EI2BG_HUMAN
ID EI2BG_HUMAN Reviewed; 452 AA.
AC Q9NR50; B2RBH8; D3DPZ2; Q5QP89; Q5QP90; Q8NDB5; Q8WV57; Q9H850;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Translation initiation factor eIF-2B subunit gamma;
DE AltName: Full=eIF-2B GDP-GTP exchange factor subunit gamma;
GN Name=EIF2B3;
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).
RX PubMed=10900014; DOI=10.1073/pnas.97.15.8566;
RA Krueger M., Beger C., Li Q.-X., Welch P.J., Tritz R., Leavitt M.,
RA Barber J.R., Wong-Staal F.;
RT "Identification of eIF2B gamma and eIF2 gamma as cofactors of hepatitis C
RT virus internal ribosome entry site-mediated translation using a functional
RT genomics approach.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:8566-8571(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 2).
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Blood;
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 PROTEIN SEQUENCE OF 1-15; 226-234 AND 260-268, ACETYLATION AT MET-1, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Hepatoma;
RA Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.;
RL Submitted (JUL-2007) to UniProtKB.
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 ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [12]
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 [13]
RP VARIANTS VWM VAL-87 AND GLN-225.
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 [14]
RP VARIANTS VWM GLU-47; GLN-225 AND THR-346.
RX PubMed=19158808; DOI=10.1038/jhg.2008.10;
RA Wu Y., Pan Y., Du L., Wang J., Gu Q., Gao Z., Li J., Leng X., Qin J.,
RA Wu X., Jiang Y.;
RT "Identification of novel EIF2B mutations in Chinese patients with vanishing
RT white matter disease.";
RL J. Hum. Genet. 54:74-77(2009).
RN [15]
RP VARIANT VWM GLN-27.
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).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=1;
CC IsoId=Q9NR50-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NR50-2; Sequence=VSP_001436;
CC Name=3;
CC IsoId=Q9NR50-3; Sequence=VSP_001435;
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:19158808,
CC ECO:0000269|PubMed:21484434}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the eIF-2B gamma/epsilon subunits family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Mendelian genes eukaryotic translation initiation
CC factor 2B, subunit 3 gamma, 58kDa (EIF2B3); Note=Leiden Open Variation
CC Database (LOVD);
CC URL="https://databases.lovd.nl/shared/genes/EIF2B3";
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DR EMBL; AF257077; AAF91351.1; -; mRNA.
DR EMBL; AK024006; BAB14770.1; -; mRNA.
DR EMBL; AK314668; BAG37225.1; -; mRNA.
DR EMBL; AL834288; CAD38962.1; -; mRNA.
DR EMBL; AL136380; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07013.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07015.1; -; Genomic_DNA.
DR EMBL; BC018728; AAH18728.1; -; mRNA.
DR CCDS; CCDS517.1; -. [Q9NR50-1]
DR CCDS; CCDS53313.1; -. [Q9NR50-2]
DR CCDS; CCDS72775.1; -. [Q9NR50-3]
DR RefSeq; NP_001160060.1; NM_001166588.2. [Q9NR50-2]
DR RefSeq; NP_001248347.1; NM_001261418.1. [Q9NR50-3]
DR RefSeq; NP_065098.1; NM_020365.4. [Q9NR50-1]
DR PDB; 6CAJ; EM; 2.80 A; I/J=1-452.
DR PDB; 6EZO; EM; 4.10 A; E/F=1-452.
DR PDB; 6K71; EM; 4.30 A; E/F=1-452.
DR PDB; 6K72; EM; 4.60 A; E/F=1-452.
DR PDB; 6O81; EM; 3.21 A; I/J=1-452.
DR PDB; 6O85; EM; 3.03 A; I/J=1-452.
DR PDB; 6O9Z; EM; 3.03 A; I/J=1-452.
DR PDB; 7D43; EM; 4.30 A; E/F=1-452.
DR PDB; 7D44; EM; 4.00 A; E/F=1-452.
DR PDB; 7D45; EM; 3.80 A; E/F=1-452.
DR PDB; 7D46; EM; 4.00 A; E/F=1-452.
DR PDB; 7F64; EM; 2.42 A; E/F=1-452.
