ID EI2BB_HUMAN Reviewed; 351 AA. AC P49770; O43201; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 3. DT 04-NOV-2026, entry version 206. DE RecName: Full=Translation initiation factor eIF2B subunit beta; DE AltName: Full=S20I15; DE AltName: Full=S20III15; DE AltName: Full=eIF2B GDP-GTP exchange factor subunit beta; GN Name=EIF2B2; Synonyms=EIF2BB; 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 [LARGE SCALE MRNA]. RC TISSUE=Brain; RA Yu W., Sarginson J., Gibbs R.A.; RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX PubMed=7596406; DOI=10.1038/375754a0; RA Sherrington R., Rogaev E.I., Liang Y., Rogaeva E.A., Levesque G., Ikeda M., RA Chi H., Lin C., Li G., Holman K., Tsuda T., Mar L., Foncin J.-F., RA Bruni A.C., Montesi M.P., Sorbi S., Rainero I., Pinessi L., Nee L., RA Chumakov I., Pollen D., Brookes A., Sanseau P., Polinsky R.J., Wasco W., RA da Silva H.A.R., Haines J.L., Pericak-Vance M.A., Tanzi R.E., Roses A.D., RA Fraser P.E., Rommens J.M., St George-Hyslop P.H.; RT "Cloning of a gene bearing missense mutations in early-onset familial RT Alzheimer's disease."; RL Nature 375:754-760(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12508121; DOI=10.1038/nature01348; RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., RA Waterston R., Hood L., Weissenbach J.; RT "The DNA sequence and analysis of human chromosome 14."; RL Nature 421:601-607(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung; 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 [5] 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 [6] RP IDENTIFICATION BY MASS 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 [7] RP FUNCTION, ACTIVITY REGULATION, IDENTIFICATION BY MASS SPECTROMETRY, AND RP IDENTIFICATION IN THE EIF2B COMPLEX. RX PubMed=25858979; DOI=10.1126/science.aaa6986; RA Sekine Y., Zyryanova A., Crespillo-Casado A., Fischer P.M., Harding H.P., RA Ron D.; RT "Stress responses. Mutations in a translation initiation factor identify RT the target of a memory-enhancing compound."; RL Science 348:1027-1030(2015). RN [8] RP FUNCTION, AND IDENTIFICATION IN THE EIF2B COMPLEX. RX PubMed=27023709; DOI=10.1007/s10969-016-9203-3; RA Kashiwagi K., Shigeta T., Imataka H., Ito T., Yokoyama S.; RT "Expression, purification, and crystallization of Schizosaccharomyces pombe RT eIF2B."; RL J. Struct. Funct. Genomics 17:33-38(2016). RN [9] {ECO:0007744|PDB:6K71, ECO:0007744|PDB:6K72} RP STRUCTURE BY ELECTRON MICROSCOPY IN COMPLEX WITH THE EIF2 COMPLEX, RP FUNCTION, SUBUNIT, AND IDENTIFICATION IN THE EIF2B COMPLEX. RX PubMed=31048492; DOI=10.1126/science.aaw4104; RA Kashiwagi K., Yokoyama T., Nishimoto M., Takahashi M., Sakamoto A., RA Yonemochi M., Shirouzu M., Ito T.; RT "Structural basis for eIF2B inhibition in integrated stress response."; RL Science 364:495-499(2019). RN [10] RP VARIANTS VWM2 GLY-213; ARG-273; ASP-316 