CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-039876
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 
Gene Name
 EIF3A 
Gene Synonyms/Alias
 EIF3S10 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
11KKHRTWQKIHEPIMLubiquitination[1, 2, 3]
34LRKSHLAKEGLYQYKacetylation[4, 5]
34LRKSHLAKEGLYQYKubiquitination[2, 5]
41KEGLYQYKNICQQVNubiquitination[2, 5, 6, 7]
50ICQQVNIKSLEDVVRubiquitination[2]
71EEKTEAAKEESQQMVubiquitination[3]
162TRKAEFRKLCDNLRMacetylation[5]
162TRKAEFRKLCDNLRMubiquitination[2]
251KVSTVFWKSGNALFHubiquitination[2, 3, 5, 8]
274HLSREMRKNLTQDEMubiquitination[2]
317MDGIIVEKQRRLATLubiquitination[2, 3, 5, 6, 7, 8]
368EVEFNPLKLCERVTKubiquitination[6]
375KLCERVTKVLNWVREubiquitination[1, 2]
386WVREQPEKEPELQQYubiquitination[1, 2, 3, 5, 6, 9, 10]
498AMSSVLAKALEVIKPubiquitination[3]
504AKALEVIKPAHILQEacetylation[4]
525LAVTAYLKNSRKEHQubiquitination[3]
557SLNIQREKEELEQREubiquitination[5]
569QREAELQKVRKAEEEubiquitination[2]
598LQEHEQIKKKTVRERmethylation[11]
598LQEHEQIKKKTVRERubiquitination[2, 5, 6]
599QEHEQIKKKTVRERLmethylation[11]
599QEHEQIKKKTVRERLubiquitination[2, 3, 5]
600EHEQIKKKTVRERLEmethylation[11]
600EHEQIKKKTVRERLEubiquitination[2]
617KKTELGAKAFKDIDIubiquitination[5, 6]
620ELGAKAFKDIDIEDLubiquitination[2, 3, 6]
638DPDFIMAKQVEQLEKubiquitination[3, 6]
660RLKNQEKKIDYFERAubiquitination[2, 6]
677LEEIPLIKSAYEEQRubiquitination[1, 2, 3, 5, 6]
686AYEEQRIKDMDLWEQubiquitination[6]
741RQSVYEEKLKQFEERubiquitination[1, 2, 3, 5, 6, 7, 8, 9, 10]
743SVYEEKLKQFEERLAubiquitination[1, 2]
790RAEEQMLKEREERERubiquitination[2, 3, 5, 6]
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] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [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] 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]
 [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] Large-scale global identification of protein lysine methylation in vivo.
 Cao XJ, Arnaudo AM, Garcia BA.
 Epigenetics. 2013 May 1;8(5):477-85. [PMID: 23644510] 
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 332 460 PCI (By similarity).
 REGION 630 801 Interaction with EIF3B (By similarity).
 MOD_RES 847 847 Phosphoserine (By similarity).
 MOD_RES 1164 1164 Phosphoserine (By similarity).
 MOD_RES 1302 1302 Phosphoserine (By similarity).
 MOD_RES 1330 1330 Phosphoserine (By similarity).  
Keyword
 Coiled coil; Complete proteome; Cytoplasm; Initiation factor; Phosphoprotein; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1348 AA 
Protein Sequence
MKSKKHRTWQ KIHEPIMLKY LELCVDLRKS HLAKEGLYQY KNICQQVNIK SLEDVVRAYL 60
KMAEEKTEAA KEESQQMVLD IEDLDNIQTP ESVLLSAVSG EDTQDRTDRL LLTPWVKFLW 120
ESYRQCLDLL RNNSRVERLY HDIAQQAFKF CLQYTRKAEF RKLCDNLRMH LSQIQRHHNQ 180
STAINLNNPE SQSMHLETRL VQLDSAISME LWQEAFKAVE DIHGLFSLSK KPPKPQLMAN 240
YYNKVSTVFW KSGNALFHAS TLHRLYHLSR EMRKNLTQDE MQRMSTRVLL ATLSIPITPE 300
RTDIARLLDM DGIIVEKQRR LATLLGLQAP PTRIGLINDM VRFNVLQYVV PEVKDLYNWL 360
EVEFNPLKLC ERVTKVLNWV REQPEKEPEL QQYVPQLQNN TILRLLQQVS QIYQSIEFSR 420
LTSLVPFVDA FQLERAIVDA ARHCDLQVRI DHTSRTLSFG SDLNYATRED APIGPHLQSM 480
PSEQIRNQLT AMSSVLAKAL EVIKPAHILQ EKEEQHQLAV TAYLKNSRKE HQRILARRQT 540
IEERKERLES LNIQREKEEL EQREAELQKV RKAEEERLRQ EAKEREKERI LQEHEQIKKK 600
TVRERLEQIK KTELGAKAFK DIDIEDLEEL DPDFIMAKQV EQLEKEKKEL QERLKNQEKK 660
IDYFERAKRL EEIPLIKSAY EEQRIKDMDL WEQQEEERIT TMQLEREKAL EHKNRMSRML 720
EDRDLFVMRL KAARQSVYEE KLKQFEERLA EERHNRLEER KRQRKEERRI TYYREKEEEE 780
QRRAEEQMLK EREERERAER AKREEELREY QERVKKLEEV ERKKRQRELE IEERERRREE 840
ERRLGDSSLS RKDSRWGDRD SEGTWRKGPE ADSEWRRGPP EKEWRRGEGR DEDRSHRRDE 900
ERPRRLGDDE DREPSLRPDD DRVPRRGMDD DRGPRRGPEE DRFSRRGADD DRPSWRNTDD 960
DRPPRRIADE DRGNWRHADD DRPPRRGLDE DRGSWRTADE DRGPRRGMDD DRGPRRGGAD 1020
DERSSWRNAD DDRGPRRGLD DDRGPRRGMD DDRGPRRGMD DDRGPRRGMD DDRGPRRGLD 1080
DDRGPWRNAD DDRIPRRGAE DDRGPWRNMD DDRLSRRADD DRFPRRGDDS RPGPWRPLVK 1140
PGGWREKEKA REESWGPPRE SRPSEEREWD REKERDRDNQ DREENDKDPE RERDRERDVD 1200
REDRFRRPRD EGGWRRGPAE ESSSWRDSSR RDDRDRDDRR RERDDRRDLR ERRDLRDDRD 1260
RRGPPLRSER EEVSSWRRAD DRKDDRVEER DPPRRVPPPA LSRDRERDRD REREGEKEKA 1320
SWRAEKDRES LRRTKNETDE DGWTTVRR 1348 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 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:0005730; C:nucleolus; IDA:HPA.
 GO:0003743; F:translation initiation factor activity; IEA:HAMAP.
 GO:0001732; P:formation of translation initiation complex; IEA:Compara.
 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