EIF2A_HUMAN
ID EIF2A_HUMAN Reviewed; 585 AA.
AC Q9BY44; A8MPS6; B4DF96; B4DQ14; D3DNI9; Q5QTR2; Q7Z4E9; Q8NFM1; Q96EW9;
AC Q96K81;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 3.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Eukaryotic translation initiation factor 2A;
DE Short=eIF-2A;
DE AltName: Full=65 kDa eukaryotic translation initiation factor 2A;
DE Contains:
DE RecName: Full=Eukaryotic translation initiation factor 2A, N-terminally processed;
GN Name=EIF2A; ORFNames=CDA02, MSTP004, MSTP089;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP VARIANT SER-97.
RX PubMed=12133843; DOI=10.1074/jbc.m207109200;
RA Zoll W.L., Horton L.E., Komar A.A., Hensold J.O., Merrick W.C.;
RT "Characterization of mammalian eIF2A and identification of the yeast
RT homolog.";
RL J. Biol. Chem. 277:37079-37087(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4), AND VARIANT
RP SER-97.
RC TISSUE=Cerebellum, and Embryo;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-97.
RC TISSUE=Pheochromocytoma;
RA Li Y., Huang Q., Peng Y., Song H., Yu Y., Xu S., Ren S., Chen Z., Han Z.;
RT "A novel gene expressed in human pheochromocytoma.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 4-585 (ISOFORM 1), AND VARIANT SER-97.
RC TISSUE=Aorta, and Heart;
RA Liu B., Song L., Sheng H., Qin B.M., Liu Y.Q., Zhao B., Wang X.Y.,
RA Zhang Q., Ji X.Y., Liu B.H., Lu H., Xu H.S., Chen J.Z., Cai M.Q.,
RA Zheng W.Y., Teng C.Y., Liu Q., Yu L.T., Lin J., Gong J., Zhang A.M.,
RA Gao R.L., Hui R.T.;
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT SER-97.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LYS-582.
RC TISSUE=Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 2-11; 184-192 AND 506-520, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-506, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-506; SER-517 AND THR-518, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503 AND THR-518, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-506, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-5; SER-506 AND SER-526, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Functions in the early steps of protein synthesis of a small
CC number of specific mRNAs. Acts by directing the binding of methionyl-
CC tRNAi to 40S ribosomal subunits. In contrast to the eIF-2 complex, it
CC binds methionyl-tRNAi to 40S subunits in a codon-dependent manner,
CC whereas the eIF-2 complex binds methionyl-tRNAi to 40S subunits in a
CC GTP-dependent manner. {ECO:0000269|PubMed:12133843}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9BY44-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BY44-2; Sequence=VSP_024975, VSP_024976;
CC Name=3;
CC IsoId=Q9BY44-3; Sequence=VSP_056047;
CC Name=4;
CC IsoId=Q9BY44-4; Sequence=VSP_056048;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in
CC pancreas, heart, brain and placenta. {ECO:0000269|PubMed:12133843}.
CC -!- SIMILARITY: Belongs to the WD repeat EIF2A family. {ECO:0000305}.
CC -!- CAUTION: This gene should not be confused with EIF2S1, frequently
CC called eIF2-alpha in the literature, and with which it shares the alias
CC EIF2A. EIF2S1 is the alpha subunit of the eIF2 translation initiation
CC complex. Although both of these proteins function in binding initiator
CC tRNA to the 40S ribosomal subunit, the EIF2A protein does so in a
CC codon-dependent manner, whereas eIF2 complex requires GTP. Was
CC initially thought to constitute the ortholog of prokaryotic IF-2 (infB)
CC protein. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK14926.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAM83402.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAQ13506.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAQ13612.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF497978; AAM83402.1; ALT_FRAME; mRNA.
DR EMBL; AK027356; BAB55058.1; -; mRNA.
DR EMBL; AK298586; BAG60776.1; -; mRNA.
DR EMBL; AK293993; BAG57357.1; -; mRNA.
DR EMBL; AF212241; AAK14926.1; ALT_INIT; mRNA.
DR EMBL; AF109358; AAQ13506.1; ALT_FRAME; mRNA.
DR EMBL; AF172818; AAQ13612.1; ALT_INIT; mRNA.
DR EMBL; AC107426; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW78830.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78831.1; -; Genomic_DNA.
DR EMBL; BC011885; AAH11885.1; -; mRNA.
