Leucine--tRNA ligase, cytoplasmic

Details

Name
Leucine--tRNA ligase, cytoplasmic
Kind
protein
Synonyms
  • 6.1.1.4
  • cLRS
  • KIAA1352
  • LARS
  • Leucyl-tRNA synthetase
  • LeuRS
Gene Name
LARS1
UniProtKB Entry
Q9P2J5Swiss-Prot
Organism
Humans
NCBI Taxonomy ID
9606
Amino acid sequence
>lcl|BSEQ0001534|Leucine--tRNA ligase, cytoplasmic
MAERKGTAKVDFLKKIEKEIQQKWDTERVFEVNASNLEKQTSKGKYFVTFPYPYMNGRLH
LGHTFSLSKCEFAVGYQRLKGKCCLFPFGLHCTGMPIKACADKLKREIELYGCPPDFPDE
EEEEEETSVKTEDIIIKDKAKGKKSKAAAKAGSSKYQWGIMKSLGLSDEEIVKFSEAEHW
LDYFPPLAIQDLKRMGLKVDWRRSFITTDVNPYYDSFVRWQFLTLRERNKIKFGKRYTIY
SPKDGQPCMDHDRQTGEGVGPQEYTLLKLKVLEPYPSKLSGLKGKNIFLVAATLRPETMF
GQTNCWVRPDMKYIGFETVNGDIFICTQKAARNMSYQGFTKDNGVVPVVKELMGEEILGA
SLSAPLTSYKVIYVLPMLTIKEDKGTGVVTSVPSDSPDDIAALRDLKKKQALRAKYGIRD
DMVLPFEPVPVIEIPGFGNLSAVTICDELKIQSQNDREKLAEAKEKIYLKGFYEGIMLVD
GFKGQKVQDVKKTIQKKMIDAGDALIYMEPEKQVMSRSSDECVVALCDQWYLDYGEENWK
KQTSQCLKNLETFCEETRRNFEATLGWLQEHACSRTYGLGTHLPWDEQWLIESLSDSTIY
MAFYTVAHLLQGGNLHGQAESPLGIRPQQMTKEVWDYVFFKEAPFPKTQIAKEKLDQLKQ
EFEFWYPVDLRVSGKDLVPNHLSYYLYNHVAMWPEQSDKWPTAVRANGHLLLNSEKMSKS
TGNFLTLTQAIDKFSADGMRLALADAGDTVEDANFVEAMADAGILRLYTWVEWVKEMVAN
WDSLRSGPASTFNDRVFASELNAGIIKTDQNYEKMMFKEALKTGFFEFQAAKDKYRELAV
EGMHRELVFRFIEVQTLLLAPFCPHLCEHIWTLLGKPDSIMNASWPVAGPVNEVLIHSSQ
YLMEVTHDLRLRLKNYMMPAKGKKTDKQPLQKPSHCTIYVAKNYPPWQHTTLSVLRKHFE
ANNGKLPDNKVIASELGSMPELKKYMKKVMPFVAMIKENLEKMGPRILDLQLEFDEKAVL
MENIVYLTNSLELEHIEVKFASEAEDKIREDCCPGKPLNVFRIEPGVSVSLVNPQPSNGH
FSTKIEIRQGDNCDSIIRRLMKMNRGIKDLSKVKLMRFDDPLLGPRRVPVLGKEYTEKTP
ISEHAVFNVDLMSKKIHLTENGIRVDIGDTIIYLVH
Number of residues
1176
Molecular Weight
134465.155
Theoretical pI
7.31
GO Classification
Functions
aminoacyl-tRNA editing activity / ATP binding / leucine-tRNA ligase activity
Processes
leucyl-tRNA aminoacylation / tRNA aminoacylation for protein translation
Components
cytoplasm / cytosol
General Function
Aminoacyl-tRNA synthetase that catalyzes the specific attachment of leucine to its cognate tRNA (tRNA(Leu)) (PubMed:25051973, PubMed:32232361). It performs tRNA aminoacylation in a two-step reaction: Leu is initially activated by ATP to form a leucyl-adenylate (Leu-AMP) intermediate; then the leucyl moiety is transferred to the acceptor 3' end of the tRNA to yield leucyl-tRNA (PubMed:25051973). To improve the fidelity of catalytic reactions, it is also able to hydrolyze misactivated aminoacyl-adenylate intermediates (pre-transfer editing) and mischarged aminoacyl-tRNAs (post-transfer editing) (PubMed:25051973)
