Full text data of EEF1G
EEF1G
(EF1G)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Elongation factor 1-gamma; EF-1-gamma (eEF-1B gamma)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Elongation factor 1-gamma; EF-1-gamma (eEF-1B gamma)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P26641
ID EF1G_HUMAN Reviewed; 437 AA.
AC P26641; Q6PJ62; Q6PK31; Q96CU2; Q9P196;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 156.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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
RT oncogenic transformation.";
RL Nucleic Acids Res. 20:5907-5910(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
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
RT protein L19.";
RL Nucleic Acids Res. 20:2598-2598(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
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.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [5]
RP PROTEIN SEQUENCE OF 2-14, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (OCT-2004) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 80-437.
RC TISSUE=Pancreatic carcinoma;
RX PubMed=1372736;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 121-437.
RC TISSUE=Fetal liver;
RA Zhang C., Yu Y., Zhang S., Wei H., Zhang Y., Zhou G., Bi J., Liu M.,
RA He F.;
RT "Functional prediction of the coding sequences of 79 new genes deduced
RT by analysis of cDNA clones from human fetal liver.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP INDUCTION, AND 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
RT reveal differential cellular gene expression in response to
RT enterovirus 71 infection.";
RL Cell. Microbiol. 8:565-580(2006).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-147 AND LYS-434, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [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.,
RA Buerckstuemmer T., 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 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.,
RA He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,
RA Dai J., 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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
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
RT C-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,
CC and gamma.
CC -!- INTERACTION:
CC P24534:EEF1B2; NbExp=3; IntAct=EBI-351467, EBI-354334;
CC P29692:EEF1D; NbExp=3; IntAct=EBI-351467, EBI-358607;
CC Q969Q1:TRIM63; NbExp=2; IntAct=EBI-351467, EBI-5661333;
CC -!- TISSUE SPECIFICITY: Highly expressed in pancreatic tumor tissue
CC and to a lesser extent in normal kidney, intestine, pancreas,
CC stomach, lung, brain, spleen and liver.
CC -!- INDUCTION: Down-regulated in response to enterovirus 71 (EV71)
CC infection.
CC -!- SIMILARITY: Contains 1 EF-1-gamma C-terminal domain.
CC -!- SIMILARITY: Contains 1 GST C-terminal domain.
CC -!- SIMILARITY: Contains 1 GST N-terminal domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X63526; CAA45089.1; -; mRNA.
DR EMBL; Z11531; CAA77630.1; -; mRNA.
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 PIR; S22655; S22655.
DR RefSeq; NP_001395.1; NM_001404.4.
DR UniGene; Hs.144835; -.
DR UniGene; Hs.444467; -.
DR PDB; 1PBU; NMR; -; A=276-437.
DR PDBsum; 1PBU; -.
DR ProteinModelPortal; P26641; -.
DR SMR; P26641; 6-202, 276-437.
DR IntAct; P26641; 110.
DR MINT; MINT-1191315; -.
DR PhosphoSite; P26641; -.
DR DMDM; 119165; -.
DR OGP; P26641; -.
DR PaxDb; P26641; -.
DR PRIDE; P26641; -.
DR DNASU; 1937; -.
DR Ensembl; ENST00000329251; ENSP00000331901; ENSG00000254772.
DR GeneID; 1937; -.
DR KEGG; hsa:1937; -.
DR UCSC; uc001ntm.1; human.
DR CTD; 1937; -.
DR GeneCards; GC11M062332; -.
DR HGNC; HGNC:3213; EEF1G.
DR HPA; HPA040688; -.
DR MIM; 130593; gene.
DR neXtProt; NX_P26641; -.
DR PharmGKB; PA27649; -.
DR eggNOG; COG0625; -.
DR HOGENOM; HOG000235245; -.
DR HOVERGEN; HBG051444; -.
DR InParanoid; P26641; -.
DR KO; K03233; -.
DR OrthoDB; EOG72G177; -.
DR PhylomeDB; P26641; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; EEF1G; human.
DR EvolutionaryTrace; P26641; -.
DR GeneWiki; EEF1G; -.
DR GenomeRNAi; 1937; -.
DR NextBio; 7847; -.
DR PRO; PR:P26641; -.
DR ArrayExpress; P26641; -.
DR CleanEx; HS_EEF1G; -.
DR Genevestigator; P26641; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; NAS:UniProtKB.
DR GO; GO:0009615; P:response to virus; IEP:UniProtKB.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.30.70.1010; -; 1.
DR Gene3D; 3.40.30.10; -; 1.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR001662; Transl_elong_EF1_G_con.
DR Pfam; PF00647; EF1G; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 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; Complete proteome;
KW Direct protein sequencing; Elongation factor; Protein biosynthesis;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 437 Elongation factor 1-gamma.
FT /FTId=PRO_0000208813.
FT DOMAIN 2 87 GST N-terminal.
FT DOMAIN 88 216 GST C-terminal.
FT DOMAIN 276 437 EF-1-gamma C-terminal.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 147 147 N6-acetyllysine.
FT MOD_RES 434 434 N6-acetyllysine; alternate.
FT MOD_RES 434 434 N6-malonyllysine; alternate.
FT CONFLICT 102 102 A -> V (in Ref. 3; AAH13918).
FT HELIX 279 281
FT HELIX 290 299
FT HELIX 302 304
FT HELIX 306 311
FT TURN 316 318
FT STRAND 320 324
FT HELIX 329 331
FT HELIX 338 348
FT HELIX 349 351
FT HELIX 353 355
FT STRAND 356 358
FT STRAND 361 364
FT STRAND 370 381
FT HELIX 384 386
FT HELIX 388 390
FT HELIX 394 396
FT HELIX 408 418
FT TURN 424 426
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
//
ID EF1G_HUMAN Reviewed; 437 AA.
AC P26641; Q6PJ62; Q6PK31; Q96CU2; Q9P196;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 156.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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
RT oncogenic transformation.";
RL Nucleic Acids Res. 20:5907-5910(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
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
RT protein L19.";
RL Nucleic Acids Res. 20:2598-2598(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
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.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [5]
RP PROTEIN SEQUENCE OF 2-14, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (OCT-2004) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 80-437.
RC TISSUE=Pancreatic carcinoma;
RX PubMed=1372736;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 121-437.
RC TISSUE=Fetal liver;
RA Zhang C., Yu Y., Zhang S., Wei H., Zhang Y., Zhou G., Bi J., Liu M.,
RA He F.;
RT "Functional prediction of the coding sequences of 79 new genes deduced
RT by analysis of cDNA clones from human fetal liver.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP INDUCTION, AND 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
RT reveal differential cellular gene expression in response to
RT enterovirus 71 infection.";
RL Cell. Microbiol. 8:565-580(2006).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-147 AND LYS-434, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [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.,
RA Buerckstuemmer T., 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 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.,
RA He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,
RA Dai J., 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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
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
RT C-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,
CC and gamma.
CC -!- INTERACTION:
CC P24534:EEF1B2; NbExp=3; IntAct=EBI-351467, EBI-354334;
CC P29692:EEF1D; NbExp=3; IntAct=EBI-351467, EBI-358607;
CC Q969Q1:TRIM63; NbExp=2; IntAct=EBI-351467, EBI-5661333;
CC -!- TISSUE SPECIFICITY: Highly expressed in pancreatic tumor tissue
CC and to a lesser extent in normal kidney, intestine, pancreas,
CC stomach, lung, brain, spleen and liver.
CC -!- INDUCTION: Down-regulated in response to enterovirus 71 (EV71)
CC infection.
CC -!- SIMILARITY: Contains 1 EF-1-gamma C-terminal domain.
CC -!- SIMILARITY: Contains 1 GST C-terminal domain.
CC -!- SIMILARITY: Contains 1 GST N-terminal domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X63526; CAA45089.1; -; mRNA.
DR EMBL; Z11531; CAA77630.1; -; mRNA.
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 PIR; S22655; S22655.
DR RefSeq; NP_001395.1; NM_001404.4.
DR UniGene; Hs.144835; -.
DR UniGene; Hs.444467; -.
DR PDB; 1PBU; NMR; -; A=276-437.
DR PDBsum; 1PBU; -.
DR ProteinModelPortal; P26641; -.
DR SMR; P26641; 6-202, 276-437.
DR IntAct; P26641; 110.
DR MINT; MINT-1191315; -.
DR PhosphoSite; P26641; -.
DR DMDM; 119165; -.
DR OGP; P26641; -.
DR PaxDb; P26641; -.
DR PRIDE; P26641; -.
DR DNASU; 1937; -.
DR Ensembl; ENST00000329251; ENSP00000331901; ENSG00000254772.
DR GeneID; 1937; -.
DR KEGG; hsa:1937; -.
DR UCSC; uc001ntm.1; human.
DR CTD; 1937; -.
DR GeneCards; GC11M062332; -.
DR HGNC; HGNC:3213; EEF1G.
DR HPA; HPA040688; -.
DR MIM; 130593; gene.
DR neXtProt; NX_P26641; -.
DR PharmGKB; PA27649; -.
DR eggNOG; COG0625; -.
DR HOGENOM; HOG000235245; -.
DR HOVERGEN; HBG051444; -.
DR InParanoid; P26641; -.
DR KO; K03233; -.
DR OrthoDB; EOG72G177; -.
DR PhylomeDB; P26641; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; EEF1G; human.
DR EvolutionaryTrace; P26641; -.
DR GeneWiki; EEF1G; -.
DR GenomeRNAi; 1937; -.
DR NextBio; 7847; -.
DR PRO; PR:P26641; -.
DR ArrayExpress; P26641; -.
DR CleanEx; HS_EEF1G; -.
DR Genevestigator; P26641; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; NAS:UniProtKB.
DR GO; GO:0009615; P:response to virus; IEP:UniProtKB.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.30.70.1010; -; 1.
DR Gene3D; 3.40.30.10; -; 1.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR001662; Transl_elong_EF1_G_con.
DR Pfam; PF00647; EF1G; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 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; Complete proteome;
KW Direct protein sequencing; Elongation factor; Protein biosynthesis;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 437 Elongation factor 1-gamma.
FT /FTId=PRO_0000208813.
FT DOMAIN 2 87 GST N-terminal.
FT DOMAIN 88 216 GST C-terminal.
FT DOMAIN 276 437 EF-1-gamma C-terminal.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 147 147 N6-acetyllysine.
FT MOD_RES 434 434 N6-acetyllysine; alternate.
FT MOD_RES 434 434 N6-malonyllysine; alternate.
FT CONFLICT 102 102 A -> V (in Ref. 3; AAH13918).
FT HELIX 279 281
FT HELIX 290 299
FT HELIX 302 304
FT HELIX 306 311
FT TURN 316 318
FT STRAND 320 324
FT HELIX 329 331
FT HELIX 338 348
FT HELIX 349 351
FT HELIX 353 355
FT STRAND 356 358
FT STRAND 361 364
FT STRAND 370 381
FT HELIX 384 386
FT HELIX 388 390
FT HELIX 394 396
FT HELIX 408 418
FT TURN 424 426
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
//
MIM
130593
*RECORD*
*FIELD* NO
130593
*FIELD* TI
*130593 EUKARYOTIC TRANSLATION ELONGATION FACTOR 1, GAMMA; EEF1G
;;ELONGATION FACTOR 1, GAMMA; EF1G;;
read moreEEF1B-GAMMA
*FIELD* TX
DESCRIPTION
Eukaryotic elongation factor-1 (EF1) consists of 4 subunits, EF1-alpha
(EEF1A1; 130590), EF1-beta (EEF1B2; 600655), EF1-gamma, and EF1-delta
(EEF1D; 130592). EIF-alpha-GTP transfers aminoacyl-tRNA to the ribosome,
and the release of animoacyl-tRNA from EIF-alpha-GTP is driven by GTP
hydrolysis. EF1-alpha-GDP is recycled to EF1-alpha-GTP by the EF1-beta,
-gamma, and -delta subunits (Sanders et al., 1996).
