SYLC_HUMAN
ID SYLC_HUMAN Reviewed; 1176 AA.
AC Q9P2J5; A2RRR4; A7E266; B4DJ10; Q2TU79; Q9NSE1;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Leucine--tRNA ligase, cytoplasmic;
DE EC=6.1.1.4;
DE AltName: Full=Leucyl-tRNA synthetase;
DE Short=LeuRS;
GN Name=LARS1 {ECO:0000312|HGNC:HGNC:6512}; Synonyms=KIAA1352, LARS;
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), AND VARIANT LYS-1088.
RC TISSUE=Brain;
RA Motegi H., Noda T., Shiba K.;
RT "Cloning and sequence determination of a human cytoplasmic leucyl-tRNA
RT synthetase gene.";
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Hippocampus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RA Kim J.W., Kim H.K., Shin S.M.;
RT "Identification of a human cell proliferation gene.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167 AND SER-720, 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 [10]
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 [11]
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 [12]
RP X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 260-509 IN COMPLEX WITH SYNTHETIC
RP INHIBITOR AND AMP, AND FUNCTION.
RX PubMed=19426743; DOI=10.1016/j.jmb.2009.04.073;
RA Seiradake E., Mao W., Hernandez V., Baker S.J., Plattner J.J.,
RA Alley M.R.K., Cusack S.;
RT "Crystal structures of the human and fungal cytosolic Leucyl-tRNA
RT synthetase editing domains: A structural basis for the rational design of
RT antifungal benzoxaboroles.";
RL J. Mol. Biol. 390:196-207(2009).
RN [13]
RP VARIANT ILFS1 CYS-373, AND VARIANT ARG-82.
RX PubMed=22607940; DOI=10.1016/j.ymgme.2012.04.017;
RA Casey J.P., McGettigan P., Lynam-Lennon N., McDermott M., Regan R.,
RA Conroy J., Bourke B., O'Sullivan J., Crushell E., Lynch S., Ennis S.;
RT "Identification of a mutation in LARS as a novel cause of infantile
RT hepatopathy.";
RL Mol. Genet. Metab. 106:351-358(2012).
CC -!- FUNCTION: Catalyzes the specific attachment of an amino acid to its
CC cognate tRNA in a two 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. Exhibits a post-transfer editing activity to hydrolyze
CC mischarged tRNAs. {ECO:0000269|PubMed:19426743}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-
CC tRNA(Leu); Xref=Rhea:RHEA:11688, Rhea:RHEA-COMP:9613, Rhea:RHEA-
CC COMP:9622, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57427,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78494, ChEBI:CHEBI:456215; EC=6.1.1.4;
CC -!- ACTIVITY REGULATION: 5-fluoro-1,3-dihydro-1-hydroxy-1,2-benzoxaborole
CC inhibits LARS1 by forming a covalent adduct with the 3' adenosine of
CC tRNA(Leu) at the editing site, thus locking the enzyme in an inactive
CC conformation.
CC -!- INTERACTION:
CC Q9P2J5; P54136: RARS1; NbExp=4; IntAct=EBI-356077, EBI-355482;
CC Q9P2J5; Q8N122: RPTOR; NbExp=3; IntAct=EBI-356077, EBI-1567928;
CC Q9P2J5; Q9NQL2: RRAGD; NbExp=13; IntAct=EBI-356077, EBI-992949;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9P2J5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P2J5-2; Sequence=VSP_057205;
CC Name=3;
CC IsoId=Q9P2J5-3; Sequence=VSP_057204;
CC -!- DISEASE: Infantile liver failure syndrome 1 (ILFS1) [MIM:615438]: A
CC life-threatening disorder of hepatic function that manifests with acute
CC liver failure in the first few months of life. Clinical features
CC include anemia, renal tubulopathy, developmental delay, seizures,
CC failure to thrive, and liver steatosis and fibrosis.
CC {ECO:0000269|PubMed:22607940}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92590.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D84223; BAA95667.1; -; mRNA.
DR EMBL; AB037773; BAA92590.1; ALT_INIT; mRNA.
