ID   EF1G_HUMAN              Reviewed;         437 AA.
AC   P26641; Q6PJ62; Q6PK31; Q96CU2; Q9P196;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   11-SEP-2007, entry version 92.
DE   Elongation factor 1-gamma (EF-1-gamma) (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   MEDLINE=93096576; 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   MEDLINE=92285147; 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   MEDLINE=22608298; 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   MEDLINE=92204908; 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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-43, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Epithelium;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [9]
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=2; IntAct=EBI-351467, EBI-354334;
CC       Q92597:NDRG1; NbExp=1; IntAct=EBI-351467, EBI-716486;
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   -!- SIMILARITY: Contains 1 EF-1-gamma C-terminal domain.
CC   -!- SIMILARITY: Contains 1 GST-like domain.
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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   UniGene; Hs.144835; -.
DR   PDB; 1PBU; NMR; A=276-437.
DR   IntAct; P26641; -.
DR   OGP; P26641; -.
DR   REPRODUCTION-2DPAGE; P26641; HUMAN.
DR   Ensembl; ENSG00000186676; Homo sapiens.
DR   KEGG; hsa:1937; -.
DR   H-InvDB; HIX0020040; -.
DR   HGNC; HGNC:3213; EEF1G.
DR   MIM; 130593; gene.
DR   PharmGKB; PA27649; -.
DR   Reactome; REACT_71.1; Gene Expression.
DR   LinkHub; P26641; -.
DR   ArrayExpress; P26641; -.
DR   GermOnline; ENSG00000186676; Homo sapiens.
DR   GO; GO:0005622; C:intracellular; NAS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0003746; F:translation elongation factor activity; NAS:UniProtKB.
DR   GO; GO:0006414; P:translational elongation; NAS:UniProtKB.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR010987; GST_C_like.
DR   InterPro; IPR004045; GST_N.
DR   InterPro; IPR001662; Transl_elong_EF1_G_con.
DR   Gene3D; G3DSA:1.20.1050.10; GST_C_like; 1.
DR   Gene3D; G3DSA:3.30.70.1010; Transl_elong_EF1_G_con; 1.
DR   Pfam; PF00647; EF1G; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   ProDom; PD006217; EF1_G; 1.
DR   PROSITE; PS50040; EF1G_C; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Direct protein sequencing;
KW   Elongation factor; Phosphorylation; Protein biosynthesis.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    437       Elongation factor 1-gamma.
FT                                /FTId=PRO_0000208813.
FT   DOMAIN        2    198       GST-like.
FT   DOMAIN      276    437       EF-1-gamma C-terminal.
FT   MOD_RES       2      2       N-acetylalanine.
FT   MOD_RES      43     43       Phosphothreonine.
FT   CONFLICT    102    102       A -> V (in Ref. 3; AAH13918).
FT   HELIX       278    280
FT   HELIX       289    298
FT   HELIX       301    303
FT   HELIX       305    310
FT   TURN        315    317
FT   STRAND      319    323
FT   HELIX       328    330
FT   HELIX       337    347
FT   HELIX       348    350
FT   HELIX       352    354
FT   STRAND      355    357
FT   STRAND      360    363
FT   STRAND      369    380
FT   HELIX       383    385
FT   HELIX       387    389
FT   HELIX       393    395
FT   HELIX       407    417
FT   TURN        423    425
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
//