CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021790
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serine--tRNA ligase, mitochondrial 
Protein Synonyms/Alias
 SerRSmt; Seryl-tRNA synthetase; SerRS; Seryl-tRNA(Ser/Sec) synthetase 
Gene Name
 Sars2 
Gene Synonyms/Alias
 Sarsm 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
110IRSLEAEKEAVAEAVacetylation[1, 2, 3, 4]
195VVRVVGEKPAFSFQPacetylation[4, 5]
195VVRVVGEKPAFSFQPsuccinylation[5]
337RAETDTGKEPWGLYRacetylation[5]
337RAETDTGKEPWGLYRsuccinylation[5]
Reference
 [1] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [2] 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]
 [3] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [4] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [5] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337
Functional Description
 Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec) (By similarity). 
Sequence Annotation
 NP_BIND 330 332 ATP (By similarity).
 NP_BIND 418 421 ATP (By similarity).
 REGION 299 301 Serine binding (By similarity).
 BINDING 345 345 ATP; via amide nitrogen and carbonyl
 BINDING 352 352 Serine (By similarity).
 BINDING 453 453 Serine (By similarity).  
Keyword
 Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Ligase; Mitochondrion; Nucleotide-binding; Protein biosynthesis; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 518 AA 
Protein Sequence
MAASMARLWW PFLARQGLRS RGRCVCSQNP RRSFATEKRV RNLLYEHARE GYSELPYLDM 60
ESVCACPEKA ARSLELRKGE LRPADLPAII STWQELRQLR EQIRSLEAEK EAVAEAVRAL 120
LANQDSDQVQ KDPQYQGLRA RGREIRKQLT PLYPQETQLE EQLYQQALRL PNQTHPDTPV 180
GDESQARVVR VVGEKPAFSF QPRGHLEIGE KLDIIRQKRL SHVSGHRSYY LRGAGALLQH 240
GLVNFTLSKL VSRGFTPMTV PDLLRGAVFE GCGMTPNANP SQIYNIDPSR FEDLNLAGTA 300
EVGLAGYFMD HSVAFRDLPV RMVCASTCYR AETDTGKEPW GLYRVHHFTK VEMFGVTGPG 360
LEQSSQLLDE FLSLQVEILT ELGLHFRVLD MPTQELGLPA YRKFDIEAWM PGRGRYGEVT 420
SASNCTDFQS RRLYIMFETE TGELQFAHTV NATACAVPRV LIALLESNQQ KDGSVLVPAA 480
LQPYLGTDRI TAPTHVPLQY IGPNQPQKPR LPGQSATR 518 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
 GO:0005739; C:mitochondrion; ISS:UniProtKB.
 GO:0005524; F:ATP binding; ISS:UniProtKB.
 GO:0004828; F:serine-tRNA ligase activity; ISS:UniProtKB.
 GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0006434; P:seryl-tRNA aminoacylation; ISS:UniProtKB. 
Interpro
 IPR002314; aa-tRNA-synt_IIb_cons-dom.
 IPR006195; aa-tRNA-synth_II.
 IPR002317; Ser-tRNA-ligase_type_1.
 IPR015866; Ser-tRNA-synth_1_N.
 IPR010978; tRNA-bd_arm. 
Pfam
 PF02403; Seryl_tRNA_N
 PF00587; tRNA-synt_2b 
SMART
  
PROSITE
 PS50862; AA_TRNA_LIGASE_II 
PRINTS
 PR00981; TRNASYNTHSER.