Full text data of EEF2
EEF2
(EF2)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Elongation factor 2; EF-2
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Elongation factor 2; EF-2
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P13639
ID EF2_HUMAN Reviewed; 858 AA.
AC P13639; B2RMP5; D6W618; Q58J86;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 155.
DE RecName: Full=Elongation factor 2;
DE Short=EF-2;
GN Name=EEF2; Synonyms=EF2;
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].
RC TISSUE=Ovary;
RX PubMed=2610926;
RA Rapp G., Klaudiny J., Hagendorff G., Luck M.R., Heinz K.;
RT "Complete sequence of the coding region of human elongation factor 2
RT (EF-2) by enzymatic amplification of cDNA from human ovarian granulosa
RT cells.";
RL Biol. Chem. Hoppe-Seyler 370:1071-1075(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1596361;
RA Hanes J., Freudenstein J., Rapp G., Scheit K.H.;
RT "Construction of a plasmid containing the complete coding region of
RT human elongation factor 2.";
RL Biol. Chem. Hoppe-Seyler 373:201-204(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Peripheral blood;
RA Ustek D., Bektas M., Cakiris A., Oku B., Bermek E.;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 501-858.
RX PubMed=2840927;
RA Rapp G., Mucha J., Einspanier R., Luck M., Scheit K.H.;
RT "Cloning and sequence analysis of a cDNA from human ovarian granulosa
RT cells encoding the C-terminal part of human elongation factor 2.";
RL Biol. Chem. Hoppe-Seyler 369:247-250(1988).
RN [7]
RP PROTEIN SEQUENCE OF 796-801, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Vishwanath V.;
RL Submitted (MAR-2007) to UniProtKB.
RN [8]
RP CLEAVAGE OF INITIATOR METHIONINE.
RA Bienvenut W.V.;
RL Submitted (AUG-2001) to UniProtKB.
RN [9]
RP ISGYLATION.
RX PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
RA Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
RA Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
RT "Proteomic identification of proteins conjugated to ISG15 in mouse and
RT human cells.";
RL Biochem. Biophys. Res. Commun. 336:496-506(2005).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-435 AND SER-502, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [13]
RP IDENTIFICATION IN THE SURF COMPLEX.
RX PubMed=19417104; DOI=10.1101/gad.1767209;
RA Yamashita A., Izumi N., Kashima I., Ohnishi T., Saari B.,
RA Katsuhata Y., Muramatsu R., Morita T., Iwamatsu A., Hachiya T.,
RA Kurata R., Hirano H., Anderson P., Ohno S.;
RT "SMG-8 and SMG-9, two novel subunits of the SMG-1 complex, regulate
RT remodeling of the mRNA surveillance complex during nonsense-mediated
RT mRNA decay.";
RL Genes Dev. 23:1091-1105(2009).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-235; LYS-239; LYS-272;
RP LYS-275 AND LYS-445, AND MASS 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-57; THR-59 AND THR-435,
RP AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-54; THR-57 AND THR-59,
RP AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [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.,
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).
CC -!- FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step
CC during translation elongation. During this step, the ribosome
CC changes from the pre-translocational (PRE) to the post-
CC translocational (POST) state as the newly formed A-site-bound
CC peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E
CC sites, respectively. Catalyzes the coordinated movement of the two
CC tRNA molecules, the mRNA and conformational changes in the
CC ribosome.
CC -!- SUBUNIT: Component of the mRNA surveillance SURF complex, at least
CC composed of ERF1, ERF3 (ERF3A or ERF3B), EEF2, UPF1/RENT1, SMG1,
CC SMG8 and SMG9.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- PTM: Phosphorylation by EF-2 kinase completely inactivates EF-2.
CC -!- PTM: Diphthamide is 2-[3-carboxyamido-3-(trimethyl-
CC ammonio)propyl]histidine. Diphthamide can be ADP-ribosylated by
CC diphtheria toxin and by Pseudomonas exotoxin A, thus arresting
CC protein synthesis.
CC -!- PTM: ISGylated.
CC -!- SIMILARITY: Belongs to the GTP-binding elongation factor family.
CC EF-G/EF-2 subfamily.
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DR EMBL; X51466; CAA35829.1; -; mRNA.
DR EMBL; Z11692; CAA77750.1; -; mRNA.
