CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015753
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Eukaryotic translation initiation factor 3 subunit M 
Protein Synonyms/Alias
 eIF3m; Fetal lung protein B5; hFL-B5; PCI domain-containing protein 1 
Gene Name
 EIF3M 
Gene Synonyms/Alias
 HFLB5; PCID1; GA17; PNAS-125 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
115NLFHGMDKNTPVRYTubiquitination[1, 2, 3, 4, 5, 6]
149TELDQVRKWISDWNLubiquitination[1, 4, 6]
160DWNLTTEKKHTLLRLubiquitination[2]
161WNLTTEKKHTLLRLLubiquitination[4]
176YEALVDCKKSDAASKubiquitination[4, 7]
177EALVDCKKSDAASKVubiquitination[4]
183KKSDAASKVMVELLGubiquitination[2, 4]
213RCIVRALKDPNAFLFacetylation[8]
213RCIVRALKDPNAFLFubiquitination[1, 2, 4, 5, 6]
227FDHLLTLKPVKFLEGubiquitination[1, 2, 4, 5, 6]
254AKLASYVKFYQNNKDacetylation[8]
254AKLASYVKFYQNNKDubiquitination[1, 2, 3, 6]
260VKFYQNNKDFIDSLGubiquitination[4]
319VIDAVRTKMVYCKIDubiquitination[4]
324RTKMVYCKIDQTQRKubiquitination[3, 4, 7]
344STHRTFGKQQWQQLYubiquitination[1, 2, 3, 4, 5, 6, 7]
358YDTLNAWKQNLNKVKubiquitination[4, 5]
363AWKQNLNKVKNSLLSubiquitination[1, 6]
365KQNLNKVKNSLLSLSubiquitination[1, 2, 3, 4, 5, 6, 7]
Reference
 [1] 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]
 [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] 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]
 [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] 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]
 [6] 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]
 [7] 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]
 [8] 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] 
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. May favor virus entry in case of infection with herpes simplex virus 1 (HSV1) or herpes simplex virus 2 (HSV2). 
Sequence Annotation
 DOMAIN 235 336 PCI.
 REGION 344 374 Interaction with HSV-1 and HSV-2.
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 2 2 Phosphoserine.
 MOD_RES 254 254 N6-acetyllysine.  
Keyword
 Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Initiation factor; Phosphoprotein; Polymorphism; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 374 AA 
Protein Sequence
MSVPAFIDIS EEDQAAELRA YLKSKGAEIS EENSEGGLHV DLAQIIEACD VCLKEDDKDV 60
ESVMNSVVSL LLILEPDKQE ALIESLCEKL VKFREGERPS LRLQLLSNLF HGMDKNTPVR 120
YTVYCSLIKV AASCGAIQYI PTELDQVRKW ISDWNLTTEK KHTLLRLLYE ALVDCKKSDA 180
ASKVMVELLG SYTEDNASQA RVDAHRCIVR ALKDPNAFLF DHLLTLKPVK FLEGELIHDL 240
LTIFVSAKLA SYVKFYQNNK DFIDSLGLLH EQNMAKMRLL TFMGMAVENK EISFDTMQQE 300
LQIGADDVEA FVIDAVRTKM VYCKIDQTQR KVVVSHSTHR TFGKQQWQQL YDTLNAWKQN 360
LNKVKNSLLS LSDT 374 
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; 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; IC:UniProtKB. 
Interpro
 IPR027528; eIF3m.
 IPR000717; PCI_dom.
 IPR011991; WHTH_DNA-bd_dom. 
Pfam
 PF01399; PCI 
SMART
 SM00088; PINT 
PROSITE
  
PRINTS