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Protein Page:
eIF3S3 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
eIF3S3 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. Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and EIF3H of module B, thereby linking the three modules. EIF3J is a labile subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex interacts with RPS6KB1 under conditions of nutrient depletion. Mitogenic stimulation leads to binding and activation of a complex composed of MTOR and RPTOR, leading to phosphorylation and release of RPS6KB1 and binding of EIF4B to eIF-3. Interacts with RNF139; the interaction leads to protein translation inhibitions in a ubiquitination- dependent manner. Belongs to the eIF-3 subunit H family. Note: This description may include information from UniProtKB.
Protein type: Translation; Translation initiation
Cellular Component: eukaryotic translation initiation factor 3 complex; membrane; cytosol
Molecular Function: protein binding; translation initiation factor activity
Biological Process: cellular protein metabolic process; translation; translational initiation; gene expression; formation of translation preinitiation complex; regulation of translational initiation
Reference #:  O15372 (UniProtKB)
Alt. Names/Synonyms: eIF-3-gamma; eIF3 p40 subunit; eIF3-gamma; eIF3-p40; EIF3H; EIF3S3; Eukaryotic translation initiation factor 3 subunit 3; Eukaryotic translation initiation factor 3 subunit H; eukaryotic translation initiation factor 3, subunit 2 (beta, 36kD); eukaryotic translation initiation factor 3, subunit 3 (gamma, 40kD); eukaryotic translation initiation factor 3, subunit 3 gamma, 40kDa; eukaryotic translation initiation factor 3, subunit H; MGC102958
Gene Symbols: EIF3H
Molecular weight: 39,930 Da
Basal Isoelectric point: 6.09  Predict pI for various phosphorylation states
CST Pathways:  Translational Control
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

eIF3S3

Protein Structure Not Found.


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Sites Implicated In
cell growth, altered: S183‑p
activity, induced: S183‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 S3-p _____MAsRkEGtGs
0 8 K5-ub ___MAsRkEGtGstA
0 3 T8-p MAsRkEGtGstATSS
0 1 S10-p sRkEGtGstATSSSs
0 1 T11-p RkEGtGstATSSSsT
0 1 S17-p stATSSSsTAGAAGk
0 2 K24-ac sTAGAAGkGkGkGGs
0 3 K24-ub sTAGAAGkGkGkGGs
0 2 K26-ac AGAAGkGkGkGGsGD
0 1 K28-ub AAGkGkGkGGsGDSA
0 1 S31-p kGkGkGGsGDSAVkQ
0 1 K37-ub GsGDSAVkQVQIDGL
0 1 K156-ub VLIYDPIkTAQGSLs
0 1 S163-p kTAQGSLsLkAYRLT
0 1 K165-ub AQGSLsLkAYRLTPK
1 16 S183-p VCKEKDFsPEALkKA
0 2 K188-ub DFsPEALkKANITFE
0 1 N191 PEALkKANITFEYMF
0 1 K220-ub VLMWELEkKSAVADk
0 3 K227-ub kKSAVADkHELLSLA
0 1 K241-ub ASSNHLGkNLQLLMD
0 3 K259-ub EMSQDIVkYNtyMRN
0 1 T262-p QDIVkYNtyMRNTSK
0 2 Y263-p DIVkYNtyMRNTSKQ
0 1 K274-ub TSKQQQQkHQYQQRR
0 1 S290-p QENMQRQsRGEPPLP
0 2 K303-ub LPEEDLSkLFkPPQP
0 7 K306-ub EDLSkLFkPPQPPAR
0 1 S316-p QPPARMDsLLIAGQI
0 3 K331-ub NTYCQNIkEFTAQNL
0 1 K340-ub FTAQNLGkLFMAQAL
  mouse

 
S3 _____MASRKEGTGS
K5 ___MASRKEGTGSTA
T8 MASRKEGTGSTATSS
S10 SRKEGTGSTATSSGS
T11 RKEGTGSTATSSGSA
S17 STATSSGSAGGAVGk
K24-ac SAGGAVGkGkGKGGS
K24 SAGGAVGKGkGKGGS
K26-ac GGAVGkGkGKGGSGD
K28 AVGkGkGKGGSGDSA
S31 kGkGKGGSGDSAVKQ
K37 GSGDSAVKQVQIDGL
K156 VLIYDPIKTAQGSLS
S163 KTAQGSLSLKAYRLT
K165 AQGSLSLKAYRLTPK
S183-p VCKEKDFsPEALkKA
K188-ub DFsPEALkKAsITFE
S191-p PEALkKAsITFEHMF
K220 VLMWELEKKSAVADk
K227-ub KKSAVADkHELLSLA
K241 ASSNHLGKSLQLLMD
K259-ub EMSQDIIkYNTYMRN
T262 QDIIkYNTYMRNTSK
Y263 DIIkYNTYMRNTSKQ
K274 TSKQQQQKHQYQQRR
S290 QENMQRQSRGEPPLP
K303-ub LPEEDLSkLFkPHQA
K306-ub EDLSkLFkPHQAPAR
S316 QAPARMDSLLIAGQI
K331 NTYCQNIKEFTAQNL
K340 FTAQNLGKLFMAQAL
  rat

 
S3 _____MASRKEGTGS
K5 ___MASRKEGTGSTA
T8 MASRKEGTGSTATSS
S10 SRKEGTGSTATSSSS
T11 RKEGTGSTATSSSST
S17 STATSSSSTGGAVGK
K24 STGGAVGKGKGKGGS
K24 STGGAVGKGKGKGGS
K26 GGAVGKGKGKGGSGD
K28 AVGKGKGKGGSGDSA
S31 KGKGKGGSGDSAVKQ
K37 GSGDSAVKQVQIDGL
K156 VLIYDPIKTAQGSLS
S163 KTAQGSLSLKAYRLT
K165 AQGSLSLKAYRLTPK
S183-p VCKEKDFsPEALKKA
K188 DFsPEALKKANITFE
N191 PEALKKANITFEHMF
K220 VLMWELEKKSAVADK
K227 KKSAVADKHELLSLA
K241 ASSNHLGKNLQLLMD
K259 EMSQDIIKYNTYMRN
T262 QDIIKYNTYMRNSSK
Y263 DIIKYNTYMRNSSKQ
K274 SSKQQQQKHQYQQRR
S290 QENMQRQSRGEPPLP
K303 LPEEDLSKLFkPHQA
K306-ub EDLSKLFkPHQAPAR
S316 QAPARMDSLLIAGQI
K331 NTYCQNIKEFTAQNL
K340 FTAQNLGKLFMAQAL
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