DR EMBL; AY942181; AAX34409.1; -; mRNA.
DR EMBL; CH471139; EAW69274.1; -; Genomic_DNA.
DR EMBL; CH471139; EAW69275.1; -; Genomic_DNA.
DR EMBL; BC126259; AAI26260.1; -; mRNA.
DR EMBL; BC136313; AAI36314.1; -; mRNA.
DR EMBL; M19997; AAA50388.1; -; mRNA.
DR PIR; S18294; EFHU2.
DR RefSeq; NP_001952.1; NM_001961.3.
DR UniGene; Hs.515070; -.
DR PDB; 3J3A; EM; 5.00 A; z=1-858.
DR PDBsum; 3J3A; -.
DR ProteinModelPortal; P13639; -.
DR SMR; P13639; 3-858.
DR IntAct; P13639; 45.
DR MINT; MINT-4999025; -.
DR STRING; 9606.ENSP00000307940; -.
DR ChEMBL; CHEMBL1795108; -.
DR PhosphoSite; P13639; -.
DR DMDM; 119172; -.
DR REPRODUCTION-2DPAGE; IPI00186290; -.
DR PaxDb; P13639; -.
DR PeptideAtlas; P13639; -.
DR PRIDE; P13639; -.
DR DNASU; 1938; -.
DR Ensembl; ENST00000309311; ENSP00000307940; ENSG00000167658.
DR GeneID; 1938; -.
DR KEGG; hsa:1938; -.
DR UCSC; uc002lze.3; human.
DR CTD; 1938; -.
DR GeneCards; GC19M003976; -.
DR HGNC; HGNC:3214; EEF2.
DR HPA; CAB007795; -.
DR MIM; 130610; gene.
DR neXtProt; NX_P13639; -.
DR PharmGKB; PA27650; -.
DR eggNOG; COG0480; -.
DR HOGENOM; HOG000231589; -.
DR HOVERGEN; HBG001838; -.
DR InParanoid; P13639; -.
DR KO; K03234; -.
DR OMA; YACCLTA; -.
DR OrthoDB; EOG7WDN1S; -.
DR PhylomeDB; P13639; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; EEF2; human.
DR GeneWiki; EEF2; -.
DR GenomeRNAi; 1938; -.
DR NextBio; 7853; -.
DR PRO; PR:P13639; -.
DR ArrayExpress; P13639; -.
DR Bgee; P13639; -.
DR CleanEx; HS_EEF2; -.
DR Genevestigator; P13639; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005844; C:polysome; IEA:Ensembl.
DR GO; GO:0030529; C:ribonucleoprotein complex; IDA:MGI.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:Ensembl.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0006414; P:translational elongation; TAS:Reactome.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.240; -; 1.
DR InterPro; IPR000795; EF_GTP-bd_dom.
DR InterPro; IPR009022; EFG_III-V.
DR InterPro; IPR000640; EFG_V.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel.
DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR InterPro; IPR004161; Transl_elong_EFTu/EF1A_2.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF14492; EFG_II; 1.
DR Pfam; PF03764; EFG_IV; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00838; EFG_C; 1.
DR SMART; SM00889; EFG_IV; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF54980; SSF54980; 2.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00301; EFACTOR_GTP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Elongation factor; GTP-binding;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 858 Elongation factor 2.
FT /FTId=PRO_0000091000.
FT NP_BIND 26 33 GTP (By similarity).
FT NP_BIND 104 108 GTP (By similarity).
FT NP_BIND 158 161 GTP (By similarity).
FT MOD_RES 54 54 Phosphothreonine.
FT MOD_RES 57 57 Phosphothreonine.
FT MOD_RES 59 59 Phosphothreonine.
FT MOD_RES 235 235 N6-acetyllysine.
FT MOD_RES 239 239 N6-acetyllysine.
FT MOD_RES 272 272 N6-acetyllysine.
FT MOD_RES 275 275 N6-acetyllysine.
FT MOD_RES 435 435 Phosphothreonine.
FT MOD_RES 445 445 N6-acetyllysine.
FT MOD_RES 502 502 Phosphoserine.
FT MOD_RES 715 715 Diphthamide.