DR EMBL; AY513284; AAT08037.1; -; mRNA.
DR EMBL; AY926480; AAX10025.1; -; mRNA.
DR EMBL; AK295874; BAG58672.1; -; mRNA.
DR EMBL; AC091887; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC091959; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW61848.1; -; Genomic_DNA.
DR EMBL; BC131798; AAI31799.1; -; mRNA.
DR EMBL; BC150213; AAI50214.1; -; mRNA.
DR EMBL; BC151214; AAI51215.1; -; mRNA.
DR EMBL; BC152422; AAI52423.1; -; mRNA.
DR CCDS; CCDS34265.1; -. [Q9P2J5-1]
DR CCDS; CCDS83029.1; -. [Q9P2J5-2]
DR RefSeq; NP_001304893.1; NM_001317964.1.
DR RefSeq; NP_001304894.1; NM_001317965.1. [Q9P2J5-2]
DR RefSeq; NP_057544.2; NM_016460.3.
DR RefSeq; NP_064502.9; NM_020117.10. [Q9P2J5-1]
DR RefSeq; XP_011535958.1; XM_011537656.2. [Q9P2J5-2]
DR PDB; 2WFD; X-ray; 3.25 A; A/B=260-509.
DR PDB; 6KID; X-ray; 3.15 A; A=1-1176.
DR PDB; 6KIE; X-ray; 3.15 A; A=1-1061.
DR PDB; 6KQY; X-ray; 3.30 A; A=1-1176.
DR PDB; 6KR7; X-ray; 4.00 A; A=1-1176.
DR PDB; 6LPF; X-ray; 2.49 A; A/B=1-1070.
DR PDB; 6LR6; X-ray; 3.01 A; A/B=1-1070.
DR PDBsum; 2WFD; -.
DR PDBsum; 6KID; -.
DR PDBsum; 6KIE; -.
DR PDBsum; 6KQY; -.
DR PDBsum; 6KR7; -.
DR PDBsum; 6LPF; -.
DR PDBsum; 6LR6; -.
DR AlphaFoldDB; Q9P2J5; -.
DR SMR; Q9P2J5; -.
DR BioGRID; 119584; 272.
DR CORUM; Q9P2J5; -.
DR IntAct; Q9P2J5; 65.
DR MINT; Q9P2J5; -.
DR STRING; 9606.ENSP00000377954; -.
DR BindingDB; Q9P2J5; -.
DR ChEMBL; CHEMBL3258; -.
DR DrugBank; DB00149; Leucine.
DR MoonProt; Q9P2J5; -.
DR GlyGen; Q9P2J5; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; Q9P2J5; -.
DR MetOSite; Q9P2J5; -.
DR PhosphoSitePlus; Q9P2J5; -.
DR SwissPalm; Q9P2J5; -.
DR BioMuta; LARS; -.
DR DMDM; 48428689; -.
DR EPD; Q9P2J5; -.
DR jPOST; Q9P2J5; -.
DR MassIVE; Q9P2J5; -.
DR MaxQB; Q9P2J5; -.
DR PaxDb; Q9P2J5; -.
DR PeptideAtlas; Q9P2J5; -.
DR PRIDE; Q9P2J5; -.
DR ProteomicsDB; 4339; -.
DR ProteomicsDB; 83822; -. [Q9P2J5-1]
DR ABCD; Q9P2J5; 2 sequenced antibodies.
DR Antibodypedia; 45640; 123 antibodies from 31 providers.
DR DNASU; 51520; -.
DR Ensembl; ENST00000274562.13; ENSP00000274562.10; ENSG00000133706.19. [Q9P2J5-3]
DR Ensembl; ENST00000394434.7; ENSP00000377954.2; ENSG00000133706.19. [Q9P2J5-1]
DR Ensembl; ENST00000510191.5; ENSP00000426005.1; ENSG00000133706.19. [Q9P2J5-2]
DR Ensembl; ENST00000674174.1; ENSP00000501434.1; ENSG00000133706.19. [Q9P2J5-2]
DR GeneID; 51520; -.