AND VAL-329. RX PubMed=11704758; DOI=10.1038/ng764; RA Leegwater P.A.J., Vermeulen G., Koenst A.A.M., Naidu S., Mulders J., RA Visser A., Kersbergen P., Mobach D., Fonds D., van Berkel C.G.M., RA Lemmers R.J.L.F., Frants R.R., Oudejans C.B.M., Schutgens R.B.H., RA Pronk J.C., van der Knaap M.S.; RT "Subunits of the translation initiation factor eIF2B are mutant in RT leukoencephalopathy with vanishing white matter."; RL Nat. Genet. 29:383-388(2001). RN [11] RP VARIANTS VWM2 PHE-171 AND GLY-213. RX PubMed=12707859; DOI=10.1086/375404; RA Fogli A., Rodriguez D., Eymard-Pierre E., Bouhour F., Labauge P., RA Meaney B.F., Zeesman S., Kaneski C.R., Schiffmann R., Boespflug-Tanguy O.; RT "Ovarian failure related to eukaryotic initiation factor 2B mutations."; RL Am. J. Hum. Genet. 72:1544-1550(2003). RN [12] RP VARIANTS VWM2 PHE-171; SER-196; VAL-200 AND GLY-213. RX PubMed=15776425; DOI=10.1002/humu.9325; RA Ohlenbusch A., Henneke M., Brockmann K., Goerg M., Hanefeld F., RA Kohlschutter A., Gartner J.; RT "Identification of ten novel mutations in patients with eIF2B-related RT disorders."; RL Hum. Mutat. 25:411-411(2005). RN [13] RP VARIANT VWM2 GLU-85. RX PubMed=21484434; DOI=10.1007/s10048-011-0284-7; RA Matsukawa T., Wang X., Liu R., Wortham N.C., Onuki Y., Kubota A., Hida A., RA Kowa H., Fukuda Y., Ishiura H., Mitsui J., Takahashi Y., Aoki S., RA Takizawa S., Shimizu J., Goto J., Proud C.G., Tsuji S.; RT "Adult-onset leukoencephalopathies with vanishing white matter with novel RT missense mutations in EIF2B2, EIF2B3, and EIF2B5."; RL Neurogenetics 12:259-261(2011). RN [14] RP VARIANT VWM2 TYR-268. RX PubMed=22285377; DOI=10.1016/j.gene.2011.12.047; RA Alsalem A., Shaheen R., Alkuraya F.S.; RT "Vanishing white matter disease caused by EIF2B2 mutation with the RT presentation of an adrenoleukodystrophy phenotype."; RL Gene 496:141-143(2012). RN [15] RP VARIANT VWM2 GLY-213. RX PubMed=22729508; DOI=10.1007/s10072-012-1129-3; RA Sambati L., Agati R., Bacci A., Bianchi S., Capellari S.; RT "Vanishing white matter disease: an Italian case with A638G mutation in RT exon 5 of EIF2B2 gene, an unusual early onset and a long course."; RL Neurol. Sci. 34:1235-1238(2013). RN [16] RP VARIANT VAL-127. RX PubMed=26740508; DOI=10.1136/jmedgenet-2015-103568; RA Lopes F., Barbosa M., Ameur A., Soares G., de Sa J., Dias A.I., RA Oliveira G., Cabral P., Temudo T., Calado E., Cruz I.F., Vieira J.P., RA Oliveira R., Esteves S., Sauer S., Jonasson I., Syvaenen A.C., RA Gyllensten U., Pinto D., Maciel P.; RT "Identification of novel genetic causes of Rett syndrome-like phenotypes."; RL J. Med. Genet. 53:190-199(2016). CC -!