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Eukaryotic translation initiation factor 2 subunit 1 (Eukaryotic translation initiation factor 2 subunit alpha) (eIF-2-alpha) (eIF-2A) (eIF-2alpha)

 IF2A_HUMAN              Reviewed;         315 AA.
P05198;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
18-JUL-2018, entry version 195.
RecName: Full=Eukaryotic translation initiation factor 2 subunit 1;
AltName: Full=Eukaryotic translation initiation factor 2 subunit alpha;
Short=eIF-2-alpha;
Short=eIF-2A;
Short=eIF-2alpha;
Name=EIF2S1; Synonyms=EIF2A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Fibroblast;
PubMed=2948954;
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[3]
PHOSPHORYLATION STATE REGULATION BY VACCINIA VIRUS PROTEIN E3.
PubMed=15207627; DOI=10.1016/j.virol.2004.03.012;
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).
[4]
INTERACTION WITH ABCF1, AND ASSOCIATION WITH RIBOSOMES.
PubMed=17894550; DOI=10.1042/BJ20070811;
Paytubi S., Morrice N.A., Boudeau J., Proud C.G.;
"The N-terminal region of ABC50 interacts with eukaryotic initiation
factor eIF2 and is a target for regulatory phosphorylation by CK2.";
Biochem. J. 409:223-231(2008).
[5]
PHOSPHORYLATION STATE REGULATION BY ROTAVIRUS A.
PubMed=18032499; DOI=10.1128/JVI.01779-07;
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).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-141, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[9]
SUBUNIT.
PubMed=23063529; DOI=10.1016/j.molcel.2012.09.005;
Borck G., Shin B.S., Stiller B., Mimouni-Bloch A., Thiele H.,
Kim J.R., Thakur M., Skinner C., Aschenbach L., Smirin-Yosef P.,
Har-Zahav A., Nuernberg G., Altmueller J., Frommolt P., Hofmann K.,
Konen O., Nuernberg P., Munnich A., Schwartz C.E., Gothelf D.,
Colleaux L., Dever T.E., Kubisch C., Basel-Vanagaite L.;
"eIF2gamma mutation that disrupts eIF2 complex integrity links
intellectual disability to impaired translation initiation.";
Mol. Cell 48:641-646(2012).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158; THR-279 AND
THR-281, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[13]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-183.
PubMed=11859078; DOI=10.1074/jbc.M111804200;
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).
[14]
STRUCTURE BY NMR OF 5-303.
PubMed=15341733; DOI=10.1016/j.str.2004.07.010;
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).
-!- 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 pre-initiation 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 (PubMed:23063529). Component of an EIF2 complex at least
composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and
HSPA5. Interaction with METAP2 protects EIF2S1 from inhibitory
phosphorylation (By similarity). Interacts with ABCF1 isoform 2
(PubMed:17894550). Associates with ribosomes (PubMed:17894550).
{ECO:0000250, ECO:0000269|PubMed:17894550,
ECO:0000269|PubMed:23063529}.
-!- INTERACTION:
P12814:ACTN1; NbExp=4; IntAct=EBI-1056162, EBI-351710;
O00571:DDX3X; NbExp=3; IntAct=EBI-1056162, EBI-353779;
P19525:EIF2AK2; NbExp=5; IntAct=EBI-1056162, EBI-640775;
Q9Z2B5:Eif2ak3 (xeno); NbExp=4; IntAct=EBI-1056162, EBI-1226344;
P20042:EIF2S2; NbExp=6; IntAct=EBI-1056162, EBI-711977;
P41091:EIF2S3; NbExp=4; IntAct=EBI-1056162, EBI-1054228;
-!- SUBCELLULAR LOCATION: Cytoplasm, Stress granule
{ECO:0000250|UniProtKB:Q6ZWX6}. Note=Colocalizes with NANOS3 in
the stress granules. {ECO:0000250|UniProtKB:Q6ZWX6}.
-!- PTM: Substrate for at least 4 kinases: EIF2AK1/HRI, EIF2AK2/PKR,
EIF2AK3/PERK and EIF2AK4/GCN2. 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
(PubMed:15207627, PubMed:18032499). Phosphorylated;
phosphorylation on Ser-52 by the EIF2AK4/GCN2 protein kinase
occurs in response to amino acid starvation and UV irradiation (By
similarity). {ECO:0000250|UniProtKB:Q6ZWX6,
ECO:0000269|PubMed:15207627, ECO:0000269|PubMed:18032499}.
-!- SIMILARITY: Belongs to the eIF-2-alpha family. {ECO:0000305}.
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EMBL; J02645; AAA52373.1; -; mRNA.
