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Protein Page:
eIF3C (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
eIF3C 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. Identified in a HCV IRES-mediated translation complex, at least composed of EIF3C, IGF2BP1, RPS3 and HCV RNA-replicon. Belongs to the eIF-3 subunit C family. Note: This description may include information from UniProtKB.
Protein type: Translation initiation; Translation
Cellular Component: eukaryotic translation initiation factor 3 complex; cytosol
Molecular Function: protein binding; translation initiation factor 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 #:  Q99613 (UniProtKB)
Alt. Names/Synonyms: cell migration-inducing protein 17; eIF3 p110; eIF3-p110; EIF3C; EIF3CL; EIF3S8; Eukaryotic translation initiation factor 3 subunit 8; Eukaryotic translation initiation factor 3 subunit C; eukaryotic translation initiation factor 3, subunit 8 (110kD); eukaryotic translation initiation factor 3, subunit 8, 110kDa; eukaryotic translation initiation factor 3, subunit C; FLJ78287; MGC189744
Gene Symbols: EIF3C
Molecular weight: 105,344 Da
Basal Isoelectric point: 5.48  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

eIF3C

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 3 T6-p __MSRFFtTGsDsEs
0 11 S9-p SRFFtTGsDsEsEss
0 14 S11-p FFtTGsDsEsEssLs
0 8 S13-p tTGsDsEsEssLsGE
0 6 S15-p GsDsEsEssLsGEEL
0 9 S16-p sDsEsEssLsGEELV
0 14 S18-p sEsEssLsGEELVTK
0 84 S39-p GKQPLLLsEDEEDtK
0 3 T45-p LsEDEEDtKRVVRSA
0 1 S51 DtKRVVRSAKDKRFE
0 2 S95-p KAYGKAKsIVDKEGV
0 1 K99 KAKsIVDKEGVPRFY
0 2 K127-ac LWEDKEGkkKMNKNN
0 1 K128-ac WEDKEGkkKMNKNNA
0 1 K132 EGkkKMNKNNAKALS
0 1 K136 KMNKNNAKALSTLRQ
0 30 S166-p YKQNPEQsADEDAEK
0 15 S178-p AEKNEEDsEGssDED
0 15 S181-p NEEDsEGssDEDEDE
0 15 S182-p EEDsEGssDEDEDED
0 3 A194 DEDGVSAATFLKKKS
0 2 T195 EDGVSAATFLKKKSE
0 1 R255 KQTALASRFLKKAPt
0 5 T262-p RFLKKAPttDEDKKA
0 2 T263-p FLKKAPttDEDKKAA
0 2 K312-ub RGGVPLVkEKPKMFA
0 4 K331-ub ITHAVVIkKLNEILQ
0 1 K493-ub VQRYLEEkGTTEEVC
0 10 T524-p KAHQRQLtPPEGSSk
0 2 K531-ub tPPEGSSksEQDQAE
0 1 S532-p PPEGSSksEQDQAEN
0 4 K627-ub AFRQGLTkDAHNALL
0 11 K643-ub IQSSGRAkELLGQGL
0 4 K664-ub ERNQEQEkVERRRQV
0 1 K712-ac ARRRMISkQFHHQLR
0 3 K712-ub ARRRMISkQFHHQLR
0 3 K742-ub EHVVAASkAMKMGDW
0 1 K760 HSFIINEKMNGKVWD
0 1 K764 INEKMNGKVWDLFPE
0 33 K862-ub LALQLAEkLGsLVEN
0 4 S865-p QLAEkLGsLVENNER
0 31 K877-ub NERVFDHkQGTyGGy
0 115 Y881-p FDHkQGTyGGyFRDQ
0 17 Y884-p kQGTyGGyFRDQkDG
0 6 K889-ub GGyFRDQkDGyRkNE
0 1 Y892-p FRDQkDGyRkNEGYM
0 6 K894-ub DQkDGyRkNEGYMRR
0 1 R901 kNEGYMRRGGYRQQQ
0 19 S909-p GGYRQQQsQTAy___
0 2 Y913-p QQQsQTAy_______
  mouse

