CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010496
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Eukaryotic translation initiation factor 2 subunit 3 
Protein Synonyms/Alias
 Eukaryotic translation initiation factor 2 subunit gamma; eIF-2-gamma; PP42 
Gene Name
 Eif2s3 
Gene Synonyms/Alias
 Eif2g 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
303VRPGIVSKDSEGKLMacetylation[1]
421GGRVSAVKADLGKIVacetylation[1]
449ALSRRVEKHWRLIGWacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405
Functional Description
 eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S preinitiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B. 
Sequence Annotation
 NP_BIND 48 55 GTP (By similarity).
 NP_BIND 134 138 GTP (By similarity).
 NP_BIND 190 193 GTP (By similarity).
 MOD_RES 2 2 N-acetylalanine (By similarity).
 MOD_RES 22 22 Phosphothreonine (By similarity).  
Keyword
 Acetylation; Complete proteome; Direct protein sequencing; GTP-binding; Initiation factor; Nucleotide-binding; Phosphoprotein; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 472 AA 
Protein Sequence
MAGGEAGVTL GQPHLSRQDL ATLDVTKLTP LSHEVISRQA TINIGTIGHV AHGKSTVVKA 60
ISGVHTVRFK NELERNITIK LGYANAKIYK LDDPSCPRPE CYRSCGSSTP DEFPTDIPGT 120
KGNFKLVRHV SFVDCPGHDI LMATMLNGAA VMDAALLLIA GNESCPQPQT SEHLAAIEIM 180
KLKHILILQN KIDLVKESQA KEQYEQILAF VQGTVAEGAP IIPISAQLKY NIEVVCEYIV 240
KKIPVPPRDF TSEPRLIVIR SFDVNKPGCE VDDLKGGVAG GSILKGVLKV GQEIEVRPGI 300
VSKDSEGKLM CKPIFSKIVS LFAEHNDLQY AAPGGLIGVG TKIDPTLCRA DRMVGQVLGA 360
VGALPEIFTE LEISYFLLRR LLGVRTEGDK KAAKVQKLSK NEVLMVNIGS LSTGGRVSAV 420
KADLGKIVLT NPVCTEVGEK IALSRRVEKH WRLIGWGQIR RGVTIKPTVD DD 472 
Gene Ontology
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; IEA:InterPro.
 GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
 GO:0006184; P:GTP catabolic process; IEA:GOC. 
Interpro
 IPR000795; EF_GTP-bd_dom.
 IPR027417; P-loop_NTPase.
 IPR015256; TIF2_gsu_C.
 IPR009001; Transl_elong_EF1A/Init_IF2_C.
 IPR004161; Transl_elong_EFTu/EF1A_2.
 IPR009000; Transl_elong_init/rib_B-barrel. 
Pfam
 PF09173; eIF2_C
 PF00009; GTP_EFTU
 PF03144; GTP_EFTU_D2 
SMART
  
PROSITE
  
PRINTS
 PR00315; ELONGATNFCT.