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 K  

UniProtKB / Swiss-Prot ID :  EIF3K_HUMAN

Gene Name (Synonyms) : 
EIF3K, EIF3S12ARG134, HSPC029, MSTP001, PTD001  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. Cytoplasm. 

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. 

Protein Sequence MAMFEQMRANVGKLLKGIDRYNPENLATLERYVETQAKENAYDLEANLAVLKLYQFNPAFFQTTVTAQIL...
Predicted Secondary Structure  -
Protein Variant -
- top -

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
- top -

Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAMFEQ
---
16.04UniProtKB
Link
13Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ANVGKLLKG
46.49Phosphositeplus
Link
16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GKLLKGIDR
65.34Phosphositeplus
Link
21PhosphotyrosineGIDRYNPEN
31.18Phosphositeplus
Link
38Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ETQAKENAY
41.50Phosphositeplus
Link
209PhosphoserineIDFDSVSSI
24.72Phosphositeplus
Link
212PhosphoserineDSVSSIMAS
17.77HPRD
Link
216PhosphoserineSIMASSQ
16.34HPRD
Link-
216PhosphoserineSIMASSQ
16.34SysPTM
Link-
217PhosphoserineIMASSQ
30.30HPRD
Link-
217PhosphoserineIMASSQ
30.30PhosphoELM
Link-
217PhosphoserineIMASSQ
30.30Phosphositeplus
Link-
217PhosphoserineIMASSQ
30.30SysPTM
Link-
217Phosphoserine.IMASSQ
30.30UniProtKB
Link-
- top -

Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
CCND3_HUMANphysical interactionMINT-50582MINT15327989
CCND3_HUMANphysical interactionMINT-50583MINT15327989
IF3EI_HUMANphysical interactionMINT-66591MINT16189514
IF3EI_HUMANphysical interactionEBI-754273
intact16189514
CCND3_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:11740HPRD15327989
EIF3J_HUMANin vitroHPRD:11740HPRD14519125
EIF3H_HUMANin vitroHPRD:11740HPRD14519125
EIF3G_HUMANin vitroHPRD:11740HPRD14519125
EIF3C_HUMANin vitroHPRD:11740HPRD14519125
RS20_HUMANENSP00000248342STRING
RS5_HUMANENSP00000248342STRING
RS18_HUMANENSP00000248342STRING
EIF3D_HUMANENSP00000248342STRING
IF5_HUMANENSP00000248342STRING
EIF3E_HUMANENSP00000248342STRING
RS19_HUMANENSP00000248342STRING
RS13_HUMANENSP00000248342STRING
RS12_HUMANENSP00000248342STRING
RS15_HUMANENSP00000248342STRING
RS25_HUMANENSP00000248342STRING
RS4Y1_HUMANENSP00000248342STRING
RS16_HUMANENSP00000248342STRING
IF2G_HUMANENSP00000248342STRING
EIF3G_HUMANENSP00000248342STRING
IF2A_HUMANENSP00000248342STRING
EIF3J_HUMANENSP00000248342STRING
IF4B_HUMANENSP00000248342STRING
IF4H_HUMANENSP00000248342STRING
RS11_HUMANENSP00000248342STRING
RL13A_HUMANENSP00000248342STRING
RS27A_HUMANENSP00000248342STRING
UBIQ_HUMANENSP00000248342STRING
EIF3H_HUMANENSP00000248342STRING
RS3_HUMANENSP00000248342STRING
UBIM_HUMANENSP00000248342STRING
RS30_HUMANENSP00000248342STRING
IF4E_HUMANENSP00000248342STRING
RS23_HUMANENSP00000248342STRING
RS9_HUMANENSP00000248342STRING
EIF3F_HUMANENSP00000248342STRING
EIF3F_HUMANENSP00000248342STRING
RS14_HUMANENSP00000248342STRING
PABP1_HUMANENSP00000248342STRING
RS15A_HUMANENSP00000248342STRING
IF4G1_HUMANENSP00000248342STRING
IF4A2_HUMANENSP00000248342STRING
EIF3C_HUMANENSP00000248342STRING
RS7_HUMANENSP00000248342STRING
RS2_HUMANENSP00000248342STRING
RS17_HUMANENSP00000248342STRING
RS3A_HUMANENSP00000248342STRING
RSSA_HUMANENSP00000248342STRING
RS26_HUMANENSP00000248342STRING
RS28_HUMANENSP00000248342STRING
- top -

Disease Reference
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
- top -
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, 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-217, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-217, 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 SER-217, 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-217, AND MASS SPECTROMETRY.
"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 SER-217, AND MASSSPECTROMETRY.
- top -
Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures