CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004874
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Eukaryotic translation initiation factor 2 subunit alpha 
Protein Synonyms/Alias
 eIF-2-alpha 
Gene Name
 SUI2 
Gene Synonyms/Alias
 TIF211; YJR007W; J1429 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
137IAWPLSRKFGHAYEAacetylation[1]
183RLTPQAVKIRADVEVubiquitination[2]
221EQMQVKVKLVAAPLYubiquitination[2]
237LTTQALDKQKGIEQLacetylation[1]
237LTTQALDKQKGIEQLubiquitination[2]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301
Functional Description
 eIF-2 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 52 52 Phosphoserine; by GCN2.
 MOD_RES 292 292 Phosphoserine.
 MOD_RES 294 294 Phosphoserine.  
Keyword
 3D-structure; Complete proteome; Initiation factor; Phosphoprotein; Protein biosynthesis; Reference proteome; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 304 AA 
Protein Sequence
MSTSHCRFYE NKYPEIDDIV MVNVQQIAEM GAYVKLLEYD NIEGMILLSE LSRRRIRSIQ 60
KLIRVGKNDV AVVLRVDKEK GYIDLSKRRV SSEDIIKCEE KYQKSKTVHS ILRYCAEKFQ 120
IPLEELYKTI AWPLSRKFGH AYEAFKLSII DETVWEGIEP PSKDVLDELK NYISKRLTPQ 180
AVKIRADVEV SCFSYEGIDA IKDALKSAED MSTEQMQVKV KLVAAPLYVL TTQALDKQKG 240
IEQLESAIEK ITEVITKYGG VCNITMPPKA VTATEDAELQ ALLESKELDN RSDSEDDEDE 300
SDDE 304 
Gene Ontology
 GO:0005850; C:eukaryotic translation initiation factor 2 complex; IMP:SGD.
 GO:0043614; C:multi-eIF complex; IDA:SGD.
 GO:0005840; C:ribosome; TAS:SGD.
 GO:0003743; F:translation initiation factor activity; TAS:SGD. 
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