SQ SEQUENCE 858 AA; 95338 MW; 78BD1710236C0D9C CRC64;
MVNFTVDQIR AIMDKKANIR NMSVIAHVDH GKSTLTDSLV CKAGIIASAR AGETRFTDTR
KDEQERCITI KSTAISLFYE LSENDLNFIK QSKDGAGFLI NLIDSPGHVD FSSEVTAALR
VTDGALVVVD CVSGVCVQTE TVLRQAIAER IKPVLMMNKM DRALLELQLE PEELYQTFQR
IVENVNVIIS TYGEGESGPM GNIMIDPVLG TVGFGSGLHG WAFTLKQFAE MYVAKFAAKG
EGQLGPAERA KKVEDMMKKL WGDRYFDPAN GKFSKSATSP EGKKLPRTFC QLILDPIFKV
FDAIMNFKKE ETAKLIEKLD IKLDSEDKDK EGKPLLKAVM RRWLPAGDAL LQMITIHLPS
PVTAQKYRCE LLYEGPPDDE AAMGIKSCDP KGPLMMYISK MVPTSDKGRF YAFGRVFSGL
VSTGLKVRIM GPNYTPGKKE DLYLKPIQRT ILMMGRYVEP IEDVPCGNIV GLVGVDQFLV
KTGTITTFEH AHNMRVMKFS VSPVVRVAVE AKNPADLPKL VEGLKRLAKS DPMVQCIIEE
SGEHIIAGAG ELHLEICLKD LEEDHACIPI KKSDPVVSYR ETVSEESNVL CLSKSPNKHN
RLYMKARPFP DGLAEDIDKG EVSARQELKQ RARYLAEKYE WDVAEARKIW CFGPDGTGPN
ILTDITKGVQ YLNEIKDSVV AGFQWATKEG ALCEENMRGV RFDVHDVTLH ADAIHRGGGQ
IIPTARRCLY ASVLTAQPRL MEPIYLVEIQ CPEQVVGGIY GVLNRKRGHV FEESQVAGTP
MFVVKAYLPV NESFGFTADL RSNTGGQAFP QCVFDHWQIL PGDPFDNSSR PSQVVAETRK
RKGLKEGIPA LDNFLDKL
//
ID EF2_HUMAN Reviewed; 858 AA.
AC P13639; B2RMP5; D6W618; Q58J86;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 155.
DE RecName: Full=Elongation factor 2;
DE Short=EF-2;
GN Name=EEF2; Synonyms=EF2;
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].
RC TISSUE=Ovary;
RX PubMed=2610926;
RA Rapp G., Klaudiny J., Hagendorff G., Luck M.R., Heinz K.;
RT "Complete sequence of the coding region of human elongation factor 2
RT (EF-2) by enzymatic amplification of cDNA from human ovarian granulosa
RT cells.";
RL Biol. Chem. Hoppe-Seyler 370:1071-1075(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1596361;
RA Hanes J., Freudenstein J., Rapp G., Scheit K.H.;
RT "Construction of a plasmid containing the complete coding region of
RT human elongation factor 2.";
RL Biol. Chem. Hoppe-Seyler 373:201-204(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Peripheral blood;
RA Ustek D., Bektas M., Cakiris A., Oku B., Bermek E.;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 501-858.
RX PubMed=2840927;
RA Rapp G., Mucha J., Einspanier R., Luck M., Scheit K.H.;
RT "Cloning and sequence analysis of a cDNA from human ovarian granulosa
RT cells encoding the C-terminal part of human elongation factor 2.";
RL Biol. Chem. Hoppe-Seyler 369:247-250(1988).
RN [7]
RP PROTEIN SEQUENCE OF 796-801, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Vishwanath V.;
RL Submitted (MAR-2007) to UniProtKB.
RN [8]
RP CLEAVAGE OF INITIATOR METHIONINE.
RA Bienvenut W.V.;
RL Submitted (AUG-2001) to UniProtKB.
RN [9]
RP ISGYLATION.
RX PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
RA Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
RA Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
RT "Proteomic identification of proteins conjugated to ISG15 in mouse and
RT human cells.";
RL Biochem. Biophys. Res. Commun. 336:496-506(2005).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-435 AND SER-502, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [13]
RP IDENTIFICATION IN THE SURF COMPLEX.