EMBL; BC002513; AAH02513.1; -; mRNA.
CCDS; CCDS9781.1; -.
RefSeq; NP_004085.1; NM_004094.4.
UniGene; Hs.151777; -.
PDB; 1KL9; X-ray; 1.90 A; A=2-183.
PDB; 1Q8K; NMR; -; A=5-303.
PDBsum; 1KL9; -.
PDBsum; 1Q8K; -.
ProteinModelPortal; P05198; -.
SMR; P05198; -.
BioGrid; 108285; 77.
CORUM; P05198; -.
DIP; DIP-39418N; -.
IntAct; P05198; 33.
MINT; P05198; -.
STRING; 9606.ENSP00000256383; -.
ChEMBL; CHEMBL1255131; -.
iPTMnet; P05198; -.
PhosphoSitePlus; P05198; -.
SwissPalm; P05198; -.
BioMuta; EIF2S1; -.
DMDM; 124200; -.
OGP; P05198; -.
REPRODUCTION-2DPAGE; IPI00219678; -.
EPD; P05198; -.
PaxDb; P05198; -.
PeptideAtlas; P05198; -.
PRIDE; P05198; -.
ProteomicsDB; 51824; -.
TopDownProteomics; P05198; -.
DNASU; 1965; -.
Ensembl; ENST00000256383; ENSP00000256383; ENSG00000134001.
Ensembl; ENST00000466499; ENSP00000425299; ENSG00000134001.
GeneID; 1965; -.
KEGG; hsa:1965; -.
CTD; 1965; -.
DisGeNET; 1965; -.
EuPathDB; HostDB:ENSG00000134001.12; -.
GeneCards; EIF2S1; -.
HGNC; HGNC:3265; EIF2S1.
HPA; CAB011663; -.
HPA; HPA064885; -.
MIM; 603907; gene.
neXtProt; NX_P05198; -.
OpenTargets; ENSG00000134001; -.
PharmGKB; PA27695; -.
eggNOG; KOG2916; Eukaryota.
eggNOG; COG1093; LUCA.
GeneTree; ENSGT00390000007015; -.
HOGENOM; HOG000199476; -.
HOVERGEN; HBG001910; -.
InParanoid; P05198; -.
KO; K03237; -.
OMA; KDVNEHQ; -.
OrthoDB; EOG091G07NN; -.
PhylomeDB; P05198; -.
TreeFam; TF101502; -.
Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
Reactome; R-HSA-381042; PERK regulates gene expression.
Reactome; R-HSA-382556; ABC-family proteins mediated transport.
Reactome; R-HSA-72649; Translation initiation complex formation.
Reactome; R-HSA-72695; Formation of the ternary complex, and subsequently, the 43S complex.
Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition.
Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
Reactome; R-HSA-72731; Recycling of eIF2:GDP.
SIGNOR; P05198; -.
ChiTaRS; EIF2S1; human.
EvolutionaryTrace; P05198; -.
GeneWiki; EIF2S1; -.
GenomeRNAi; 1965; -.
PMAP-CutDB; P05198; -.
PRO; PR:P05198; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000134001; -.
CleanEx; HS_EIF2A; -.
CleanEx; HS_EIF2S1; -.
ExpressionAtlas; P05198; baseline and differential.
Genevisible; P05198; HS.
GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IBA:GO_Central.
GO; GO:0005850; C:eukaryotic translation initiation factor 2 complex; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0097451; C:glial limiting end-foot; IEA:Ensembl.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0043614; C:multi-eIF complex; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0005844; C:polysome; TAS:ProtInc.
GO; GO:0005840; C:ribosome; IBA:GO_Central.
GO; GO:0044207; C:translation initiation ternary complex; IEA:Ensembl.
GO; GO:0043022; F:ribosome binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0003743; F:translation initiation factor activity; IDA:UniProtKB.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0034198; P:cellular response to amino acid starvation; ISS:UniProtKB.
GO; GO:0034605; P:cellular response to heat; IEA:Ensembl.
GO; GO:0034599; P:cellular response to oxidative stress; ISS:ARUK-UCL.
GO; GO:0034644; P:cellular response to UV; ISS:UniProtKB.
GO; GO:1905098; P:negative regulation of guanyl-nucleotide exchange factor activity; IEA:Ensembl.
GO; GO:0032057; P:negative regulation of translational initiation in response to stress; ISS:UniProtKB.
GO; GO:0036499; P:PERK-mediated unfolded protein response; NAS:ParkinsonsUK-UCL.
GO; GO:1901216; P:positive regulation of neuron death; IMP:ParkinsonsUK-UCL.
GO; GO:2000676; P:positive regulation of type B pancreatic cell apoptotic process; IEA:Ensembl.
