CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012465
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 116 kDa U5 small nuclear ribonucleoprotein component 
Protein Synonyms/Alias
 Elongation factor Tu GTP-binding domain-containing protein 2; SNU114 homolog; hSNU114; U5 snRNP-specific protein, 116 kDa; U5-116 kDa 
Gene Name
 EFTUD2 
Gene Synonyms/Alias
 KIAA0031; SNRP116 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
95PLTEPIIKPVKTKKFubiquitination[1]
182QERGVGIKSTPVTVVubiquitination[1, 2]
277PPTDAYYKLRHIVDEubiquitination[1]
341INYQEFAKRLWGDIYubiquitination[1, 2]
352GDIYFNPKTRKFTKKubiquitination[1, 2, 3, 4]
405ELGIHLTKEELKLNIubiquitination[1, 2, 3, 4, 5]
409HLTKEELKLNIRPLLubiquitination[2, 3, 4]
508IHAGQPVKVLGENYTubiquitination[2]
561GVDQPIVKTATITEPubiquitination[1, 2]
581AQIFRPLKFNTTSVIubiquitination[2, 3, 4]
589FNTTSVIKIAVEPVNubiquitination[2]
602VNPSELPKMLDGLRKubiquitination[2, 3, 4]
609KMLDGLRKVNKSYPSubiquitination[2]
646CVMHDLRKMYSEIDIubiquitination[2]
673VVETSSLKCFAETPNubiquitination[2]
684ETPNKKNKITMIAEPubiquitination[2]
712VQITWNRKKLGEFFQubiquitination[2]
713QITWNRKKLGEFFQTubiquitination[1, 2]
721LGEFFQTKYDWDLLAubiquitination[1]
763KALLGSVKDSIVQGFubiquitination[1, 2, 6]
790LIRNVKFKILDAVVAubiquitination[2, 3, 4]
936LAREFMIKTRRRKGLubiquitination[2]
941MIKTRRRKGLSEDVSubiquitination[2]
951SEDVSISKFFDDPMLubiquitination[1, 6]
963PMLLELAKQDVVLNYubiquitination[1]
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] 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]
 [4] 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]
 [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] 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
 Component of the U5 snRNP and the U4/U6-U5 tri-snRNP complex required for pre-mRNA splicing. Binds GTP. 
Sequence Annotation
 NP_BIND 136 143 GTP (Potential).
 NP_BIND 204 208 GTP (Potential).
 NP_BIND 258 261 GTP (Potential).
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 19 19 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; Complete proteome; Disease mutation; GTP-binding; Mental retardation; mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Spliceosome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 972 AA 
Protein Sequence
MDTDLYDEFG NYIGPELDSD EDDDELGRET KDLDEMDDDD DDDDVGDHDD DHPGMEVVLH 60
EDKKYYPTAE EVYGPEVETI VQEEDTQPLT EPIIKPVKTK KFTLMEQTLP VTVYEMDFLA 120
DLMDNSELIR NVTLCGHLHH GKTCFVDCLI EQTHPEIRKR YDQDLCYTDI LFTEQERGVG 180
IKSTPVTVVL PDTKGKSYLF NIMDTPGHVN FSDEVTAGLR ISDGVVLFID AAEGVMLNTE 240
RLIKHAVQER LAVTVCINKI DRLILELKLP PTDAYYKLRH IVDEVNGLIS MYSTDENLIL 300
SPLLGNVCFS SSQYSICFTL GSFAKIYADT FGDINYQEFA KRLWGDIYFN PKTRKFTKKA 360
PTSSSQRSFV EFILEPLYKI LAQVVGDVDT SLPRTLDELG IHLTKEELKL NIRPLLRLVC 420
KKFFGEFTGF VDMCVQHIPS PKVGAKPKIE HTYTGGVDSD LGEAMSDCDP DGPLMCHTTK 480
MYSTDDGVQF HAFGRVLSGT IHAGQPVKVL GENYTLEDEE DSQICTVGRL WISVARYHIE 540
VNRVPAGNWV LIEGVDQPIV KTATITEPRG NEEAQIFRPL KFNTTSVIKI AVEPVNPSEL 600
PKMLDGLRKV NKSYPSLTTK VEESGEHVIL GTGELYLDCV MHDLRKMYSE IDIKVADPVV 660
TFCETVVETS SLKCFAETPN KKNKITMIAE PLEKGLAEDI ENEVVQITWN RKKLGEFFQT 720
KYDWDLLAAR SIWAFGPDAT GPNILVDDTL PSEVDKALLG SVKDSIVQGF QWGTREGPLC 780
DELIRNVKFK ILDAVVAQEP LHRGGGQIIP TARRVVYSAF LMATPRLMEP YYFVEVQAPA 840
DCVSAVYTVL ARRRGHVTQD APIPGSPLYT IKAFIPAIDS FGFETDLRTH TQGQAFSLSV 900
FHHWQIVPGD PLDKSIVIRP LEPQPAPHLA REFMIKTRRR KGLSEDVSIS KFFDDPMLLE 960
LAKQDVVLNY PM 972 
Gene Ontology
 GO:0015030; C:Cajal body; IDA:BHF-UCL.
 GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0016607; C:nuclear speck; IDA:BHF-UCL.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; TAS:ProtInc.
 GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB. 
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.
 IPR005225; Small_GTP-bd_dom.
 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
 PS00301; EFACTOR_GTP 
PRINTS
 PR00315; ELONGATNFCT.