RX PubMed=19417104; DOI=10.1101/gad.1767209;
RA Yamashita A., Izumi N., Kashima I., Ohnishi T., Saari B.,
RA Katsuhata Y., Muramatsu R., Morita T., Iwamatsu A., Hachiya T.,
RA Kurata R., Hirano H., Anderson P., Ohno S.;
RT "SMG-8 and SMG-9, two novel subunits of the SMG-1 complex, regulate
RT remodeling of the mRNA surveillance complex during nonsense-mediated
RT mRNA decay.";
RL Genes Dev. 23:1091-1105(2009).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-235; LYS-239; LYS-272;
RP LYS-275 AND LYS-445, AND MASS 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-57; THR-59 AND THR-435,
RP AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-54; THR-57 AND THR-59,
RP AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [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.,
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).
CC -!- FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step
CC during translation elongation. During this step, the ribosome
CC changes from the pre-translocational (PRE) to the post-
CC translocational (POST) state as the newly formed A-site-bound
CC peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E
CC sites, respectively. Catalyzes the coordinated movement of the two
CC tRNA molecules, the mRNA and conformational changes in the
CC ribosome.
CC -!- SUBUNIT: Component of the mRNA surveillance SURF complex, at least
CC composed of ERF1, ERF3 (ERF3A or ERF3B), EEF2, UPF1/RENT1, SMG1,
CC SMG8 and SMG9.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- PTM: Phosphorylation by EF-2 kinase completely inactivates EF-2.
CC -!- PTM: Diphthamide is 2-[3-carboxyamido-3-(trimethyl-
CC ammonio)propyl]histidine. Diphthamide can be ADP-ribosylated by
CC diphtheria toxin and by Pseudomonas exotoxin A, thus arresting
CC protein synthesis.
CC -!- PTM: ISGylated.
CC -!- SIMILARITY: Belongs to the GTP-binding elongation factor family.
CC EF-G/EF-2 subfamily.
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DR EMBL; X51466; CAA35829.1; -; mRNA.
DR EMBL; Z11692; CAA77750.1; -; mRNA.
DR EMBL; AY942181; AAX34409.1; -; mRNA.
DR EMBL; CH471139; EAW69274.1; -; Genomic_DNA.
DR EMBL; CH471139; EAW69275.1; -; Genomic_DNA.
DR EMBL; BC126259; AAI26260.1; -; mRNA.
DR EMBL; BC136313; AAI36314.1; -; mRNA.
DR EMBL; M19997; AAA50388.1; -; mRNA.
DR PIR; S18294; EFHU2.
DR RefSeq; NP_001952.1; NM_001961.3.
DR UniGene; Hs.515070; -.
DR PDB; 3J3A; EM; 5.00 A; z=1-858.
DR PDBsum; 3J3A; -.
DR ProteinModelPortal; P13639; -.
DR SMR; P13639; 3-858.
DR IntAct; P13639; 45.
DR MINT; MINT-4999025; -.
DR STRING; 9606.ENSP00000307940; -.
DR ChEMBL; CHEMBL1795108; -.
DR PhosphoSite; P13639; -.
DR DMDM; 119172; -.
DR REPRODUCTION-2DPAGE; IPI00186290; -.
DR PaxDb; P13639; -.
DR PeptideAtlas; P13639; -.
DR PRIDE; P13639; -.
DR DNASU; 1938; -.
DR Ensembl; ENST00000309311; ENSP00000307940; ENSG00000167658.
DR GeneID; 1938; -.
DR KEGG; hsa:1938; -.
DR UCSC; uc002lze.3; human.
DR CTD; 1938; -.
DR GeneCards; GC19M003976; -.
DR HGNC; HGNC:3214; EEF2.
DR HPA; CAB007795; -.
DR MIM; 130610; gene.
DR neXtProt; NX_P13639; -.
DR PharmGKB; PA27650; -.
DR eggNOG; COG0480; -.
DR HOGENOM; HOG000231589; -.
DR HOVERGEN; HBG001838; -.
DR InParanoid; P13639; -.
DR KO; K03234; -.
DR OMA; YACCLTA; -.
DR OrthoDB; EOG7WDN1S; -.
DR PhylomeDB; P13639; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; EEF2; human.
DR GeneWiki; EEF2; -.
DR GenomeRNAi; 1938; -.
DR NextBio; 7853; -.
DR PRO; PR:P13639; -.
