CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005524
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serine--tRNA ligase, cytoplasmic 
Protein Synonyms/Alias
 Seryl-tRNA synthetase; SerRS; Seryl-tRNA(Ser/Sec) synthetase 
Gene Name
 Sars 
Gene Synonyms/Alias
 Sars1; Sers 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
419QTKKMMDKVEFVHMLacetylation[1]
448LENYQAEKGIAVPEKubiquitination[2]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
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 302 304 ATP (By similarity).
 NP_BIND 391 394 ATP (By similarity).
 REGION 271 273 Serine binding (By similarity).
 BINDING 318 318 ATP; via amide nitrogen and carbonyl
 BINDING 325 325 Serine (By similarity).
 BINDING 429 429 Serine (By similarity).
 MOD_RES 1 1 N-acetylmethionine (By similarity).
 MOD_RES 241 241 Phosphoserine (By similarity).
 MOD_RES 323 323 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; Phosphoprotein; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 512 AA 
Protein Sequence
MVLDLDLFRV DKGGDPALIR ETQEKRFKDP GLVDQLVKAD SEWRRCRFRA DNLNKLKNLC 60
SKTIGEKMKK KEAVGDDESV PENVLNFDDL TADALAALKV SQIKKVRLLI DEAIQKCDGE 120
RVKLEAERFE NLREIGNLLH PSVPISNDED ADNKVERIWG DCTVRKKYSH VDLVVMVDGF 180
EGEKGAVVAG SRGYFLKGPL VFLEQALIQY ALRTLGSRGY TPIYTPFFMR KEVMQEVAQL 240
SQFDEELYKV IGKGSEKSDD NSYDEKYLIA TSEQPIAALH RDEWLRPEDL PIKYAGLSTC 300
FRQEVGSHGR DTRGIFRVHQ FEKIEQFVYS SPHDNKSWEM FDEMIATAEE FYQSLGIPYH 360
IVNIVSGSLN HAASKKLDLE AWFPGSGAFR ELVSCSNCTD YQARRLRIRY GQTKKMMDKV 420
EFVHMLNATM CATTRTICAI LENYQAEKGI AVPEKLREFM PPGLQELIPF VKPAPIDQEP 480
SKKQKKQHEG SKKKAKEVPL ENQLQSMEVT EA 512 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004828; F:serine-tRNA ligase activity; IEA:EC.
 GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0006434; P:seryl-tRNA aminoacylation; IEA:InterPro. 
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.