DR KEGG; hsa:51520; -.
DR MANE-Select; ENST00000394434.7; ENSP00000377954.2; NM_020117.11; NP_064502.9.
DR UCSC; uc003lnx.2; human. [Q9P2J5-1]
DR CTD; 51520; -.
DR DisGeNET; 51520; -.
DR GeneCards; LARS1; -.
DR HGNC; HGNC:6512; LARS1.
DR HPA; ENSG00000133706; Low tissue specificity.
DR MalaCards; LARS1; -.
DR MIM; 151350; gene.
DR MIM; 615438; phenotype.
DR neXtProt; NX_Q9P2J5; -.
DR OpenTargets; ENSG00000133706; -.
DR Orphanet; 370088; Acute infantile liver failure-multisystemic involvement syndrome.
DR PharmGKB; PA30297; -.
DR VEuPathDB; HostDB:ENSG00000133706; -.
DR eggNOG; KOG0437; Eukaryota.
DR GeneTree; ENSGT00390000012163; -.
DR HOGENOM; CLU_004174_2_1_1; -.
DR InParanoid; Q9P2J5; -.
DR OMA; AWNMAFQ; -.
DR OrthoDB; 75155at2759; -.
DR PhylomeDB; Q9P2J5; -.
DR TreeFam; TF105718; -.
DR BRENDA; 6.1.1.4; 2681.
DR PathwayCommons; Q9P2J5; -.
DR Reactome; R-HSA-2408522; Selenoamino acid metabolism.
DR Reactome; R-HSA-379716; Cytosolic tRNA aminoacylation.
DR SABIO-RK; Q9P2J5; -.
DR SignaLink; Q9P2J5; -.
DR BioGRID-ORCS; 51520; 772 hits in 1083 CRISPR screens.
DR ChiTaRS; LARS; human.
DR EvolutionaryTrace; Q9P2J5; -.
DR GeneWiki; Leucyl-tRNA_synthetase; -.
DR GenomeRNAi; 51520; -.
DR Pharos; Q9P2J5; Tchem.
DR PRO; PR:Q9P2J5; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9P2J5; protein.
DR Bgee; ENSG00000133706; Expressed in Brodmann (1909) area 23 and 209 other tissues.
DR ExpressionAtlas; Q9P2J5; baseline and differential.
DR Genevisible; Q9P2J5; HS.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:CAFA.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0012505; C:endomembrane system; IDA:CAFA.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:CAFA.
DR GO; GO:0005764; C:lysosome; IMP:CAFA.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004819; F:glutamine-tRNA ligase activity; IDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IMP:CAFA.
DR GO; GO:0004823; F:leucine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0034198; P:cellular response to amino acid starvation; IMP:CAFA.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IMP:CAFA.
DR GO; GO:0071233; P:cellular response to leucine; IMP:CAFA.
DR GO; GO:1990253; P:cellular response to leucine starvation; IMP:CAFA.
DR GO; GO:0006425; P:glutaminyl-tRNA aminoacylation; IDA:UniProtKB.
DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IBA:GO_Central.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IMP:CAFA.
DR GO; GO:0032008; P:positive regulation of TOR signaling; IMP:CAFA.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IMP:CAFA.
DR GO; GO:0008361; P:regulation of cell size; IMP:CAFA.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; TAS:Reactome.
DR Gene3D; 3.40.50.620; -; 1.
