UniProt Accession

 EIF3E_HUMAN; P60228; O43902; Q64058; Q64059; Q64252; Q6FG33; Q8WVK4 

Genbank Protein ID

 U54562; U94174; U94162; U94163; U94164; U94165; U94166; U94167; U94168; U94169; U94170; U94171; U94172; U94173; U94175; U62962; U85947; CR542275; CH471060; BC000734; BC008419; BC016706; BC017887; BC021679 

Genbank Nucleotide ID

 AAC51760.1; AAC51917.1; AAC51917.1; AAC51917.1; AAC51917.1; AAC51917.1; AAC51917.1; AAC51917.1; AAC51917.1; AAC51917.1; AAC51917.1; AAC51917.1; AAC51917.1; AAC51917.1; AAC51919.1; AAB58251.1; AAB88873.1; CAG47071.1; EAW91918.1; AAH00734.1; AAH08419.1; AAH16706.1; AAH17887.1; AAH21679.1 

Protein Name

 Eukaryotic translation initiation factor 3 subunit E 

Protein Synonyms/Alias

 eIF3e; Eukaryotic translation initiation factor 3 subunit 6; Viral integration site protein INT-6 homolog; 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
29	LLEFLSVKEIYNEKE	ubiquitination	[1]
35	VKEIYNEKELLQGKL	ubiquitination	[1, 2, 3, 4]
41	EKELLQGKLDLLSDT	ubiquitination	[1, 4]
82	TTVVAQLKQLQAETE	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 8, 9]
93	AETEPIVKMFEDPET	ubiquitination	[1, 3, 4, 5, 8, 9]
120	LFDYLADKHGFRQEY	ubiquitination	[1, 2, 3, 4]
193	MEDLTRLKETIDNNS	acetylation	[10]
193	MEDLTRLKETIDNNS	ubiquitination	[1, 3, 4]
265	TTAVITNKDVRKRRQ	ubiquitination	[1, 3, 4, 8]
269	ITNKDVRKRRQVLKD	ubiquitination	[3]
275	RKRRQVLKDLVKVIQ	acetylation	[11]
275	RKRRQVLKDLVKVIQ	ubiquitination	[3]
279	QVLKDLVKVIQQESY	ubiquitination	[1]
359	SINMLADKLNMTPEE	ubiquitination	[3]
383	RNARLDAKIDSKLGH	ubiquitination	[1, 3, 4]
387	LDAKIDSKLGHVVMG	ubiquitination	[1, 3, 4, 5, 8, 9]
407	PYQQVIEKTKSLSFR	ubiquitination	[1, 3, 4, 5, 8, 9]
409	QQVIEKTKSLSFRSQ	ubiquitination	[1, 3, 4, 5, 9]
424	MLAMNIEKKLNQNSR	ubiquitination	[1, 3, 4, 5, 8, 9]
425	LAMNIEKKLNQNSRS	ubiquitination	[1, 3, 4, 5, 9]

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] 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]
 [4] 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]
 [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] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [7] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [8] 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]
 [9] 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]
 [10] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [11] 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] 

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. 

Sequence Annotation

 DOMAIN 290 395 PCI.
 REGION 4 128 Sufficient for interaction with EPAS1.
 REGION 9 195 Sufficient for interaction with TRIM27.
 REGION 351 445 Sufficient for interaction with MCM7.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 399 399 Phosphoserine.
 MOD_RES 439 439 Phosphothreonine (By similarity).  

Keyword

 Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Initiation factor; Nucleus; Phosphoprotein; Polymorphism; Protein biosynthesis; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 445 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; TAS:Reactome.
 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; IDA:UniProtKB.
 GO:0005654; C:nucleoplasm; NAS:UniProtKB.
 GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
 GO:0003743; F:translation initiation factor activity; IC:UniProtKB.
 GO:0001731; P:formation of translation preinitiation complex; IEA:HAMAP.
 GO:0045947; P:negative regulation of translational initiation; NAS:UniProtKB.
 GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IMP:UniProtKB. 

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