- FUNCTION: Acts as a component of the translation initiation factor 2B CC (eIF2B) complex, which catalyzes the exchange of GDP for GTP on CC eukaryotic initiation factor 2 (eIF2) gamma subunit (PubMed:25858979, CC PubMed:27023709, PubMed:31048492). Its guanine nucleotide exchange CC factor activity is repressed when bound to eIF2 complex phosphorylated CC on the alpha subunit, thereby limiting the amount of methionyl- CC initiator methionine tRNA available to the ribosome and consequently CC global translation is repressed (PubMed:25858979, PubMed:31048492). CC {ECO:0000269|PubMed:25858979, ECO:0000269|PubMed:27023709, CC ECO:0000269|PubMed:31048492}. CC -!- ACTIVITY REGULATION: Activated by the chemical integrated stress CC response (ISR) inhibitor ISRIB which stimulates guanine nucleotide CC exchange factor activity for both phosphorylated and unphosphorylated CC eIF2. {ECO:0000269|PubMed:25858979}. CC -!- SUBUNIT: Component of the translation initiation factor 2B (eIF2B) CC complex which is a heterodecamer of two sets of five different CC subunits: alpha, beta, gamma, delta and epsilon. Subunits alpha, beta CC and delta comprise a regulatory subcomplex and subunits epsilon and CC gamma comprise a catalytic subcomplex (PubMed:25858979, CC PubMed:27023709, PubMed:31048492). Within the complex, the hexameric CC regulatory complex resides at the center, with the two heterodimeric CC catalytic subcomplexes bound on opposite sides (PubMed:31048492). CC {ECO:0000269|PubMed:25858979, ECO:0000269|PubMed:27023709, CC ECO:0000269|PubMed:31048492}. CC -!- INTERACTION: CC P49770; Q96LT7: C9orf72; NbExp=6; IntAct=EBI-718773, EBI-2961725; CC P49770; Q9UI10: EIF2B4; NbExp=12; IntAct=EBI-718773, EBI-2340132; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:Q9UT76}. CC -!- DISEASE: Leukoencephalopathy with vanishing white matter 2 (VWM2) CC [MIM:620312]: An autosomal recessive brain disease characterized by CC neurological features including progressive cerebellar ataxia, CC spasticity, and cognitive deficits. Brain imaging shows abnormal white CC matter that vanishes over time and is replaced by cerebrospinal fluid. CC Disease severity ranges from fatal infantile forms to adult forms CC without neurological deterioration. The disease is progressive with, in CC most individuals, additional episodes of rapid deterioration following CC febrile infections or minor head trauma. Death may occurs after a CC variable period after disease onset, usually following an episode of CC fever and coma. A subset of affected females with milder forms of the CC disease who survive to adolescence exhibit ovarian dysfunction. This CC variant of the disorder is called ovarioleukodystrophy. CC {ECO:0000269|PubMed:11704758, ECO:0000269|PubMed:12707859, CC ECO:0000269|PubMed:15776425, ECO:0000269|PubMed:21484434, CC ECO:0000269|PubMed:22285377, ECO:0000269|PubMed:22729508}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC42002.1; Type=Frameshift; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Mendelian genes eukaryotic translation initiation CC factor 2B, subunit 