DR CCDS; CCDS46935.1; -. [Q9BY44-1]
DR CCDS; CCDS82859.1; -. [Q9BY44-4]
DR CCDS; CCDS82861.1; -. [Q9BY44-3]
DR RefSeq; NP_001305972.1; NM_001319043.1. [Q9BY44-3]
DR RefSeq; NP_001305973.1; NM_001319044.1. [Q9BY44-4]
DR RefSeq; NP_001305974.1; NM_001319045.1.
DR RefSeq; NP_001305975.1; NM_001319046.1. [Q9BY44-2]
DR RefSeq; NP_114414.2; NM_032025.4. [Q9BY44-1]
DR AlphaFoldDB; Q9BY44; -.
DR SMR; Q9BY44; -.
DR BioGRID; 123822; 142.
DR DIP; DIP-40272N; -.
DR ELM; Q9BY44; -.
DR IntAct; Q9BY44; 35.
DR MINT; Q9BY44; -.
DR STRING; 9606.ENSP00000417229; -.
DR ChEMBL; CHEMBL4295938; -.
DR GlyGen; Q9BY44; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BY44; -.
DR PhosphoSitePlus; Q9BY44; -.
DR SwissPalm; Q9BY44; -.
DR BioMuta; EIF2A; -.
DR DMDM; 209572747; -.
DR EPD; Q9BY44; -.
DR jPOST; Q9BY44; -.
DR MassIVE; Q9BY44; -.
DR MaxQB; Q9BY44; -.
DR PaxDb; Q9BY44; -.
DR PeptideAtlas; Q9BY44; -.
DR PRIDE; Q9BY44; -.
DR ProteomicsDB; 4015; -.
DR ProteomicsDB; 4834; -.
DR ProteomicsDB; 79581; -. [Q9BY44-1]
DR ProteomicsDB; 79582; -. [Q9BY44-2]
DR Antibodypedia; 33590; 348 antibodies from 35 providers.
DR CPTC; Q9BY44; 2 antibodies.
DR DNASU; 83939; -.
DR Ensembl; ENST00000406576.7; ENSP00000385292.3; ENSG00000144895.12. [Q9BY44-4]
DR Ensembl; ENST00000460851.6; ENSP00000417229.1; ENSG00000144895.12. [Q9BY44-1]
DR Ensembl; ENST00000487799.5; ENSP00000420537.1; ENSG00000144895.12. [Q9BY44-3]
DR GeneID; 83939; -.
DR KEGG; hsa:83939; -.
DR MANE-Select; ENST00000460851.6; ENSP00000417229.1; NM_032025.5; NP_114414.2.
DR UCSC; uc003eya.4; human. [Q9BY44-1]
DR CTD; 83939; -.
DR DisGeNET; 83939; -.
DR GeneCards; EIF2A; -.
DR HGNC; HGNC:3254; EIF2A.
DR HPA; ENSG00000144895; Low tissue specificity.
DR MIM; 609234; gene.
DR neXtProt; NX_Q9BY44; -.
DR OpenTargets; ENSG00000144895; -.
DR PharmGKB; PA143485453; -.
DR VEuPathDB; HostDB:ENSG00000144895; -.
DR eggNOG; KOG2315; Eukaryota.
DR GeneTree; ENSGT00730000111053; -.
DR HOGENOM; CLU_013809_1_0_1; -.
DR InParanoid; Q9BY44; -.
DR OMA; LITWQRP; -.
DR OrthoDB; 464990at2759; -.
DR PhylomeDB; Q9BY44; -.
DR TreeFam; TF105866; -.
DR PathwayCommons; Q9BY44; -.
DR SignaLink; Q9BY44; -.
DR SIGNOR; Q9BY44; -.
DR BioGRID-ORCS; 83939; 21 hits in 1074 CRISPR screens.
DR ChiTaRS; EIF2A; human.
DR GeneWiki; EIF2A; -.
DR GenomeRNAi; 83939; -.
DR Pharos; Q9BY44; Tbio.
DR PRO; PR:Q9BY44; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9BY44; protein.
DR Bgee; ENSG00000144895; Expressed in secondary oocyte and 185 other tissues.
DR ExpressionAtlas; Q9BY44; baseline and differential.
DR Genevisible; Q9BY44; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0005850; C:eukaryotic translation initiation factor 2 complex; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; IMP:UniProtKB.
DR GO; GO:0003743; F:translation initiation factor activity; IMP:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; IMP:UniProtKB.
DR GO; GO:0009967; P:positive regulation of signal transduction; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
DR GO; GO:0006417; P:regulation of translation; IMP:UniProtKB.
DR GO; GO:1990928; P:response to amino acid starvation; IEA:Ensembl.
