CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015595
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
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
101EAIKCEDKFTKSKTVubiquitination[1]
106EDKFTKSKTVYSILRacetylation[2]
106EDKFTKSKTVYSILRubiquitination[1]
141TAWVFDDKYKRPGYGacetylation[2]
141TAWVFDDKYKRPGYGubiquitination[1]
259NQAMAVIKEKIEEKRacetylation[2]
259NQAMAVIKEKIEEKRubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441
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 (By similarity). 
Sequence Annotation
 DOMAIN 17 88 S1 motif.
 MOD_RES 49 49 Phosphoserine; by HRI (By similarity).
 MOD_RES 52 52 Phosphoserine; by EIF2AK3, GCN2, HRI and
 MOD_RES 141 141 N6-acetyllysine (By similarity).  
Keyword
 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 ETMPIKINLI APPRYVMTTT 240
TLERTEGLSV LNQAMAVIKE KIEEKRGVFN VQMEPKVVTD TDETELARQL ERLERENAEV 300
DGDDDAEEME AKAED 315 
Gene Ontology
 GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
 GO:0005850; C:eukaryotic translation initiation factor 2 complex; IEA:InterPro.
 GO:0005851; C:eukaryotic translation initiation factor 2B complex; IEA:Compara.
 GO:0005634; C:nucleus; IDA:MGI.
 GO:0043022; F:ribosome binding; ISS:UniProtKB.
 GO:0003743; F:translation initiation factor activity; ISS:UniProtKB.
 GO:0046777; P:protein autophosphorylation; IDA:MGI.
 GO:0043558; P:regulation of translational initiation in response to stress; IDA:MGI. 
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