EI2BA_HUMAN
ID EI2BA_HUMAN Reviewed; 305 AA.
AC Q14232; A6NLY9; B4DGX0; Q3SXP4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Translation initiation factor eIF-2B subunit alpha;
DE AltName: Full=eIF-2B GDP-GTP exchange factor subunit alpha;
GN Name=EIF2B1; Synonyms=EIF2BA;
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).
RA Torp A.;
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-35, AND IDENTIFICATION BY MASS
RP 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 [8]
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 [9]
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 [10]
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 [11]
RP VARIANT VWM TYR-208.
RX PubMed=11835386; DOI=10.1002/ana.10112;
RA van der Knaap M.S., Leegwater P.A.J., Koenst A.A.M., Visser A., Naidu S.,
RA Oudejans C.B.M., Schutgens R.B.H., Pronk J.C.;
RT "Mutations in each of the five subunits of translation initiation factor
RT eIF2B can cause leukoencephalopathy with vanishing white matter.";
RL Ann. Neurol. 51:264-270(2002).
RN [12]
RP VARIANT VWM PHE-183.
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).
CC -!- FUNCTION: Catalyzes the exchange of eukaryotic initiation factor 2-
CC bound GDP for GTP.
CC -!- SUBUNIT: Complex of five different subunits; alpha, beta, gamma, delta
CC and epsilon.
CC -!- INTERACTION:
CC Q14232; Q9Y2D1: ATF5; NbExp=5; IntAct=EBI-491065, EBI-492509;
CC Q14232; Q9BV19: C1orf50; NbExp=3; IntAct=EBI-491065, EBI-2874661;
CC Q14232; Q14232: EIF2B1; NbExp=6; IntAct=EBI-491065, EBI-491065;
CC Q14232; Q9H8Y8: GORASP2; NbExp=8; IntAct=EBI-491065, EBI-739467;
CC Q14232; Q9NX70: MED29; NbExp=3; IntAct=EBI-491065, EBI-394656;
CC Q14232; Q96HA8: NTAQ1; NbExp=7; IntAct=EBI-491065, EBI-741158;
CC Q14232; Q7Z3Z2: RD3; NbExp=10; IntAct=EBI-491065, EBI-10257497;
CC Q14232; Q8IWR1: TRIM59; NbExp=3; IntAct=EBI-491065, EBI-10262539;
CC Q14232; Q8N7C3: TRIML2; NbExp=3; IntAct=EBI-491065, EBI-11059915;
CC Q14232; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-491065, EBI-10180829;
CC Q14232; Q01338: Adra2a; Xeno; NbExp=2; IntAct=EBI-491065, EBI-491073;
CC Q14232; P30545: Adra2b; Xeno; NbExp=2; IntAct=EBI-491065, EBI-491084;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q14232-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14232-2; Sequence=VSP_055469, VSP_055470;
CC -!- DISEASE: Leukodystrophy with vanishing white matter (VWM) [MIM:603896]:
CC A leukodystrophy that occurs mainly in children. Neurological signs
CC include progressive cerebellar ataxia, spasticity, inconstant optic
CC atrophy and relatively preserved mental abilities. The disease is
CC chronic-progressive with, in most individuals, additional episodes of
CC rapid deterioration following febrile infections or minor head trauma.
CC While childhood onset is the most common form of the disorder, some
CC severe forms are apparent at birth. A severe, early-onset form seen
CC among the Cree and Chippewayan populations of Quebec and Manitoba is
CC called Cree leukoencephalopathy. Milder forms may not become evident
CC until adolescence or adulthood. Some 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:11835386, ECO:0000269|PubMed:15776425}. 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 -!- WEB RESOURCE: Name=Mendelian genes eukaryotic translation initiation
CC factor 2B, subunit 1 alpha, 26kDa (EIF2B1); Note=Leiden Open Variation
CC Database (LOVD);
CC URL="https://databases.lovd.nl/shared/genes/EIF2B1";
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DR EMBL; X95648; CAA64950.1; -; mRNA.
DR EMBL; AK294815; BAG57931.1; -; mRNA.
DR EMBL; CR456831; CAG33112.1; -; mRNA.
DR EMBL; AC117503; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW98424.1; -; Genomic_DNA.
DR EMBL; BC103763; AAI03764.1; -; mRNA.
DR EMBL; BC104188; AAI04189.1; -; mRNA.
DR EMBL; BC104189; AAI04190.1; -; mRNA.