CLONING
Using RT-PCR with degenerate oligonucleotides based on 2 peptides
conserved between Artemia and Xenopus EF1-gamma, Sanders et al. (1992)
isolated a human fibroblast cDNA encoding EEF1G. The predicted 437-amino
acid human protein is 60% and 85% similar to the Artemia and Xenopus
proteins, respectively.
Using computer methods for protein sequence analyses, Koonin et al.
(1994) found that EEF1G contains an N-terminal domain related to the
theta class of glutathione S-transferases (GSTs; e.g., 600436). They
proposed that the GST domain in EEF1G is involved in regulating the
assembly of multisubunit complexes containing EEF1G and aminoacyl-tRNA
synthetases.
By immunofluorescence analysis, Sanders et al. (1996) found that
EF1-beta, -gamma, and -delta showed a perinuclear distribution and
colocalized with an endoplasmic reticulum resident protein in human
foreskin fibroblasts. In contrast, EF1-alpha showed strong nuclear
staining and diffuse cytoplasmic staining.
GENE FUNCTION
Using Northern blot analysis, Sanders et al. (1992) found that
expression of the Eef1g, Eef1b2, and Ef1a genes was 20-fold higher in
cultured rat cells than in rat tissues. However, oncogenic
transformation of human and rat cells did not have a major effect on EF1
mRNA levels. Sanders et al. (1992) suggested that the levels of the EF1
mRNAs rise as a result of a loss of contact inhibition, leading to the
increases seen in tumors and cultured cells.
Lew et al. (1992) found that EEF1G mRNA was expressed at higher levels
in 7 of 9 pancreatic tumors than in the corresponding normal tissues.
*FIELD* RF
1. Koonin, E. V.; Mushegian, A. R.; Tatusov, R. L.; Altschul, S. F.;
Bryant, S. H.; Bork, P.; Valencia, A.: Eukaryotic translation elongation
factor 1 gamma contains a glutathione transferase domain--study of
a diverse, ancient protein superfamily using motif search and structural
modeling. Protein Science 3: 2045-2054, 1994.
2. Lew, Y.; Jones, D. V.; Mars, W. M.; Evans, D.; Byrd, D.; Frazier,
M. L.: Expression of elongation factor-1 gamma-related sequence in
human pancreatic cancer. Pancreas 7: 144-152, 1992.
3. Sanders, J.; Brandsma, M.; Janssen, G. M. C.; Dijk, J.; Moller,
W.: Immunofluorescence studies of human fibroblasts demonstrate the
presence of the complex of elongation factor-1-beta-gamma-delta in
the endoplasmic reticulum. J. Cell Sci. 109: 1113-1117, 1996.
4. Sanders, J.; Maassen, J. A.; Moller, W.: Elongation factor-1 messenger-RNA
levels in cultured cells are high compared to tissue and are not drastically
affected further by oncogenic transformation. Nucleic Acids Res. 20:
5907-5910, 1992.
*FIELD* CN
Patricia A. Hartz - updated: 10/3/2008
Rebekah S. Rasooly - updated: 6/17/1998
*FIELD* CD
Victor A. McKusick: 7/12/1991
*FIELD* ED
mgross: 10/08/2008
terry: 10/3/2008
mgross: 6/3/2008
terry: 8/11/1998
psherman: 6/17/1998
mark: 4/1/1996
mark: 8/7/1995
carol: 3/1/1995
supermim: 3/16/1992
carol: 7/12/1991
*RECORD*
*FIELD* NO
130593
*FIELD* TI
*130593 EUKARYOTIC TRANSLATION ELONGATION FACTOR 1, GAMMA; EEF1G
;;ELONGATION FACTOR 1, GAMMA; EF1G;;
read moreEEF1B-GAMMA
*FIELD* TX
DESCRIPTION
Eukaryotic elongation factor-1 (EF1) consists of 4 subunits, EF1-alpha
(EEF1A1; 130590), EF1-beta (EEF1B2; 600655), EF1-gamma, and EF1-delta
(EEF1D; 130592). EIF-alpha-GTP transfers aminoacyl-tRNA to the ribosome,
and the release of animoacyl-tRNA from EIF-alpha-GTP is driven by GTP
hydrolysis. EF1-alpha-GDP is recycled to EF1-alpha-GTP by the EF1-beta,
-gamma, and -delta subunits (Sanders et al., 1996).
CLONING
Using RT-PCR with degenerate oligonucleotides based on 2 peptides
conserved between Artemia and Xenopus EF1-gamma, Sanders et al. (1992)
isolated a human fibroblast cDNA encoding EEF1G. The predicted 437-amino
acid human protein is 60% and 85% similar to the Artemia and Xenopus
proteins, respectively.
Using computer methods for protein sequence analyses, Koonin et al.
(1994) found that EEF1G contains an N-terminal domain related to the
theta class of glutathione S-transferases (GSTs; e.g., 600436). They
proposed that the GST domain in EEF1G is involved in regulating the
assembly of multisubunit complexes containing EEF1G and aminoacyl-tRNA
synthetases.
By immunofluorescence analysis, Sanders et al. (1996) found that
EF1-beta, -gamma, and -delta showed a perinuclear distribution and
colocalized with an endoplasmic reticulum resident protein in human
foreskin fibroblasts. In contrast, EF1-alpha showed strong nuclear
staining and diffuse cytoplasmic staining.
GENE FUNCTION
Using Northern blot analysis, Sanders et al. (1992) found that
expression of the Eef1g, Eef1b2, and Ef1a genes was 20-fold higher in
cultured rat cells than in rat tissues. However, oncogenic
transformation of human and rat cells did not have a major effect on EF1
mRNA levels. Sanders et al. (1992) suggested that the levels of the EF1
mRNAs rise as a result of a loss of contact inhibition, leading to the
increases seen in tumors and cultured cells.
Lew et al. (1992) found that EEF1G mRNA was expressed at higher levels
in 7 of 9 pancreatic tumors than in the corresponding normal tissues.
*FIELD* RF
1. Koonin, E. V.; Mushegian, A. R.; Tatusov, R. L.; Altschul, S. F.;
Bryant, S. H.; Bork, P.; Valencia, A.: Eukaryotic translation elongation
factor 1 gamma contains a glutathione transferase domain--study of
a diverse, ancient protein superfamily using motif search and structural
modeling. Protein Science 3: 2045-2054, 1994.
2. Lew, Y.; Jones, D. V.; Mars, W. M.; Evans, D.; Byrd, D.; Frazier,
M. L.: Expression of elongation factor-1 gamma-related sequence in
human pancreatic cancer. Pancreas 7: 144-152, 1992.
3. Sanders, J.; Brandsma, M.; Janssen, G. M. C.; Dijk, J.; Moller,
W.: Immunofluorescence studies of human fibroblasts demonstrate the
presence of the complex of elongation factor-1-beta-gamma-delta in
the endoplasmic reticulum. J. Cell Sci. 109: 1113-1117, 1996.
4. Sanders, J.; Maassen, J. A.; Moller, W.: Elongation factor-1 messenger-RNA
levels in cultured cells are high compared to tissue and are not drastically
affected further by oncogenic transformation. Nucleic Acids Res. 20:
5907-5910, 1992.
*FIELD* CN
Patricia A. Hartz - updated: 10/3/2008
Rebekah S. Rasooly - updated: 6/17/1998
*FIELD* CD
Victor A. McKusick: 7/12/1991
*FIELD* ED
mgross: 10/08/2008
terry: 10/3/2008
mgross: 6/3/2008
terry: 8/11/1998
psherman: 6/17/1998
mark: 4/1/1996
mark: 8/7/1995
carol: 3/1/1995
supermim: 3/16/1992
carol: 7/12/1991