UniProt Accession

 B0QY89_HUMAN; B0QY89; E9PB84 

Genbank Protein ID

 AL022311; Z97630 

Genbank Nucleotide ID

  

Protein Name

 Eukaryotic translation initiation factor 3 subunit L 

Protein Synonyms/Alias

 eIF3l; Eukaryotic translation initiation factor 3 subunit 6-interacting protein; Eukaryotic translation initiation factor 3 subunit E-interacting protein 

Gene Name

 EIF3L 

Gene Synonyms/Alias

 EIF3EIP; EIF3S6IP 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
104	NFIQYFHKTVSDLID	ubiquitination	[1]
113	VSDLIDQKVYELQAS	ubiquitination	[1, 2, 3, 4]
130	SSDVIDQKVYEIQDI	ubiquitination	[2, 3, 4]
144	IYENSWTKLTERFFK	ubiquitination	[1, 2, 3, 4, 5, 6]
186	YYRHIYAKVSGGPSL	ubiquitination	[1, 2, 3, 4]
249	QYRCKTAKKSEEEID	ubiquitination	[1]
250	YRCKTAKKSEEEIDF	ubiquitination	[1]
263	DFLRSNPKIWNVHSV	ubiquitination	[1, 3]
280	VLHSLVDKSNINRQL	ubiquitination	[3]
344	LENIELNKKSMYSRV	acetylation	[7, 8]
344	LENIELNKKSMYSRV	ubiquitination	[2, 4]
345	ENIELNKKSMYSRVP	ubiquitination	[1, 8]
399	MFQRTTYKYEMINKQ	ubiquitination	[1, 2, 3, 4]
436	IHLQLREKYGDKMLR	ubiquitination	[1]
440	LREKYGDKMLRMQKG	ubiquitination	[1]
446	DKMLRMQKGDPQVYE	ubiquitination	[1, 8]
462	LFSYSCPKFLSPVVP	ubiquitination	[3, 5, 6]
480	NVHPNYHKEPFLQQL	acetylation	[7, 8, 9]
480	NVHPNYHKEPFLQQL	ubiquitination	[1, 2, 4, 5, 6, 10]
488	EPFLQQLKVFSDEVQ	ubiquitination	[2]
508	STIRSFLKLYTTMPV	acetylation	[7, 8, 9]
508	STIRSFLKLYTTMPV	ubiquitination	[1, 2, 3, 4, 8]
537	RIQLLVFKHKMKNLV	ubiquitination	[1, 4, 5, 6]
539	QLLVFKHKMKNLVWT	ubiquitination	[1]
577	MIHIADTKVARRYGD	ubiquitination	[2, 4]
592	FFIRQIHKFEELNRT	acetylation	[7, 8, 9]
592	FFIRQIHKFEELNRT	ubiquitination	[1, 8]

Reference

 [1] 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]
 [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] 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] 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]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] 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] 

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 (By similarity). 

Sequence Annotation

 MOD_RES 45 45 N-acetylserine (By similarity).  

Keyword

 Acetylation; Complete proteome; Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 607 AA 

Protein Sequence

Gene Ontology

 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: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

 IPR019382; eIF3l. 

Pfam

 PF10255; Paf67 

SMART

  

PROSITE

  

PRINTS