EI2BD_HUMAN
ID EI2BD_HUMAN Reviewed; 523 AA.
AC Q9UI10; Q53RY7; Q5BJF4; Q9BUV9; Q9UBG4; Q9UIQ9; Q9UJ95;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 12-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Translation initiation factor eIF-2B subunit delta;
DE AltName: Full=eIF-2B GDP-GTP exchange factor subunit delta;
GN Name=EIF2B4; Synonyms=EIF2BD;
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] (ISOFORM 1).
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2 AND 3).
RA Wightman P.J., Bonthron D.T.;
RT "cDNA cloning, genomic organization and chromosomal localization of the
RT human eIF2B delta subunit.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung, and Testis;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-86, AND IDENTIFICATION BY
RP 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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-86, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-86, AND IDENTIFICATION BY
RP 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 [11]
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; THR-86 AND SER-130, 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 [14]
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 [15]
RP VARIANTS VWM VAL-228; GLN-357 AND CYS-374, AND VARIANT GLY-306.
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 [16]
RP VARIANTS VWM ARG-465 AND HIS-489.
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 [17]
RP VARIANTS VWM GLN-209; ARG-269 AND CYS-374.
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 Q9UI10; P01019: AGT; NbExp=3; IntAct=EBI-2340132, EBI-751728;
CC Q9UI10; P49770: EIF2B2; NbExp=7; IntAct=EBI-2340132, EBI-718773;
CC Q9UI10; Q53XC2: EIF2B2; NbExp=4; IntAct=EBI-2340132, EBI-10288660;
CC Q9UI10; P01100: FOS; NbExp=3; IntAct=EBI-2340132, EBI-852851;
CC Q9UI10; P50440: GATM; NbExp=3; IntAct=EBI-2340132, EBI-2552594;
CC Q9UI10; P62993: GRB2; NbExp=3; IntAct=EBI-2340132, EBI-401755;
CC Q9UI10; P03952: KLKB1; NbExp=3; IntAct=EBI-2340132, EBI-10087153;
CC Q9UI10; P06858: LPL; NbExp=3; IntAct=EBI-2340132, EBI-715909;
CC Q9UI10; P31930: UQCRC1; NbExp=3; IntAct=EBI-2340132, EBI-1052596;
CC Q9UI10; P40337-2: VHL; NbExp=3; IntAct=EBI-2340132, EBI-12157263;
CC Q9UI10; P06821: M; Xeno; NbExp=3; IntAct=EBI-2340132, EBI-2547404;
CC Q9UI10; Q6DPW5: M; Xeno; NbExp=2; IntAct=EBI-2340132, EBI-12562156;
CC Q9UI10; C5E519: M2; Xeno; NbExp=2; IntAct=EBI-2340132, EBI-12562139;
CC Q9UI10; Q20MH8: M2; Xeno; NbExp=3; IntAct=EBI-2340132, EBI-12576433;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UI10-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UI10-2; Sequence=VSP_001433, VSP_040130;
CC Name=3;
CC IsoId=Q9UI10-3; Sequence=VSP_040130;
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:12707859,
CC ECO:0000269|PubMed:15776425}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB57305.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Mendelian genes eukaryotic translation initiation
CC factor 2B, subunit 4 delta, 67kDa (EIF2B4); Note=Leiden Open Variation
CC Database (LOVD);
CC URL="https://databases.lovd.nl/shared/genes/EIF2B4";
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DR EMBL; AF112207; AAF17195.1; -; mRNA.
DR EMBL; AJ011305; CAB57260.1; -; mRNA.
DR EMBL; AJ011306; CAB57261.1; -; mRNA.
DR EMBL; AJ011307; CAB57304.1; -; Genomic_DNA.
DR EMBL; AJ011308; CAB57304.1; JOINED; Genomic_DNA.
DR EMBL; AJ011307; CAB57305.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AJ011308; CAB57305.1; JOINED; Genomic_DNA.
DR EMBL; AC074117; AAY14843.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00591.1; -; Genomic_DNA.
DR EMBL; BC001870; AAH01870.1; -; mRNA.
DR EMBL; BC091502; AAH91502.1; -; mRNA.
DR CCDS; CCDS33164.1; -. [Q9UI10-1]
DR CCDS; CCDS46244.1; -. [Q9UI10-3]
DR CCDS; CCDS46245.1; -. [Q9UI10-2]
DR RefSeq; NP_001029288.1; NM_001034116.1. [Q9UI10-1]
DR RefSeq; NP_001305894.1; NM_001318965.1.
DR RefSeq; NP_001305895.1; NM_001318966.1.
DR RefSeq; NP_001305896.1; NM_001318967.1.
DR RefSeq; NP_001305897.1; NM_001318968.1.
DR RefSeq; NP_056451.3; NM_015636.3. [Q9UI10-3]
DR RefSeq; NP_751945.2; NM_172195.3. [Q9UI10-2]
DR PDB; 6CAJ; EM; 2.80 A; E/F=1-523.
