EF1G_HUMAN
ID EF1G_HUMAN Reviewed; 437 AA.
AC P26641; B4DTG2; Q6PJ62; Q6PK31; Q96CU2; Q9P196;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 232.
DE RecName: Full=Elongation factor 1-gamma;
DE Short=EF-1-gamma;
DE AltName: Full=eEF-1B gamma;
GN Name=EEF1G; Synonyms=EF1G; ORFNames=PRO1608;
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=1461723; DOI=10.1093/nar/20.22.5907;
RA Sanders J., Maassen J.A., Moeller W.;
RT "Elongation factor-1 messenger-RNA levels in cultured cells are high
RT compared to tissue and are not drastically affected further by oncogenic
RT transformation.";
RL Nucleic Acids Res. 20:5907-5910(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1598220; DOI=10.1093/nar/20.10.2598;
RA Kumabe T., Schma Y., Yamamoto T.;
RT "Human cDNAs encoding elongation factor 1 gamma and the ribosomal protein
RT L19.";
RL Nucleic Acids Res. 20:2598-2598(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow, Eye, Liver, Lung, Muscle, Testis, and Uterus;
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 PROTEIN SEQUENCE OF 2-14.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [7]
RP PROTEIN SEQUENCE OF 2-14, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (OCT-2004) to UniProtKB.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 80-437 (ISOFORM 1).
RC TISSUE=Pancreatic carcinoma;
RX PubMed=1372736; DOI=10.1097/00006676-199203000-00003;
RA Lew Y., Jones D.V., Mars W.M., Evans D., Byrd D., Frazier M.L.;
RT "Expression of elongation factor-1 gamma-related sequence in human
RT pancreatic cancer.";
RL Pancreas 7:144-152(1992).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 121-437 (ISOFORM 1).
RC TISSUE=Fetal liver;
RA Zhang C., Yu Y., Zhang S., Wei H., Zhang Y., Zhou G., Bi J., Liu M., He F.;
RT "Functional prediction of the coding sequences of 79 new genes deduced by
RT analysis of cDNA clones from human fetal liver.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [11]
RP INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16548883; DOI=10.1111/j.1462-5822.2005.00644.x;
RA Leong W.F., Chow V.T.;
RT "Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal
RT differential cellular gene expression in response to enterovirus 71
RT infection.";
RL Cell. Microbiol. 8:565-580(2006).
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=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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-147 AND LYS-434, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [14]
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 [15]
RP MALONYLATION AT LYS-434.
RX PubMed=21908771; DOI=10.1074/mcp.m111.012658;
RA Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y., He W.,
RA Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C., Dai J.,
RA Verdin E., Ye Y., Zhao Y.;
RT "The first identification of lysine malonylation substrates and its
RT regulatory enzyme.";
RL Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011).
RN [16]
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=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 [17]
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 [18]
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 [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-253, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-285, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [22]
RP STRUCTURE BY NMR OF 276-437.
RX PubMed=12766415; DOI=10.1023/a:1023504611632;
RA Vanwetswinkel S., Kriek J., Andersen G.R., Dijk J., Siegal G.;
RT "1H, 15N and 13C resonance assignments of the highly conserved 19 kDa C-
RT terminal domain from human elongation factor 1Bgamma.";
RL J. Biomol. NMR 26:189-190(2003).
CC -!- FUNCTION: Probably plays a role in anchoring the complex to other
CC cellular components.
CC -!- SUBUNIT: EF-1 is composed of four subunits: alpha, beta, delta, and
CC gamma.
CC -!- INTERACTION:
CC P26641; Q8WUW1: BRK1; NbExp=3; IntAct=EBI-351467, EBI-2837444;
CC P26641; P24534: EEF1B2; NbExp=9; IntAct=EBI-351467, EBI-354334;
CC P26641; P29692: EEF1D; NbExp=4; IntAct=EBI-351467, EBI-358607;
CC P26641; P29692-2: EEF1D; NbExp=4; IntAct=EBI-351467, EBI-5280572;
CC P26641; Q04695: KRT17; NbExp=2; IntAct=EBI-351467, EBI-297873;
CC P26641; Q9HB07: MYG1; NbExp=3; IntAct=EBI-351467, EBI-709754;
CC P26641; Q16512: PKN1; NbExp=3; IntAct=EBI-351467, EBI-602382;
CC P26641; Q969Q1: TRIM63; NbExp=2; IntAct=EBI-351467, EBI-5661333;
CC P26641; P14679-2: TYR; NbExp=3; IntAct=EBI-351467, EBI-25894402;
CC P26641; P31930: UQCRC1; NbExp=3; IntAct=EBI-351467, EBI-1052596;
CC P26641-2; P24534: EEF1B2; NbExp=3; IntAct=EBI-10177695, EBI-354334;
CC P26641-2; P29692: EEF1D; NbExp=3; IntAct=EBI-10177695, EBI-358607;
CC P26641-2; P29692-2: EEF1D; NbExp=3; IntAct=EBI-10177695, EBI-5280572;
CC P26641-2; Q658K8: EEF1DP3; NbExp=4; IntAct=EBI-10177695, EBI-10248874;
CC P26641-2; O94889: KLHL18; NbExp=3; IntAct=EBI-10177695, EBI-2510096;
CC P26641-2; Q9HBL7: PLGRKT; NbExp=3; IntAct=EBI-10177695, EBI-714824;
CC P26641-2; P78332: RBM6; NbExp=3; IntAct=EBI-10177695, EBI-2692323;
CC P26641-2; F4ZW62; NbExp=3; IntAct=EBI-10177695, EBI-10177680;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P26641-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P26641-2; Sequence=VSP_056204;
CC -!- TISSUE SPECIFICITY: Highly expressed in pancreatic tumor tissue and to
CC a lesser extent in normal kidney, intestine, pancreas, stomach, lung,
CC brain, spleen and liver.
CC -!- INDUCTION: Down-regulated in response to enterovirus 71 (EV71)
CC infection. {ECO:0000269|PubMed:16548883}.
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DR EMBL; X63526; CAA45089.1; -; mRNA.
DR EMBL; Z11531; CAA77630.1; -; mRNA.
DR EMBL; AK300203; BAG61974.1; -; mRNA.
DR EMBL; AP001363; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP002990; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000384; AAH00384.1; -; mRNA.
DR EMBL; BC006509; AAH06509.1; -; mRNA.
DR EMBL; BC006520; AAH06520.1; -; mRNA.
DR EMBL; BC007949; AAH07949.2; -; mRNA.
DR EMBL; BC009865; AAH09865.1; -; mRNA.
DR EMBL; BC013918; AAH13918.1; -; mRNA.
DR EMBL; BC015813; AAH15813.1; -; mRNA.
DR EMBL; BC021974; AAH21974.2; -; mRNA.
DR EMBL; BC028179; AAH28179.1; -; mRNA.
DR EMBL; BC031012; AAH31012.1; -; mRNA.
DR EMBL; BC067738; AAH67738.1; -; mRNA.
DR EMBL; M55409; AAC18414.1; -; mRNA.
DR EMBL; AF119850; AAF69604.1; -; mRNA.
DR CCDS; CCDS44626.1; -. [P26641-1]
DR PIR; S22655; S22655.
DR RefSeq; NP_001395.1; NM_001404.4. [P26641-1]
DR PDB; 1PBU; NMR; -; A=276-437.
DR PDB; 5DQS; X-ray; 2.10 A; A=2-218.
DR PDB; 5JPO; X-ray; 2.00 A; A/B/C/D=1-218.
DR PDBsum; 1PBU; -.
DR PDBsum; 5DQS; -.
DR PDBsum; 5JPO; -.
DR AlphaFoldDB; P26641; -.
DR BMRB; P26641; -.
DR SMR; P26641; -.
DR BioGRID; 108257; 325.
DR CORUM; P26641; -.
DR DIP; DIP-32516N; -.
DR IntAct; P26641; 219.
DR MINT; P26641; -.
DR STRING; 9606.ENSP00000331901; -.
DR ChEMBL; CHEMBL4295735; -.
DR GlyGen; P26641; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P26641; -.
DR MetOSite; P26641; -.
DR PhosphoSitePlus; P26641; -.
DR SwissPalm; P26641; -.
DR BioMuta; EEF1G; -.
DR DMDM; 119165; -.
DR OGP; P26641; -.
DR EPD; P26641; -.
DR jPOST; P26641; -.
DR MassIVE; P26641; -.
DR MaxQB; P26641; -.
DR PaxDb; P26641; -.
DR PeptideAtlas; P26641; -.
DR PRIDE; P26641; -.
DR ProteomicsDB; 5107; -.
DR ProteomicsDB; 54359; -. [P26641-1]
DR TopDownProteomics; P26641-1; -. [P26641-1]
DR Antibodypedia; 52234; 378 antibodies from 30 providers.
DR DNASU; 1937; -.
DR Ensembl; ENST00000329251.5; ENSP00000331901.4; ENSG00000254772.10. [P26641-1]
DR GeneID; 1937; -.
DR KEGG; hsa:1937; -.
DR MANE-Select; ENST00000329251.5; ENSP00000331901.4; NM_001404.5; NP_001395.1.
DR CTD; 1937; -.
DR DisGeNET; 1937; -.
DR GeneCards; EEF1G; -.
DR HGNC; HGNC:3213; EEF1G.
DR HPA; ENSG00000254772; Low tissue specificity.
DR MIM; 130593; gene.
DR neXtProt; NX_P26641; -.
DR OpenTargets; ENSG00000254772; -.
DR PharmGKB; PA27649; -.
DR VEuPathDB; HostDB:ENSG00000254772; -.
DR eggNOG; KOG0867; Eukaryota.
DR eggNOG; KOG1627; Eukaryota.
DR GeneTree; ENSGT00390000007552; -.
DR HOGENOM; CLU_011226_3_1_1; -.
DR InParanoid; P26641; -.
DR OMA; TRWYETI; -.
DR PhylomeDB; P26641; -.
