Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Eukaryotic translation initiation factor 3 subunit J  

UniProtKB / Swiss-Prot ID :  EIF3J_HUMAN

Gene Name (Synonyms) : 
EIF3J, EIF3S1 PRO0391  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm (Probable). 

Protein Function :  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 posttermination 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. 

Protein Sequence MAAAAAAAGDSDSWDADAFSVEDPVRKVGGGGTAGGDRWEGEDEDEDVKDNWDDDDDEKKEEAEVKPEVK...
Predicted Secondary Structure  -
Protein Variant
LocationDescription
141A -> T (in dbSNP:rs2303578). VAR_034007
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAAAAA
---
13.05UniProtKB
Link-
11PhosphoserineAAGDSDSWD
32.40HPRD
Link-
11PhosphoserineAAGDSDSWD
32.40PhosphoELM
Link-
11PhosphoserineAAGDSDSWD
32.40Phosphositeplus
Link-
11PhosphoserineAAGDSDSWD
32.40SysPTM
Link-
11Phosphoserine.AAGDSDSWD
32.40UniProtKB
Link-
13PhosphoserineGDSDSWDAD
30.70HPRD
Link-
13PhosphoserineGDSDSWDAD
30.70PhosphoELM
Link-
13PhosphoserineGDSDSWDAD
30.70Phosphositeplus
Link-
13PhosphoserineGDSDSWDAD
30.70SysPTM
Link-
13Phosphoserine.GDSDSWDAD
30.70UniProtKB
Link-
20PhosphoserineADAFSVEDP
26.73Phosphositeplus
Link-
20Phosphoserine.ADAFSVEDP
26.73UniProtKB
Link-
109PhosphothreoninePKVLTPEEQ
31.48HPRD
Link-
109PhosphothreoninePKVLTPEEQ
31.48PhosphoELM
Link-
109PhosphothreoninePKVLTPEEQ
31.48Phosphositeplus
Link-
109PhosphothreoninePKVLTPEEQ
31.48SysPTM
Link-
109Phosphothreonine.PKVLTPEEQ
31.48UniProtKB
Link-
127PhosphoserineLQEESDLEL
46.90HPRD
Link-
127PhosphoserineLQEESDLEL
46.90PhosphoELM
Link-
127PhosphoserineLQEESDLEL
46.90Phosphositeplus
Link-
127PhosphoserineLQEESDLEL
46.90SysPTM
Link-
127Phosphoserine.LQEESDLEL
46.90UniProtKB
Link-
161Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TEFGKLLKD
56.84Phosphositeplus
Link-
175PhosphotyrosineEKSLYYASF
12.22Phosphositeplus
Link-
207S-nitrosocysteineLTVLCSEKQ
4.25dbSNO
Link-
242noneDDLADYGGY
50.32HPRD
Link-
246PhosphotyrosineDYGGYDGGY
13.67Phosphositeplus
Link-
250PhosphotyrosineYDGGYVQDY
10.64Phosphositeplus
Link-
254PhosphotyrosineYVQDYEDFM
10.58Phosphositeplus
Link-
254Phosphotyrosine.YVQDYEDFM
10.58UniProtKB
Link-
256noneQDYEDFM
38.39HPRD
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
IF4G2_HUMANphysical interactionMINT-2984013MINT16932749
IF4G1_HUMANphysical interactionMINT-2984145MINT16932749
GOLM1_HUMANphysical interactionMINT-64959MINT16169070
EIF3G_HUMANphysical interaction
physical interaction
EBI-366663
EBI-366669
intact14688252
14688252
EIF3I_HUMANphysical interaction
physical interaction
EBI-366669
EBI-366676
intact14688252
14688252
EIF3J_HUMANin vivoHPRD:04883HPRD9822659
EIF3A_HUMANin vitro
in vivo
HPRD:04883HPRD9822659
SIAH1_HUMANin vivoHPRD:04883HPRD9822659
MAGD1_HUMANyeast 2-hybridHPRD:04883HPRD16169070
TAD3L_HUMANyeast 2-hybridHPRD:04883HPRD16169070
GOLM1_HUMANyeast 2-hybridHPRD:04883HPRD16169070
GBB5_HUMANyeast 2-hybridHPRD:04883HPRD16169070
RS20_HUMANENSP00000261868STRING
RS5_HUMANENSP00000261868STRING
RS18_HUMANENSP00000261868STRING
EIF3D_HUMANENSP00000261868STRING
IF5_HUMANENSP00000261868STRING
EIF3E_HUMANENSP00000261868STRING
RS19_HUMANENSP00000261868STRING
RS13_HUMANENSP00000261868STRING
RS12_HUMANENSP00000261868STRING
RS15_HUMANENSP00000261868STRING
RS25_HUMANENSP00000261868STRING
EIF3K_HUMANENSP00000261868STRING
RS4Y1_HUMANENSP00000261868STRING
RS16_HUMANENSP00000261868STRING
IF2G_HUMANENSP00000261868STRING
EIF3G_HUMANENSP00000261868STRING
IF2A_HUMANENSP00000261868STRING
IF4B_HUMANENSP00000261868STRING
IF4H_HUMANENSP00000261868STRING
RS11_HUMANENSP00000261868STRING
RL13A_HUMANENSP00000261868STRING
RS27A_HUMANENSP00000261868STRING
UBIQ_HUMANENSP00000261868STRING
EIF3H_HUMANENSP00000261868STRING
RS3_HUMANENSP00000261868STRING
UBIM_HUMANENSP00000261868STRING
RS30_HUMANENSP00000261868STRING
IF4E_HUMANENSP00000261868STRING
RS23_HUMANENSP00000261868STRING
RS9_HUMANENSP00000261868STRING
EIF3F_HUMANENSP00000261868STRING
EIF3F_HUMANENSP00000261868STRING
RS14_HUMANENSP00000261868STRING
PABP1_HUMANENSP00000261868STRING
RS15A_HUMANENSP00000261868STRING
IF4G1_HUMANENSP00000261868STRING
IF4A2_HUMANENSP00000261868STRING
EIF3C_HUMANENSP00000261868STRING
RS7_HUMANENSP00000261868STRING
RS2_HUMANENSP00000261868STRING
RS17_HUMANENSP00000261868STRING
RS3A_HUMANENSP00000261868STRING
RSSA_HUMANENSP00000261868STRING
RS26_HUMANENSP00000261868STRING
RS28_HUMANENSP00000261868STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Structural characterization of the human eukaryotic initiation factor3 protein complex by mass spectrometry.";
Damoc E., Fraser C.S., Zhou M., Videler H., Mayeur G.L.,Hershey J.W.B., Doudna J.A., Robinson C.V., Leary J.A.;
Mol. Cell. Proteomics 6:1135-1146(2007).
Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3COMPLEX, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2,PHOSPHORYLATION AT SER-11; SER-13; SER-20 AND THR-109, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-11; SER-13 AND THR-109, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-109, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-109, AND MASSSPECTROMETRY.
"Structural characterization of the human eukaryotic initiation factor3 protein complex by mass spectrometry.";
Damoc E., Fraser C.S., Zhou M., Videler H., Mayeur G.L.,Hershey J.W.B., Doudna J.A., Robinson C.V., Leary J.A.;
Mol. Cell. Proteomics 6:1135-1146(2007).
Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3COMPLEX, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2,PHOSPHORYLATION AT SER-11; SER-13; SER-20 AND THR-109, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-109 AND SER-127, ANDMASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-11; SER-13 AND THR-109, AND MASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-109; SER-127 ANDTYR-254, AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 AND SER-13, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures