EI2BB_MOUSE
ID EI2BB_MOUSE Reviewed; 351 AA.
AC Q99LD9;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Translation initiation factor eIF-2B subunit beta;
DE AltName: Full=eIF-2B GDP-GTP exchange factor subunit beta;
GN Name=Eif2b2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the exchange of eukaryotic initiation factor 2-
CC bound GDP for GTP. {ECO:0000250}.
CC -!- SUBUNIT: Complex of five different subunits; alpha, beta, gamma, delta
CC and epsilon. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family.
CC {ECO:0000305}.
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DR EMBL; AK049731; BAC33897.1; -; mRNA.
DR EMBL; BC003326; AAH03326.1; -; mRNA.
DR CCDS; CCDS26053.1; -.
DR RefSeq; NP_663420.1; NM_145445.4.
DR AlphaFoldDB; Q99LD9; -.
DR SMR; Q99LD9; -.
DR BioGRID; 229952; 2.
DR IntAct; Q99LD9; 2.
DR MINT; Q99LD9; -.
DR STRING; 10090.ENSMUSP00000004910; -.
DR iPTMnet; Q99LD9; -.
DR PhosphoSitePlus; Q99LD9; -.
DR EPD; Q99LD9; -.
DR MaxQB; Q99LD9; -.
DR PaxDb; Q99LD9; -.
DR PeptideAtlas; Q99LD9; -.
DR PRIDE; Q99LD9; -.
DR ProteomicsDB; 277577; -.
DR Antibodypedia; 57; 184 antibodies from 30 providers.
DR DNASU; 217715; -.
DR Ensembl; ENSMUST00000004910; ENSMUSP00000004910; ENSMUSG00000004788.
DR GeneID; 217715; -.
DR KEGG; mmu:217715; -.
DR UCSC; uc007ogr.1; mouse.
DR CTD; 8892; -.
DR MGI; MGI:2145118; Eif2b2.
DR VEuPathDB; HostDB:ENSMUSG00000004788; -.
DR eggNOG; KOG1465; Eukaryota.
DR GeneTree; ENSGT00550000074908; -.
DR HOGENOM; CLU_016218_4_3_1; -.
DR InParanoid; Q99LD9; -.
DR OMA; TSHTSYA; -.
DR OrthoDB; 918011at2759; -.
DR PhylomeDB; Q99LD9; -.
DR TreeFam; TF101506; -.
DR Reactome; R-MMU-72731; Recycling of eIF2:GDP.
DR BioGRID-ORCS; 217715; 29 hits in 72 CRISPR screens.
DR ChiTaRS; Eif2b2; mouse.
DR PRO; PR:Q99LD9; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q99LD9; protein.
DR Bgee; ENSMUSG00000004788; Expressed in metanephric mesenchyme and 269 other tissues.
DR ExpressionAtlas; Q99LD9; baseline and differential.
DR Genevisible; Q99LD9; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005851; C:eukaryotic translation initiation factor 2B complex; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:MGI.
DR GO; GO:0003743; F:translation initiation factor activity; ISO:MGI.
DR GO; GO:0007417; P:central nervous system development; ISS:UniProtKB.
DR GO; GO:0042552; P:myelination; ISS:UniProtKB.
DR GO; GO:0014003; P:oligodendrocyte development; ISS:UniProtKB.
DR GO; GO:0001541; P:ovarian follicle development; ISS:UniProtKB.
DR GO; GO:0045773; P:positive regulation of axon extension; ISO:MGI.
DR GO; GO:0009749; P:response to glucose; ISO:MGI.
DR GO; GO:0009408; P:response to heat; ISO:MGI.
DR GO; GO:0043434; P:response to peptide hormone; ISO:MGI.
DR GO; GO:0050852; P:T cell receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0006413; P:translational initiation; ISS: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 Initiation factor; Protein biosynthesis; Reference proteome.
FT CHAIN 1..351
FT /note="Translation initiation factor eIF-2B subunit beta"
FT /id="PRO_0000156062"
SQ SEQUENCE 351 AA; 38898 MW; 56FF1B8A96845853 CRC64;
MPGAAAKGSE LSERIEGFVE TLKRGGGQRS SEDMARETLG LLRRLITDHH WNNAGDLMDL
IRREGRRMTA AQPSETTVGN MVRRVLKIIR EEYGRLHGRS DESDQQESLH KLLTSGGLSE
DFSFHFAPLK ANIIEAINEL LVELEGTMEN IAAQALEHIH SNEVIMTIGY SRTVEAFLKE
AARKRKFHVI VAECAPFCQG HEMAVNLSKE GIETTVMTDA AIFAVMSRVN KVIIGTKTIL
ANGSLRAVAG THTLALAAKH HSTPLIVCAP MFKLSPQFPS EEDSFHKFVA PEEVLPFTEG
DILEKVSVHC PVFDYVPPDL ITLFISNIGG NAPSYIYRLM SELYHPDDHV L
