CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-036646
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Eukaryotic translation initiation factor 3 subunit E 
Protein Synonyms/Alias
 eIF3e; Eukaryotic translation initiation factor 3 subunit 6; eIF-3 p48 
Gene Name
 EIF3E 
Gene Synonyms/Alias
 EIF3S6; INT6 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
27LFDYLADKHGFRQEYacetylation[1]
27LFDYLADKHGFRQEYubiquitination[2, 3, 4, 5]
43DTLYRYAKFQYECGNubiquitination[3]
100MEDLTRLKETIDNNSubiquitination[2, 3, 4, 5]
172TTAVITNKDVRKRRQubiquitination[2, 3, 4, 5, 6, 7]
176ITNKDVRKRRQVLKDubiquitination[4]
182RKRRQVLKDLVKVIQacetylation[7, 8, 9]
182RKRRQVLKDLVKVIQubiquitination[4]
186QVLKDLVKVIQQESYubiquitination[2]
266SINMLADKLNMTPEEubiquitination[3, 4]
290RNARLDAKIDSKLGHubiquitination[2, 3, 4, 5, 7]
294LDAKIDSKLGHVVMGubiquitination[2, 3, 4, 5, 6, 7, 10]
314PYQQVIEKTKSLSFRubiquitination[2, 3, 4, 5, 6, 7, 10]
316QQVIEKTKSLSFRSQubiquitination[2, 3, 4, 5, 7, 10]
331MLAMNIEKKLNQNSRubiquitination[2, 3, 4, 5, 6, 7, 10]
332LAMNIEKKLNQNSRSubiquitination[2, 3, 4, 5, 7, 10]
Reference
 [1] Monoclonal antibody cocktail as an enrichment tool for acetylome analysis.
 Shaw PG, Chaerkady R, Zhang Z, Davidson NE, Pandey A.
 Anal Chem. 2011 May 15;83(10):3623-6. [PMID: 21466224]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] 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] 
Functional Description
 Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. Required for nonsense- mediated mRNA decay (NMD); may act in conjunction with UPF2 to divert mRNAs from translation to the NMD pathway. May interact with MCM7 and EPAS1 and regulate the proteasome-mediated degradation of these proteins (By similarity). 
Sequence Annotation
 DOMAIN 199 302 PCI (By similarity).
 REGION 258 352 Sufficient for interaction with MCM7 (By  
Keyword
 Complete proteome; Cytoplasm; Initiation factor; Nucleus; Phosphoprotein; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 352 AA 
Protein Sequence
MFEDPETTRQ MQSTRDGRML FDYLADKHGF RQEYLDTLYR YAKFQYECGN YSGAAEYLYF 60
FRVLVPATDR NALSSLWGKL ASEILMQNWD AAMEDLTRLK ETIDNNSVSS PLQSLQQRTW 120
LIHWSLFVFF NHPKGRDNII DLFLYQPQYL NAIQTMCPHI LRYLTTAVIT NKDVRKRRQV 180
LKDLVKVIQQ ESYTYKDPIT EFVECLYVNF DFDGAQKKLR ECESVLVNDF FLVACLEDFI 240
ENARLFIFET FCRIHQCISI NMLADKLNMT PEEAERWIVN LIRNARLDAK IDSKLGHVVM 300
GNNAVSPYQQ VIEKTKSLSF RSQMLAMNIE KKLNQNSRSE APNWATQDSG FY 352 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:HAMAP.
 GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:HAMAP.
 GO:0005852; C:eukaryotic translation initiation factor 3 complex; IEA:HAMAP.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
 GO:0003743; F:translation initiation factor activity; IEA:HAMAP.
 GO:0001731; P:formation of translation preinitiation complex; IEA:HAMAP.
 GO:0006446; P:regulation of translational initiation; IEA:HAMAP. 
Interpro
 IPR016650; eIF3e.
 IPR019010; eIF3e_N.
 IPR000717; PCI_dom.
 IPR011991; WHTH_DNA-bd_dom. 
Pfam
 PF09440; eIF3_N
 PF01399; PCI 
SMART
 SM00088; PINT 
PROSITE
  
PRINTS