DR TreeFam; TF314343; -.
DR PathwayCommons; P26641; -.
DR Reactome; R-HSA-156842; Eukaryotic Translation Elongation.
DR Reactome; R-HSA-9725370; Signaling by ALK fusions and activated point mutants.
DR SignaLink; P26641; -.
DR BioGRID-ORCS; 1937; 565 hits in 1084 CRISPR screens.
DR ChiTaRS; EEF1G; human.
DR EvolutionaryTrace; P26641; -.
DR GeneWiki; EEF1G; -.
DR GenomeRNAi; 1937; -.
DR Pharos; P26641; Tbio.
DR PRO; PR:P26641; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P26641; protein.
DR Bgee; ENSG00000254772; Expressed in cortical plate and 101 other tissues.
DR ExpressionAtlas; P26641; baseline and differential.
DR Genevisible; P26641; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
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; IEP:UniProtKB.
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 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing;
KW Elongation factor; Isopeptide bond; Protein biosynthesis;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801, ECO:0000269|Ref.7,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..437
FT /note="Elongation factor 1-gamma"
FT /id="PRO_0000208813"
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:0000269|Ref.7, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 147
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 212
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9D8N0"
FT MOD_RES 401
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9D8N0"
FT MOD_RES 434
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 434
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21908771"
FT CROSSLNK 253
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 285
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..4
FT /note="MAAG -> MAERWVAPAVLRRARFASTFFLSPQIYAHKDGDLRSAFFILSFK
FT RGEFIPFLNW (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056204"
FT CONFLICT 102
FT /note="A -> V (in Ref. 5; AAH13918)"
FT /evidence="ECO:0000305"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:5JPO"
FT HELIX 13..25
FT /evidence="ECO:0007829|PDB:5JPO"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:5JPO"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:5JPO"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:5JPO"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:5JPO"
FT HELIX 47..52
FT /evidence="ECO:0007829|PDB:5JPO"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:5JPO"
FT HELIX 72..78
FT /evidence="ECO:0007829|PDB:5JPO"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:5JPO"
FT HELIX 89..105
FT /evidence="ECO:0007829|PDB:5JPO"
FT HELIX 107..117
FT /evidence="ECO:0007829|PDB:5JPO"
FT HELIX 125..145
FT /evidence="ECO:0007829|PDB:5JPO"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:5JPO"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:5JPO"
FT HELIX 159..174
FT /evidence="ECO:0007829|PDB:5JPO"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:5JPO"
FT HELIX 185..195
FT /evidence="ECO:0007829|PDB:5JPO"
FT HELIX 198..204
FT /evidence="ECO:0007829|PDB:5JPO"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:1PBU"
FT HELIX 290..299
FT /evidence="ECO:0007829|PDB:1PBU"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:1PBU"
FT HELIX 306..311
FT /evidence="ECO:0007829|PDB:1PBU"
FT TURN 316..318
FT /evidence="ECO:0007829|PDB:1PBU"
FT STRAND 320..324
FT /evidence="ECO:0007829|PDB:1PBU"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:1PBU"
FT HELIX 338..348
FT /evidence="ECO:0007829|PDB:1PBU"
FT HELIX 349..351
FT /evidence="ECO:0007829|PDB:1PBU"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:1PBU"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:1PBU"
FT STRAND 361..364
FT /evidence="ECO:0007829|PDB:1PBU"
FT STRAND 370..381
FT /evidence="ECO:0007829|PDB:1PBU"
FT HELIX 384..386
FT /evidence="ECO:0007829|PDB:1PBU"
FT HELIX 388..390
FT /evidence="ECO:0007829|PDB:1PBU"
FT HELIX 394..396
FT /evidence="ECO:0007829|PDB:1PBU"
FT HELIX 408..418
FT /evidence="ECO:0007829|PDB:1PBU"
FT TURN 424..426
FT /evidence="ECO:0007829|PDB:1PBU"
SQ SEQUENCE 437 AA; 50119 MW; A6110663110CF3FC CRC64;
MAAGTLYTYP ENWRAFKALI AAQYSGAQVR VLSAPPHFHF GQTNRTPEFL RKFPAGKVPA
FEGDDGFCVF ESNAIAYYVS NEELRGSTPE AAAQVVQWVS FADSDIVPPA STWVFPTLGI
MHHNKQATEN AKEEVRRILG LLDAYLKTRT FLVGERVTLA DITVVCTLLW LYKQVLEPSF
RQAFPNTNRW FLTCINQPQF RAVLGEVKLC EKMAQFDAKK FAETQPKKDT PRKEKGSREE
KQKPQAERKE EKKAAAPAPE EEMDECEQAL AAEPKAKDPF AHLPKSTFVL DEFKRKYSNE
DTLSVALPYF WEHFDKDGWS LWYSEYRFPE ELTQTFMSCN LITGMFQRLD KLRKNAFASV
ILFGTNNSSS ISGVWVFRGQ ELAFPLSPDW QVDYESYTWR KLDPGSEETQ TLVREYFSWE
GAFQHVGKAF NQGKIFK