DR PDB; 7F66; EM; 2.76 A; E/F=1-452.
DR PDB; 7F67; EM; 3.59 A; E/F=1-452.
DR PDB; 7KMF; EM; 2.91 A; J/K=1-452.
DR PDB; 7L70; EM; 2.80 A; I/J=1-452.
DR PDB; 7L7G; EM; 3.00 A; I/J=1-452.
DR PDB; 7RLO; EM; 2.60 A; I/J=1-452.
DR PDB; 7VLK; EM; 2.27 A; E/F=1-452.
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; 7KMF; -.
DR PDBsum; 7L70; -.
DR PDBsum; 7L7G; -.
DR PDBsum; 7RLO; -.
DR PDBsum; 7VLK; -.
DR AlphaFoldDB; Q9NR50; -.
DR SMR; Q9NR50; -.
DR BioGRID; 114408; 105.
DR CORUM; Q9NR50; -.
DR IntAct; Q9NR50; 46.
DR MINT; Q9NR50; -.
DR STRING; 9606.ENSP00000353575; -.
DR ChEMBL; CHEMBL4295961; -.
DR GlyGen; Q9NR50; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NR50; -.
DR MetOSite; Q9NR50; -.
DR PhosphoSitePlus; Q9NR50; -.
DR SwissPalm; Q9NR50; -.
DR BioMuta; EIF2B3; -.
DR DMDM; 18203317; -.
DR REPRODUCTION-2DPAGE; IPI00006504; -.
DR EPD; Q9NR50; -.
DR jPOST; Q9NR50; -.
DR MassIVE; Q9NR50; -.
DR MaxQB; Q9NR50; -.
DR PaxDb; Q9NR50; -.
DR PeptideAtlas; Q9NR50; -.
DR PRIDE; Q9NR50; -.
DR ProteomicsDB; 82275; -. [Q9NR50-1]
DR ProteomicsDB; 82276; -. [Q9NR50-2]
DR ProteomicsDB; 82277; -. [Q9NR50-3]
DR Antibodypedia; 18525; 296 antibodies from 27 providers.
DR DNASU; 8891; -.
DR Ensembl; ENST00000360403.7; ENSP00000353575.2; ENSG00000070785.17. [Q9NR50-1]
DR Ensembl; ENST00000372183.7; ENSP00000361257.3; ENSG00000070785.17. [Q9NR50-2]
DR Ensembl; ENST00000620860.4; ENSP00000483996.1; ENSG00000070785.17. [Q9NR50-3]
DR GeneID; 8891; -.
DR KEGG; hsa:8891; -.
DR MANE-Select; ENST00000360403.7; ENSP00000353575.2; NM_020365.5; NP_065098.1.
DR UCSC; uc001cmt.4; human. [Q9NR50-1]
DR CTD; 8891; -.
DR DisGeNET; 8891; -.
DR GeneCards; EIF2B3; -.
DR GeneReviews; EIF2B3; -.
DR HGNC; HGNC:3259; EIF2B3.
DR HPA; ENSG00000070785; Low tissue specificity.
DR MalaCards; EIF2B3; -.
DR MIM; 603896; phenotype.
DR MIM; 606273; gene.
DR neXtProt; NX_Q9NR50; -.
DR OpenTargets; ENSG00000070785; -.
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; PA27690; -.
DR VEuPathDB; HostDB:ENSG00000070785; -.
DR eggNOG; KOG1462; Eukaryota.
DR GeneTree; ENSGT00510000047486; -.
DR HOGENOM; CLU_016743_0_0_1; -.
DR InParanoid; Q9NR50; -.
DR OMA; LLQAWMV; -.
DR OrthoDB; 1388750at2759; -.
DR PhylomeDB; Q9NR50; -.
DR TreeFam; TF101507; -.
DR PathwayCommons; Q9NR50; -.
DR Reactome; R-HSA-72731; Recycling of eIF2:GDP.
DR SignaLink; Q9NR50; -.
DR SIGNOR; Q9NR50; -.
DR BioGRID-ORCS; 8891; 776 hits in 1089 CRISPR screens.
DR ChiTaRS; EIF2B3; human.