DR GO; GO:0042255; P:ribosome assembly; IMP:UniProtKB.
DR GO; GO:0032933; P:SREBP signaling pathway; IEA:Ensembl.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR011387; TIF2A.
DR InterPro; IPR013979; TIF_beta_prop-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR13227; PTHR13227; 1.
DR Pfam; PF08662; eIF2A; 1.
DR PIRSF; PIRSF017222; eIF2A; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Direct protein sequencing;
KW Initiation factor; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; Repeat; Translation regulation; WD repeat.
FT CHAIN 1..585
FT /note="Eukaryotic translation initiation factor 2A"
FT /id="PRO_0000424466"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000269|Ref.8"
FT CHAIN 2..585
FT /note="Eukaryotic translation initiation factor 2A, N-
FT terminally processed"
FT /id="PRO_0000286076"
FT REPEAT 56..100
FT /note="WD 1"
FT REPEAT 101..159
FT /note="WD 2"
FT REPEAT 160..210
FT /note="WD 3"
FT REPEAT 211..264
FT /note="WD 4"
FT REPEAT 265..306
FT /note="WD 5"
FT REPEAT 307..348
FT /note="WD 6"
FT REPEAT 349..391
FT /note="WD 7"
FT REGION 434..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 531..582
FT /evidence="ECO:0000255"
FT COMPBIAS 515..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 2
FT /note="N-acetylalanine; in Eukaryotic translation
FT initiation factor 2A, N-terminally processed"
FT /evidence="ECO:0000269|Ref.8"
FT MOD_RES 5
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES 506
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 518
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 526
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..213
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_024975"
FT VAR_SEQ 34..58
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056047"
FT VAR_SEQ 98..158
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056048"
FT VAR_SEQ 214..219
FT /note="ANKSFF -> MFQEV (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_024976"
FT VARIANT 97
FT /note="T -> S (in dbSNP:rs1132979)"
FT /evidence="ECO:0000269|PubMed:12133843,
FT ECO:0000269|PubMed:14702039, ECO:0000269|Ref.3,
FT ECO:0000269|Ref.4, ECO:0000269|Ref.6"
FT /id="VAR_032066"
FT VARIANT 582
FT /note="E -> K (in dbSNP:rs17850813)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_032067"
FT CONFLICT 7
FT /note="L -> F (in Ref. 4; AAQ13612)"
FT /evidence="ECO:0000305"
FT CONFLICT 14..16
FT /note="EGL -> LRT (in Ref. 4; AAQ13612)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="G -> A (in Ref. 1; AAM83402)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="N -> I (in Ref. 1; AAM83402)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="S -> P (in Ref. 2; BAB55058)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="V -> A (in Ref. 4; AAQ13612)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="F -> S (in Ref. 4; AAQ13612)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="T -> P (in Ref. 1; AAM83402)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="G -> F (in Ref. 1; AAM83402)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="V -> L (in Ref. 1; AAM83402)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="Y -> S (in Ref. 1; AAM83402)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 585 AA; 64990 MW; 63D63C0676F232C9 CRC64;
MAPSTPLLTV RGSEGLYMVN GPPHFTESTV FPRESGKNCK VCIFSKDGTL FAWGNGEKVN
IISVTNKGLL HSFDLLKAVC LEFSPKNTVL ATWQPYTTSK DGTAGIPNLQ LYDVKTGTCL
KSFIQKKMQN WCPSWSEDET LCARNVNNEV HFFENNNFNT IANKLHLQKI NDFVLSPGPQ
PYKVAVYVPG SKGAPSFVRL YQYPNFAGPH AALANKSFFK ADKVTMLWNK KATAVLVIAS
TDVDKTGASY YGEQTLHYIA TNGESAVVQL PKNGPIYDVV WNSSSTEFCA VYGFMPAKAT
IFNLKCDPVF DFGTGPRNAA YYSPHGHILV LAGFGNLRGQ MEVWDVKNYK LISKPVASDS
TYFAWCPDGE HILTATCAPR LRVNNGYKIW HYTGSILHKY DVPSNAELWQ VSWQPFLDGI
FPAKTITYQA VPSEVPNEEP KVATAYRPPA LRNKPITNSK LHEEEPPQNM KPQSGNDKPL
SKTALKNQRK HEAKKAAKQE ARSDKSPDLA PTPAPQSTPR NTVSQSISGD PEIDKKIKNL
KKKLKAIEQL KEQAATGKQL EKNQLEKIQK ETALLQELED LELGI