DR CCDS; CCDS31924.1; -. [Q14232-1]
DR RefSeq; NP_001405.1; NM_001414.3. [Q14232-1]
DR PDB; 3ECS; X-ray; 2.65 A; A/B/C/D/E/F/G/H=1-305.
DR PDB; 6CAJ; EM; 2.80 A; G/H=1-305.
DR PDB; 6EZO; EM; 4.10 A; A/B=1-305.
DR PDB; 6K71; EM; 4.30 A; A/B=1-305.
DR PDB; 6K72; EM; 4.60 A; A/B=1-305.
DR PDB; 6O81; EM; 3.21 A; G/H=1-305.
DR PDB; 6O85; EM; 3.03 A; G/H=1-305.
DR PDB; 6O9Z; EM; 3.03 A; G/H=1-305.
DR PDB; 7D43; EM; 4.30 A; A/B=1-305.
DR PDB; 7D44; EM; 4.00 A; A/B=1-305.
DR PDB; 7D45; EM; 3.80 A; A/B=1-305.
DR PDB; 7D46; EM; 4.00 A; A/B=1-305.
DR PDB; 7F64; EM; 2.42 A; A/B=1-305.
DR PDB; 7F66; EM; 2.76 A; A/B=1-305.
DR PDB; 7F67; EM; 3.59 A; A/B=1-305.
DR PDB; 7KMA; X-ray; 2.70 A; A/B/C/D/E/F/G/H=1-305.
DR PDB; 7KMF; EM; 2.91 A; G/H=1-305.
DR PDB; 7L70; EM; 2.80 A; G/H=2-305.
DR PDB; 7L7G; EM; 3.00 A; G/H=1-305.
DR PDB; 7RLO; EM; 2.60 A; G/H=1-305.
DR PDB; 7VLK; EM; 2.27 A; A/B=1-305.
DR PDBsum; 3ECS; -.
DR PDBsum; 6CAJ; -.
DR PDBsum; 6EZO; -.
DR PDBsum; 6K71; -.
DR PDBsum; 6K72; -.
DR PDBsum; 6O81; -.
DR PDBsum; 6O85; -.
DR PDBsum; 6O9Z; -.
DR PDBsum; 7D43; -.
DR PDBsum; 7D44; -.
DR PDBsum; 7D45; -.
DR PDBsum; 7D46; -.
DR PDBsum; 7F64; -.
DR PDBsum; 7F66; -.
DR PDBsum; 7F67; -.
DR PDBsum; 7KMA; -.
DR PDBsum; 7KMF; -.
DR PDBsum; 7L70; -.
DR PDBsum; 7L7G; -.
DR PDBsum; 7RLO; -.
DR PDBsum; 7VLK; -.
DR AlphaFoldDB; Q14232; -.
DR SMR; Q14232; -.
DR BioGRID; 108286; 116.
DR CORUM; Q14232; -.
DR IntAct; Q14232; 64.
DR MINT; Q14232; -.
DR STRING; 9606.ENSP00000416250; -.
DR iPTMnet; Q14232; -.
DR MetOSite; Q14232; -.
DR PhosphoSitePlus; Q14232; -.
DR SwissPalm; Q14232; -.
DR BioMuta; EIF2B1; -.
DR DMDM; 2494303; -.
DR EPD; Q14232; -.
DR jPOST; Q14232; -.
DR MassIVE; Q14232; -.
DR MaxQB; Q14232; -.
DR PaxDb; Q14232; -.
DR PeptideAtlas; Q14232; -.
DR PRIDE; Q14232; -.
DR ProteomicsDB; 4168; -.
DR ProteomicsDB; 59934; -. [Q14232-1]
DR Antibodypedia; 31819; 160 antibodies from 26 providers.
DR DNASU; 1967; -.
DR Ensembl; ENST00000424014.7; ENSP00000416250.2; ENSG00000111361.13. [Q14232-1]
DR Ensembl; ENST00000537073.1; ENSP00000444183.1; ENSG00000111361.13. [Q14232-2]
DR GeneID; 1967; -.
DR KEGG; hsa:1967; -.
DR MANE-Select; ENST00000424014.7; ENSP00000416250.2; NM_001414.4; NP_001405.1.
DR UCSC; uc001ufm.4; human. [Q14232-1]
DR CTD; 1967; -.
DR DisGeNET; 1967; -.
DR GeneCards; EIF2B1; -.
DR GeneReviews; EIF2B1; -.
DR HGNC; HGNC:3257; EIF2B1.
