CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012260
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Eukaryotic translation initiation factor 3 subunit A 
Protein Synonyms/Alias
 eIF3a; Eukaryotic translation initiation factor 3 subunit 10; eIF-3-theta; eIF3 p167; eIF3 p180; eIF3 p185 
Gene Name
 EIF3A 
Gene Synonyms/Alias
 EIF3S10; KIAA0139 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
13QRPENALKRANEFLEubiquitination[1, 2]
23NEFLEVGKKQPALDVubiquitination[3, 4]
24EFLEVGKKQPALDVLubiquitination[4]
36DVLYDVMKSKKHRTWubiquitination[4]
45KKHRTWQKIHEPIMLubiquitination[1, 2, 4, 5, 6]
68LRKSHLAKEGLYQYKacetylation[7]
68LRKSHLAKEGLYQYKubiquitination[4]
75KEGLYQYKNICQQVNubiquitination[3, 4, 8]
84ICQQVNIKSLEDVVRubiquitination[4]
105EEKTEAAKEESQQMVubiquitination[3, 6]
196TRKAEFRKLCDNLRMubiquitination[4]
285KVSTVFWKSGNALFHubiquitination[4, 5, 6]
308HLSREMRKNLTQDEMubiquitination[4, 5]
351MDGIIVEKQRRLATLubiquitination[3, 4, 6, 8]
402EVEFNPLKLCERVTKubiquitination[3]
409KLCERVTKVLNWVREubiquitination[1, 2, 4]
420WVREQPEKEPELQQYubiquitination[1, 2, 3, 4, 5, 6, 9, 10]
532AMSSVLAKALEVIKPubiquitination[6]
559LAVTAYLKNSRKEHQubiquitination[6]
603QREAELQKVRKAEEEubiquitination[4]
632LQEHEQIKKKTVRERubiquitination[3, 4]
633QEHEQIKKKTVRERLubiquitination[4, 6]
634EHEQIKKKTVRERLEubiquitination[4]
651KKTELGAKAFKDIDIubiquitination[3]
654ELGAKAFKDIDIEDLubiquitination[3, 4, 6]
672DPDFIMAKQVEQLEKubiquitination[3, 6]
694RLKNQEKKIDYFERAubiquitination[3, 4]
711LEEIPLIKSAYEEQRubiquitination[1, 2, 3, 4, 5, 6]
720AYEEQRIKDMDLWEQubiquitination[3]
775RQSVYEEKLKQFEERubiquitination[1, 2, 3, 4, 5, 6, 8, 9, 10]
777SVYEEKLKQFEERLAubiquitination[1, 2, 4]
824RAEEQMLKEREERERubiquitination[3, 4, 6]
1351DREREGEKEKASWRAacetylation[11]
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] 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]
 [3] 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]
 [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] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [10] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [11] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786] 
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 366 494 PCI.
 REPEAT 925 934 1.
 REPEAT 935 942 2; truncated.
 REPEAT 943 952 3.
 REPEAT 953 962 4.
 REPEAT 963 972 5.
 REPEAT 973 982 6.
 REPEAT 983 992 7.
 REPEAT 993 1002 8.
 REPEAT 1003 1012 9.
 REPEAT 1013 1022 10.
 REPEAT 1023 1032 11.
 REPEAT 1033 1042 12.
 REPEAT 1043 1052 13.
 REPEAT 1054 1063 14.
 REPEAT 1064 1073 15.
 REPEAT 1074 1083 16.
 REPEAT 1084 1093 17.
 REPEAT 1094 1103 18.
 REPEAT 1104 1113 19.
 REPEAT 1114 1123 20.
 REPEAT 1124 1133 21.
 REPEAT 1134 1143 22.
 REPEAT 1144 1152 23; truncated.
 REPEAT 1153 1162 24.
 REPEAT 1163 1172 25; approximate.
 REGION 664 835 Interaction with EIF3B.
 REGION 925 1172 25 X 10 AA approximate tandem repeats of
 MOD_RES 68 68 N6-acetyllysine.
 MOD_RES 492 492 Phosphoserine.
 MOD_RES 881 881 Phosphoserine.
 MOD_RES 882 882 Phosphoserine.
 MOD_RES 1198 1198 Phosphoserine.
 MOD_RES 1336 1336 Phosphoserine.
 MOD_RES 1364 1364 Phosphoserine.  
