IF2B_HUMAN
ID IF2B_HUMAN Reviewed; 333 AA.
AC P20042; Q9BVU0; Q9UJE4;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=Eukaryotic translation initiation factor 2 subunit 2;
DE AltName: Full=Eukaryotic translation initiation factor 2 subunit beta;
DE Short=eIF-2-beta;
GN Name=EIF2S2; Synonyms=EIF2B;
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].
RX PubMed=3044606; DOI=10.1016/s0092-8674(88)80007-2;
RA Pathak V.K., Nielsen P.J., Trachsel H., Hershey J.W.B.;
RT "Structure of the beta subunit of translational initiation factor eIF-2.";
RL Cell 54:633-639(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-177.
RC TISSUE=Lung, and Placenta;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY MASS
RP 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 [5]
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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105 AND THR-111, AND
RP IDENTIFICATION BY 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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-265 AND LYS-293, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-67 AND SER-158, 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 [10]
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 [11]
RP INTERACTION WITH BZW2/5MP1 AND EIF5.
RX PubMed=21745818; DOI=10.1093/nar/gkr339;
RA Singh C.R., Watanabe R., Zhou D., Jennings M.D., Fukao A., Lee B.,
RA Ikeda Y., Chiorini J.A., Campbell S.G., Ashe M.P., Fujiwara T., Wek R.C.,
RA Pavitt G.D., Asano K.;
RT "Mechanisms of translational regulation by a human eIF5-mimic protein.";
RL Nucleic Acids Res. 39:8314-8328(2011).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-2; SER-67; SER-105 AND THR-111, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [13]
RP SUBUNIT.
RX PubMed=23063529; DOI=10.1016/j.molcel.2012.09.005;
RA Borck G., Shin B.S., Stiller B., Mimouni-Bloch A., Thiele H., Kim J.R.,
RA Thakur M., Skinner C., Aschenbach L., Smirin-Yosef P., Har-Zahav A.,
RA Nuernberg G., Altmueller J., Frommolt P., Hofmann K., Konen O.,
RA Nuernberg P., Munnich A., Schwartz C.E., Gothelf D., Colleaux L.,
RA Dever T.E., Kubisch C., Basel-Vanagaite L.;
RT "eIF2gamma mutation that disrupts eIF2 complex integrity links intellectual
RT disability to impaired translation initiation.";
RL Mol. Cell 48:641-646(2012).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-13; THR-31; THR-36;
RP SER-67; SER-105 AND THR-111, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP 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 [16]
RP IDENTIFICATION BY 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).
RN [17]
RP INTERACTION WITH BZW2/5MP1.
RX PubMed=25147208; DOI=10.1093/nar/gku670;
RA Hiraishi H., Oatman J., Haller S.L., Blunk L., McGivern B., Morris J.,
RA Papadopoulos E., Gutierrez W., Gordon M., Bokhari W., Ikeda Y., Miles D.,
RA Fellers J., Asano M., Wagner G., Tazi L., Rothenburg S., Brown S.J.,
RA Asano K.;
RT "Essential role of eIF5-mimic protein in animal development is linked to
RT control of ATF4 expression.";
RL Nucleic Acids Res. 42:10321-10330(2014).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-102, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [20]
RP INTERACTION WITH BZW2/5MP1.
RX PubMed=34260931; DOI=10.1016/j.celrep.2021.109376;
RA Singh C.R., Glineburg M.R., Moore C., Tani N., Jaiswal R., Zou Y., Aube E.,
RA Gillaspie S., Thornton M., Cecil A., Hilgers M., Takasu A., Asano I.,
RA Asano M., Escalante C.R., Nakamura A., Todd P.K., Asano K.;
RT "Human oncoprotein 5MP suppresses general and repeat-associated non-AUG
RT translation via eIF3 by a common mechanism.";
RL Cell Rep. 36:109376-109376(2021).
CC -!- FUNCTION: eIF-2 functions in the early steps of protein synthesis by
CC forming a ternary complex with GTP and initiator tRNA. This complex
CC binds to a 40S ribosomal subunit, followed by mRNA binding to form a
CC 43S preinitiation complex. Junction of the 60S ribosomal subunit to
CC form the 80S initiation complex is preceded by hydrolysis of the GTP
CC bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for
CC eIF-2 to recycle and catalyze another round of initiation, the GDP
CC bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by
CC eIF-2B.
CC -!- SUBUNIT: Heterotrimer composed of an alpha, a beta and a gamma chain
CC (PubMed:23063529). Component of an EIF2 complex at least composed of
CC CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5 (By
CC similarity). Interacts with BZW2/5MP1 (PubMed:21745818,
CC PubMed:25147208, PubMed:34260931). Interacts with EIF5
CC (PubMed:21745818). {ECO:0000250|UniProtKB:Q99L45,
CC ECO:0000269|PubMed:21745818, ECO:0000269|PubMed:23063529,
CC ECO:0000269|PubMed:34260931}.
CC -!- INTERACTION:
CC P20042; P05067: APP; NbExp=6; IntAct=EBI-711977, EBI-77613;
CC P20042; P54253: ATXN1; NbExp=3; IntAct=EBI-711977, EBI-930964;
CC P20042; Q9Y6E2: BZW2; NbExp=2; IntAct=EBI-711977, EBI-1051021;
CC P20042; P43681: CHRNA4; NbExp=3; IntAct=EBI-711977, EBI-7132379;
CC P20042; P05198: EIF2S1; NbExp=7; IntAct=EBI-711977, EBI-1056162;
CC P20042; P41091: EIF2S3; NbExp=4; IntAct=EBI-711977, EBI-1054228;
CC P20042; P78344: EIF4G2; NbExp=4; IntAct=EBI-711977, EBI-296519;
CC P20042; P42858: HTT; NbExp=12; IntAct=EBI-711977, EBI-466029;
CC P20042; P05412: JUN; NbExp=4; IntAct=EBI-711977, EBI-852823;
CC P20042; Q92993: KAT5; NbExp=3; IntAct=EBI-711977, EBI-399080;
CC P20042; Q99683: MAP3K5; NbExp=3; IntAct=EBI-711977, EBI-476263;
CC P20042; P19404: NDUFV2; NbExp=3; IntAct=EBI-711977, EBI-713665;
CC P20042; P01138: NGF; NbExp=3; IntAct=EBI-711977, EBI-1028250;
CC P20042; D3DTS7: PMP22; NbExp=3; IntAct=EBI-711977, EBI-25882629;
CC P20042; P20340-2: RAB6A; NbExp=3; IntAct=EBI-711977, EBI-8840191;
CC P20042; Q92673: SORL1; NbExp=3; IntAct=EBI-711977, EBI-1171329;
CC -!- SIMILARITY: Belongs to the eIF-2-beta/eIF-5 family. {ECO:0000305}.
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DR EMBL; M29536; AAA52383.1; -; mRNA.
DR EMBL; AL031668; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000461; AAH00461.1; -; mRNA.
DR EMBL; BC000934; AAH00934.1; -; mRNA.
DR CCDS; CCDS13231.1; -.
DR PIR; A31226; A31226.
DR RefSeq; NP_003899.2; NM_003908.4.
DR PDB; 6K71; EM; 4.30 A; M=1-333.
DR PDB; 6K72; EM; 4.60 A; M=1-333.
DR PDB; 6YBV; EM; 3.80 A; s=1-333.
DR PDB; 6ZMW; EM; 3.70 A; s=1-333.
DR PDB; 6ZP4; EM; 2.90 A; 4=1-333.
DR PDB; 7A09; EM; 3.50 A; 4=1-333.
DR PDB; 7D43; EM; 4.30 A; M=1-333.
DR PDBsum; 6K71; -.
DR PDBsum; 6K72; -.
DR PDBsum; 6YBV; -.
DR PDBsum; 6ZMW; -.
DR PDBsum; 6ZP4; -.
DR PDBsum; 7A09; -.
DR PDBsum; 7D43; -.
DR AlphaFoldDB; P20042; -.
DR SMR; P20042; -.
DR BioGRID; 114411; 156.
DR CORUM; P20042; -.
DR IntAct; P20042; 67.
DR MINT; P20042; -.
DR STRING; 9606.ENSP00000364119; -.
DR GlyGen; P20042; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P20042; -.
DR MetOSite; P20042; -.
DR PhosphoSitePlus; P20042; -.
DR SwissPalm; P20042; -.
DR BioMuta; EIF2S2; -.
DR DMDM; 12644154; -.
DR EPD; P20042; -.
DR jPOST; P20042; -.
DR MassIVE; P20042; -.
DR PaxDb; P20042; -.
DR PeptideAtlas; P20042; -.
DR PRIDE; P20042; -.
DR ProteomicsDB; 53718; -.
DR TopDownProteomics; P20042; -.
DR Antibodypedia; 25771; 347 antibodies from 31 providers.
DR DNASU; 8894; -.
DR Ensembl; ENST00000374980.3; ENSP00000364119.2; ENSG00000125977.7.
DR GeneID; 8894; -.
DR KEGG; hsa:8894; -.
DR MANE-Select; ENST00000374980.3; ENSP00000364119.2; NM_003908.5; NP_003899.2.
DR CTD; 8894; -.