DR PDB; 6EZO; EM; 4.10 A; G/H=1-523.
DR PDB; 6K71; EM; 4.30 A; G/H=1-523.
DR PDB; 6K72; EM; 4.60 A; G/H=1-523.
DR PDB; 6O81; EM; 3.21 A; E/F=1-523.
DR PDB; 6O85; EM; 3.03 A; E/F=1-523.
DR PDB; 6O9Z; EM; 3.03 A; E/F=1-523.
DR PDB; 7D43; EM; 4.30 A; G/H=1-523.
DR PDB; 7D44; EM; 4.00 A; G/H=1-523.
DR PDB; 7D45; EM; 3.80 A; G/H=1-523.
DR PDB; 7D46; EM; 4.00 A; G/H=1-523.
DR PDB; 7F64; EM; 2.42 A; G/H=1-523.
DR PDB; 7F66; EM; 2.76 A; G/H=1-523.
DR PDB; 7F67; EM; 3.59 A; G/H=1-523.
DR PDB; 7KMF; EM; 2.91 A; E/F=1-523.
DR PDB; 7L70; EM; 2.80 A; E/F=1-523.
DR PDB; 7L7G; EM; 3.00 A; E/F=1-523.
DR PDB; 7RLO; EM; 2.60 A; E/F=1-523.
DR PDB; 7VLK; EM; 2.27 A; G/H=1-523.
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; Q9UI10; -.
DR SMR; Q9UI10; -.
DR BioGRID; 114407; 129.
DR CORUM; Q9UI10; -.
DR IntAct; Q9UI10; 54.
DR MINT; Q9UI10; -.
DR STRING; 9606.ENSP00000394869; -.
DR GlyGen; Q9UI10; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UI10; -.
DR PhosphoSitePlus; Q9UI10; -.
DR SwissPalm; Q9UI10; -.
DR BioMuta; EIF2B4; -.
DR DMDM; 28381357; -.
DR EPD; Q9UI10; -.
DR jPOST; Q9UI10; -.
DR MassIVE; Q9UI10; -.
DR MaxQB; Q9UI10; -.
DR PaxDb; Q9UI10; -.
DR PeptideAtlas; Q9UI10; -.
DR PRIDE; Q9UI10; -.
DR ProteomicsDB; 84448; -. [Q9UI10-1]
DR ProteomicsDB; 84449; -. [Q9UI10-2]
DR ProteomicsDB; 84450; -. [Q9UI10-3]
DR Antibodypedia; 47347; 199 antibodies from 32 providers.
DR DNASU; 8890; -.
DR Ensembl; ENST00000347454.9; ENSP00000233552.6; ENSG00000115211.17. [Q9UI10-1]
DR Ensembl; ENST00000445933.6; ENSP00000394397.2; ENSG00000115211.17. [Q9UI10-3]
DR Ensembl; ENST00000451130.6; ENSP00000394869.2; ENSG00000115211.17. [Q9UI10-2]
DR GeneID; 8890; -.
DR KEGG; hsa:8890; -.
DR MANE-Select; ENST00000347454.9; ENSP00000233552.6; NM_001034116.2; NP_001029288.1.
DR UCSC; uc002rjz.4; human. [Q9UI10-1]
DR CTD; 8890; -.
DR DisGeNET; 8890; -.
DR GeneCards; EIF2B4; -.
DR GeneReviews; EIF2B4; -.
DR HGNC; HGNC:3260; EIF2B4.
DR HPA; ENSG00000115211; Low tissue specificity.
DR MalaCards; EIF2B4; -.
DR MIM; 603896; phenotype.
DR MIM; 606687; gene.
DR neXtProt; NX_Q9UI10; -.
DR OpenTargets; ENSG00000115211; -.
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; PA27691; -.
DR VEuPathDB; HostDB:ENSG00000115211; -.
DR eggNOG; KOG1467; Eukaryota.
DR GeneTree; ENSGT00550000075009; -.
DR HOGENOM; CLU_016218_3_3_1; -.
DR InParanoid; Q9UI10; -.
DR OMA; YIDMVIT; -.
DR OrthoDB; 797227at2759; -.
DR PhylomeDB; Q9UI10; -.
DR TreeFam; TF101508; -.
DR PathwayCommons; Q9UI10; -.
DR Reactome; R-HSA-72731; Recycling of eIF2:GDP.
DR SignaLink; Q9UI10; -.
DR SIGNOR; Q9UI10; -.
DR BioGRID-ORCS; 8890; 792 hits in 1083 CRISPR screens.
DR ChiTaRS; EIF2B4; human.
DR GeneWiki; EIF2B4; -.
DR GenomeRNAi; 8890; -.
DR Pharos; Q9UI10; Tbio.
DR PRO; PR:Q9UI10; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9UI10; protein.
DR Bgee; ENSG00000115211; Expressed in lower esophagus mucosa and 201 other tissues.
DR ExpressionAtlas; Q9UI10; baseline and differential.