DR Gene3D; 3.90.740.10; -; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR004493; Leu-tRNA-synth_Ia_arc/euk.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR PANTHER; PTHR45794; PTHR45794; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00395; leuS_arch; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
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..1176
FT /note="Leucine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000152150"
FT REGION 260..509
FT /note="Editing domain"
FT MOTIF 53..63
FT /note="'HIGH' region"
FT MOTIF 716..720
FT /note="'KMSKS' region"
FT BINDING 719
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 720
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 970
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BMJ2"
FT MOD_RES 1047
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BMJ2"
FT VAR_SEQ 1..691
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_057204"
FT VAR_SEQ 1..54
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057205"
FT VARIANT 82
FT /note="K -> R (in dbSNP:rs112954500)"
FT /evidence="ECO:0000269|PubMed:22607940"
FT /id="VAR_070437"
FT VARIANT 373
FT /note="Y -> C (in ILFS1; dbSNP:rs201861847)"
FT /evidence="ECO:0000269|PubMed:22607940"
FT /id="VAR_070438"
FT VARIANT 1088
FT /note="R -> K (in dbSNP:rs10988)"
FT /evidence="ECO:0000269|Ref.1"
FT /id="VAR_052637"
FT CONFLICT 271
FT /note="V -> A (in Ref. 1; BAA95667)"
FT /evidence="ECO:0000305"
FT CONFLICT 892
FT /note="N -> D (in Ref. 1; BAA95667)"
FT /evidence="ECO:0000305"
FT CONFLICT 1026
FT /note="Y -> C (in Ref. 7; AAI31799)"
FT /evidence="ECO:0000305"
FT HELIX 8..27
FT /evidence="ECO:0007829|PDB:6LPF"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:6LPF"
FT HELIX 34..37
FT /evidence="ECO:0007829|PDB:6LPF"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:6LPF"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:6KID"
FT HELIX 61..79
FT /evidence="ECO:0007829|PDB:6LPF"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:6LPF"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:6KIE"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:6KIE"
FT HELIX 96..110
FT /evidence="ECO:0007829|PDB:6LPF"
FT TURN 112..115
FT /evidence="ECO:0007829|PDB:6KID"
FT HELIX 157..163
FT /evidence="ECO:0007829|PDB:6LPF"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:6LPF"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:6LPF"
FT HELIX 177..195
FT /evidence="ECO:0007829|PDB:6LPF"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:6LPF"
FT HELIX 212..227
FT /evidence="ECO:0007829|PDB:6LPF"
FT STRAND 231..241
FT /evidence="ECO:0007829|PDB:6LPF"
FT TURN 242..245
FT /evidence="ECO:0007829|PDB:6LPF"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:6KID"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:6LPF"
FT STRAND 261..271
FT /evidence="ECO:0007829|PDB:6LPF"
FT HELIX 277..282
FT /evidence="ECO:0007829|PDB:6LPF"
FT STRAND 287..294