2 beta, 39kDa (EIF2B2); Note=Leiden Open Variation CC Database (LOVD); CC URL="https://databases.lovd.nl/shared/genes/EIF2B2"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF035280; AAB88176.1; -; mRNA. DR EMBL; L40395; AAC42002.1; ALT_FRAME; mRNA. DR EMBL; AC006530; AAD30183.1; -; Genomic_DNA. DR EMBL; BC011750; AAH11750.1; -; mRNA. DR CCDS; CCDS9836.1; -. DR RefSeq; NP_055054.1; NM_014239.4. DR PDB; 12FH; X-ray; 3.50 A; C/D=1-351. DR PDB; 6CAJ; EM; 2.80 A; C/D=2-351. DR PDB; 6EZO; EM; 4.10 A; C/D=5-351. DR PDB; 6K71; EM; 4.30 A; C/D=1-351. DR PDB; 6K72; EM; 4.60 A; C/D=1-351. DR PDB; 6O81; EM; 3.21 A; C/D=2-351. DR PDB; 6O85; EM; 3.03 A; C/D=2-351. DR PDB; 6O9Z; EM; 3.03 A; C/D=2-351. DR PDB; 7D43; EM; 4.30 A; C/D=1-351. DR PDB; 7D44; EM; 4.00 A; C/D=1-351. DR PDB; 7D45; EM; 3.80 A; C/D=1-351. DR PDB; 7D46; EM; 4.00 A; C/D=1-351. DR PDB; 7F64; EM; 2.42 A; C/D=1-351. DR PDB; 7F66; EM; 2.76 A; C/D=1-351. DR PDB; 7F67; EM; 3.59 A; C/D=1-351. DR PDB; 7KMF; EM; 2.91 A; C/D=1-351. DR PDB; 7L70; EM; 2.80 A; C/D=2-351. DR PDB; 7L7G; EM; 3.00 A; C/D=2-351. DR PDB; 7RLO; EM; 2.60 A; C/D=1-351. DR PDB; 7TRJ; EM; 2.80 A; C/D=1-351. DR PDB; 7VLK; EM; 2.27 A; C/D=1-351. DR PDB; 8TQO; EM; 3.10 A; D=2-351. DR PDB; 8TQZ; EM; 2.90 A; C/D=2-351. DR PDB; 9HVD; EM; 3.04 A; C/D=1-351. DR PDB; 9HVE; EM; 2.70 A; C/D=1-351. DR PDB; 9QC6; EM; 2.83 A; C/D=1-351. DR PDB; 9Y3P; EM; 2.90 A; C/D=8-351. DR PDB; 9Y3Q; EM; 3.30 A; C/D=2-351. DR PDB; 9Y3T; EM; 2.50 A; C/D=2-351. DR PDB; 9Y3U; EM; 2.40 A; C/D=2-99, C/D=115-351. DR PDB; 9Y3V; EM; 2.90 A; C/D=2-351. DR PDB; 9Y4B; EM; 2.10 A; C/D=2-99, C/D=115-351. DR PDB; 9Y4W; EM; 2.40 A; C/D=2-99, C/D=115-351. DR PDB; 9Y5R; EM; 3.01 A; C/D=2-351. DR PDB; 9Y5S; EM; 3.10 A; C/D=2-351. DR PDB; 9Y5T; EM; 2.78 A; C/D=2-99, C/D=115-351. DR PDB; 9Y5U; EM; 2.90 A; C/D=2-99, C/D=115-351. DR PDB; 9ZUZ; X-ray; 2.25 A; B=1-351. DR AlphaFoldDB; P49770; -. DR EMDB; EMD-0649; -. DR EMDB; EMD-0651; -. DR EMDB; EMD-0664; -. DR EMDB; EMD-22924; -. DR EMDB; EMD-23209; -. DR EMDB; EMD-24535; -. DR EMDB; EMD-26098; -. DR EMDB; EMD-30568; -. DR EMDB; EMD-30569; -. DR EMDB; EMD-30570; -. DR EMDB; EMD-30571; -. DR EMDB; EMD-31472; -. DR EMDB; EMD-31474; -. DR EMDB; EMD-31475; -. DR EMDB; EMD-32023; -. DR EMDB; EMD-41510; -. DR EMDB; EMD-41566; -. DR EMDB; EMD-4162; -. DR EMDB; EMD-52432; -. DR EMDB; EMD-52433; -. DR EMDB; EMD-53004; -. DR EMDB; EMD-72462; -. DR EMDB; EMD-72463; -. DR EMDB; EMD-72466; -. DR EMDB; EMD-72467; -. DR EMDB; EMD-72468; -. DR EMDB; EMD-72477; -. DR EMDB; EMD-72499; -. DR EMDB; EMD-7442; -. DR EMDB; EMD-9840; -. DR EMDB; EMD-9841; -. DR EMDB; EMD-9842; -. DR SMR; P49770; -. DR BioGRID; 114409; 149. DR ComplexPortal; CPX-8343; Eukaryotic translation initiation factor 2B complex. DR CORUM; P49770; -. DR FunCoup; P49770; 2208. DR IntAct; P49770; 97. DR NDEx; IQUERY-CP-EIF2B2; 3 