CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-043451
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Eukaryotic peptide chain release factor GTP-binding subunit ERF3A 
Protein Synonyms/Alias
  
Gene Name
 GSPT1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
114VDKRTLEKYEREAKEacetylation[1]
114VDKRTLEKYEREAKEubiquitination[2]
158AYFETEKKHFTILDAubiquitination[2]
193VLVISARKGEFETGFubiquitination[2]
202EFETGFEKGGQTREHacetylation[3]
202EFETGFEKGGQTREHubiquitination[1, 2, 4]
214REHAMLAKTAGVKHLacetylation[1, 3]
244NERYEECKEKLVPFLacetylation[1]
246RYEECKEKLVPFLKKacetylation[3]
246RYEECKEKLVPFLKKubiquitination[2]
252EKLVPFLKKVGFNPKacetylation[3]
253KLVPFLKKVGFNPKKubiquitination[2]
259KKVGFNPKKDIHFMPacetylation[1]
315IRLPIVDKYKDMGTVubiquitination[5]
326MGTVVLGKLESGSICubiquitination[2]
373ENLKIRLKGIEEEEIubiquitination[2]
424KTRPRFVKQDQVCIAacetylation[3]
424KTRPRFVKQDQVCIAubiquitination[1, 2, 4, 6]
445TICLETFKDFPQMGRubiquitination[2]
466GKTIAIGKVLKLVPEacetylation[3]
466GKTIAIGKVLKLVPEubiquitination[5]
469IAIGKVLKLVPEKD*acetylation[7]
469IAIGKVLKLVPEKD*ubiquitination[2]
Reference
 [1] 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]
 [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] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; GTP-binding; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 475 AA 
Protein Sequence
XSNSAVSMEL SEPIENGETE MSPEESWEHK EEISEAEPGG GSLGDGRPPE ESAHEMMEEE 60
EEIPKPKSVV APPGAPKKEH VNVVFIGHVD AGKSTIGGQI MYLTGMVDKR TLEKYEREAK 120
EKNRETWYLS WALDTNQEER DKGKTVEVGR AYFETEKKHF TILDAPGHKS FVPNMIGGAS 180
QADLAVLVIS ARKGEFETGF EKGGQTREHA MLAKTAGVKH LIVLINKMDD PTVNWSNERY 240
EECKEKLVPF LKKVGFNPKK DIHFMPCSGL TGANLKEQSD FCPWYIGLPF IPYLDNLPNF 300
NRSVDGPIRL PIVDKYKDMG TVVLGKLESG SICKGQQLVM MPNKHNVEVL GILSDDVETD 360
TVAPGENLKI RLKGIEEEEI LPGFILCDPN NLCHSGRTFD AQALICLVDK KSGEKSKTRP 420
RFVKQDQVCI ARLRTAGTIC LETFKDFPQM GRFTLRDEGK TIAIGKVLKL VPEKD 475 
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.
 IPR027417; P-loop_NTPase.
 IPR009001; Transl_elong_EF1A/Init_IF2_C.
 IPR004161; Transl_elong_EFTu/EF1A_2.
 IPR004160; Transl_elong_EFTu/EF1A_C.
 IPR009000; Transl_elong_init/rib_B-barrel. 
Pfam
 PF00009; GTP_EFTU
 PF03144; GTP_EFTU_D2
 PF03143; GTP_EFTU_D3 
SMART
  
PROSITE
 PS00301; EFACTOR_GTP 
PRINTS
 PR00315; ELONGATNFCT.