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[1]
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NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Fibroblast;
PubMed=2948954 [NCBI, ExPASy, EBI, Israel, Japan]
Ernst H.,
Duncan R.F.,
Hershey J.W.B.;
"Cloning and sequencing of complementary DNAs encoding the alpha-subunit of translational initiation factor eIF-2. Characterization of the protein and its messenger RNA.";
J. Biol. Chem. 262:1206-1212(1987).
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[2]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
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[3]
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PHOSPHORYLATION STATE REGULATION BY VACCINIA VIRUS PROTEIN E3.
DOI=10.1016/j.virol.2004.03.012; PubMed=15207627 [NCBI, ExPASy, EBI, Israel, Japan]
Langland J.O.,
Jacobs B.L.;
"Inhibition of PKR by vaccinia virus: role of the N- and C-terminal domains of E3L.";
Virology 324:419-429(2004).
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[4]
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PHOSPHORYLATION STATE REGULATION BY ROTAVIRUS A.
DOI=10.1128/JVI.01779-07; PubMed=18032499 [NCBI, ExPASy, EBI, Israel, Japan]
Montero H.,
Rojas M.,
Arias C.F.,
Lopez S.;
"Rotavirus infection induces the phosphorylation of eIF2alpha but prevents the formation of stress granules.";
J. Virol. 82:1496-1504(2008).
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[5]
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IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J.,
Superti-Furga G.,
Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
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[6]
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X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-183.
DOI=10.1074/jbc.M111804200; PubMed=11859078 [NCBI, ExPASy, EBI, Israel, Japan]
Nonato M.C.,
Widom J.,
Clardy J.;
"Crystal structure of the N-terminal segment of human eukaryotic translation initiation factor 2alpha.";
J. Biol. Chem. 277:17057-17061(2002).
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[7]
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STRUCTURE BY NMR OF 5-303.
DOI=10.1016/j.str.2004.07.010; PubMed=15341733 [NCBI, ExPASy, EBI, Israel, Japan]
Ito T.,
Marintchev A.,
Wagner G.;
"Solution structure of human initiation factor eIF2alpha reveals homology to the elongation factor eEF1B.";
Structure 12:1693-1704(2004).
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- FUNCTION: 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.
- SUBUNIT: Heterotrimer composed of an alpha, a beta and a gamma chain. Component of an EIF2 complex at least composed of CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5 (By similarity).
- INTERACTION:
O60739:EIF1B; NbExp=1; IntAct=EBI-1056162, EBI-1043343;
P19525:EIF2AK2; NbExp=1; IntAct=EBI-1056162, EBI-640775;
Q9Z2B5:Eif2ak3 (xeno); NbExp=4; IntAct=EBI-1056162, EBI-1226344;
P20042:EIF2S2; NbExp=1; IntAct=EBI-1056162, EBI-711977;
P41091:EIF2S3; NbExp=1; IntAct=EBI-1056162, EBI-1054228;
P36873-1:PPP1CC; NbExp=1; IntAct=EBI-1056162, EBI-356289;
- PTM: Substrate for at least 4 kinases: EIF2AK3/PERK, GCN2, HRI and PKR. Phosphorylation stabilizes the eIF-2/GDP/eIF-2B complex and prevents GDP/GTP exchange reaction, thus impairing the recycling of eIF-2 between successive rounds of initiation and leading to global inhibition of translation. In case of infection by vaccinia virus or rotavirus A, eIF2S1 phosphorylation state is modulated.
- SIMILARITY: Belongs to the eIF-2-alpha family.
- SIMILARITY: Contains 1 S1 motif domain.
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Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 315 AA [This is the length of the unprocessed precursor] |
Molecular weight: 36112 Da [This is the MW of the unprocessed precursor] |
CRC64: FF3E75E3816E6B1E [This is a checksum on the sequence] |
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10 20 30 40 50 60
MPGLSCRFYQ HKFPEVEDVV MVNVRSIAEM GAYVSLLEYN NIEGMILLSE LSRRRIRSIN
70 80 90 100 110 120
KLIRIGRNEC VVVIRVDKEK GYIDLSKRRV SPEEAIKCED KFTKSKTVYS ILRHVAEVLE
130 140 150 160 170 180
YTKDEQLESL FQRTAWVFDD KYKRPGYGAY DAFKHAVSDP SILDSLDLNE DEREVLINNI
190 200 210 220 230 240
NRRLTPQAVK IRADIEVACY GYEGIDAVKE ALRAGLNCST ENMPIKINLI APPRYVMTTT
250 260 270 280 290 300
TLERTEGLSV LSQAMAVIKE KIEEKRGVFN VQMEPKVVTD TDETELARQM ERLERENAEV
310
DGDDDAEEME AKAED
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P05198 in FASTA format |
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