 
T6-p __MSRFFtTGsDsEs
S9-p SRFFtTGsDsEsEss
S11-p FFtTGsDsEsEssLs
S13-p tTGsDsEsEssLsGE
S15-p GsDsEsEssLsGEEL
S16-p sDsEsEssLsGEELV
S18-p sEsEssLsGEELVTK
S39-p GKQPLLLsEDEEDtK
T45-p LsEDEEDtKRVVRsA
S51-p DtKRVVRsAKDKRFE
S95 KAYGKAKSIVDkEGV
K99-ac KAKSIVDkEGVPRFY
K127 LWEDKEGKKKMNkNN
K128 WEDKEGKKKMNkNNA
K132-ac EGKKKMNkNNAkALS
K136-ac KMNkNNAkALSTLRQ
S166-p YKQNPEQsADEDAEK
S178-p AEKNEEDsEGssDED
S181-p NEEDsEGssDEDEDE
S182-p EEDsEGssDEDEDED
T194-p DEDGVGNttFLKKKQ
T195-p EDGVGNttFLKKKQE
K253-ac KQTVLASkFLKKAPT
T260 kFLKKAPTTEEDKKA
T261 FLKKAPTTEEDKKAA
K310 RGGVPLVKEKPKMFA
K329 ITHAVVIKKLNEILQ
K491 VQRYLEEKGTTEEIC
T522-p KAHQRQLtPPEGSSk
K529-ub tPPEGSSkSEQDQAE
S530 PPEGSSkSEQDQAEN
K625 AFRQGLTKDAHNALL
K641-ub IQSSGRAkELLGQGL
K662 ERNQEQEKVERRRQV
K710 ARRRMISKQFHHQLR
K710-ub ARRRMISkQFHHQLR
K740 EHVVAASKAMKMGDW
K758-ub HSFIINEkMNGkVWD
K762-ub INEkMNGkVWDLFPE
K860-ub LALQLAEkLGSLVEN
S863 QLAEkLGSLVENNER
K875-ub NERVFDHkQGTyGGy
Y879-p FDHkQGTyGGyFRDQ
Y882-p kQGTyGGyFRDQKDG
K887 GGyFRDQKDGYRkNE
Y890 FRDQKDGYRkNEGYM
K892-ub DQKDGYRkNEGYMRR
R899 kNEGYMRRGGYRQQQ
S907-p GGYRQQQsQTAY___
Y911 QQQsQTAY_______
  rat

 
T6 __MSRFFTTGSDsES
S9 SRFFTTGSDsESESS
S11-p FFTTGSDsESESSLs
S13 TTGSDsESESSLsGE
S15 GSDsESESSLsGEEL
S16 SDsESESSLsGEELV
S18-p sESESSLsGEELVTK
S39-p GKQPLLLsEDEEDTK
T45 LsEDEEDTKRVVRSA
S51 DTKRVVRSAKDKRFE
S95 KAYGKAKSIVDKEGV
K99 KAKSIVDKEGVPRFY
K127 LWEDKEGKKKMNKNN
K128 WEDKEGKKKMNKNNA
K132 EGKKKMNKNNAKALS
K136 KMNKNNAKALSTLRQ
S166-p YKQNPEQsADEDAEK
S178-p AEKNEEDsEGssDED
S181-p NEEDsEGssDEDEDD
S182-p EEDsEGssDEDEDDD
T194 DDDGVSGTAFLKKKP
A195 DDGVSGTAFLKKKPD
K253 KQTVLASKFLKKAPT
T260 KFLKKAPTTEEDKKA
T261 FLKKAPTTEEDKKAA
K310 RGGVPLVKEKPKMFA
K329 ITHAVVIKKLNEILQ
K491 VQRYLEEKGTTEEIC
T522 KAHQRQLTPPEGSSK
K529 TPPEGSSKSEQDQAE
S530 PPEGSSKSEQDQAEN
K625 AFRQGLTKDAHNALL
K641 IQSSGRAKELLGQGL
K662 ERNQEQEKVERRRQV
K710-ac ARRRMISkQFHHQLR
K710 ARRRMISKQFHHQLR
K740 EHVVAASKAMKMGDW
K758 HSFIINEKMNGKVWD
K762 INEKMNGKVWDLFPE
K860 LALQLAEKLGSLVEN
S863 QLAEKLGSLVENNER
K875 NERVFDHKQGTYGGY
Y879 FDHKQGTYGGYFRDQ
Y882 KQGTYGGYFRDQKDG
K887 GGYFRDQKDGYRKNE
Y890 FRDQKDGYRKNEGYM
K892 DQKDGYRKNEGYMRr
R899-m1 KNEGYMRrGGYRQQQ
S907 GGYRQQQSQTAY___
Y911 QQQSQTAY_______
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