CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024690
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Eukaryotic translation initiation factor 3 subunit C-like protein 
Protein Synonyms/Alias
  
Gene Name
 EIF3CL 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
88EEFELLGKAYGKAKSubiquitination[1]
92LLGKAYGKAKSIVDKubiquitination[1]
94GKAYGKAKSIVDKEGubiquitination[2]
99KAKSIVDKEGVPRFYacetylation[3]
99KAKSIVDKEGVPRFYubiquitination[2, 4]
313RGGVPLVKEKPKMFAubiquitination[2, 4]
315GVPLVKEKPKMFAKGubiquitination[4]
321EKPKMFAKGTEITHAubiquitination[4]
332ITHAVVIKKLNEILQubiquitination[1, 5, 6]
333THAVVIKKLNEILQAubiquitination[2, 4, 6]
475QEYVEHLKDEAQVCAubiquitination[4]
494VQRYLEEKGTTEEVCubiquitination[4, 7]
514RILHTYYKFDYKAHQubiquitination[4]
518TYYKFDYKAHQRQLTubiquitination[4]
532TPPEGSSKSEQDQAEubiquitination[1, 4, 5, 7]
554VLMERLCKYIYAKDRubiquitination[2, 4]
559LCKYIYAKDRTDRIRubiquitination[4]
628AFRQGLTKDAHNALLubiquitination[4, 5]
644IQSSGRAKELLGQGLubiquitination[1, 2, 4, 5, 6, 7, 8, 9]
665ERNQEQEKVERRRQVacetylation[2, 10]
665ERNQEQEKVERRRQVubiquitination[5]
713ARRRMISKQFHHQLRacetylation[2]
713ARRRMISKQFHHQLRubiquitination[2, 4, 8, 9]
743EHVVAASKAMKMGDWubiquitination[4]
746VAASKAMKMGDWKTCubiquitination[4]
751AMKMGDWKTCHSFIIubiquitination[4]
761HSFIINEKMNGKVWDubiquitination[2, 4]
765INEKMNGKVWDLFPEubiquitination[4]
775DLFPEADKVRTMLVRubiquitination[4]
783VRTMLVRKIQEESLRubiquitination[4]
863LALQLAEKLGSLVENubiquitination[1, 2, 4, 5, 8, 11, 12]
878NERVFDHKQGTYGGYubiquitination[1, 2, 4, 5, 6, 7, 8, 9]
890GGYFRDQKDGYRKNEubiquitination[1, 4, 5, 8]
895DQKDGYRKNEGYMRRubiquitination[4, 5]
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] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [3] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [4] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [5] 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]
 [6] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [7] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [8] 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]
 [9] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [10] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [11] A data set of human endogenous protein ubiquitination sites.
 Shi Y, Chan DW, Jung SY, Malovannaya A, Wang Y, Qin J.
 Mol Cell Proteomics. 2011 May;10(5):M110.002089. [PMID: 20972266]
 [12] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572] 
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 (By similarity). 
Sequence Annotation
 DOMAIN 714 847 PCI (By similarity).  
Keyword
 Complete proteome; Cytoplasm; Initiation factor; Phosphoprotein; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 914 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 EEEEEDNEGG 300
EWERVRGGVP LVKEKPKMFA KGTEITHAVV IKKLNEILQA RGKKGTDRAA QIELLQLLVQ 360
IAAENNLGEG VIVKIKFNII ASLYDYNPNL ATYMKPEMWG KCLDCINELM DILFANPNIF 420
VGENILEESE NLHNADQPLR VRGCILTLVE RMDEEFTKIM QNTDPHSQEY VEHLKDEAQV 480
CAIIERVQRY LEEKGTTEEV CRIYLLRILH TYYKFDYKAH QRQLTPPEGS SKSEQDQAEN 540
EGEDSAVLME RLCKYIYAKD RTDRIRTCAI LCHIYHHALH SRWYQARDLM LMSHLQDNIQ 600
HADPPVQILY NRTMVQLGIC AFRQGLTKDA HNALLDIQSS GRAKELLGQG LLLRSLQERN 660
QEQEKVERRR QVPFHLHINL ELLECVYLVS AMLLEIPYMA AHESDARRRM ISKQFHHQLR 720
VGERQPLLGP PESMREHVVA ASKAMKMGDW KTCHSFIINE KMNGKVWDLF PEADKVRTML 780
VRKIQEESLR TYLFTYSSVY DSISMETLSD MFELDLPTVH SIISKMIINE ELMASLDQPT 840
QTVVMHRTEP TAQQNLALQL AEKLGSLVEN NERVFDHKQG TYGGYFRDQK DGYRKNEGYM 900
RRGGYRQQQS QTAY 914 
Gene Ontology
 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; IEA:HAMAP.
 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. 
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