CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009167
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Eukaryotic translation initiation factor 5 
Protein Synonyms/Alias
 eIF-5 
Gene Name
 Eif5 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
55RPPTYPTKYFGCELGubiquitination[1]
95MLDGFIKKFVLCPECacetylation[2]
143KLCTFILKNPPENSDacetylation[3]
143KLCTFILKNPPENSDubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [3] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441
Functional Description
 Catalyzes the hydrolysis of GTP bound to the 40S ribosomal initiation complex (40S.mRNA.Met-tRNA[F].eIF-2.GTP) with the subsequent joining of a 60S ribosomal subunit resulting in the release of eIF-2 and the guanine nucleotide. The subsequent joining of a 60S ribosomal subunit results in the formation of a functional 80S initiation complex (80S.mRNA.Met-tRNA[F]). 
Sequence Annotation
 DOMAIN 231 390 W2.
 NP_BIND 27 34 GTP (Potential).
 MOD_RES 10 10 Phosphoserine (By similarity).
 MOD_RES 227 227 Phosphoserine (By similarity).
 MOD_RES 387 387 Phosphoserine.
 MOD_RES 388 388 Phosphoserine.
 MOD_RES 417 417 Phosphoserine (By similarity).  
Keyword
 Complete proteome; GTP-binding; Initiation factor; Nucleotide-binding; Phosphoprotein; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 429 AA 
Protein Sequence
MSVNVNRSVS DQFYRYKMPR LIAKVEGKGN GIKTVIVNMV DVAKALNRPP TYPTKYFGCE 60
LGAQTQFDVK NDRYIVNGSH EANKLQDMLD GFIKKFVLCP ECENPETDLH VNPKKQTIGN 120
SCKACGYRGM LDTHHKLCTF ILKNPPENSD IGTGKKEKEK KNRKGKDKEN GSVSTSETPP 180
PPPPNEISPP HAVEEEEDDD WGEDTTEEAQ RRRMDEISDH AKGLTLSDDL ERTVEERVNI 240
LFDFVKKKKE EGIIDSSDKE IVAEAERLDV KAMGPLVLTE VLFDEKIREQ IKKYRRHFLR 300
FCHNNKKAQR YLLHGLECVV AMHQAQLISK IPHILKEMYD ADLLEEEVII SWSEKASKKY 360
VSKELAKEIR VKAEPFIKWL KEAEEESSGG EEEDEDENIE VVYSKTASVP KVETVKSDNK 420
DDDIDIDAI 429 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:Compara.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
 GO:0016070; P:RNA metabolic process; IEA:InterPro. 
Interpro
 IPR016024; ARM-type_fold.
 IPR016021; MIF4-like_typ_1/2/3.
 IPR002735; Transl_init_fac_IF2/IF5.
 IPR016189; Transl_init_fac_IF2/IF5_N.
 IPR016190; Transl_init_fac_IF2/IF5_Zn-bd.
 IPR003307; W2_domain. 
Pfam
 PF01873; eIF-5_eIF-2B
 PF02020; W2 
SMART
 SM00653; eIF2B_5
 SM00515; eIF5C 
PROSITE
 PS51363; W2 
PRINTS