CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019746
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Eukaryotic translation initiation factor 3 subunit C 
Protein Synonyms/Alias
 eIF3c; Eukaryotic translation initiation factor 3 subunit 8; eIF3 p110 
Gene Name
 EIF3C 
Gene Synonyms/Alias
 EIF3S8 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
88EEFELLGKAYGKAKSubiquitination[1]
92LLGKAYGKAKSIVDKubiquitination[1]
124LNELWEDKEGKKKMNubiquitination[2]
331ITHAVVIKKLNEILQubiquitination[1, 2]
513RILHTYYKFDYKAHQubiquitination[2]
517TYYKFDYKAHQRQLTubiquitination[2]
531TPPEGSSKSEQDQAEubiquitination[1, 2]
558LCKYIYAKDRTDRIRacetylation[3]
627AFRQGLTKDAHNALLubiquitination[2]
643IQSSGRAKELLGQGLubiquitination[1, 2, 4, 5]
664ERNQEQEKVERRRQVubiquitination[2]
712ARRRMISKQFHHQLRubiquitination[4, 5]
764INEKMNGKVWDLFPEubiquitination[2]
862LALQLAEKLGSLVENubiquitination[1, 2, 4, 5]
877NERVFDHKQGTYGGYubiquitination[1, 2, 4, 5]
889GGYFRDQKDGYRKNEubiquitination[1, 2, 4, 5]
894DQKDGYRKNEGYMRRubiquitination[2]
Reference
 [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789
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. 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 post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. 
Sequence Annotation
 DOMAIN 712 846 PCI.
 MOD_RES 9 9 Phosphoserine.
 MOD_RES 11 11 Phosphoserine.
 MOD_RES 13 13 Phosphoserine.
 MOD_RES 15 15 Phosphoserine.
 MOD_RES 16 16 Phosphoserine.
 MOD_RES 18 18 Phosphoserine.
 MOD_RES 39 39 Phosphoserine.
 MOD_RES 166 166 Phosphoserine.
 MOD_RES 178 178 Phosphoserine (By similarity).
 MOD_RES 181 181 Phosphoserine (By similarity).
 MOD_RES 182 182 Phosphoserine (By similarity).
 MOD_RES 524 524 Phosphothreonine.
 MOD_RES 909 909 Phosphoserine.  
Keyword
 Complete proteome; Cytoplasm; Initiation factor; Phosphoprotein; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 913 AA 
Protein Sequence
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 913 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:HAMAP.
 GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:HAMAP.
 GO:0005852; C:eukaryotic translation initiation factor 3 complex; IDA:UniProtKB.
 GO:0003743; F:translation initiation factor activity; IEA:HAMAP.
 GO:0001731; P:formation of translation preinitiation complex; IEA:HAMAP.
 GO:0006446; P:regulation of translational initiation; IEA:HAMAP.
 GO:0006413; P:translational initiation; IDA:UniProtKB. 
Interpro
 IPR027516; EIF3C.
 IPR008905; EIF3C_N_dom.
 IPR000717; PCI_dom.
 IPR011991; WHTH_DNA-bd_dom. 
Pfam
 PF05470; eIF-3c_N
 PF01399; PCI 
SMART
 SM00088; PINT 
PROSITE
  
PRINTS