DR ArrayExpress; P13639; -.
DR Bgee; P13639; -.
DR CleanEx; HS_EEF2; -.
DR Genevestigator; P13639; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005844; C:polysome; IEA:Ensembl.
DR GO; GO:0030529; C:ribonucleoprotein complex; IDA:MGI.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:Ensembl.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0006414; P:translational elongation; TAS:Reactome.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.240; -; 1.
DR InterPro; IPR000795; EF_GTP-bd_dom.
DR InterPro; IPR009022; EFG_III-V.
DR InterPro; IPR000640; EFG_V.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel.
DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR InterPro; IPR004161; Transl_elong_EFTu/EF1A_2.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF14492; EFG_II; 1.
DR Pfam; PF03764; EFG_IV; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00838; EFG_C; 1.
DR SMART; SM00889; EFG_IV; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF54980; SSF54980; 2.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00301; EFACTOR_GTP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Elongation factor; GTP-binding;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 858 Elongation factor 2.
FT /FTId=PRO_0000091000.
FT NP_BIND 26 33 GTP (By similarity).
FT NP_BIND 104 108 GTP (By similarity).
FT NP_BIND 158 161 GTP (By similarity).
FT MOD_RES 54 54 Phosphothreonine.
FT MOD_RES 57 57 Phosphothreonine.
FT MOD_RES 59 59 Phosphothreonine.
FT MOD_RES 235 235 N6-acetyllysine.
FT MOD_RES 239 239 N6-acetyllysine.
FT MOD_RES 272 272 N6-acetyllysine.
FT MOD_RES 275 275 N6-acetyllysine.
FT MOD_RES 435 435 Phosphothreonine.
FT MOD_RES 445 445 N6-acetyllysine.
FT MOD_RES 502 502 Phosphoserine.
FT MOD_RES 715 715 Diphthamide.
SQ SEQUENCE 858 AA; 95338 MW; 78BD1710236C0D9C CRC64;
MVNFTVDQIR AIMDKKANIR NMSVIAHVDH GKSTLTDSLV CKAGIIASAR AGETRFTDTR
KDEQERCITI KSTAISLFYE LSENDLNFIK QSKDGAGFLI NLIDSPGHVD FSSEVTAALR
VTDGALVVVD CVSGVCVQTE TVLRQAIAER IKPVLMMNKM DRALLELQLE PEELYQTFQR
IVENVNVIIS TYGEGESGPM GNIMIDPVLG TVGFGSGLHG WAFTLKQFAE MYVAKFAAKG
EGQLGPAERA KKVEDMMKKL WGDRYFDPAN GKFSKSATSP EGKKLPRTFC QLILDPIFKV
FDAIMNFKKE ETAKLIEKLD IKLDSEDKDK EGKPLLKAVM RRWLPAGDAL LQMITIHLPS
PVTAQKYRCE LLYEGPPDDE AAMGIKSCDP KGPLMMYISK MVPTSDKGRF YAFGRVFSGL
VSTGLKVRIM GPNYTPGKKE DLYLKPIQRT ILMMGRYVEP IEDVPCGNIV GLVGVDQFLV
KTGTITTFEH AHNMRVMKFS VSPVVRVAVE AKNPADLPKL VEGLKRLAKS DPMVQCIIEE
SGEHIIAGAG ELHLEICLKD LEEDHACIPI KKSDPVVSYR ETVSEESNVL CLSKSPNKHN
RLYMKARPFP DGLAEDIDKG EVSARQELKQ RARYLAEKYE WDVAEARKIW CFGPDGTGPN
ILTDITKGVQ YLNEIKDSVV AGFQWATKEG ALCEENMRGV RFDVHDVTLH ADAIHRGGGQ
IIPTARRCLY ASVLTAQPRL MEPIYLVEIQ CPEQVVGGIY GVLNRKRGHV FEESQVAGTP
MFVVKAYLPV NESFGFTADL RSNTGGQAFP QCVFDHWQIL PGDPFDNSSR PSQVVAETRK
RKGLKEGIPA LDNFLDKL
//
MIM
130610
*RECORD*
*FIELD* NO
130610
*FIELD* TI
*130610 EUKARYOTIC TRANSLATION ELONGATION FACTOR 2; EEF2
;;ELONGATION FACTOR 2; EF2;;
read morePOLYPEPTIDYL-tRNA TRANSLOCASE
*FIELD* TX
DESCRIPTION
The EEF2 gene encodes eukaryotic translation elongation factor-2, which
is required for the translocation step in protein synthesis, where
peptidyl-tRNA is moved to the next codon on mRNA from the acceptor site
on the ribosome at the expense of the energy provided by hydrolysis of
GTP bound to EF2 (summary by Kaneda et al., 1984 and Hekman et al.,
2012).
CLONING
Rapp et al. (1989) reported the complete sequence of the predicted
858-amino acid EF2 protein. Sequence comparisons revealed that the
hamster, rat, and human EF2 protein sequences differ in only 8
positions.
GENE FUNCTION
Diphtheria toxin and Pseudomonas exotoxin A (PA toxin) inhibit protein
synthesis by catalyzing covalent binding of the ADP-ribose moiety of NAD
to elongation factor-2 (EF2). Class I diphtheria toxin resistance
(sensitivity) is related to binding of the toxin, a function coded by
chromosome 5. Class II resistance is due to a defect in protein
synthesis such that EF2 is not ADP-ribosylated by diphtheria toxin or PA
toxin. In one subclass this is due to a mutation in the structural gene
for EF2; in a second subclass it is due to mutation in a gene for
posttranslational modification of EF2 (Kaneda et al., 1984).
MAPPING
Kaneda et al. (1984) isolated cells with PA toxin resistance of the
first class II type from primary cultures from human embryos. By
analysis of hybrid cells constructed from these cells and mouse L cells,
they showed that chromosome 19 carries the gene for the resistance,
i.e., the EF2 structural locus.
By analysis of human-mouse hybrid cells, Kaneda et al. (1987) narrowed
the assignment of EF2 to chromosome 19pter-q12.
MOLECULAR GENETICS
In affected members of a family of Norwegian origin with autosomal
dominant late-onset spinocerebellar ataxia-26 (SCA26; 609306),
previously reported by Yu et al. (2005), Hekman et al. (2012) identified
a heterozygous mutation in the EEF2 gene (P596H; 130610.0001). Detailed
studies of the equivalent mutation in yeast (P580Y) showed that it
caused impaired translocation with an increased rate of -1 programmed
ribosomal frameshift read-through during translation. Yeast carrying
this mutation also showed greater susceptibility to proteostatic
disruption, as evidenced by a more robust activation of a reporter gene
driven by unfolded protein response activation upon challenge. The
results suggested that the mutation disrupted the normal mechanical
processes involved in translocation, and indicated that proteostatic
disruption can cause a neurodegenerative disease.
*FIELD* AV
.0001
SPINOCEREBELLAR ATAXIA 26 (1 family)
EEF2, PRO596HIS
In affected members of a 5-generation family of Norwegian origin with
late-onset autosomal dominant spinocerebellar ataxia-26 (SCA26; 609306),
previously reported by Yu et al. (2005), Hekman et al. (2012) identified
a heterozygous C-to-A transversion in exon 12 of the EEF2 gene,
resulting in a pro596-to-his (P596H) substitution at a highly conserved
residue in a domain critical for maintaining the reading frame during
translation. The mutation was found by deep sequencing of the critical
interval identified by linkage analysis on chromosome 19p13.3. The
mutation was found in 24 affected individuals and 2 unaffected
individuals, suggesting incomplete penetrance. The mutation was not
present in the dbSNP, 1000 Genomes Project, or CEPH databases, or in 104
Norwegian control individuals. In vitro expression studies showed that
the mutant protein was properly expressed, localized properly to the
endoplasmic reticulum, and was able to sustain growth in a yeast model.
However, detailed studies of the equivalent mutation in yeast (P580Y)
showed that it caused impaired translocation with an increased rate of
-1 programmed ribosomal frameshift read-through during translation.
Yeast carrying this mutation also showed greater susceptibility to
proteostatic disruption, as evidenced by a more robust activation of a
reporter gene driven by unfolded protein response activation upon
challenge. The results indicated that proteostatic disruption can cause
a neurodegenerative disease.
*FIELD* RF
1. Hekman, K. E.; Yu, G.-Y.; Brown, C. D.; Zhu, H.; Du, X.; Gervin,
K.; Undlien, D. E.; Peterson, A.; Stevanin, G.; Clark, H. B.; Pulst,
S. M.; Bird, T. D.; White, K. P.; Gomez, C. M.: A conserved eEF2
coding variant in SCA26 leads to loss of translational fidelity and
increased susceptibility to proteostatic insult. Hum. Molec. Genet. 21:
5472-5483, 2012.
2. Kaneda, Y.; Hayes, H.; Uchida, T.; Yoshida, M. C.; Okada, Y.:
Regional assignment of five genes on human chromosome 19. Chromosoma 95:
8-12, 1987.
3. Kaneda, Y.; Yoshida, M. C.; Kohno, K.; Uchida, T.; Okada, Y.:
Chromosomal assignment of the gene for human elongation factor-2. Proc.
Nat. Acad. Sci. 81: 3158-3162, 1984.
4. Rapp, G.; Klaudiny, J.; Hagendorff, G.; Luck, M. R.; Scheit, K.
H.: Complete sequence of the coding region of human elongation factor
2 (EF-2) by enzymatic amplification of cDNA from human ovarian granulosa
cells. Biol. Chem. Hoppe Seyler 370: 1071-1075, 1989.
5. Yu, G.-Y.; Howell, M. J.; Roller, M. J.; Xie, T.-D.; Gomez, C.
M.: Spinocerebellar ataxia type 26 maps to chromosome 19p13.3 adjacent
to SCA6. Ann. Neurol. 57: 349-354, 2005.
*FIELD* CN
Cassandra L. Kniffin - updated: 10/7/2013
Rebekah S. Rasooly - updated: 2/10/1999
*FIELD* CD
Victor A. McKusick: 6/4/1986
*FIELD* ED
carol: 10/09/2013
ckniffin: 10/7/2013
terry: 9/17/2010
alopez: 2/10/1999
alopez: 2/5/1999
carol: 8/11/1998
dkim: 6/30/1998
carol: 11/10/1994
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/26/1989
marie: 3/25/1988
carol: 4/29/1987
*RECORD*
*FIELD* NO
130610
*FIELD* TI
*130610 EUKARYOTIC TRANSLATION ELONGATION FACTOR 2; EEF2
;;ELONGATION FACTOR 2; EF2;;
read morePOLYPEPTIDYL-tRNA TRANSLOCASE
*FIELD* TX
DESCRIPTION
The EEF2 gene encodes eukaryotic translation elongation factor-2, which
is required for the translocation step in protein synthesis, where
peptidyl-tRNA is moved to the next codon on mRNA from the acceptor site
on the ribosome at the expense of the energy provided by hydrolysis of
GTP bound to EF2 (summary by Kaneda et al., 1984 and Hekman et al.,
2012).
CLONING
Rapp et al. (1989) reported the complete sequence of the predicted
858-amino acid EF2 protein. Sequence comparisons revealed that the
hamster, rat, and human EF2 protein sequences differ in only 8
positions.
GENE FUNCTION
Diphtheria toxin and Pseudomonas exotoxin A (PA toxin) inhibit protein
synthesis by catalyzing covalent binding of the ADP-ribose moiety of NAD
to elongation factor-2 (EF2). Class I diphtheria toxin resistance
(sensitivity) is related to binding of the toxin, a function coded by
chromosome 5. Class II resistance is due to a defect in protein
synthesis such that EF2 is not ADP-ribosylated by diphtheria toxin or PA
toxin. In one subclass this is due to a mutation in the structural gene
for EF2; in a second subclass it is due to mutation in a gene for
posttranslational modification of EF2 (Kaneda et al., 1984).
MAPPING
Kaneda et al. (1984) isolated cells with PA toxin resistance of the
first class II type from primary cultures from human embryos. By
analysis of hybrid cells constructed from these cells and mouse L cells,
they showed that chromosome 19 carries the gene for the resistance,
i.e., the EF2 structural locus.
By analysis of human-mouse hybrid cells, Kaneda et al. (1987) narrowed
the assignment of EF2 to chromosome 19pter-q12.