FT /evidence="ECO:0007829|PDB:6LPF"
FT HELIX 296..301
FT /evidence="ECO:0007829|PDB:6LPF"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:6LPF"
FT STRAND 311..317
FT /evidence="ECO:0007829|PDB:6LPF"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:6KID"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:6LPF"
FT HELIX 328..336
FT /evidence="ECO:0007829|PDB:6LPF"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:6LPF"
FT STRAND 348..353
FT /evidence="ECO:0007829|PDB:6LPF"
FT HELIX 354..357
FT /evidence="ECO:0007829|PDB:6LPF"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:6LPF"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:2WFD"
FT STRAND 372..376
FT /evidence="ECO:0007829|PDB:6LPF"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:6LPF"
FT STRAND 387..391
FT /evidence="ECO:0007829|PDB:6LPF"
FT TURN 393..395
FT /evidence="ECO:0007829|PDB:6LPF"
FT HELIX 397..408
FT /evidence="ECO:0007829|PDB:6LPF"
FT HELIX 410..415
FT /evidence="ECO:0007829|PDB:6LPF"
FT HELIX 420..422
FT /evidence="ECO:0007829|PDB:6LPF"
FT TURN 423..425
FT /evidence="ECO:0007829|PDB:6LPF"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:6LPF"
FT TURN 435..437
FT /evidence="ECO:0007829|PDB:6LPF"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:6LPF"
FT HELIX 441..448
FT /evidence="ECO:0007829|PDB:6LPF"
FT HELIX 457..466
FT /evidence="ECO:0007829|PDB:6LPF"
FT STRAND 467..469
FT /evidence="ECO:0007829|PDB:6KQY"
FT TURN 470..472
FT /evidence="ECO:0007829|PDB:6LPF"
FT STRAND 479..482
FT /evidence="ECO:0007829|PDB:6KIE"
FT HELIX 487..489
FT /evidence="ECO:0007829|PDB:6LPF"
FT HELIX 491..500
FT /evidence="ECO:0007829|PDB:6LPF"
FT STRAND 503..512
FT /evidence="ECO:0007829|PDB:6LPF"
FT STRAND 516..519
FT /evidence="ECO:0007829|PDB:6KQY"
FT STRAND 523..533
FT /evidence="ECO:0007829|PDB:6LPF"
FT HELIX 537..549
FT /evidence="ECO:0007829|PDB:6LPF"
FT STRAND 550..554
FT /evidence="ECO:0007829|PDB:6LPF"
FT HELIX 555..567
FT /evidence="ECO:0007829|PDB:6LPF"
FT STRAND 570..572
FT /evidence="ECO:0007829|PDB:6LPF"
FT STRAND 574..580
FT /evidence="ECO:0007829|PDB:6LPF"
FT TURN 593..595
FT /evidence="ECO:0007829|PDB:6LPF"
FT STRAND 596..599
FT /evidence="ECO:0007829|PDB:6LPF"
FT HELIX 601..610
FT /evidence="ECO:0007829|PDB:6LPF"
FT TURN 611..613
FT /evidence="ECO:0007829|PDB:6LPF"
FT HELIX 627..629
FT /evidence="ECO:0007829|PDB:6KID"
FT HELIX 632..639
FT /evidence="ECO:0007829|PDB:6LPF"
FT STRAND 640..643
FT /evidence="ECO:0007829|PDB:6KQY"
FT HELIX 652..665
FT /evidence="ECO:0007829|PDB:6LPF"
FT STRAND 670..674
FT /evidence="ECO:0007829|PDB:6LPF"
FT HELIX 675..677
FT /evidence="ECO:0007829|PDB:6LPF"
FT TURN 678..680
FT /evidence="ECO:0007829|PDB:6LPF"
FT HELIX 681..692
FT /evidence="ECO:0007829|PDB:6LPF"
FT STRAND 693..695
FT /evidence="ECO:0007829|PDB:6KID"
FT HELIX 697..699
FT /evidence="ECO:0007829|PDB:6LPF"
FT STRAND 703..707
FT /evidence="ECO:0007829|PDB:6LPF"
FT STRAND 710..712
FT /evidence="ECO:0007829|PDB:6LPF"