DR HPA; ENSG00000111361; Low tissue specificity.
DR MalaCards; EIF2B1; -.
DR MIM; 603896; phenotype.
DR MIM; 606686; gene.
DR neXtProt; NX_Q14232; -.
DR OpenTargets; ENSG00000111361; -.
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 PharmGKB; PA27688; -.
DR VEuPathDB; HostDB:ENSG00000111361; -.
DR eggNOG; KOG1466; Eukaryota.
DR GeneTree; ENSGT00550000074853; -.
DR HOGENOM; CLU_016218_0_2_1; -.
DR InParanoid; Q14232; -.
DR OMA; LYPLGQY; -.
DR OrthoDB; 865202at2759; -.
DR PhylomeDB; Q14232; -.
DR TreeFam; TF101505; -.
DR PathwayCommons; Q14232; -.
DR Reactome; R-HSA-72731; Recycling of eIF2:GDP.
DR SignaLink; Q14232; -.
DR SIGNOR; Q14232; -.
DR BioGRID-ORCS; 1967; 525 hits in 1081 CRISPR screens.
DR ChiTaRS; EIF2B1; human.
DR EvolutionaryTrace; Q14232; -.
DR GeneWiki; EIF2B1; -.
DR GenomeRNAi; 1967; -.
DR Pharos; Q14232; Tbio.
DR PRO; PR:Q14232; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q14232; protein.
DR Bgee; ENSG00000111361; Expressed in oocyte and 191 other tissues.
DR ExpressionAtlas; Q14232; baseline and differential.
DR Genevisible; Q14232; HS.
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:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0014003; P:oligodendrocyte development; IMP:UniProtKB.
DR GO; GO:0050790; P:regulation of catalytic activity; IEA:GOC.
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 Gene3D; 1.20.120.1070; -; 1.
DR Gene3D; 3.40.50.10470; -; 1.
DR InterPro; IPR042528; elF-2B_alpha_N.
DR InterPro; IPR000649; IF-2B-related.
DR InterPro; IPR042529; IF_2B-like_C.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR Pfam; PF01008; IF-2B; 1.
DR SUPFAM; SSF100950; SSF100950; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Disease variant;
KW Initiation factor; Leukodystrophy; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..305
FT /note="Translation initiation factor eIF-2B subunit alpha"
FT /id="PRO_0000156055"
FT MOD_RES 35
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 162..222
FT /note="KKMAKALCHLNVPVTVVLDAAVGYIMEKADLVIVGAEGVVENGGIINKIGTN
FT QMAVCAKAQ -> QVPFCSVMCPAIILQSKLRITVQQDQNQNVPPACQQSALPFIVPFP
FT AFGRKITEFAAGRSI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055469"
FT VAR_SEQ 223..305
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055470"
FT VARIANT 183
FT /note="V -> F (in VWM; dbSNP:rs863225048)"
FT /evidence="ECO:0000269|PubMed:15776425"
FT /id="VAR_068450"
FT VARIANT 208
FT /note="N -> Y (in VWM; dbSNP:rs113994007)"
FT /evidence="ECO:0000269|PubMed:11835386"
FT /id="VAR_015404"
FT HELIX 3..16
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 17..20
FT /evidence="ECO:0007829|PDB:7L70"
FT HELIX 22..35
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 46..59
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 63..82
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 86..115
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 132..143
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:7VLK"
FT TURN 156..159
FT /evidence="ECO:0007829|PDB:7F64"
FT HELIX 160..170
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:7VLK"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 191..195
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:7L70"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 212..221
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 248..251
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 272..276
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 283..286
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 294..303
FT /evidence="ECO:0007829|PDB:7VLK"
SQ SEQUENCE 305 AA; 33712 MW; 91A915FF1B80B780 CRC64;
MDDKELIEYF KSQMKEDPDM ASAVAAIRTL LEFLKRDKGE TIQGLRANLT SAIETLCGVD
SSVAVSSGGE LFLRFISLAS LEYSDYSKCK KIMIERGELF LRRISLSRNK IADLCHTFIK
DGATILTHAY SRVVLRVLEA AVAAKKRFSV YVTESQPDLS GKKMAKALCH LNVPVTVVLD
AAVGYIMEKA DLVIVGAEGV VENGGIINKI GTNQMAVCAK AQNKPFYVVA ESFKFVRLFP
LNQQDVPDKF KYKADTLKVA QTGQDLKEEH PWVDYTAPSL ITLLFTDLGV LTPSAVSDEL
IKLYL
