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UniProtKB/Swiss-Prot entry P13639


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name EF2_HUMAN
Primary accession number P13639
Secondary accession number Q58J86
Integrated into Swiss-Prot on January 1, 1990
Sequence was last modified on January 23, 2007 (Sequence version 4)
Annotations were last modified on    June 16, 2009 (Entry version 104)
Name and origin of the protein
Protein name Elongation factor 2
Synonym EF-2
Gene name
Name: EEF2
Synonyms: EF2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Ovary;
PubMed=2610926 [NCBI, ExPASy, EBI, Israel, Japan]
Rapp G., Klaudiny J., Hagendorff G., Luck M.R., Heinz K.;
"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).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1596361 [NCBI, ExPASy, EBI, Israel, Japan]
Hanes J., Freudenstein J., Rapp G., Scheit K.H.;
"Construction of a plasmid containing the complete coding region of human elongation factor 2.";
Biol. Chem. Hoppe-Seyler 373:201-204(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Peripheral blood;
Ustek D., Bektas M., Cakiris A., Oku B., Bermek E.;
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 501-858.
PubMed=2840927 [NCBI, ExPASy, EBI, Israel, Japan]
Rapp G., Mucha J., Einspanier R., Luck M., Scheit K.H.;
"Cloning and sequence analysis of a cDNA from human ovarian granulosa cells encoding the C-terminal part of human elongation factor 2.";
Biol. Chem. Hoppe-Seyler 369:247-250(1988).
[6]
PROTEIN SEQUENCE OF 796-801, AND MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Vishwanath V.;
Submitted (MAR-2007) to UniProtKB.
[7]
CLEAVAGE OF INITIATOR METHIONINE.
Bienvenut W.V.;
Submitted (AUG-2001) to UniProtKB.
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-57, AND MASS SPECTROMETRY.
DOI=10.1021/pr050048h; PubMed=16083285 [NCBI, ExPASy, EBI, Israel, Japan]
Kim J.-E., Tannenbaum S.R., White F.M.;
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
J. Proteome Res. 4:1339-1346(2005).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-265, AND MASS SPECTROMETRY.
TISSUE=Hepatocyte;
DOI=10.1002/pmic.200401217; PubMed=16097034 [NCBI, ExPASy, EBI, Israel, Japan]
Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K., Demol H., Martens L., Goethals M., Vandekerckhove J.;
"Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC.";
Proteomics 5:3589-3599(2005).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-57, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-57, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan]
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-435 AND SER-502, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[15]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[16]
IDENTIFICATION IN THE SURF COMPLEX.
DOI=10.1101/gad.1767209; PubMed=19417104 [NCBI, ExPASy, EBI, Israel, Japan]
Yamashita A., Izumi N., Kashima I., Ohnishi T., Saari B., Katsuhata Y., Muramatsu R., Morita T., Iwamatsu A., Hachiya T., Kurata R., Hirano H., Anderson P., Ohno S.;
"SMG-8 and SMG-9, two novel subunits of the SMG-1 complex, regulate remodeling of the mRNA surveillance complex during nonsense-mediated mRNA decay.";
Genes Dev. 23:1091-1105(2009).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X51466; CAA35829.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z11692; CAA77750.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY942181; AAX34409.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC126259; AAI26260.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M19997; AAA50388.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00186290; -.
PIR S18294; EFHU2.
RefSeq NP_001952.1; -.
UniGene Hs.515070
3D structure databases
HSSP P32324; 1N0U. [HSSP ENTRY / PDB]
ModBase P13639.
Protein-protein interaction databases
IntAct P13639; 9.
PTM databases
PhosphoSite P13639; -.
Enzyme and pathway databases
Pathway_Interaction_DB mtor_4pathway; mTOR signaling pathway.
Reactome REACT_71; Gene Expression.
2D gel databases
PMMA-2DPAGE P13639; -.
REPRODUCTION-2DPAGE IPI00186290; -.
Organism-specific databases
GeneCards GC19M003927; -.
H-InvDB HIX0040078; -.
HGNC HGNC:3214; EEF2.
GenAtlas EEF2.
HPA CAB007795; -.
MIM 130610; gene. [NCBI / EBI]
PharmGKB PA27650; -.
Gene expression databases
ArrayExpress P13639; -.
Bgee P13639; -.
CleanEx HS_EEF2; -.
GermOnline ENSG00000167658; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-SubCell).
GO:0030529; Cellular component: ribonucleoprotein complex (inferred from direct assay from MGI).
GO:0005525; Molecular function: GTP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0003924; Molecular function: GTPase activity (inferred from electronic annotation from InterPro).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0003746; Molecular function: translation elongation factor activity (inferred from electronic annotation from UniProtKB-KW).
GO:0006414; Biological process: translational elongation (inferred from experiment from Reactome).
QuickGo view.
Family and domain databases
InterPro IPR000795; ProtSyn_GTP_bd.
IPR014721; Ribosomal_S5_D2-type_fold.
IPR005225; Small_GTP_bd.
IPR000640; Transl_elong_EFG/EF2_C.
IPR005517; Transl_elong_EFG/EF2_IV.
IPR004161; Transl_elong_EFTu/EF1A_2.
Graphical view of domain structure.
Gene3D G3DSA:3.30.230.10; Ribosomal_S5_D2-type_fold; 2.
Pfam PF00679; EFG_C; 1.
PF03764; EFG_IV; 1.
PF00009; GTP_EFTU; 1.
PF03144; GTP_EFTU_D2; 1.
Pfam graphical view of domain structure.
PRINTS PR00315; ELONGATNFCT.
TIGRFAMs TIGR00231; small_GTP; 1.
PROSITE PS00301; EFACTOR_GTP; 1.
Proteomic databases
PeptideAtlas P13639; -.
PRIDE P13639; -.
Genome annotation databases
Ensembl ENSG00000167658; Homo sapiens. [Contig view]
GeneID 1938; -.
KEGG hsa:1938; -.
NMPDR fig|9606.3.peg.15406; -.
Phylogenomic databases
HOGENOM P13639; -.
HOVERGEN P13639; -.
OMA P13639; LNETMEL.
Other
NextBio 7853; -.
SOURCE EEF2; Homo sapiens.
ProtoNet P13639.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cytoplasm; Direct protein sequencing; Elongation factor; GTP-binding; Nucleotide-binding; Phosphoprotein; Protein biosynthesis.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   858  857     Elongation factor 2. PRO_0000091000
NP_BIND   26    33  8     GTP (By similarity). 
NP_BIND   104   108  5     GTP (By similarity). 
NP_BIND   158   161  4     GTP (By similarity). 
MOD_RES   54    54        Phosphothreonine (By similarity). 
MOD_RES   57    57        Phosphothreonine. 
MOD_RES   59    59        Phosphothreonine (By similarity). 
MOD_RES   265   265        Phosphotyrosine. 
MOD_RES   435   435        Phosphothreonine. 
MOD_RES   502   502        Phosphoserine. 
MOD_RES   715   715        Diphthamide. 
Sequence information
Length: 858 AA [This is the length of the unprocessed precursor] Molecular weight: 95338 Da [This is the MW of the unprocessed precursor] CRC64: 78BD1710236C0D9C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVNFTVDQIR AIMDKKANIR NMSVIAHVDH GKSTLTDSLV CKAGIIASAR AGETRFTDTR 

