CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021946
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
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
110IRSLEEEKAAVTEAVacetylation[1, 2]
195VLHMVGDKPVFSFQPubiquitination[3, 4]
Reference
 [1] 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]
 [2] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [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] 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
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
 Alternative splicing; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Ligase; Mitochondrion; Nucleotide-binding; Polymorphism; Protein biosynthesis; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 518 AA 
Protein Sequence
MAASMARRLW PLLTRRGFRP RGGCISNDSP RRSFTTEKRN RNLLYEYARE GYSALPQLDI 60
ERFCACPEEA AHALELRKGE LRSADLPAII STWQELRQLQ EQIRSLEEEK AAVTEAVRAL 120
LANQDSGEVQ QDPKYQGLRA RGREIRKELV HLYPREAQLE EQFYLQALKL PNQTHPDVPV 180
GDESQARVLH MVGDKPVFSF QPRGHLEIGE KLDIIRQKRL SHVSGHRSYY LRGAGALLQH 240
GLVNFTFNKL LRRGFTPMTV PDLLRGAVFE GCGMTPNANP SQIYNIDPAR FKDLNLAGTA 300
EVGLAGYFMD HTVAFRDLPV RMVCSSTCYR AETNTGQEPR GLYRVHHFTK VEMFGVTGPG 360
LEQSSQLLEE FLSLQMEILT ELGLHFRVLD MPTQELGLPA YRKFDIEAWM PGRGRFGEVT 420
SASNCTDFQS RRLHIMFQTE AGELQFAHTV NATACAVPRL LIALLESNQQ KDGSVLVPPA 480
LQSYLGTDRI TAPTHVPLQY IGPNQPRKPG LPGQPAVS 518 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; TAS:Reactome.
 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
 PF00587; tRNA-synt_2b 
SMART
  
PROSITE
 PS50862; AA_TRNA_LIGASE_II 
PRINTS
 PR00981; TRNASYNTHSER.