EF1G_MOUSE
ID EF1G_MOUSE Reviewed; 437 AA.
AC Q9D8N0; Q920C5; Q9CRT5; Q9CSU3; Q9D004;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Elongation factor 1-gamma;
DE Short=EF-1-gamma;
DE AltName: Full=eEF-1B gamma;
GN Name=Eef1g;
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 [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Thymus;
RA Lee Y., Lu X., He W.;
RT "Mouse elongation factor-like protein, mRNA sequence.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, Embryonic head, Pancreas, and Thymus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [4]
RP PROTEIN SEQUENCE OF 234-241, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-147; LYS-212; LYS-401 AND
RP LYS-434, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Probably plays a role in anchoring the complex to other
CC cellular components. {ECO:0000250}.
CC -!- SUBUNIT: EF-1 is composed of four subunits: alpha, beta, delta, and
CC gamma. {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF321126; AAL23895.1; -; mRNA.
DR EMBL; AK007869; BAB25320.1; -; mRNA.
DR EMBL; AK011951; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK011973; BAB27948.1; -; mRNA.
DR EMBL; AK014277; BAB29238.3; -; mRNA.
DR EMBL; AK050636; BAC34356.1; -; mRNA.
DR EMBL; AK081859; BAC38351.1; -; mRNA.
DR EMBL; BC083071; AAH83071.1; -; mRNA.
DR CCDS; CCDS29563.1; -.
DR RefSeq; NP_080283.3; NM_026007.4.
DR AlphaFoldDB; Q9D8N0; -.
DR SMR; Q9D8N0; -.
DR BioGRID; 211986; 58.
DR CORUM; Q9D8N0; -.
DR DIP; DIP-32124N; -.
DR IntAct; Q9D8N0; 14.
DR STRING; 10090.ENSMUSP00000093955; -.
DR iPTMnet; Q9D8N0; -.
DR PhosphoSitePlus; Q9D8N0; -.
DR SwissPalm; Q9D8N0; -.
DR REPRODUCTION-2DPAGE; Q9D8N0; -.
DR CPTAC; non-CPTAC-3788; -.
DR EPD; Q9D8N0; -.
DR jPOST; Q9D8N0; -.
DR MaxQB; Q9D8N0; -.
DR PaxDb; Q9D8N0; -.
DR PRIDE; Q9D8N0; -.
DR ProteomicsDB; 275906; -.
DR Antibodypedia; 52234; 378 antibodies from 30 providers.
DR Ensembl; ENSMUST00000052248; ENSMUSP00000093955; ENSMUSG00000071644.
DR GeneID; 67160; -.
DR KEGG; mmu:67160; -.
DR UCSC; uc008goi.1; mouse.
DR CTD; 1937; -.
DR MGI; MGI:1914410; Eef1g.
DR VEuPathDB; HostDB:ENSMUSG00000071644; -.
DR eggNOG; KOG0867; Eukaryota.
DR eggNOG; KOG1627; Eukaryota.
DR GeneTree; ENSGT00390000007552; -.
DR HOGENOM; CLU_011226_3_1_1; -.
DR InParanoid; Q9D8N0; -.
DR OMA; TRWYETI; -.
DR OrthoDB; 1341490at2759; -.
DR PhylomeDB; Q9D8N0; -.
DR TreeFam; TF314343; -.
DR Reactome; R-MMU-156842; Eukaryotic Translation Elongation.
DR BioGRID-ORCS; 67160; 27 hits in 76 CRISPR screens.
DR ChiTaRS; Eef1g; mouse.
DR PRO; PR:Q9D8N0; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9D8N0; protein.
DR Bgee; ENSMUSG00000071644; Expressed in cortical plate and 78 other tissues.
DR ExpressionAtlas; Q9D8N0; baseline and differential.
DR Genevisible; Q9D8N0; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR GO; GO:0009615; P:response to virus; IEA:Ensembl.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR Gene3D; 3.30.70.1010; -; 1.
DR InterPro; IPR001662; EF1B_G_C.
DR InterPro; IPR036433; EF1B_G_C_sf.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF00647; EF1G; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SMART; SM01183; EF1G; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR SUPFAM; SSF89942; SSF89942; 1.
DR PROSITE; PS50040; EF1G_C; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Elongation factor; Isopeptide bond;
KW Protein biosynthesis; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P26641"
FT CHAIN 2..437
FT /note="Elongation factor 1-gamma"
FT /id="PRO_0000208814"
FT DOMAIN 2..87
FT /note="GST N-terminal"
FT DOMAIN 88..216
FT /note="GST C-terminal"
FT DOMAIN 276..437
FT /note="EF-1-gamma C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00519"
FT REGION 221..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P26641"
FT MOD_RES 147
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 212
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 401
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 434
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 434
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 253
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:P26641"
FT CROSSLNK 285
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P26641"
FT CONFLICT 4
FT /note="G -> E (in Ref. 2; BAB29238)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="K -> R (in Ref. 1; AAL23895)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="K -> N (in Ref. 2; BAB27948)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="N -> T (in Ref. 1; AAL23895)"
FT /evidence="ECO:0000305"
FT CONFLICT 413
FT /note="V -> G (in Ref. 1; AAL23895)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 437 AA; 50061 MW; 403A9C0E95E27454 CRC64;
MAAGTLYTYP ENWRAFKALI AAQYSGAQVR VLSAPPHFHF GQTNRTPEFL RKFPAGKVPA
FEGDDGFCVF ESNAIAYYVS NEELRGSTPE AAAQVVQWVS FADSDIVPPA STWVFPTLGI
MHHNKQATEN AKEEVKRILG LLDTHLKTRT FLVGERVTLA DITVVCTLLW LYKQVLEPSF
RQAFPNTNRW FLTCINQPQF RAILGEVKLC EKMAQFDAKK FAESQPKKDT PRKEKGSREE
KQKPQAERKE EKKAAAPAPE EEMDECEQAL AAEPKAKDPF AHLPKSTFVL DEFKRKYSNE
DTLSVALPYF WEHFDKDGWS LWYAEYRFPE ELTQTFMSCN LITGMFQRLD KLRKNAFASV
ILFGTNNSSS ISGVWVFRGQ ELAFPLSPDW QVDYESYTWR KLDPGSEETQ TLVREYFSWE
GTFQHVGKAV NQGKIFK