MOLECULAR GENETICS
In affected members of a family of Norwegian origin with autosomal
dominant late-onset spinocerebellar ataxia-26 (SCA26; 609306),
previously reported by Yu et al. (2005), Hekman et al. (2012) identified
a heterozygous mutation in the EEF2 gene (P596H; 130610.0001). Detailed
studies of the equivalent mutation in yeast (P580Y) showed that it
caused impaired translocation with an increased rate of -1 programmed
ribosomal frameshift read-through during translation. Yeast carrying
this mutation also showed greater susceptibility to proteostatic
disruption, as evidenced by a more robust activation of a reporter gene
driven by unfolded protein response activation upon challenge. The
results suggested that the mutation disrupted the normal mechanical
processes involved in translocation, and indicated that proteostatic
disruption can cause a neurodegenerative disease.
*FIELD* AV
.0001
SPINOCEREBELLAR ATAXIA 26 (1 family)
EEF2, PRO596HIS
In affected members of a 5-generation family of Norwegian origin with
late-onset autosomal dominant spinocerebellar ataxia-26 (SCA26; 609306),
previously reported by Yu et al. (2005), Hekman et al. (2012) identified
a heterozygous C-to-A transversion in exon 12 of the EEF2 gene,
resulting in a pro596-to-his (P596H) substitution at a highly conserved
residue in a domain critical for maintaining the reading frame during
translation. The mutation was found by deep sequencing of the critical
interval identified by linkage analysis on chromosome 19p13.3. The
mutation was found in 24 affected individuals and 2 unaffected
individuals, suggesting incomplete penetrance. The mutation was not
present in the dbSNP, 1000 Genomes Project, or CEPH databases, or in 104
Norwegian control individuals. In vitro expression studies showed that
the mutant protein was properly expressed, localized properly to the
endoplasmic reticulum, and was able to sustain growth in a yeast model.
However, detailed studies of the equivalent mutation in yeast (P580Y)
showed that it caused impaired translocation with an increased rate of
-1 programmed ribosomal frameshift read-through during translation.
Yeast carrying this mutation also showed greater susceptibility to
proteostatic disruption, as evidenced by a more robust activation of a
reporter gene driven by unfolded protein response activation upon
challenge. The results indicated that proteostatic disruption can cause
a neurodegenerative disease.
*FIELD* RF
1. Hekman, K. E.; Yu, G.-Y.; Brown, C. D.; Zhu, H.; Du, X.; Gervin,
K.; Undlien, D. E.; Peterson, A.; Stevanin, G.; Clark, H. B.; Pulst,
S. M.; Bird, T. D.; White, K. P.; Gomez, C. M.: A conserved eEF2
coding variant in SCA26 leads to loss of translational fidelity and
increased susceptibility to proteostatic insult. Hum. Molec. Genet. 21:
5472-5483, 2012.
2. Kaneda, Y.; Hayes, H.; Uchida, T.; Yoshida, M. C.; Okada, Y.:
Regional assignment of five genes on human chromosome 19. Chromosoma 95:
8-12, 1987.
3. Kaneda, Y.; Yoshida, M. C.; Kohno, K.; Uchida, T.; Okada, Y.:
Chromosomal assignment of the gene for human elongation factor-2. Proc.
Nat. Acad. Sci. 81: 3158-3162, 1984.
4. Rapp, G.; Klaudiny, J.; Hagendorff, G.; Luck, M. R.; Scheit, K.
H.: Complete sequence of the coding region of human elongation factor
2 (EF-2) by enzymatic amplification of cDNA from human ovarian granulosa
cells. Biol. Chem. Hoppe Seyler 370: 1071-1075, 1989.
5. Yu, G.-Y.; Howell, M. J.; Roller, M. J.; Xie, T.-D.; Gomez, C.
M.: Spinocerebellar ataxia type 26 maps to chromosome 19p13.3 adjacent
to SCA6. Ann. Neurol. 57: 349-354, 2005.
*FIELD* CN
Cassandra L. Kniffin - updated: 10/7/2013
Rebekah S. Rasooly - updated: 2/10/1999
*FIELD* CD
Victor A. McKusick: 6/4/1986
*FIELD* ED
carol: 10/09/2013
ckniffin: 10/7/2013
terry: 9/17/2010
alopez: 2/10/1999
alopez: 2/5/1999
carol: 8/11/1998
dkim: 6/30/1998
carol: 11/10/1994
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/26/1989
marie: 3/25/1988
carol: 4/29/1987