Specific Function
aminoacyl-tRNA editing activity
Pfam Domain Function
Signal Regions
Not Available
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0010545|Leucine--tRNA ligase, cytoplasmic (LARS)
ATGGCGGAAAGAAAAGGAACAGCCAAAGTGGACTTTTTGAAGAAGATTGAGAAAGAAATC
CAACAGAAATGGGATACTGAGAGAGTGTTTGAGGTCAATGCATCTAATTTAGAGAAACAG
ACCAGCAAGGGCAAGTATTTTGTAACCTTCCCATATCCATATATGAATGGACGCCTTCAT
TTGGGACACACGTTTTCTTTATCCAAATGTGAGTTTGCTGTAGGGTACCAGCGATTGAAA
GGAAAATGTTGTCTGTTTCCCTTTGGCCTGCACTGTACTGGAATGCCTATTAAGGCATGT
GCTGATAAGTTGAAAAGAGAAATAGAGCTGTATGGTTGCCCCCCTGATTTTCCAGATGAA
GAAGAGGAAGAGGAAGAAACCAGTGTTAAAACAGAAGATATAATAATTAAGGATAAAGCT
AAAGGAAAAAAGAGTAAAGCTGCTGCTAAAGCTGGATCTTCTAAATACCAGTGGGGCATT
ATGAAATCCCTTGGCCTGTCTGATGAAGAGATAGTAAAATTTTCTGAAGCAGAACATTGG
CTTGATTATTTCCCGCCACTGGCTATTCAGGATTTAAAAAGAATGGGTTTGAAGGTAGAC
TGGCGTCGTTCCTTCATCACCACTGATGTTAATCCTTACTATGATTCATTTGTCAGATGG
CAATTTTTAACATTAAGAGAAAGAAACAAAATTAAATTTGGGAAGCGGTATACAATTTAC
TCTCCGAAAGATGGACAGCCTTGCATGGATCATGATAGACAAACTGGAGAGGGTGTTGGA
CCTCAGGAATATACTTTACTCAAATTGAAGGTGCTTGAGCCATACCCATCTAAATTAAGT
GGCCTGAAAGGTAAAAATATTTTCTTGGTGGCTGCTACTCTCAGACCTGAGACCATGTTT
GGGCAGACAAATTGTTGGGTTCGTCCTGATATGAAGTACATTGGATTTGAGACGGTGAAT
GGTGATATATTCATCTGTACCCAAAAAGCAGCCAGGAATATGTCATACCAGGGCTTTACC
AAAGACAATGGCGTGGTGCCTGTTGTTAAGGAATTAATGGGGGAGGAAATTCTTGGTGCA
TCACTTTCTGCACCTTTAACATCATACAAGGTGATCTATGTTCTCCCAATGCTAACTATT
AAGGAGGATAAAGGCACTGGTGTGGTTACAAGTGTTCCTTCCGACTCCCCTGATGATATT
GCTGCCCTCAGAGACTTGAAGAAAAAGCAAGCCTTACGAGCAAAATATGGAATTAGAGAT
GACATGGTCTTGCCATTTGAGCCGGTGCCAGTCATTGAAATCCCAGGTTTTGGAAATCTT
TCTGCTGTAACCATTTGTGATGAGTTGAAAATTCAGAGCCAGAATGACCGGGAAAAACTT
GCAGAAGCAAAGGAGAAGATATATCTAAAAGGATTTTATGAGGGTATCATGTTGGTGGAT
GGATTTAAAGGACAGAAGGTTCAAGATGTAAAGAAGACTATTCAGAAAAAGATGATTGAC
GCTGGAGATGCACTTATTTACATGGAACCAGAGAAACAAGTGATGTCCAGGTCGTCAGAT
GAATGTGTTGTGGCTCTGTGTGACCAGTGGTACTTGGATTATGGAGAAGAGAATTGGAAG
AAACAGACATCTCAGTGCTTGAAGAACCTGGAAACATTCTGTGAGGAGACCAGGAGGAAT