        70         80         90        100        110        120 
KDEQERCITI KSTAISLFYE LSENDLNFIK QSKDGAGFLI NLIDSPGHVD FSSEVTAALR 

       130        140        150        160        170        180 
VTDGALVVVD CVSGVCVQTE TVLRQAIAER IKPVLMMNKM DRALLELQLE PEELYQTFQR 

       190        200        210        220        230        240 
IVENVNVIIS TYGEGESGPM GNIMIDPVLG TVGFGSGLHG WAFTLKQFAE MYVAKFAAKG 

       250        260        270        280        290        300 
EGQLGPAERA KKVEDMMKKL WGDRYFDPAN GKFSKSATSP EGKKLPRTFC QLILDPIFKV 

       310        320        330        340        350        360 
FDAIMNFKKE ETAKLIEKLD IKLDSEDKDK EGKPLLKAVM RRWLPAGDAL LQMITIHLPS 

       370        380        390        400        410        420 
PVTAQKYRCE LLYEGPPDDE AAMGIKSCDP KGPLMMYISK MVPTSDKGRF YAFGRVFSGL 

       430        440        450        460        470        480 
VSTGLKVRIM GPNYTPGKKE DLYLKPIQRT ILMMGRYVEP IEDVPCGNIV GLVGVDQFLV 

       490        500        510        520        530        540 
KTGTITTFEH AHNMRVMKFS VSPVVRVAVE AKNPADLPKL VEGLKRLAKS DPMVQCIIEE 

       550        560        570        580        590        600 
SGEHIIAGAG ELHLEICLKD LEEDHACIPI KKSDPVVSYR ETVSEESNVL CLSKSPNKHN 

       610        620        630        640        650        660 
RLYMKARPFP DGLAEDIDKG EVSARQELKQ RARYLAEKYE WDVAEARKIW CFGPDGTGPN 

       670        680        690        700        710        720 
ILTDITKGVQ YLNEIKDSVV AGFQWATKEG ALCEENMRGV RFDVHDVTLH ADAIHRGGGQ 

       730        740        750        760        770        780 
IIPTARRCLY ASVLTAQPRL MEPIYLVEIQ CPEQVVGGIY GVLNRKRGHV FEESQVAGTP 

       790        800        810        820        830        840 
MFVVKAYLPV NESFGFTADL RSNTGGQAFP QCVFDHWQIL PGDPFDNSSR PSQVVAETRK 

       850 
RKGLKEGIPA LDNFLDKL 

P13639 in FASTA format

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