DR DisGeNET; 8894; -.
DR GeneCards; EIF2S2; -.
DR HGNC; HGNC:3266; EIF2S2.
DR HPA; ENSG00000125977; Low tissue specificity.
DR MIM; 603908; gene.
DR neXtProt; NX_P20042; -.
DR OpenTargets; ENSG00000125977; -.
DR PharmGKB; PA27696; -.
DR VEuPathDB; HostDB:ENSG00000125977; -.
DR eggNOG; KOG2768; Eukaryota.
DR GeneTree; ENSGT00390000001804; -.
DR HOGENOM; CLU_026663_0_1_1; -.
DR InParanoid; P20042; -.
DR OMA; CMREGNK; -.
DR OrthoDB; 1178655at2759; -.
DR PhylomeDB; P20042; -.
DR TreeFam; TF101503; -.
DR BRENDA; 3.6.5.3; 2681.
DR PathwayCommons; P20042; -.
DR Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-HSA-381042; PERK regulates gene expression.
DR Reactome; R-HSA-382556; ABC-family proteins mediated transport.
DR Reactome; R-HSA-72649; Translation initiation complex formation.
DR Reactome; R-HSA-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-HSA-72731; Recycling of eIF2:GDP.
DR Reactome; R-HSA-9633012; Response of EIF2AK4 (GCN2) to amino acid deficiency.
DR Reactome; R-HSA-9648895; Response of EIF2AK1 (HRI) to heme deficiency.
DR SignaLink; P20042; -.
DR SIGNOR; P20042; -.
DR BioGRID-ORCS; 8894; 614 hits in 1027 CRISPR screens.
DR ChiTaRS; EIF2S2; human.
DR GeneWiki; EIF2S2; -.
DR GenomeRNAi; 8894; -.
DR Pharos; P20042; Tbio.
DR PRO; PR:P20042; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; P20042; protein.
DR Bgee; ENSG00000125977; Expressed in cartilage tissue and 214 other tissues.
DR ExpressionAtlas; P20042; baseline and differential.
DR Genevisible; P20042; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005850; C:eukaryotic translation initiation factor 2 complex; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0008135; F:translation factor activity, RNA binding; TAS:ProtInc.
DR GO; GO:0003743; F:translation initiation factor activity; IDA:UniProtKB.
DR GO; GO:0031369; F:translation initiation factor binding; IBA:GO_Central.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IBA:GO_Central.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IBA:GO_Central.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0002176; P:male germ cell proliferation; IEA:Ensembl.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR InterPro; IPR045196; IF2/IF5.
DR InterPro; IPR002735; Transl_init_fac_IF2/IF5_dom.
DR InterPro; IPR016189; Transl_init_fac_IF2/IF5_N.
DR InterPro; IPR016190; Transl_init_fac_IF2/IF5_Zn-bd.
DR PANTHER; PTHR23001; PTHR23001; 1.
DR Pfam; PF01873; eIF-5_eIF-2B; 1.
DR SMART; SM00653; eIF2B_5; 1.
DR SUPFAM; SSF100966; SSF100966; 1.
DR SUPFAM; SSF75689; SSF75689; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Initiation factor; Isopeptide bond;
KW Metal-binding; Phosphoprotein; Protein biosynthesis; Reference proteome;
KW Ubl conjugation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895"
FT CHAIN 2..333
FT /note="Eukaryotic translation initiation factor 2 subunit
FT 2"
FT /id="PRO_0000137406"
FT ZN_FING 281..305
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT REGION 1..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 31
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 36
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 111
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41035"
FT MOD_RES 265
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 293
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 102
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 177
FT /note="E -> D (in dbSNP:rs17856024)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_048909"
FT CONFLICT 295
FT /note="T -> I (in Ref. 1; AAA52383)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 333 AA; 38388 MW; 3E9FD4B48AA61A51 CRC64;
MSGDEMIFDP TMSKKKKKKK KPFMLDEEGD TQTEETQPSE TKEVEPEPTE DKDLEADEED
TRKKDASDDL DDLNFFNQKK KKKKTKKIFD IDEAEEGVKD LKIESDVQEP TEPEDDLDIM
LGNKKKKKKN VKFPDEDEIL EKDEALEDED NKKDDGISFS NQTGPAWAGS ERDYTYEELL
NRVFNIMREK NPDMVAGEKR KFVMKPPQVV RVGTKKTSFV NFTDICKLLH RQPKHLLAFL
LAELGTSGSI DGNNQLVIKG RFQQKQIENV LRRYIKEYVT CHTCRSPDTI LQKDTRLYFL
QCETCHSRCS VASIKTGFQA VTGKRAQLRA KAN
