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Protein Page:
eIF3-alpha (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
eIF3-alpha 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. 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. Belongs to the eIF-3 subunit J family. Note: This description may include information from UniProtKB.
Protein type: Translation; Translation initiation
Chromosomal Location of Human Ortholog: 15q21.1
Cellular Component: eukaryotic translation initiation factor 3 complex; 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 #:  O75822 (UniProtKB)
Alt. Names/Synonyms: eIF-3-alpha; eIF3 p35; eIF3-alpha; eIF3-p35; EIF3J; EIF3S1; Eukaryotic translation initiation factor 3 subunit 1; Eukaryotic translation initiation factor 3 subunit J; eukaryotic translation initiation factor 3, subunit 1 (alpha, 35kD); eukaryotic translation initiation factor 3, subunit 1 alpha, 35kDa; eukaryotic translation initiation factor 3, subunit J
Gene Symbols: EIF3J
Molecular weight: 29,062 Da
Basal Isoelectric point: 4.72  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

eIF3-alpha

Protein Structure Not Found.


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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 18 S11-p AAAAAGDsDsWDADA
0 17 S13-p AAAGDsDsWDADAFs
0 3 S20-p sWDADAFsVEDPVRK
0 1 T33-p RKVGGGGtAGGDRWE
0 2 S72-p VKPEVKIsEKKKIAE
0 25 T109-p PEEPKVLtPEEQLAD
0 1 K117-ac PEEQLADkLRLKKLQ
0 24 S127-p LKKLQEEsDLELAKE
0 4 Y143-p FGVNNAVyGIDAMNP
0 1 T157-p PSSRDDFtEFGkLLK
0 2 K161-ub DDFtEFGkLLKDKIT
0 2 Y175-p TQYEKSLyYASFLEV
0 2 K197-ac SLEIDDLkKITNSLT
0 3 S208-p NSLTVLCsEKQKQEK
0 1 K220-ac QEKQSKAkkkkKGVV
0 1 K221-ac EKQSKAkkkkKGVVP
0 1 K222-ac KQSKAkkkkKGVVPG
0 1 K223-ac QSKAkkkkKGVVPGG
0 2 T235-p PGGGLKAtMKDDLAD
0 56 Y243-p MKDDLADyGGyDGGy
0 61 Y246-p DLADyGGyDGGyVQD
0 61 Y250-p yGGyDGGyVQDyEDF
0 255 Y254-p DGGyVQDyEDFM___
  mouse

 
S14-p AAAAAGDsDsWDADT
S16-p AAAGDsDsWDADTFS
S23 sWDADTFSMEDPVRK
T36 RKVAGGGTAGGDRWE
S75 VKPEVKISEKKKIAE
T112-p PEESKVLtPEEQLAD
K120 PEEQLADKLRLKKLQ
S130-p LKKLQEEsDLELAKE
Y146 FGVNNTVYGIDAMNP
T160 PSSRDDFTEFGkLLK
K164-ub DDFTEFGkLLKDKIT
Y178 TQYEKSLYYASFLEA
K200 SLEIDDLKKITNSLT
S211-p NSLTVLCsEKQKQEK
K223 QEKQSKAKKKKKGVV
K224 EKQSKAKKKKKGVVP
K225 KQSKAKKKKKGVVPG
K226 QSKAKKKKKGVVPGG
T238 PGGGLKATMKDDLAD
Y246-p MKDDLADyGGYEGGY
Y249 DLADyGGYEGGYVQD
Y253 yGGYEGGYVQDYEDF
Y257 EGGYVQDYEDFM___
  rat

 
S12-p AAAAAGDsDsWDADT
S14-p AAAGDsDsWDADTFS
S21 sWDADTFSMEDPVRK
T34 RKVAGGGTAGGDRWE
S73 VKPEVKISEKKKIAE
T110-p PEESKVLtPEEQLAD
K118-ac PEEQLADkLRLKKLQ
S128-p LKKLQEEsDLELAKE
Y144 FGVNNTVYGIDAMNP
T158 PSSRDDFTEFGKLLK
K162 DDFTEFGKLLKDKIT
Y176-p TQYEKSLyYASFLEA
K198 SLEIDDLKKITNSLT
S209 NSLTVLCSEKQKQEK
K221 QEKQSKAKKKKKGVV
K222 EKQSKAKKKKKGVVP
K223 KQSKAKKKKKGVVPG
K224 QSKAKKKKKGVVPGG
T236 PGGGLKATMKDDLAD
Y244-p MKDDLADyGGYDGGy
Y247 DLADyGGYDGGyVQD
Y251-p yGGYDGGyVQDyEDF
Y255-p DGGyVQDyEDFM___
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