DR GeneWiki; EIF2B3; -.
DR GenomeRNAi; 8891; -.
DR Pharos; Q9NR50; Tbio.
DR PRO; PR:Q9NR50; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9NR50; protein.
DR Bgee; ENSG00000070785; Expressed in triceps brachii and 195 other tissues.
DR ExpressionAtlas; Q9NR50; baseline and differential.
DR Genevisible; Q9NR50; 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:0032045; C:guanyl-nucleotide exchange factor complex; IBA:GO_Central.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0002183; P:cytoplasmic translational initiation; IBA:GO_Central.
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; 3.90.550.10; -; 1.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing;
KW Disease variant; Initiation factor; Leukodystrophy; Phosphoprotein;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..452
FT /note="Translation initiation factor eIF-2B subunit gamma"
FT /id="PRO_0000156079"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 402..452
FT /note="SNIQGSVICNNAVIEKGADIKDCLIGSGQRIEAKAKRVNEVIVGNDQLMEI
FT -> YVSPCTHLRQR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_001436"
FT VAR_SEQ 402..452
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_001435"
FT VARIANT 27
FT /note="L -> Q (in VWM; dbSNP:rs397514647)"
FT /evidence="ECO:0000269|PubMed:21484434"
FT /id="VAR_068470"
FT VARIANT 47
FT /note="G -> E (in VWM)"
FT /evidence="ECO:0000269|PubMed:19158808"
FT /id="VAR_068471"
FT VARIANT 87
FT /note="A -> V (in VWM; dbSNP:rs113994022)"
FT /evidence="ECO:0000269|PubMed:11835386"
FT /id="VAR_015409"
FT VARIANT 225
FT /note="R -> Q (in VWM; dbSNP:rs113994024)"
FT /evidence="ECO:0000269|PubMed:11835386,
FT ECO:0000269|PubMed:19158808"
FT /id="VAR_015410"
FT VARIANT 288
FT /note="D -> E (in dbSNP:rs3738247)"
FT /id="VAR_048920"
FT VARIANT 346
FT /note="I -> T (in VWM; dbSNP:rs119474039)"
FT /evidence="ECO:0000269|PubMed:19158808"
FT /id="VAR_068472"
FT CONFLICT 356
FT /note="S -> G (in Ref. 2; BAB14770)"
FT /evidence="ECO:0000305"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:7RLO"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 37..46
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 63..67
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 86..92
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 115..123
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 127..134
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:7L70"
FT STRAND 166..172
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:7L7G"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 184..189
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 192..207
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 209..217
FT /evidence="ECO:0007829|PDB:7VLK"
FT TURN 224..227
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 228..235
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 263..270
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 272..275
FT /evidence="ECO:0007829|PDB:6CAJ"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 281..292
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 300..304
FT /evidence="ECO:0007829|PDB:7RLO"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:7RLO"
FT HELIX 316..333
FT /evidence="ECO:0007829|PDB:7RLO"
SQ SEQUENCE 452 AA; 50240 MW; 6F73137F59E52773 CRC64;
MEFQAVVMAV GGGSRMTDLT SSIPKPLLPV GNKPLIWYPL NLLERVGFEE VIVVTTRDVQ
KALCAEFKMK MKPDIVCIPD DADMGTADSL RYIYPKLKTD VLVLSCDLIT DVALHEVVDL
FRAYDASLAM LMRKGQDSIE PVPGQKGKKK AVEQRDFIGV DSTGKRLLFM ANEADLDEEL
VIKGSILQKH PRIRFHTGLV DAHLYCLKKY IVDFLMENGS ITSIRSELIP YLVRKQFSSA
SSQQGQEEKE EDLKKKELKS LDIYSFIKEA NTLNLAPYDA CWNACRGDRW EDLSRSQVRC
YVHIMKEGLC SRVSTLGLYM EANRQVPKLL SALCPEEPPV HSSAQIVSKH LVGVDSLIGP
ETQIGEKSSI KRSVIGSSCL IKDRVTITNC LLMNSVTVEE GSNIQGSVIC NNAVIEKGAD
IKDCLIGSGQ RIEAKAKRVN EVIVGNDQLM EI
