CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008167
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
 SERS 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
12LDLFRVDKGGDPALIubiquitination[1, 2, 3]
28ETQEKRFKDPGLVDQubiquitination[3, 4]
38GLVDQLVKADSEWRRubiquitination[1]
55FRADNLNKLKNLCSKubiquitination[3]
62KLKNLCSKTIGEKMKubiquitination[2, 3]
70TIGEKMKKKEPVGDDubiquitination[3]
116LIDEAILKCDAERIKubiquitination[3, 4]
123KCDAERIKLEAERFEubiquitination[3]
154NDEDVDNKVERIWGDubiquitination[1, 3]
231YTPFFMRKEVMQEVAubiquitination[2, 3]
249QFDEELYKVIGKGSEubiquitination[1, 3]
257VIGKGSEKSDDNSYDubiquitination[1]
266DDNSYDEKYLIATSEubiquitination[1, 3, 4]
293RPEDLPIKYAGLSTCubiquitination[2, 3]
323FRVHQFEKIEQFVYSacetylation[5]
376LNHAASKKLDLEAWFubiquitination[1, 3, 4, 6, 7]
448LENYQTEKGITVPEKubiquitination[2, 3]
455KGITVPEKLKEFMPPubiquitination[2, 3]
472QELIPFVKPAPIEQEubiquitination[3]
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] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [3] 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]
 [4] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [5] 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]
 [6] 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]
 [7] 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] 
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 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.
 MOD_RES 241 241 Phosphoserine.
 MOD_RES 323 323 N6-acetyllysine.  
Keyword
 3D-structure; 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
 514 AA 
Protein Sequence
MVLDLDLFRV DKGGDPALIR ETQEKRFKDP GLVDQLVKAD SEWRRCRFRA DNLNKLKNLC 60
SKTIGEKMKK KEPVGDDESV PENVLSFDDL TADALANLKV SQIKKVRLLI DEAILKCDAE 120
RIKLEAERFE NLREIGNLLH PSVPISNDED VDNKVERIWG DCTVRKKYSH VDLVVMVDGF 180
EGEKGAVVAG SRGYFLKGVL VFLEQALIQY ALRTLGSRGY IPIYTPFFMR KEVMQEVAQL 240
SQFDEELYKV IGKGSEKSDD NSYDEKYLIA TSEQPIAALH RDEWLRPEDL PIKYAGLSTC 300
FRQEVGSHGR DTRGIFRVHQ FEKIEQFVYS SPHDNKSWEM FEEMITTAEE FYQSLGIPYH 360
IVNIVSGSLN HAASKKLDLE AWFPGSGAFR ELVSCSNCTD YQARRLRIRY GQTKKMMDKV 420
EFVHMLNATM CATTRTICAI LENYQTEKGI TVPEKLKEFM PPGLQELIPF VKPAPIEQEP 480
SKKQKKQHEG SKKKAAARDV TLENRLQNME VTDA 514 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003723; F:RNA binding; TAS:ProtInc.
 GO:0004828; F:serine-tRNA ligase activity; TAS:Reactome.
 GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0006434; P:seryl-tRNA aminoacylation; IEA:InterPro.
 GO:0006418; P:tRNA aminoacylation for protein translation; TAS:Reactome.
 GO:0008033; P:tRNA processing; TAS:ProtInc. 
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.