FT HELIX 719..721
FT /evidence="ECO:0007829|PDB:6LPF"
FT HELIX 727..744
FT /evidence="ECO:0007829|PDB:6LPF"
FT STRAND 748..751
FT /evidence="ECO:0007829|PDB:6LPF"
FT STRAND 753..755
FT /evidence="ECO:0007829|PDB:6LPF"
FT HELIX 757..779
FT /evidence="ECO:0007829|PDB:6LPF"
FT HELIX 781..783
FT /evidence="ECO:0007829|PDB:6LR6"
FT HELIX 792..813
FT /evidence="ECO:0007829|PDB:6LPF"
FT HELIX 817..824
FT /evidence="ECO:0007829|PDB:6LPF"
FT HELIX 826..838
FT /evidence="ECO:0007829|PDB:6LPF"
FT HELIX 845..859
FT /evidence="ECO:0007829|PDB:6LPF"
FT TURN 860..862
FT /evidence="ECO:0007829|PDB:6LPF"
FT HELIX 864..873
FT /evidence="ECO:0007829|PDB:6LPF"
FT HELIX 880..882
FT /evidence="ECO:0007829|PDB:6LPF"
FT HELIX 893..912
FT /evidence="ECO:0007829|PDB:6LPF"
FT TURN 913..915
FT /evidence="ECO:0007829|PDB:6KQY"
FT STRAND 935..939
FT /evidence="ECO:0007829|PDB:6LPF"
FT HELIX 946..961
FT /evidence="ECO:0007829|PDB:6LPF"
FT STRAND 962..964
FT /evidence="ECO:0007829|PDB:6KQY"
FT HELIX 969..977
FT /evidence="ECO:0007829|PDB:6LPF"
FT HELIX 980..985
FT /evidence="ECO:0007829|PDB:6LPF"
FT HELIX 986..1003
FT /evidence="ECO:0007829|PDB:6LPF"
FT HELIX 1004..1008
FT /evidence="ECO:0007829|PDB:6LPF"
FT STRAND 1009..1011
FT /evidence="ECO:0007829|PDB:6KIE"
FT HELIX 1016..1021
FT /evidence="ECO:0007829|PDB:6LPF"
FT HELIX 1024..1031
FT /evidence="ECO:0007829|PDB:6LPF"
FT STRAND 1034..1039
FT /evidence="ECO:0007829|PDB:6LPF"
FT STRAND 1041..1044
FT /evidence="ECO:0007829|PDB:6LPF"
FT HELIX 1046..1051
FT /evidence="ECO:0007829|PDB:6LPF"
FT STRAND 1058..1060
FT /evidence="ECO:0007829|PDB:6LPF"
SQ SEQUENCE 1176 AA; 134466 MW; 44A4D1A1EF31634A CRC64;
MAERKGTAKV DFLKKIEKEI QQKWDTERVF EVNASNLEKQ TSKGKYFVTF PYPYMNGRLH
LGHTFSLSKC EFAVGYQRLK GKCCLFPFGL HCTGMPIKAC ADKLKREIEL YGCPPDFPDE
EEEEEETSVK TEDIIIKDKA KGKKSKAAAK AGSSKYQWGI MKSLGLSDEE IVKFSEAEHW
LDYFPPLAIQ DLKRMGLKVD WRRSFITTDV NPYYDSFVRW QFLTLRERNK IKFGKRYTIY
SPKDGQPCMD HDRQTGEGVG PQEYTLLKLK VLEPYPSKLS GLKGKNIFLV AATLRPETMF
GQTNCWVRPD MKYIGFETVN GDIFICTQKA ARNMSYQGFT KDNGVVPVVK ELMGEEILGA
SLSAPLTSYK VIYVLPMLTI KEDKGTGVVT SVPSDSPDDI AALRDLKKKQ ALRAKYGIRD
DMVLPFEPVP VIEIPGFGNL SAVTICDELK IQSQNDREKL AEAKEKIYLK GFYEGIMLVD
GFKGQKVQDV KKTIQKKMID AGDALIYMEP EKQVMSRSSD ECVVALCDQW YLDYGEENWK
KQTSQCLKNL ETFCEETRRN FEATLGWLQE HACSRTYGLG THLPWDEQWL IESLSDSTIY
MAFYTVAHLL QGGNLHGQAE SPLGIRPQQM TKEVWDYVFF KEAPFPKTQI AKEKLDQLKQ
EFEFWYPVDL RVSGKDLVPN HLSYYLYNHV AMWPEQSDKW PTAVRANGHL LLNSEKMSKS
TGNFLTLTQA IDKFSADGMR LALADAGDTV EDANFVEAMA DAGILRLYTW VEWVKEMVAN
WDSLRSGPAS TFNDRVFASE LNAGIIKTDQ NYEKMMFKEA LKTGFFEFQA AKDKYRELAV
EGMHRELVFR FIEVQTLLLA PFCPHLCEHI WTLLGKPDSI MNASWPVAGP VNEVLIHSSQ
YLMEVTHDLR LRLKNYMMPA KGKKTDKQPL QKPSHCTIYV AKNYPPWQHT TLSVLRKHFE
ANNGKLPDNK VIASELGSMP ELKKYMKKVM PFVAMIKENL EKMGPRILDL QLEFDEKAVL
MENIVYLTNS LELEHIEVKF ASEAEDKIRE DCCPGKPLNV FRIEPGVSVS LVNPQPSNGH
FSTKIEIRQG DNCDSIIRRL MKMNRGIKDL SKVKLMRFDD PLLGPRRVPV LGKEYTEKTP
ISEHAVFNVD LMSKKIHLTE NGIRVDIGDT IIYLVH