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000266126; -. DR BindingDB; P49770; -. DR ChEMBL; CHEMBL6067331; -. DR DrugBank; DB05992; Plinabulin. DR iPTMnet; P49770; -. DR PhosphoSitePlus; P49770; -. DR SwissPalm; P49770; -. DR BioMuta; EIF2B2; -. DR DMDM; 6226858; -. DR jPOST; P49770; -. DR MassIVE; P49770; -. DR PaxDb; 9606-ENSP00000266126; -. DR PeptideAtlas; P49770; -. DR ProteomicsDB; 56113; -. DR Pumba; P49770; -. DR Antibodypedia; 57; 206 antibodies from 32 providers. DR DNASU; 8892; -. DR Ensembl; ENST00000266126.10; ENSP00000266126.5; ENSG00000119718.12. DR GeneID; 8892; -. DR KEGG; hsa:8892; -. DR MANE-Select; ENST00000266126.10; ENSP00000266126.5; NM_014239.4; NP_055054.1. DR AGR; HGNC:3258; -. DR ClinPGx; PA27689; -. DR CTD; 8892; -. DR DisGeNET; 8892; -. DR GeneCards; EIF2B2; -. DR GeneReviews; EIF2B2; -. DR HGNC; HGNC:3258; EIF2B2. DR HPA; ENSG00000119718; Low tissue specificity. DR MalaCards; EIF2B2; -. DR MIM; 606454; gene. DR MIM; 620312; phenotype. DR OpenTargets; ENSG00000119718; -. DR Orphanet; 157713; Congenital or early infantile CACH syndrome. DR Orphanet; 99854; Cree leukoencephalopathy. DR Orphanet; 157719; Juvenile or adult CACH syndrome. DR Orphanet; 157716; Late infantile CACH syndrome. DR Orphanet; 99853; Ovarioleukodystrophy. DR VEuPathDB; HostDB:ENSG00000119718; -. DR eggNOG; KOG1465; Eukaryota. DR GeneTree; ENSGT00550000074908; -. DR HOGENOM; CLU_016218_4_3_1; -. DR InParanoid; P49770; -. DR OMA; AAEYHSV; -. DR OrthoDB; 269919at2759; -. DR PAN-GO; P49770; 3 GO annotations based on evolutionary models. DR PhylomeDB; P49770; -. DR PathwayCommons; P49770; -. DR Reactome; R-HSA-72731; Recycling of eIF2:GDP. DR SignaLink; P49770; -. DR SIGNOR; P49770; -. DR Agora; ENSG00000119718; -. DR BioGRID-ORCS; 8892; 844 hits in 1176 CRISPR screens. DR ChiTaRS; EIF2B2; human. DR GeneWiki; EIF2B2; -. DR GenomeRNAi; 8892; -. DR Pharos; P49770; Tbio. DR PRO; PR:P49770; -. DR Proteomes; UP000005640; Chromosome 14. DR RNAct; P49770; protein. DR Bgee; ENSG00000119718; Expressed in left lobe of thyroid gland and 209 other cell types or tissues. DR ExpressionAtlas; P49770; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005851; C:eukaryotic translation initiation factor 2B complex; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB. DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB. DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB. DR GO; GO:0007417; P:central nervous system development; IMP:UniProtKB. DR GO; GO:0002183; P:cytoplasmic translational initiation; IDA:UniProtKB. DR GO; GO:0042552; P:myelination; IMP:UniProtKB. DR GO; GO:0014003; P:oligodendrocyte development; IMP:UniProtKB. DR GO; GO:0001541; P:ovarian follicle development; IMP:UniProtKB. DR GO; GO:0045948; P:positive regulation of translational initiation; IDA:ComplexPortal. DR GO; GO:0006446; P:regulation of translational