAR_070040" FT VARIANT 426 FT /note="L -> F (in dbSNP:rs1803165)" FT /id="VAR_027611" FT VARIANT 460 FT /note="R -> H (in HBSL; dbSNP:rs587776985)" FT /evidence="ECO:0000269|PubMed:23643384" FT /id="VAR_070041" FT VARIANT 464 FT /note="P -> L (in HBSL; dbSNP:rs148806569)" FT /evidence="ECO:0000269|PubMed:23643384" FT /id="VAR_070042" FT VARIANT 487 FT /note="R -> C (in HBSL; dbSNP:rs587776984)" FT /evidence="ECO:0000269|PubMed:23643384" FT /id="VAR_070043" FT VARIANT 494 FT /note="R -> C (in HBSL; dbSNP:rs147077598)" FT /evidence="ECO:0000269|PubMed:23643384" FT /id="VAR_070044" FT VARIANT 494 FT /note="R -> G (in HBSL; dbSNP:rs147077598)" FT /evidence="ECO:0000269|PubMed:23643384" FT /id="VAR_070045" FT CONFLICT 5..7 FT /note="SAS -> TQ (in Ref. 1; AAA35567)" FT /evidence="ECO:0000305" FT CONFLICT 31 FT /note="I -> T (in Ref. 9; AAI07750)" FT /evidence="ECO:0000305" FT CONFLICT 38 FT /note="Q -> H (in Ref. 5; BAD96196)" FT /evidence="ECO:0000305" FT CONFLICT 164 FT /note="A -> Q (in Ref. 1; AAA35567)" FT /evidence="ECO:0000305" FT CONFLICT 312 FT /note="Q -> H (in Ref. 2; AAX07827)" FT /evidence="ECO:0000305" FT CONFLICT 414 FT /note="N -> K (in Ref. 1; AAA35567)" FT /evidence="ECO:0000305" FT CONFLICT 447 FT /note="I -> N (in Ref. 1; AAA35567)" FT /evidence="ECO:0000305" FT HELIX 26..28 FT /evidence="ECO:0007829|PDB:4J15" FT STRAND 29..31 FT /evidence="ECO:0007829|PDB:4J15" FT HELIX 48..50 FT /evidence="ECO:0007829|PDB:4J15" FT HELIX 53..55 FT /evidence="ECO:0007829|PDB:4J15" FT STRAND 59..72 FT /evidence="ECO:0007829|PDB:4J15" FT STRAND 75..82 FT /evidence="ECO:0007829|PDB:4J15" FT STRAND 85..93 FT /evidence="ECO:0007829|PDB:4J15" FT TURN 94..96 FT /evidence="ECO:0007829|PDB:4J15" FT HELIX 99..107 FT /evidence="ECO:0007829|PDB:4J15" FT STRAND 113..122 FT /evidence="ECO:0007829|PDB:4J15" FT STRAND 134..146 FT /evidence="ECO:0007829|PDB:4J15" FT HELIX 156..160 FT /evidence="ECO:0007829|PDB:4J15" FT HELIX 176..181 FT /evidence="ECO:0007829|PDB:4J15" FT HELIX 183..186 FT /evidence="ECO:0007829|PDB:4J15" FT HELIX 190..212 FT /evidence="ECO:0007829|PDB:4J15" FT HELIX 250..259 FT /evidence="ECO:0007829|PDB:4J15" FT STRAND 264..271 FT /evidence="ECO:0007829|PDB:4J15" FT STRAND 286..294 FT /evidence="ECO:0007829|PDB:4J15" FT HELIX 300..320 FT /evidence="ECO:0007829|PDB:4J15" FT HELIX 322..331 FT /evidence="ECO:0007829|PDB:4J15" FT STRAND 340..342 FT /evidence="ECO:0007829|PDB:5Y6L" FT STRAND 344..347 FT /evidence="ECO:0007829|PDB:4J15" FT HELIX 348..357 FT /evidence="ECO:0007829|PDB:4J15" FT HELIX 370..384 FT /evidence="ECO:0007829|PDB:4J15" FT STRAND 387..392 FT /evidence="ECO:0007829|PDB:4J15" FT HELIX 396..398 FT /evidence="ECO:0007829|PDB:4J15" FT STRAND 407..409 FT /evidence="ECO:0007829|PDB:4J15" FT STRAND 412..420 FT /evidence="ECO:0007829|PDB:4J15" FT STRAND 423..431 FT /evidence="ECO:0007829|PDB:4J15" FT HELIX 435..444 FT /evidence="ECO:0007829|PDB:4J15" FT HELIX 450..452 FT /evidence="ECO:0007829|PDB:4J15" FT HELIX 453..457 FT /evidence="ECO:0007829|PDB:4J15" FT TURN 458..461 FT /evidence="ECO:0007829|PDB:4J15" FT STRAND 466..472 FT /evidence="ECO:0007829|PDB:4J15" FT HELIX 473..481 FT /evidence="ECO:0007829|PDB:4J15" FT HELIX 486..489 FT /evidence="ECO:0007829|PDB:4J15" SQ SEQUENCE 501 AA; 57136 MW; B181572DF0AF5F94 CRC64; MPSASASRKS QEKPREIMDA AEDYAKERYG ISSMIQSQEK PDRVLVRVRD LTIQKADEVV WVRARVHTSR AKGKQCFLVL RQQQFNVQAL VAVGDHASKQ MVKFAANINK ESIVDVEGVV RKVNQKIGSC TQQDVELHVQ KIYVISLAEP RLPLQLDDAV RPEAEGEEEG RATVNQDTRL DNRVIDLRTS TSQAVFRLQS GICHLFRETL INKGFVEIQT PKIISAASEG GANVFTVSYF KNNAYLAQSP QLYKQMCICA DFEKVFSIGP VFRAEDSNTH RHLTEFVGLD IEMAFNYHYH EVMEEIADTM VQIFKGLQER FQTEIQTVNK QFPCEPFKFL EPTLRLEYCE ALAMLREAGV EMGDEDDLST PNEKLLGHLV KEKYDTDFYI LDKYPLAVRP FYTMPDPRNP KQSNSYDMFM RGEEILSGAQ RIHDPQLLTE RALHHGIDLE KIKAYIDSFR FGAPPHAGGG IGLERVTMLF LGLHNVRQTS MFPRDPKRLT P //