DR Genevisible; Q9UI10; 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:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0031369; F:translation initiation factor binding; ISS: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:0050790; P:regulation of catalytic activity; IEA:GOC.
DR GO; GO:0006417; P:regulation of translation; NAS: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 Gene3D; 3.40.50.10470; -; 1.
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; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..523
FT /note="Translation initiation factor eIF-2B subunit delta"
FT /id="PRO_0000156067"
FT REGION 1..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 86
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..10
FT /note="MAAVAVAVRE -> MPTQQPAAPSTRAPKPSRSLSGSLCALFSDA (in
FT isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_001433"
FT VAR_SEQ 71
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_040130"
FT VARIANT 93
FT /note="A -> V (in dbSNP:rs34155621)"
FT /id="VAR_048918"
FT VARIANT 209
FT /note="R -> Q (in VWM; dbSNP:rs113994028)"
FT /evidence="ECO:0000269|PubMed:15776425"
FT /id="VAR_068455"
FT VARIANT 228
FT /note="A -> V (in VWM; dbSNP:rs113994027)"
FT /evidence="ECO:0000269|PubMed:11835386"
FT /id="VAR_015405"
FT VARIANT 269
FT /note="L -> R (in VWM; dbSNP:rs113994031)"
FT /evidence="ECO:0000269|PubMed:15776425"
FT /id="VAR_068456"
FT VARIANT 306
FT /note="R -> G (in dbSNP:rs78599355)"
FT /evidence="ECO:0000269|PubMed:11835386"
FT /id="VAR_015406"
FT VARIANT 357
FT /note="R -> Q (in VWM; dbSNP:rs113994033)"
FT /evidence="ECO:0000269|PubMed:11835386"
FT /id="VAR_015407"
FT VARIANT 374
FT /note="R -> C (in VWM; dbSNP:rs113994035)"
FT /evidence="ECO:0000269|PubMed:11835386,
FT ECO:0000269|PubMed:15776425"
FT /id="VAR_015408"
FT VARIANT 465
FT /note="C -> R (in VWM; with ovarian failure;
FT dbSNP:rs113994038)"
FT /evidence="ECO:0000269|PubMed:12707859"
FT /id="VAR_016843"
FT VARIANT 489
FT /note="Y -> H (in VWM; with ovarian failure;
FT dbSNP:rs113994040)"
FT /evidence="ECO:0000269|PubMed:12707859"
FT /id="VAR_016844"
FT CONFLICT 197
FT /note="S -> T (in Ref. 2; CAB57260/CAB57261/CAB57304/
FT CAB57305)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="A -> S (in Ref. 1; AAF17195)"
FT /evidence="ECO:0000305"
FT CONFLICT 481
FT /note="S -> L (in Ref. 1; AAF17195)"
FT /evidence="ECO:0000305"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:6CAJ"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:6CAJ"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 205..215
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 222..239
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:7F66"
FT HELIX 248..266
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 271..285
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:7RLO"
FT HELIX 293..324
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 332..337
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 340..351
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 357..362
FT /evidence="ECO:0007829|PDB:7VLK"
FT TURN 364..366
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 369..378
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 383..387
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 388..390
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 391..394
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 395..397
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 400..404
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 410..412
FT /evidence="ECO:0007829|PDB:6CAJ"
FT STRAND 414..417
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 420..429
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 434..437
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 440..442
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 449..454
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 460..463
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 467..469
FT /evidence="ECO:0007829|PDB:6CAJ"
FT TURN 472..475
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 476..478
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 482..484
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 489..492
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 494..496
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 499..502
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 505..507
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 509..511
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 512..520
FT /evidence="ECO:0007829|PDB:7VLK"
SQ SEQUENCE 523 AA; 57557 MW; 5F38CF10CAD5A45E CRC64;
MAAVAVAVRE DSGSGMKAEL PPGPGAVGRE MTKEEKLQLR KEKKQQKKKR KEEKGAEPET
GSAVSAAQCQ VGPTRELPES GIQLGTPREK VPAGRSKAEL RAERRAKQEA ERALKQARKG
EQGGPPPKAS PSTAGETPSG VKRLPEYPQV DDLLLRRLVK KPERQQVPTR KDYGSKVSLF
SHLPQYSRQN SLTQFMSIPS SVIHPAMVRL GLQYSQGLVS GSNARCIALL RALQQVIQDY
TTPPNEELSR DLVNKLKPYM SFLTQCRPLS ASMHNAIKFL NKEITSVGSS KREEEAKSEL
RAAIDRYVQE KIVLAAQAIS RFAYQKISNG DVILVYGCSS LVSRILQEAW TEGRRFRVVV
VDSRPWLEGR HTLRSLVHAG VPASYLLIPA ASYVLPEVSK VLLGAHALLA NGSVMSRVGT
AQLALVARAH NVPVLVCCET YKFCERVQTD AFVSNELDDP DDLQCKRGEH VALANWQNHA
SLRLLNLVYD VTPPELVDLV ITELGMIPCS SVPVVLRVKS SDQ