TTTGAAGCCACCTTAGGTTGGCTACAAGAACATGCTTGCTCAAGAACTTATGGTCTAGGC
ACTCACCTGCCTTGGGATGAGCAGTGGCTGATTGAATCACTTTCTGACTCCACTATTTAC
ATGGCATTTTACACAGTTGCACACCTATTGCAGGGGGGTAACTTGCATGGACAGGCAGAG
TCTCCGCTGGGCATTAGACCGCAACAGATGACCAAGGAAGTTTGGGATTATGTTTTCTTC
AAGGAGGCTCCATTTCCTAAGACTCAGATTGCAAAGGAAAAATTAGATCAGTTAAAGCAG
GAGTTTGAATTCTGGTATCCTGTTGATCTTCGCGTCTCTGGCAAGGATCTTGTTCCAAAT
CATCTTTCATATTACCTTTATAATCATGTGGCTATGTGGCCGGAACAAAGTGACAAATGG
CCTACAGCTGTGAGAGCAAATGGACATCTCCTCCTGAACTCTGAGAAGATGTCAAAATCC
ACAGGCAACTTCCTCACTTTGACCCAAGCTATTGACAAATTTTCAGCAGATGGAATGCGT
TTGGCTCTGGCTGATGCTGGTGACACTGTAGAAGATGCCAACTTTGTGGAAGCCATGGCA
GATGCAGGTATTCTCCGTCTGTACACCTGGGTAGAGTGGGTGAAAGAAATGGTTGCCAAC
TGGGACAGCCTAAGAAGTGGTCCTGCCAGCACTTTCAATGATAGAGTTTTTGCCAGTGAA
TTGAATGCAGGAATTATAAAAACAGATCAAAACTATGAAAAGATGATGTTTAAAGAAGCT
TTGAAAACAGGGTTTTTTGAGTTTCAGGCCGCAAAAGATAAGTACCGTGAATTGGCTGTG
GAAGGGATGCACAGAGAACTTGTGTTCCGGTTTATTGAAGTTCAGACACTTCTCCTCGCT
CCATTCTGTCCACATTTGTGTGAGCACATCTGGACACTCCTGGGAAAGCCTGACTCAATT
ATGAATGCTTCATGGCCTGTGGCAGGTCCTGTTAATGAAGTTTTAATACACTCCTCACAG
TATCTTATGGAAGTAACACATGACCTTAGACTACGACTCAAGAACTATATGATGCCAGCT
AAAGGGAAGAAGACTGACAAACAACCCCTGCAGAAGCCCTCACATTGCACCATCTATGTG
GCAAAGAACTATCCACCTTGGCAACATACCACCCTGTCTGTTCTACGTAAACACTTTGAG
GCCAATAACGGAAAACTGCCTGACAACAAAGTCATTGCTAGTGAACTAGGCAGTATGCCA
GAACTGAAGAAATACATGAAGAAAGTCATGCCATTTGTTGCCATGATTAAGGAAAATCTG
GAGAAGATGGGGCCTCGTATTCTGGATTTGCAATTAGAATTTGATGAAAAGGCTGTGCTT
ATGGAGAATATAGTCTATCTGACTAATTCGCTTGAGCTAGAACACATAGAAGTCAAGTTT
GCCTCCGAAGCAGAAGATAAAATCAGGGAAGACTGCTGTCCTGGGAAACCACTTAATGTT
TTTAGAATAGAACCTGGTGTGTCCGTTTCTCTGGTGAATCCCCAGCCATCCAATGGCCAC
TTCTCAACCAAAATTGAAATCAGGCAAGGAGATAACTGTGATTCCATAATCAGGCGTTTA
ATGAAAATGAATCGAGGAATTAAAGACCTTTCCAAAGTGAAACTGATGAGATTTGATGAT
CCACTGTTGGGGCCTCGACGAGTTCCTGTCCTGGGAAAGGAGTACACCGAGAAGACCCCC
ATTTCTGAGCATGCTGTTTTCAATGTGGACCTCATGAGCAAGAAAATTCATCTGACTGAG
AATGGGATAAGGGTGGATATTGGCGATACAATAATCTATCTGGTTCATTAA
Chromosome Location
5
Locus
5q32
External Identifiers
ResourceLink
UniProtKB IDQ9P2J5
UniProtKB Entry NameSYLC_HUMAN
GenBank Protein ID7804450
GenBank Gene IDD84223
GeneCard IDLARS1
GenAtlas IDLARS
HGNC IDHGNC:6512
PDB ID(s)2WFD, 6KID, 6KIE, 6KQY, 6KR7, 6LPF, 6LR6
KEGG IDhsa:51520
NCBI Gene ID51520
