CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-026271
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Serine--tRNA ligase, cytoplasmic 
Protein Synonyms/Alias
  
Gene Name
 SARS 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
12LDLFRVDKGGDPALIubiquitination[1]
28ETQEKRFKDPGLVDQubiquitination[1]
55FRADNLNKLKNLCSKubiquitination[1]
62KLKNLCSKTIGEKMKubiquitination[1]
70TIGEKMKKKEPVGDDubiquitination[1]
71IGEKMKKKEPVGDDEubiquitination[1]
116LIDEAILKCDAERIKubiquitination[1]
123KCDAERIKLEAERFEubiquitination[1]
154NDEDVDNKVERIWGDubiquitination[1]
231YTPFFMRKEVMQEVAubiquitination[1]
249QFDEELYKVIGKGSEubiquitination[1]
266DDNSYDEKYLIATSEubiquitination[1]
293RPEDLPIKYAGLSTCubiquitination[1]
376LNHAASKKLDLEAWFubiquitination[1, 2, 3]
470LENYQTEKGITVPEKubiquitination[1]
477KGITVPEKLKEFMPPubiquitination[1]
494QELIPFVKPAPIEQEubiquitination[1]
Reference
 [1] 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]
 [2] 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]
 [3] 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
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 536 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 GQTKKMMDKR 420
KNNLHLSTQN KLEASLFSPK KVEFVHMLNA TMCATTRTIC AILENYQTEK GITVPEKLKE 480
FMPPGLQELI PFVKPAPIEQ EPSKKQKKQH EGSKKKAAAR DVTLENRLQN MEVTDA 536 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005524; F:ATP binding; IEA:InterPro.
 GO:0004828; F:serine-tRNA ligase activity; IEA:InterPro.
 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.