CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002235
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Eukaryotic translation initiation factor 2 subunit 1 
Protein Synonyms/Alias
 Eukaryotic translation initiation factor 2 subunit alpha; eIF-2-alpha; eIF-2A; eIF-2alpha 
Gene Name
 EIF2S1 
Gene Synonyms/Alias
 EIF2A 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
12SCRFYQHKFPEVEDVubiquitination[1]
61RRIRSINKLIRIGRNubiquitination[1, 2, 3]
78VVVIRVDKEKGYIDLubiquitination[1]
80VIRVDKEKGYIDLSKubiquitination[1]
87KGYIDLSKRRVSPEEubiquitination[1, 4]
97VSPEEAIKCEDKFTKubiquitination[1]
101EAIKCEDKFTKSKTVubiquitination[1]
104KCEDKFTKSKTVYSIubiquitination[1]
106EDKFTKSKTVYSILRubiquitination[1, 2, 3]
123AEVLEYTKDEQLESLubiquitination[1, 4, 5]
141TAWVFDDKYKRPGYGacetylation[6]
141TAWVFDDKYKRPGYGubiquitination[1, 2, 3, 4, 7]
143WVFDDKYKRPGYGAYubiquitination[1, 2, 3, 7, 8]
154YGAYDAFKHAVSDPSubiquitination[4]
190RLTPQAVKIRADIEVubiquitination[1, 4, 5, 7]
226STENMPIKINLIAPPubiquitination[1, 7]
259SQAMAVIKEKIEEKRubiquitination[1, 4, 5]
261AMAVIKEKIEEKRGVubiquitination[1]
276FNVQMEPKVVTDTDEubiquitination[1, 4]
312DAEEMEAKAED****ubiquitination[4]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [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] 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]
 [7] 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]
 [8] 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] 
Functional Description
 Functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S preinitiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B. 
Sequence Annotation
 DOMAIN 17 88 S1 motif.
 MOD_RES 49 49 Phosphoserine; by HRI (By similarity).
 MOD_RES 52 52 Phosphoserine.
 MOD_RES 141 141 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Initiation factor; Phosphoprotein; Protein biosynthesis; Reference proteome; RNA-binding; Translation regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 315 AA 
Protein Sequence
MPGLSCRFYQ HKFPEVEDVV MVNVRSIAEM GAYVSLLEYN NIEGMILLSE LSRRRIRSIN 60
KLIRIGRNEC VVVIRVDKEK GYIDLSKRRV SPEEAIKCED KFTKSKTVYS ILRHVAEVLE 120
YTKDEQLESL FQRTAWVFDD KYKRPGYGAY DAFKHAVSDP SILDSLDLNE DEREVLINNI 180
NRRLTPQAVK IRADIEVACY GYEGIDAVKE ALRAGLNCST ENMPIKINLI APPRYVMTTT 240
TLERTEGLSV LSQAMAVIKE KIEEKRGVFN VQMEPKVVTD TDETELARQM ERLERENAEV 300
DGDDDAEEME AKAED 315 
Gene Ontology
 GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005850; C:eukaryotic translation initiation factor 2 complex; IEA:InterPro.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0005844; C:polysome; TAS:ProtInc.
 GO:0043022; F:ribosome binding; IDA:UniProtKB.
 GO:0003743; F:translation initiation factor activity; IDA:UniProtKB.
 GO:0006987; P:activation of signaling protein activity involved in unfolded protein response; TAS:Reactome.
 GO:0046777; P:protein autophosphorylation; IEA:Compara.
 GO:0043558; P:regulation of translational initiation in response to stress; IEA:Compara. 
Interpro
 IPR012340; NA-bd_OB-fold.
 IPR003029; Rbsml_prot_S1_RNA-bd_dom.
 IPR022967; RNA-binding_domain_S1.
 IPR024055; TIF2_asu_C.
 IPR024054; TIF2_asu_middle.
 IPR011488; TIF_2_asu. 
Pfam
 PF07541; EIF_2_alpha
 PF00575; S1 
SMART
 SM00316; S1 
PROSITE
 PS50126; S1 
PRINTS