UniProt Accession

 B4DER1_HUMAN; B4DER1 

Genbank Protein ID

 AC091887; AC091959; AK293750 

Genbank Nucleotide ID

 BAG57172.1 

Protein Name

 Leucine--tRNA ligase, cytoplasmic 

Protein Synonyms/Alias

 cDNA FLJ58157, highly similar to Leucyl-tRNA synthetase, cytoplasmic (EC 6.1.1.4) 

Gene Name

 LARS 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
5	***MAERKGTAKVDF	ubiquitination	[1, 2]
9	AERKGTAKVDFLKKI	ubiquitination	[1, 2]
23	IEKEIQQKWDTERVF	ubiquitination	[1, 3]
39	VNASNLEKQTSKGKY	ubiquitination	[1, 2, 3, 4, 5]
45	EKQTSKGKYFVTFPY	ubiquitination	[1]
128	AAKAGSSKYQWGIMK	ubiquitination	[1]
135	KYQWGIMKSLGLSDE	ubiquitination	[1, 3]
166	PLAIQDLKRMGLKVD	ubiquitination	[1, 2, 3, 5, 6, 7]
171	DLKRMGLKVDWRRSF	ubiquitination	[1, 2]
216	RYTIYSPKDGQPCMD	ubiquitination	[1]
241	PQEYTLLKLKVLEPY	ubiquitination	[1, 4, 7]
243	EYTLLKLKVLEPYPS	ubiquitination	[1]
251	VLEPYPSKLSGLKGK	acetylation	[8]
251	VLEPYPSKLSGLKGK	ubiquitination	[1, 2, 4, 7]
256	PSKLSGLKGKNIFLV	ubiquitination	[1]
258	KLSGLKGKNIFLVAA	ubiquitination	[1, 2]
302	DIFICTQKAARNMSY	ubiquitination	[2]
314	MSYQGFTKDNGVVPV	ubiquitination	[1, 3, 4, 5, 7]
323	NGVVPVVKELMGEEI	ubiquitination	[1]
357	MLTIKEDKGTGVVTS	acetylation	[8]
357	MLTIKEDKGTGVVTS	ubiquitination	[1, 3]
432	QSQNDREKLAEAKEK	ubiquitination	[1]
439	KLAEAKEKIYLKGFY	ubiquitination	[1]
456	IMLVDGFKGQKVQDV	ubiquitination	[1]
459	VDGFKGQKVQDVKKT	ubiquitination	[1]
470	VKKTIQKKMIDAGDA	ubiquitination	[1]
485	LIYMEPEKQVMSRSS	ubiquitination	[1, 3]
521	KQTSQCLKNLETFCE	ubiquitination	[1]
614	VWDYVFFKEAPFPKT	ubiquitination	[1, 3, 5, 6]
620	FKEAPFPKTQIAKEK	ubiquitination	[1, 2]
625	FPKTQIAKEKLDQLK	ubiquitination	[1]
632	KEKLDQLKQEFEFWY	ubiquitination	[1, 3, 6]
689	HLLLNSEKMSKSTGN	ubiquitination	[1, 2, 5]
692	LNSEKMSKSTGNFLT	ubiquitination	[1, 3, 5, 7]
706	TLTQAIDKFSADGMR	ubiquitination	[1, 2, 3, 4, 5, 6, 7]
780	ELNAGIIKTDQNYEK	ubiquitination	[1, 2, 3, 5, 6]
787	KTDQNYEKMMFKEAL	ubiquitination	[1, 3, 4, 5]
791	NYEKMMFKEALKTGF	ubiquitination	[5]
795	MMFKEALKTGFFEFQ	ubiquitination	[1]
805	FFEFQAAKDKYRELA	ubiquitination	[1, 2, 3, 5]
807	EFQAAKDKYRELAVE	ubiquitination	[1]
887	HDLRLRLKNYMMPAK	ubiquitination	[1]
900	AKGKKTDKQPLQKPS	ubiquitination	[1]
905	TDKQPLQKPSHCTIY	ubiquitination	[2]
938	HFEANNGKLPDNKVI	ubiquitination	[1]
956	LGSMPELKKYMKKVM	acetylation	[8]
956	LGSMPELKKYMKKVM	ubiquitination	[1, 3]
957	GSMPELKKYMKKVMP	ubiquitination	[1]
961	ELKKYMKKVMPFVAM	ubiquitination	[1]
975	MIKENLEKMGPRILD	ubiquitination	[1]
1020	FASEAEDKIREDCCP	ubiquitination	[1]
1081	MKMNRGIKDLSKVKL	ubiquitination	[1]
1085	RGIKDLSKVKLMRFD	ubiquitination	[1]
1106	RRVPVLGKEYTEKTP	ubiquitination	[1]
1111	LGKEYTEKTPISEHA	ubiquitination	[1]

Reference

 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [6] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [7] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [8] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377] 

Functional Description

  

Sequence Annotation

  

Keyword

 Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 1149 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IEA:InterPro.
 GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004823; F:leucine-tRNA ligase activity; IEA:InterPro.
 GO:0006429; P:leucyl-tRNA aminoacylation; IEA:InterPro.
 GO:0006450; P:regulation of translational fidelity; IEA:GOC. 

Interpro

 IPR001412; aa-tRNA-synth_I_CS.
 IPR002300; aa-tRNA-synth_Ia.
 IPR004493; Leu-tRNA-synth_Ia_arc/euk.
 IPR014729; Rossmann-like_a/b/a_fold.
 IPR009080; tRNAsynth_1a_anticodon-bd.
 IPR013155; V/L/I-tRNA-synth_anticodon-bd.
 IPR009008; Val/Leu/Ile-tRNA-synth_edit. 

Pfam

 PF08264; Anticodon_1
 PF00133; tRNA-synt_1 

SMART

  

PROSITE

 PS00178; AA_TRNA_LIGASE_I 

PRINTS