CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001010
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Eukaryotic translation initiation factor 5B 
Protein Synonyms/Alias
 eIF-5B; Translation initiation factor IF-2 
Gene Name
 EIF5B 
Gene Synonyms/Alias
 IF2; KIAA0741 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
33IEGAGAAKEQEPQKSubiquitination[1]
424ARAEATLKLLQAQGVubiquitination[2]
784KKQKKNTKDEFEERAacetylation[3, 4]
883ILINGRLKEGDTIIVubiquitination[5]
923KNQYEKHKEVEAAQGacetylation[3, 6]
923KNQYEKHKEVEAAQGubiquitination[4, 5]
932VEAAQGVKILGKDLEubiquitination[7, 8]
1095AVFPCKIKILPQYIFubiquitination[2, 4, 5]
1170PIPGESPKMFGRHFEubiquitination[5]
1185ATDILVSKISRQSIDubiquitination[5, 9]
1195RQSIDALKDWFRDEMacetylation[10]
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] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [3] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] 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] 
Functional Description
 Function in general translation initiation by promoting the binding of the formylmethionine-tRNA to ribosomes. Seems to function along with eIF-2 (By similarity). 
Sequence Annotation
 NP_BIND 638 645 GTP (By similarity).
 MOD_RES 107 107 Phosphoserine.
 MOD_RES 113 113 Phosphoserine.
 MOD_RES 134 134 Phosphotyrosine.
 MOD_RES 135 135 Phosphoserine.
 MOD_RES 137 137 Phosphoserine.
 MOD_RES 164 164 Phosphoserine.
 MOD_RES 171 171 Phosphoserine.
 MOD_RES 178 178 Phosphoserine (By similarity).
 MOD_RES 182 182 Phosphoserine.
 MOD_RES 183 183 Phosphoserine.
 MOD_RES 186 186 Phosphoserine.
 MOD_RES 190 190 Phosphoserine.
 MOD_RES 214 214 Phosphoserine.
 MOD_RES 301 301 Phosphothreonine.
 MOD_RES 498 498 Phosphothreonine.
 MOD_RES 547 547 Phosphoserine.
 MOD_RES 560 560 Phosphoserine.
 MOD_RES 588 588 Phosphoserine.
 MOD_RES 589 589 Phosphoserine.
 MOD_RES 591 591 Phosphoserine.
 MOD_RES 595 595 Phosphoserine.  
Keyword
 Complete proteome; Cytoplasm; Direct protein sequencing; GTP-binding; Initiation factor; Nucleotide-binding; Phosphoprotein; Polymorphism; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1220 AA 
Protein Sequence
MGKKQKNKSE DSTKDDIDLD ALAAEIEGAG AAKEQEPQKS KGKKKKEKKK QDFDEDDILK 60
ELEELSLEAQ GIKADRETVA VKPTENNEEE FTSKDKKKKG QKGKKQSFDD NDSEELEDKD 120
SKSKKTAKPK VEMYSGSDDD DDFNKLPKKA KGKAQKSNKK WDGSEEDEDN SKKIKERSRI 180
NSSGESGDES DEFLQSRKGQ KKNQKNKPGP NIESGNEDDD ASFKIKTVAQ KKAEKKERER 240
KKRDEEKAKL RKLKEKEELE TGKKDQSKQK ESQRKFEEET VKSKVTVDTG VIPASEEKAE 300
TPTAAEDDNE GDKKKKDKKK KKGEKEEKEK EKKKGPSKAT VKAMQEALAK LKEEEERQKR 360
EEEERIKRLE ELEAKRKEEE RLEQEKRERK KQKEKERKER LKKEGKLLTK SQREARARAE 420
ATLKLLQAQG VEVPSKDSLP KKRPIYEDKK RKKIPQQLES KEVSESMELC AAVEVMEQGV 480
PEKEETPPPV EPEEEEDTED AGLDDWEAMA SDEETEKVEG NKVHIEVKEN PEEEEEEEEE 540
EEEDEESEEE EEEEGESEGS EGDEEDEKVS DEKDSGKTLD KKPSKEMSSD SEYDSDDDRT 600
KEERAYDKAK RRIEKRRLEH SKNVNTEKLR APIICVLGHV DTGKTKILDK LRHTHVQDGE 660
AGGITQQIGA TNVPLEAINE QTKMIKNFDR ENVRIPGMLI IDTPGHESFS NLRNRGSSLC 720
DIAILVVDIM HGLEPQTIES INLLKSKKCP FIVALNKIDR LYDWKKSPDS DVAATLKKQK 780
KNTKDEFEER AKAIIVEFAQ QGLNAALFYE NKDPRTFVSL VPTSAHTGDG MGSLIYLLVE 840
LTQTMLSKRL AHCEELRAQV MEVKALPGMG TTIDVILING RLKEGDTIIV PGVEGPIVTQ 900
IRGLLLPPPM KELRVKNQYE KHKEVEAAQG VKILGKDLEK TLAGLPLLVA YKEDEIPVLK 960
DELIHELKQT LNAIKLEEKG VYVQASTLGS LEALLEFLKT SEVPYAGINI GPVHKKDVMK 1020
ASVMLEHDPQ YAVILAFDVR IERDAQEMAD SLGVRIFSAE IIYHLFDAFT KYRQDYKKQK 1080
QEEFKHIAVF PCKIKILPQY IFNSRDPIVM GVTVEAGQVK QGTPMCVPSK NFVDIGIVTS 1140
IEINHKQVDV AKKGQEVCVK IEPIPGESPK MFGRHFEATD ILVSKISRQS IDALKDWFRD 1200
EMQKSDWQLI VELKKVFEII 1220 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; IEA:InterPro.
 GO:0003743; F:translation initiation factor activity; IDA:UniProtKB.
 GO:0006184; P:GTP catabolic process; IEA:GOC.
 GO:0006446; P:regulation of translational initiation; IDA:UniProtKB. 
Interpro
 IPR000795; EF_GTP-bd_dom.
 IPR027417; P-loop_NTPase.
 IPR005225; Small_GTP-bd_dom.
 IPR015760; TIF_IF2.
 IPR023115; TIF_IF2_dom3.
 IPR004161; Transl_elong_EFTu/EF1A_2.
 IPR009000; Transl_elong_init/rib_B-barrel. 
Pfam
 PF00009; GTP_EFTU
 PF03144; GTP_EFTU_D2
 PF11987; IF-2 
SMART
  
PROSITE
 PS01176; IF2 
PRINTS
 PR00315; ELONGATNFCT.