CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-044843
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 116 kDa U5 small nuclear ribonucleoprotein component 
Protein Synonyms/Alias
  
Gene Name
 EFTUD2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
172QERGVGIKSTPVTVVubiquitination[1, 2, 3]
234LNTERLIKHAVQERLubiquitination[3]
331INYQEFAKRLWGDIYubiquitination[1, 2]
342GDIYFNPKTRKFTKKubiquitination[1, 2, 3, 4]
395ELGIHLTKEELKLNIubiquitination[1, 2, 3, 4, 5]
399HLTKEELKLNIRPLLubiquitination[2, 3, 4]
498IHAGQPVKVLGENYTubiquitination[2]
551GVDQPIVKTATITEPubiquitination[1, 2, 6]
571AQIFRPLKFNTTSVIubiquitination[2, 3, 4]
579FNTTSVIKIAVEPVNubiquitination[2]
592VNPSELPKMLDGLRKubiquitination[2, 3, 4]
599KMLDGLRKVNKSYPSubiquitination[2]
636CVMHDLRKMYSEIDIubiquitination[2]
663VVETSSLKCFAETPNubiquitination[2, 6]
674ETPNKKNKITMIAEPubiquitination[2]
702VQITWNRKKLGEFFQubiquitination[2, 3]
703QITWNRKKLGEFFQTubiquitination[1, 2, 3]
711LGEFFQTKYDWDLLAubiquitination[1, 6]
926LAREFMIKTRRRKGLubiquitination[2]
931MIKTRRRKGLSEDVSubiquitination[2, 3]
941SEDVSISKFFDDPMLubiquitination[1, 7]
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] 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]
 [3] 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]
 [4] 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]
 [5] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [6] 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]
 [7] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661] 
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; GTP-binding; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 962 AA 
Protein Sequence
MDTDLYDEFG NYIGPELDSD EDDDELGRET KDLDEMDDDD DDDDVGDHDD DHPGMEVVLH 60
EDKKYYPTAE EVYGPEVETI VQEEDTQPLT EPIIKPVKTK KFTLMEQTLP VTVYEMDFLA 120
DLMDNSELIR NVTLCGHLHH GKTHPEIRKR YDQDLCYTDI LFTEQERGVG IKSTPVTVVL 180
PDTKGKSYLF NIMDTPGHVN FSDEVTAGLR ISDGVVLFID AAEGVMLNTE RLIKHAVQER 240
LAVTVCINKI DRLILELKLP PTDAYYKLRH IVDEVNGLIS MYSTDENLIL SPLLGNVCFS 300
SSQYSICFTL GSFAKIYADT FGDINYQEFA KRLWGDIYFN PKTRKFTKKA PTSSSQRSFV 360
EFILEPLYKI LAQVVGDVDT SLPRTLDELG IHLTKEELKL NIRPLLRLVC KKFFGEFTGF 420
VDMCVQHIPS PKVGAKPKIE HTYTGGVDSD LGEAMSDCDP DGPLMCHTTK MYSTDDGVQF 480
HAFGRVLSGT IHAGQPVKVL GENYTLEDEE DSQICTVGRL WISVARYHIE VNRVPAGNWV 540
LIEGVDQPIV KTATITEPRG NEEAQIFRPL KFNTTSVIKI AVEPVNPSEL PKMLDGLRKV 600
NKSYPSLTTK VEESGEHVIL GTGELYLDCV MHDLRKMYSE IDIKVADPVV TFCETVVETS 660
SLKCFAETPN KKNKITMIAE PLEKGLAEDI ENEVVQITWN RKKLGEFFQT KYDWDLLAAR 720
SIWAFGPDAT GPNILVDDTL PSEVDKALLG SVKDSIVQGF QWGTREGPLC DELIRNVKFK 780
ILDAVVAQEP LHRGGGQIIP TARRVVYSAF LMATPRLMEP YYFVEVQAPA DCVSAVYTVL 840
ARRRGHVTQD APIPGSPLYT IKAFIPAIDS FGFETDLRTH TQGQAFSLSV FHHWQIVPGD 900
PLDKSIVIRP LEPQPAPHLA REFMIKTRRR KGLSEDVSIS KFFDDPMLLE LAKQDVVLNY 960
PM 962 
Gene Ontology
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; IEA:InterPro.
 GO:0006184; P:GTP catabolic process; IEA:GOC. 
Interpro
 IPR000795; EF_GTP-bd_dom.
 IPR009022; EFG_III-V.
 IPR000640; EFG_V.
 IPR027417; P-loop_NTPase.
 IPR020568; Ribosomal_S5_D2-typ_fold.
 IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
 IPR005517; Transl_elong_EFG/EF2_IV.
 IPR004161; Transl_elong_EFTu/EF1A_2.
 IPR009000; Transl_elong_init/rib_B-barrel. 
Pfam
 PF00679; EFG_C
 PF03764; EFG_IV
 PF00009; GTP_EFTU
 PF03144; GTP_EFTU_D2 
SMART
 SM00838; EFG_C
 SM00889; EFG_IV 
PROSITE
  
PRINTS
 PR00315; ELONGATNFCT.