CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002479
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
 SES1 
Gene Synonyms/Alias
 SERS; YDR023W; YD9813.01 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
54FELDELNKKFNKLQKacetylation[1]
61KKFNKLQKDIGLKFKacetylation[1]
70IGLKFKNKEDASGLLubiquitination[2]
80ASGLLAEKEKLTQQKacetylation[1]
148PIASVTGKPASLSHHubiquitination[2]
215QAPVMMNKELMSKTAacetylation[1]
220MNKELMSKTAQLSEFacetylation[1]
220MNKELMSKTAQLSEFubiquitination[2]
287REAGSHGKDAWGVFRacetylation[1]
300FRVHAFEKIEQFVITacetylation[1]
351LNNAAAKKYDLEAWFubiquitination[2]
365FPYQKEYKELVSCSNubiquitination[2]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301
Functional Description
 Catalyzes the attachment of serine to tRNA(Ser). Is also probably 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). 
Sequence Annotation
 NP_BIND 279 281 ATP (By similarity).
 NP_BIND 366 369 ATP (By similarity).
 REGION 246 248 Serine binding (By similarity).
 BINDING 295 295 ATP; via amide nitrogen and carbonyl
 BINDING 302 302 Serine (By similarity).
 BINDING 404 404 Serine (By similarity).  
Keyword
 Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 462 AA 
Protein Sequence
MLDINQFIED KGGNPELIRQ SQKARNASVE IVDEIISDYK DWVKTRFELD ELNKKFNKLQ 60
KDIGLKFKNK EDASGLLAEK EKLTQQKKEL TEKEQQEDKD LKKKVFQVGN IVHPSVVVSN 120
DEENNELVRT WKPEDLEAVG PIASVTGKPA SLSHHEILLR LDGYDPDRGV KICGHRGYFF 180
RNYGVFLNQA LINYGLQFLA AKGYIPLQAP VMMNKELMSK TAQLSEFDEE LYKVIDGEDE 240
KYLIATSEQP ISAYHSGEWF EKPQEQLPIH YVGYSSCFRR EAGSHGKDAW GVFRVHAFEK 300
IEQFVITEPE KSWEEFEKMI SYSEEFYKSL KLPYRIVGIV SGELNNAAAK KYDLEAWFPY 360
QKEYKELVSC SNCTDYQSRN LEIRCGIKKM GDREKKYVHC LNSTLAATQR ALCCILENYQ 420
TEDGLVVPEV LRKYIPGEPE FLPFVNELPK NSTSSKDKKK KN 462 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004828; F:serine-tRNA ligase activity; IDA:SGD.
 GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0006434; P:seryl-tRNA aminoacylation; IDA:SGD. 
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.