GO; GO:0046777; P:protein autophosphorylation; IEA:Ensembl.
GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:ParkinsonsUK-UCL.
GO; GO:1990737; P:response to manganese-induced endoplasmic reticulum stress; IEA:Ensembl.
GO; GO:0034063; P:stress granule assembly; ISS:ARUK-UCL.
GO; GO:0006413; P:translational initiation; TAS:Reactome.
GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
Gene3D; 1.10.150.190; -; 1.
Gene3D; 3.30.70.1130; -; 1.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR022967; S1_dom.
InterPro; IPR003029; S1_domain.
InterPro; IPR024055; TIF2_asu_C.
InterPro; IPR024054; TIF2_asu_middle_sf.
InterPro; IPR011488; TIF_2_asu.
PANTHER; PTHR10602; PTHR10602; 1.
Pfam; PF07541; EIF_2_alpha; 1.
Pfam; PF00575; S1; 1.
SMART; SM00316; S1; 1.
SUPFAM; SSF110993; SSF110993; 1.
SUPFAM; SSF116742; SSF116742; 1.
SUPFAM; SSF50249; SSF50249; 1.
PROSITE; PS50126; S1; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Initiation factor; Phosphoprotein; Protein biosynthesis;
Reference proteome; RNA-binding; Translation regulation.
CHAIN 1 315 Eukaryotic translation initiation factor
2 subunit 1.
/FTId=PRO_0000137382.
DOMAIN 17 88 S1 motif. {ECO:0000255|PROSITE-
ProRule:PRU00180}.
MOD_RES 49 49 Phosphoserine; by HRI.
{ECO:0000250|UniProtKB:P83268}.
MOD_RES 52 52 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:24275569}.
MOD_RES 141 141 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 158 158 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 279 279 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 281 281 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
STRAND 8 13 {ECO:0000244|PDB:1KL9}.
STRAND 19 27 {ECO:0000244|PDB:1KL9}.
STRAND 29 36 {ECO:0000244|PDB:1KL9}.
TURN 37 41 {ECO:0000244|PDB:1KL9}.
STRAND 43 47 {ECO:0000244|PDB:1KL9}.
HELIX 48 50 {ECO:0000244|PDB:1KL9}.
TURN 60 62 {ECO:0000244|PDB:1Q8K}.
STRAND 64 66 {ECO:0000244|PDB:1Q8K}.
STRAND 68 77 {ECO:0000244|PDB:1KL9}.
TURN 78 81 {ECO:0000244|PDB:1KL9}.
STRAND 82 87 {ECO:0000244|PDB:1KL9}.
HELIX 92 118 {ECO:0000244|PDB:1KL9}.
HELIX 124 133 {ECO:0000244|PDB:1KL9}.
HELIX 135 142 {ECO:0000244|PDB:1KL9}.
HELIX 147 158 {ECO:0000244|PDB:1KL9}.
HELIX 160 163 {ECO:0000244|PDB:1KL9}.
HELIX 170 182 {ECO:0000244|PDB:1KL9}.
STRAND 190 193 {ECO:0000244|PDB:1Q8K}.
TURN 202 204 {ECO:0000244|PDB:1Q8K}.
HELIX 205 217 {ECO:0000244|PDB:1Q8K}.
STRAND 218 220 {ECO:0000244|PDB:1Q8K}.
STRAND 225 231 {ECO:0000244|PDB:1Q8K}.
STRAND 234 240 {ECO:0000244|PDB:1Q8K}.
HELIX 244 263 {ECO:0000244|PDB:1Q8K}.
HELIX 282 289 {ECO:0000244|PDB:1Q8K}.
HELIX 293 295 {ECO:0000244|PDB:1Q8K}.
SEQUENCE 315 AA; 36112 MW; FF3E75E3816E6B1E CRC64;
MPGLSCRFYQ HKFPEVEDVV MVNVRSIAEM GAYVSLLEYN NIEGMILLSE LSRRRIRSIN
KLIRIGRNEC VVVIRVDKEK GYIDLSKRRV SPEEAIKCED KFTKSKTVYS ILRHVAEVLE
YTKDEQLESL FQRTAWVFDD KYKRPGYGAY DAFKHAVSDP SILDSLDLNE DEREVLINNI
NRRLTPQAVK IRADIEVACY GYEGIDAVKE ALRAGLNCST ENMPIKINLI APPRYVMTTT
TLERTEGLSV LSQAMAVIKE KIEEKRGVFN VQMEPKVVTD TDETELARQM ERLERENAEV
DGDDDAEEME AKAED


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Genprice Inc, Invoices and accounting
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