| Tag | Content |
|---|---|
| UniProt Accession | EIF3C_HUMAN; Q99613; |
| Entrez ID | 8663 |
| GenBank Protein ID | NM_001037808.2; NM_001199142.1; NM_001267574.2; NM_001286478.1; NM_003752.4; |
| GenBank Nucleotide ID | NP_001032897.1; NP_001186071.1; NP_001254503.1; NP_001273407.1; NP_003743.1; |
| Protein Name | Eukaryotic translation initiation factor 3 subunit C (eIF3c) (Eukaryotic translation initiation factor 3 subunit 8) (eIF3 p110) |
| Gene Name | EIF3C; EIF3S8 |
| Organism | Homo sapiens |
| NCBI Taxa ID | 9606 |
| Functional Description | Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis (PubMed:17581632, PubMed:25849773, PubMed:27462815). 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 pre-initiation 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 post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation (PubMed:17581632). The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression (PubMed:25849773). |
| Sequence (Fasta) | MSRFFTTGSD SESESSLSGE ELVTKPVGGN YGKQPLLLSE DEEDTKRVVR SAKDKRFEEL 60 TNLIRTIRNA MKIRDVTKCL EEFELLGKAY GKAKSIVDKE GVPRFYIRIL ADLEDYLNEL 120 WEDKEGKKKM NKNNAKALST LRQKIRKYNR DFESHITSYK QNPEQSADED AEKNEEDSEG 180 SSDEDEDEDG VSAATFLKKK SEAPSGESRK FLKKMDDEDE DSEDSEDDED WDTGSTSSDS 240 DSEEEEGKQT ALASRFLKKA PTTDEDKKAA EKKREDKAKK KHDRKSKRLD EEEEDNEGGE 300 WERVRGGVPL VKEKPKMFAK GTEITHAVVI KKLNEILQAR GKKGTDRAAQ IELLQLLVQI 360 AAENNLGEGV IVKIKFNIIA SLYDYNPNLA TYMKPEMWGK CLDCINELMD ILFANPNIFV 420 GENILEESEN LHNADQPLRV RGCILTLVER MDEEFTKIMQ NTDPHSQEYV EHLKDEAQVC 480 AIIERVQRYL EEKGTTEEVC RIYLLRILHT YYKFDYKAHQ RQLTPPEGSS KSEQDQAENE 540 GEDSAVLMER LCKYIYAKDR TDRIRTCAIL CHIYHHALHS RWYQARDLML MSHLQDNIQH 600 ADPPVQILYN RTMVQLGICA FRQGLTKDAH NALLDIQSSG RAKELLGQGL LLRSLQERNQ 660 EQEKVERRRQ VPFHLHINLE LLECVYLVSA MLLEIPYMAA HESDARRRMI SKQFHHQLRV 720 GERQPLLGPP ESMREHVVAA SKAMKMGDWK TCHSFIINEK MNGKVWDLFP EADKVRTMLV 780 RKIQEESLRT YLFTYSSVYD SISMETLSDM FELDLPTVHS IISKMIINEE LMASLDQPTQ 840 TVVMHRTEPT AQQNLALQLA EKLGSLVENN ERVFDHKQGT YGGYFRDQKD GYRKNEGYMR 900 RGGYRQQQSQ TAY 914 |
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| PTM | Modification Sites |
|---|---|
| Phosphorylation (count: 19) (view all) | 11 FFTTGSDSESESSLS dbPAF
13 TTGSDSESESSLSGE dbPAF 15 GSDSESESSLSGEEL dbPAF 16 SDSESESSLSGEELV dbPAF 166 YKQNPEQSADEDAEK dbPAF 178 AEKNEEDSEGSSDED dbPAF |
| Acetylation (count: 21) (view all) | 136 KMNKNNAKALSTLRQ PLMD
287 KKHDRKSKRLDEEEE PLMD 320 EKPKMFAKGTEITHA PLMD 331 ITHAVVIKKLNEILQ PLMD 474 QEYVEHLKDEAQVCA PLMD 493 VQRYLEEKGTTEEVC PLMD |
| Ubiquitination (count: 34) (view all) | 124 LNELWEDKEGKKKMN PLMD
267 APTTDEDKKAAEKKR PLMD 277 AEKKREDKAKKKHDR PLMD 312 RGGVPLVKEKPKMFA PLMD 314 GVPLVKEKPKMFAKG PLMD 320 EKPKMFAKGTEITHA PLMD |
| Malonylation (count: 3) | 136 KMNKNNAKALSTLRQ PLMD
627 AFRQGLTKDAHNALL PLMD 643 IQSSGRAKELLGQGL PLMD |