CPLM-001268

Genbank Nucleotide ID

Eukaryotic translation initiation factor 3 subunit J

Protein Synonyms/Alias

eIF3j; Eukaryotic translation initiation factor 3 subunit 1; eIF-3-alpha; eIF3 p35

Homo sapiens (Human)

Position	Peptide	Type	References
27	SVEDPVRKVGGGGTA	acetylation	[1]
117	PEEQLADKLRLKKLQ	ubiquitination	[2]
161	DDFTEFGKLLKDKIT	ubiquitination	[3, 4, 5]
166	FGKLLKDKITQYEKS	ubiquitination	[4]

[1] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330]
[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] 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]
[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] 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]

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. This subunit binds directly within the mRNA entry channel of the 40S ribosome to the aminoacyl (A) site. It may regulate the interaction between the 43S PIC and mRNA.

REGION 2 69 Sufficient for interaction with EIF3B.
REGION 243 258 Promotes stable association with the 40S
MOD_RES 2 2 N-acetylalanine.
MOD_RES 11 11 Phosphoserine.
MOD_RES 13 13 Phosphoserine.
MOD_RES 20 20 Phosphoserine.
MOD_RES 109 109 Phosphothreonine.
MOD_RES 127 127 Phosphoserine.
MOD_RES 254 254 Phosphotyrosine.

3D-structure; Acetylation; Coiled coil; Complete proteome; Cytoplasm; Direct protein sequencing; Initiation factor; Phosphoprotein; Polymorphism; Protein biosynthesis; Reference proteome.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

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: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.
GO:0006413; P:translational initiation; IC:UniProtKB.

IPR023194; eIF3-like_dom.
IPR013906; eIF3j.

PF08597; eIF3_subunit