Keyword
 Acetylation; Coiled coil; Complete proteome; Cytoplasm; Direct protein sequencing; Initiation factor; Phosphoprotein; Polymorphism; Protein biosynthesis; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1382 AA 
Protein Sequence
MPAYFQRPEN ALKRANEFLE VGKKQPALDV LYDVMKSKKH RTWQKIHEPI MLKYLELCVD 60
LRKSHLAKEG LYQYKNICQQ VNIKSLEDVV RAYLKMAEEK TEAAKEESQQ MVLDIEDLDN 120
IQTPESVLLS AVSGEDTQDR TDRLLLTPWV KFLWESYRQC LDLLRNNSRV ERLYHDIAQQ 180
AFKFCLQYTR KAEFRKLCDN LRMHLSQIQR HHNQSTAINL NNPESQSMHL ETRLVQLDSA 240
ISMELWQEAF KAVEDIHGLF SLSKKPPKPQ LMANYYNKVS TVFWKSGNAL FHASTLHRLY 300
HLSREMRKNL TQDEMQRMST RVLLATLSIP ITPERTDIAR LLDMDGIIVE KQRRLATLLG 360
LQAPPTRIGL INDMVRFNVL QYVVPEVKDL YNWLEVEFNP LKLCERVTKV LNWVREQPEK 420
EPELQQYVPQ LQNNTILRLL QQVSQIYQSI EFSRLTSLVP FVDAFQLERA IVDAARHCDL 480
QVRIDHTSRT LSFGSDLNYA TREDAPIGPH LQSMPSEQIR NQLTAMSSVL AKALEVIKPA 540
HILQEKEEQH QLAVTAYLKN SRKEHQRILA RRQTIEERKE RLESLNIQRE KEELEQREAE 600
LQKVRKAEEE RLRQEAKERE KERILQEHEQ IKKKTVRERL EQIKKTELGA KAFKDIDIED 660
LEELDPDFIM AKQVEQLEKE KKELQERLKN QEKKIDYFER AKRLEEIPLI KSAYEEQRIK 720
DMDLWEQQEE ERITTMQLER EKALEHKNRM SRMLEDRDLF VMRLKAARQS VYEEKLKQFE 780
ERLAEERHNR LEERKRQRKE ERRITYYREK EEEEQRRAEE QMLKEREERE RAERAKREEE 840
LREYQERVKK LEEVERKKRQ RELEIEERER RREEERRLGD SSLSRKDSRW GDRDSEGTWR 900
KGPEADSEWR RGPPEKEWRR GEGRDEDRSH RRDEERPRRL GDDEDREPSL RPDDDRVPRR 960
GMDDDRGPRR GPEEDRFSRR GADDDRPSWR NTDDDRPPRR IADEDRGNWR HADDDRPPRR 1020
GLDEDRGSWR TADEDRGPRR GMDDDRGPRR GGADDERSSW RNADDDRGPR RGLDDDRGPR 1080
RGMDDDRGPR RGMDDDRGPR RGMDDDRGPR RGLDDDRGPW RNADDDRIPR RGAEDDRGPW 1140
RNMDDDRLSR RADDDRFPRR GDDSRPGPWR PLVKPGGWRE KEKAREESWG PPRESRPSEE 1200
REWDREKERD RDNQDREEND KDPERERDRE RDVDREDRFR RPRDEGGWRR GPAEESSSWR 1260
DSSRRDDRDR DDRRRERDDR RDLRERRDLR DDRDRRGPPL RSEREEVSSW RRADDRKDDR 1320
VEERDPPRRV PPPALSRDRE RDRDREREGE KEKASWRAEK DRESLRRTKN ETDEDGWTTV 1380
RR 1382 
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:0005730; C:nucleolus; IDA:HPA.
 GO:0005198; F:structural molecule activity; NAS:UniProtKB.
 GO:0003743; F:translation initiation factor activity; IEA:HAMAP.
 GO:0001732; P:formation of translation initiation complex; IDA:UniProtKB.
 GO:0001731; P:formation of translation preinitiation complex; IEA:HAMAP.
 GO:0006446; P:regulation of translational initiation; IEA:HAMAP. 
Interpro
 IPR027512; EIF3A.
 IPR000717; PCI_dom. 
Pfam
 PF01399; PCI 
SMART
 SM00088; PINT 
PROSITE
  
PRINTS