initiation; TAS:UniProtKB. DR GO; GO:0009749; P:response to glucose; ISS:UniProtKB. DR GO; GO:0009408; P:response to heat; ISS:UniProtKB. DR GO; GO:0043434; P:response to peptide hormone; ISS:UniProtKB. DR GO; GO:0050852; P:T cell receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0006413; P:translational initiation; IDA:UniProtKB. DR FunFam; 3.40.50.10470:FF:000004; Translation initiation factor eIF-2B subunit beta; 1. DR Gene3D; 3.40.50.10470; Translation initiation factor eif-2b, domain 2; 1. DR InterPro; IPR051855; eIF2B_beta_subunit. DR InterPro; IPR000649; IF-2B-related. DR InterPro; IPR042529; IF_2B-like_C. DR InterPro; IPR037171; NagB/RpiA_transferase-like. DR PANTHER; PTHR45859; TRANSLATION INITIATION FACTOR EIF-2B SUBUNIT BETA; 1. DR PANTHER; PTHR45859:SF1; TRANSLATION INITIATION FACTOR EIF-2B SUBUNIT BETA; 1. DR Pfam; PF01008; IF-2B; 1. DR SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Disease variant; Initiation factor; KW Leukodystrophy; Protein biosynthesis; Proteomics identification; KW Reference proteome. FT CHAIN 1..351 FT /note="Translation initiation factor eIF2B subunit beta" FT /id="PRO_0000156061" FT VARIANT 85 FT /note="V -> E (in VWM2; dbSNP:rs397514648)" FT /evidence="ECO:0000269|PubMed:21484434" FT /id="VAR_068451" FT VARIANT 127 FT /note="A -> V (found in a patient with Rett syndrome-like FT phenotype; uncertain significance; dbSNP:rs150617429)" FT /evidence="ECO:0000269|PubMed:26740508" FT /id="VAR_079034" FT VARIANT 171 FT /note="S -> F (in VWM2; with ovarian failure; FT dbSNP:rs104894428)" FT /evidence="ECO:0000269|PubMed:12707859, FT ECO:0000269|PubMed:15776425" FT /id="VAR_016842" FT VARIANT 196 FT /note="P -> S (in VWM2; dbSNP:rs113994011)" FT /evidence="ECO:0000269|PubMed:15776425" FT /id="VAR_068452" FT VARIANT 200 FT /note="G -> V (in VWM2; dbSNP:rs113994012)" FT /evidence="ECO:0000269|PubMed:15776425" FT /id="VAR_068453" FT VARIANT 213 FT /note="E -> G (in VWM2; with and without ovarian failure; FT dbSNP:rs104894425)" FT /evidence="ECO:0000269|PubMed:11704758, FT ECO:0000269|PubMed:12707859, ECO:0000269|PubMed:15776425, FT ECO:0000269|PubMed:22729508" FT /id="VAR_012289" FT VARIANT 268 FT /note="C -> Y (in VWM2; dbSNP:rs1889630768)" FT /evidence="ECO:0000269|PubMed:22285377" FT /id="VAR_068454" FT VARIANT 273 FT /note="K -> R (in VWM2; dbSNP:rs113994016)" FT /evidence="ECO:0000269|PubMed:11704758" FT /id="VAR_012321" FT VARIANT 316 FT /note="V -> D (in VWM2; dbSNP:rs104894426)" FT /evidence="ECO:0000269|PubMed:11704758" FT /id="VAR_012290" FT VARIANT 329 FT /note="G -> V (in VWM2; dbSNP:rs113994020)" FT /evidence="ECO:0000269|PubMed:11704758" FT /id="VAR_012322" FT CONFLICT 6 FT /note="A -> K (in Ref. 2; AAC42002)" FT /evidence="ECO:0000305" FT CONFLICT 23 FT /note="K -> T (in Ref. 2; AAC42002)" FT /evidence="ECO:0000305" FT CONFLICT 30 FT /note="S -> R (in Ref. 2; AAC42002)" FT /evidence="ECO:0000305" FT CONFLICT 35 FT /note="A -> V (in Ref. 2; AAC42002)" FT /evidence="ECO:0000305" FT CONFLICT 52 FT /note="S -> R (in Ref. 2; AAC42002)" FT /evidence="ECO:0000305" FT CONFLICT 95..101 FT /note="RLHGRSD -> DSMDAAT (in Ref. 2; AAC42002)" FT /evidence="ECO:0000305" FT CONFLICT 110 FT /note="H -> D (in Ref. 2; AAC42002)" FT /evidence="ECO:0000305" FT HELIX 9..24 FT /evidence="ECO:0007829|PDB:9ZUZ" FT STRAND 28..30 FT /evidence="ECO:0007829|PDB:7RLO" FT HELIX 31..48 FT /evidence="ECO:0007829|PDB:9ZUZ" FT HELIX 54..71 FT /evidence="ECO:0007829|PDB:9ZUZ" FT HELIX 76..97 FT /evidence="ECO:0007829|PDB:9ZUZ" FT STRAND 103..107 FT /evidence="ECO:0007829|PDB:9HVE" FT HELIX 109..113 FT /evidence="ECO:0007829|PDB:9ZUZ" FT HELIX 129..145 FT /evidence="ECO:0007829|PDB:9ZUZ" FT HELIX 147..152 FT /evidence="ECO:0007829|PDB:9ZUZ" FT HELIX 155..157 FT /evidence="ECO:0007829|PDB:9ZUZ" FT STRAND 164..169 FT /evidence="ECO:0007829|PDB:9ZUZ" FT HELIX 172..182 FT /evidence="ECO:0007829|PDB:9ZUZ" FT STRAND 188..192 FT /evidence="ECO:0007829|PDB:9ZUZ" FT TURN 195..198 FT /evidence="ECO:0007829|PDB:9ZUZ" FT HELIX 199..209 FT /evidence="ECO:0007829|PDB:9ZUZ" FT STRAND 213..217 FT /evidence="ECO:0007829|PDB:9ZUZ" FT HELIX 219..221 FT /evidence="ECO:0007829|PDB:9ZUZ" FT HELIX 222..226 FT /evidence="ECO:0007829|PDB:9ZUZ" FT STRAND 230..234 FT /evidence="ECO:0007829|PDB:9ZUZ" FT STRAND 237..239 FT /evidence="ECO:0007829|PDB:9ZUZ" FT STRAND 241..243 FT /evidence="ECO:0007829|PDB:7L70" FT STRAND 245..248 FT /evidence="ECO:0007829|PDB:9ZUZ" FT HELIX 251..260 FT /evidence="ECO:0007829|PDB:9ZUZ" FT STRAND 265..268 FT /evidence="ECO:0007829|PDB:9ZUZ" FT HELIX 271..273 FT /evidence="ECO:0007829|PDB:9ZUZ" FT TURN 279..281 FT /evidence="ECO:0007829|PDB:6CAJ" FT STRAND 283..286 FT /evidence="ECO:0007829|PDB:7VLK" FT HELIX 291..294 FT /evidence="ECO:0007829|PDB:9ZUZ" FT HELIX 297..299 FT /evidence="ECO:0007829|PDB:7VLK" FT HELIX 300..303 FT /evidence="ECO:0007829|PDB:9ZUZ" FT STRAND 305..308 FT /evidence="ECO:0007829|PDB:7VLK" FT STRAND 311..316 FT /evidence="ECO:0007829|PDB:9ZUZ" FT HELIX 318..320 FT /evidence="ECO:0007829|PDB:9ZUZ" FT STRAND 323..326 FT /evidence="ECO:0007829|PDB:9ZUZ" FT STRAND 329..331 FT /evidence="ECO:0007829|PDB:9ZUZ" FT HELIX 333..335 FT /evidence="ECO:0007829|PDB:9ZUZ" FT HELIX 336..343 FT /evidence="ECO:0007829|PDB:9ZUZ" FT HELIX 346..348 FT /evidence="ECO:0007829|PDB:9ZUZ" SQ SEQUENCE 351 AA; 38990 MW; C29FE477143F545A CRC64; MPGSAAKGSE LSERIESFVE TLKRGGGPRS SEEMARETLG LLRQIITDHR WSNAGELMEL IRREGRRMTA AQPSETTVGN MVRRVLKIIR EEYGRLHGRS DESDQQESLH KLLTSGGLNE DFSFHYAQLQ SNIIEAINEL LVELEGTMEN IAAQALEHIH SNEVIMTIGF SRTVEAFLKE AARKRKFHVI VAECAPFCQG HEMAVNLSKA GIETTVMTDA AIFAVMSRVN KVIIGTKTIL ANGALRAVTG THTLALAAKH HSTPLIVCAP MFKLSPQFPN EEDSFHKFVA PEEVLPFTEG DILEKVSVHC PVFDYVPPEL ITLFISNIGG NAPSYIYRLM SELYHPDDHV L //