General References
  1. Nagase T, Kikuno R, Ishikawa KI, Hirosawa M, Ohara O: Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Feb 28;7(1):65-73. [Article]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [Article]
  3. Schmutz J, Martin J, Terry A, Couronne O, Grimwood J, Lowry S, Gordon LA, Scott D, Xie G, Huang W, Hellsten U, Tran-Gyamfi M, She X, Prabhakar S, Aerts A, Altherr M, Bajorek E, Black S, Branscomb E, Caoile C, Challacombe JF, Chan YM, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Lopez F, Lou Y, Martinez D, Medina C, Morgan J, Nandkeshwar R, Noonan JP, Pitluck S, Pollard M, Predki P, Priest J, Ramirez L, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wheeler J, Wu K, Yang J, Dickson M, Cheng JF, Eichler EE, Olsen A, Pennacchio LA, Rokhsar DS, Richardson P, Lucas SM, Myers RM, Rubin EM: The DNA sequence and comparative analysis of human chromosome 5. Nature. 2004 Sep 16;431(7006):268-74. [Article]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  5. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [Article]
  6. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]
  7. Vaca Jacome AS, Rabilloud T, Schaeffer-Reiss C, Rompais M, Ayoub D, Lane L, Bairoch A, Van Dorsselaer A, Carapito C: N-terminome analysis of the human mitochondrial proteome. Proteomics. 2015 Jul;15(14):2519-24. doi: 10.1002/pmic.201400617. Epub 2015 Jun 8. [Article]
  8. Seiradake E, Mao W, Hernandez V, Baker SJ, Plattner JJ, Alley MR, Cusack S: Crystal structures of the human and fungal cytosolic Leucyl-tRNA synthetase editing domains: A structural basis for the rational design of antifungal benzoxaboroles. J Mol Biol. 2009 Jul 10;390(2):196-207. doi: 10.1016/j.jmb.2009.04.073. Epub 2009 May 6. [Article]
  9. Casey JP, McGettigan P, Lynam-Lennon N, McDermott M, Regan R, Conroy J, Bourke B, O'Sullivan J, Crushell E, Lynch S, Ennis S: Identification of a mutation in LARS as a novel cause of infantile hepatopathy. Mol Genet Metab. 2012 Jul;106(3):351-8. doi: 10.1016/j.ymgme.2012.04.017. Epub 2012 Apr 26. [Article]

Associated Data

Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
Leucineinvestigational, nutraceuticalunknowntargetDetails