IF2B_MOUSE
ID IF2B_MOUSE Reviewed; 331 AA.
AC Q99L45; Q9CSH6; Q9CT12;
DT 13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Eukaryotic translation initiation factor 2 subunit 2;
DE AltName: Full=Eukaryotic translation initiation factor 2 subunit beta;
DE Short=eIF-2-beta;
GN Name=Eif2s2;
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=Embryo;
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].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 IN AN EIF2 COMPLEX WITH EIF2S1; CELF1; CALR; CALR3; HSPA5
RP AND HSP90B1.
RX PubMed=16931514; DOI=10.1074/jbc.m605701200;
RA Timchenko L.T., Salisbury E., Wang G.-L., Nguyen H., Albrecht J.H.,
RA Hershey J.W., Timchenko N.A.;
RT "Age-specific CUGBP1-eIF2 complex increases translation of CCAAT/enhancer-
RT binding protein beta in old liver.";
RL J. Biol. Chem. 281:32806-32819(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC 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: eIF-2 functions in the early steps of protein synthesis by
CC forming a ternary complex with GTP and initiator tRNA. This complex
CC binds to a 40S ribosomal subunit, followed by mRNA binding to form a
CC 43S preinitiation complex. Junction of the 60S ribosomal subunit to
CC form the 80S initiation complex is preceded by hydrolysis of the GTP
CC bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for
CC eIF-2 to recycle and catalyze another round of initiation, the GDP
CC bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by
CC eIF-2B (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterotrimer composed of an alpha, a beta and a gamma chain
CC (By similarity). Component of an EIF2 complex at least composed of
CC CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5
CC (PubMed:16931514). Interacts with BZW2/5MP1 and EIF5 (By similarity).
CC {ECO:0000250|UniProtKB:P20042, ECO:0000269|PubMed:16931514}.
CC -!- SIMILARITY: Belongs to the eIF-2-beta/eIF-5 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB28490.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK011503; BAB27663.1; -; mRNA.
DR EMBL; AK012817; BAB28490.2; ALT_INIT; mRNA.
DR EMBL; BC003848; AAH03848.1; -; mRNA.
DR CCDS; CCDS38292.1; -.
DR RefSeq; NP_080306.1; NM_026030.2.
DR AlphaFoldDB; Q99L45; -.
DR SMR; Q99L45; -.
DR BioGRID; 212014; 31.
DR IntAct; Q99L45; 4.
DR MINT; Q99L45; -.
DR STRING; 10090.ENSMUSP00000096777; -.
DR iPTMnet; Q99L45; -.
DR PhosphoSitePlus; Q99L45; -.
DR SwissPalm; Q99L45; -.
DR EPD; Q99L45; -.
DR jPOST; Q99L45; -.
DR MaxQB; Q99L45; -.
DR PaxDb; Q99L45; -.
DR PRIDE; Q99L45; -.
DR ProteomicsDB; 267096; -.
DR Antibodypedia; 25771; 347 antibodies from 31 providers.
DR DNASU; 67204; -.
DR Ensembl; ENSMUST00000099173; ENSMUSP00000096777; ENSMUSG00000074656.
DR Ensembl; ENSMUST00000166171; ENSMUSP00000128257; ENSMUSG00000074656.
DR GeneID; 67204; -.
DR KEGG; mmu:67204; -.
DR UCSC; uc008njw.1; mouse.
DR CTD; 8894; -.
DR MGI; MGI:1914454; Eif2s2.
DR VEuPathDB; HostDB:ENSMUSG00000074656; -.
DR eggNOG; KOG2768; Eukaryota.
DR GeneTree; ENSGT00390000001804; -.
DR HOGENOM; CLU_026663_0_1_1; -.
DR InParanoid; Q99L45; -.
DR OMA; YMFAEMG; -.
DR OrthoDB; 1178655at2759; -.
DR PhylomeDB; Q99L45; -.
DR TreeFam; TF101503; -.
DR Reactome; R-MMU-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-MMU-381042; PERK regulates gene expression.
DR Reactome; R-MMU-382556; ABC-family proteins mediated transport.
DR Reactome; R-MMU-72649; Translation initiation complex formation.
DR Reactome; R-MMU-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-MMU-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-MMU-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-MMU-72731; Recycling of eIF2:GDP.
DR BioGRID-ORCS; 67204; 23 hits in 73 CRISPR screens.
DR ChiTaRS; Eif2s2; mouse.
DR PRO; PR:Q99L45; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q99L45; protein.
DR Bgee; ENSMUSG00000074656; Expressed in morula and 260 other tissues.
DR ExpressionAtlas; Q99L45; baseline and differential.
DR Genevisible; Q99L45; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005850; C:eukaryotic translation initiation factor 2 complex; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; ISS:UniProtKB.
DR GO; GO:0031369; F:translation initiation factor binding; IBA:GO_Central.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IBA:GO_Central.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IBA:GO_Central.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0002176; P:male germ cell proliferation; IMP:MGI.
DR GO; GO:0008584; P:male gonad development; IMP:MGI.
DR InterPro; IPR045196; IF2/IF5.
DR InterPro; IPR002735; Transl_init_fac_IF2/IF5_dom.
DR InterPro; IPR016189; Transl_init_fac_IF2/IF5_N.
DR InterPro; IPR016190; Transl_init_fac_IF2/IF5_Zn-bd.
DR PANTHER; PTHR23001; PTHR23001; 1.
DR Pfam; PF01873; eIF-5_eIF-2B; 1.
DR SMART; SM00653; eIF2B_5; 1.
DR SUPFAM; SSF100966; SSF100966; 1.
DR SUPFAM; SSF75689; SSF75689; 1.
PE 1: Evidence at protein level;
KW Acetylation; Initiation factor; Isopeptide bond; Metal-binding;
KW Phosphoprotein; Protein biosynthesis; Reference proteome; Ubl conjugation;
KW Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P20042"
FT CHAIN 2..331
FT /note="Eukaryotic translation initiation factor 2 subunit
FT 2"
FT /id="PRO_0000137407"
FT ZN_FING 279..303
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P20042"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20042"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41035"
FT MOD_RES 36
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20042"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20042"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41035"
FT MOD_RES 263
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P20042"
FT MOD_RES 291
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P20042"
FT CROSSLNK 102
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P20042"
SQ SEQUENCE 331 AA; 38092 MW; E91BEBBF330B7A5C CRC64;
MSGDEMIFDP TMSKKKKKKK KPFMLDEEGD AQTEETQPSE TKEVEPEPTE EKDVDADEED
SRKKDASDDL DDLNFFNQKK KKKKTKKIFD IDEAEEAIKD VKIESDAQEP AEPEDDLDIM
LGNKKKKKKN VKFPEEDEIL EKDEALEDED SKKDDGISFS SQTAWAGSER DYTYEELLNR
VFNIMREKNP DMVAGEKRKF VMKPPQVVRV GTKKTSFVNF TDICKLLHRQ PKHLLAFLLA
ELGTSGSIDG NNQLVIKGRF QQKQIENVLR RYIKEYVTCH TCRSPDTILQ KDTRLYFLQC
ETCHSRCSVA SIKTGFQAVT GKRAQLRAKA N
