CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009013
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Methionine--tRNA ligase, cytoplasmic 
Protein Synonyms/Alias
 Methionyl-tRNA synthetase; MetRS 
Gene Name
 MARS 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
109YLVVQGKKGEDVLGSubiquitination[1, 2]
191RAAETVLKQQGVLALubiquitination[1, 2, 3, 4, 5]
204ALRPYLQKQPQPSPAubiquitination[1, 2, 4]
335TPQEICDKYHIIHADubiquitination[2]
364TTTPQQTKITQDIFQubiquitination[1, 2]
375DIFQQLLKRGFVLQDubiquitination[1, 2, 3, 4, 5, 6]
420ARGDQCDKCGKLINAubiquitination[6]
423DQCDKCGKLINAVELubiquitination[2]
431LINAVELKKPQCKVCubiquitination[2]
500RCITRDLKWGTPVPLubiquitination[1, 3, 4, 5]
663RAGMFVSKFFGGYVPubiquitination[1, 4, 5, 7]
726IQVNEPWKRIKGSEAacetylation[8]
726IQVNEPWKRIKGSEAubiquitination[1, 2, 4, 6]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] 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]
 [7] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [8] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861
Functional Description
  
Sequence Annotation
 DOMAIN 74 198 GST C-terminal.
 DOMAIN 841 897 WHEP-TRS.
 MOTIF 273 283 "HIGH" region.
 MOTIF 593 597 "KMSKS" region.
 BINDING 596 596 ATP (By similarity).  
Keyword
 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; Polymorphism; Protein biosynthesis; Reference proteome; RNA-binding; tRNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 900 AA 
Protein Sequence
MRLFVSDGVP GCLPVLAAAG RARGRAEVLI STVGPEDCVV PFLTRPKVPV LQLDSGNYLF 60
STSAICRYFF LLSGWEQDDL TNQWLEWEAT ELQPALSAAL YYLVVQGKKG EDVLGSVRRA 120
LTHIDHSLSR QNCPFLAGET ESLADIVLWG ALYPLLQDPA YLPEELSALH SWFQTLSTQE 180
PCQRAAETVL KQQGVLALRP YLQKQPQPSP AEGRAVTNEP EEEELATLSE EEIAMAVTAW 240
EKGLESLPPL RPQQNPVLPV AGERNVLITS ALPYVNNVPH LGNIIGCVLS ADVFARYSRL 300
RQWNTLYLCG TDEYGTATET KALEEGLTPQ EICDKYHIIH ADIYRWFNIS FDIFGRTTTP 360
QQTKITQDIF QQLLKRGFVL QDTVEQLRCE HCARFLADRF VEGVCPFCGY EEARGDQCDK 420
CGKLINAVEL KKPQCKVCRS CPVVQSSQHL FLDLPKLEKR LEEWLGRTLP GSDWTPNAQF 480
ITRSWLRDGL KPRCITRDLK WGTPVPLEGF EDKVFYVWFD ATIGYLSITA NYTDQWERWW 540
KNPEQVDLYQ FMAKDNVPFH SLVFPCSALG AEDNYTLVSH LIATEYLNYE DGKFSKSRGV 600
GVFGDMAQDT GIPADIWRFY LLYIRPEGQD SAFSWTDLLL KNNSELLNNL GNFINRAGMF 660
VSKFFGGYVP EMVLTPDDQR LLAHVTLELQ HYHQLLEKVR IRDALRSILT ISRHGNQYIQ 720
VNEPWKRIKG SEADRQRAGT VTGLAVNIAA LLSVMLQPYM PTVSATIQAQ LQLPPPACSI 780
LLTNFLCTLP AGHQIGTVSP LFQKLENDQI ESLRQRFGGG QAKTSPKPAV VETVTTAKPQ 840
QIQALMDEVT KQGNIVRELK AQKADKNEVA AEVAKLLDLK KQLAVAEGKP PEAPKGKKKK 900 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004825; F:methionine-tRNA ligase activity; TAS:Reactome.
 GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
 GO:0006431; P:methionyl-tRNA aminoacylation; IEA:InterPro.
 GO:0006418; P:tRNA aminoacylation for protein translation; TAS:Reactome. 
Interpro
 IPR001412; aa-tRNA-synth_I_CS.
 IPR010987; Glutathione-S-Trfase_C-like.
 IPR017933; Glutathione_S_Trfase/Cl_chnl_C.
 IPR023458; Met-tRNA_ligase_1.
 IPR014758; Met-tRNA_synth.
 IPR015413; Methionyl/Leucyl_tRNA_Synth.
 IPR014729; Rossmann-like_a/b/a_fold.
 IPR009068; S15_NS1_RNA-bd.
 IPR009080; tRNAsynth_1a_anticodon-bd.
 IPR000738; WHEP-TRS. 
Pfam
 PF09334; tRNA-synt_1g
 PF00458; WHEP-TRS 
SMART
 SM00991; WHEP-TRS 
PROSITE
 PS00178; AA_TRNA_LIGASE_I
 PS50405; GST_CTER
 PS00762; WHEP_TRS_1
 PS51185; WHEP_TRS_2 
PRINTS
 PR01041; TRNASYNTHMET.