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Searching in 'World-2DPAGE Repository [0054]' for entry matching: EF2_HUMAN




World-2DPAGE Repository (0054):  EF2_HUMAN


EF2_HUMAN


General information about the entry
View entry in simple text format
Entry nameEF2_HUMAN
Primary accession numberP13639
integrated into World-2DPAGE Repository (0054) on November 28, 2012 (release 1)
2D Annotations were last modified onNovember 28, 2012 (version 1)
General Annotations were last modified on October 23, 2014 (version 2)
Name and origin of the protein
DescriptionRecName: Full=Elongation factor 2; Short=EF-2;.
Gene nameName=EEF2
Synonyms=EF2
Annotated speciesHomo sapiens (Human) [TaxID: 9606]
TaxonomyEukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
References
[1]   2D GEL CHARACTERIZATION
DOI=10.1074/mcp.M112.022947;
Vernocchi S., Battello N., Schmitz S., Revets D., Billing A.M., Turner J.D., Muller C.P.
''Membrane glucocorticoid receptor activation induces proteomic changes aligning with classical glucocorticoid-effects''
Molecular & Cellular Proteomics 12(7):1764-1779 (2013)
2D PAGE maps for identified proteins
How to interpret a protein

HSAPIENS_CCRF-CEM_3-10 {CCRF-CEM cells stimulated with Cort-BSA (internal standard)}
Homo sapiens (Human)
HSAPIENS_CCRF-CEM_3-10
  map experimental info
 
HSAPIENS_CCRF-CEM_3-10

MAP LOCATIONS:
pI=6.42; Mw=95207  [identification data]

%COV: SPOT 420: 51 [1].
SCORE: SPOT 420: 664 [1].
SEARCH ENGINE: SPOT 420: Mascot [1].
MAPPING (identification):
SPOT 420: Peptide mass fingerprinting [1]; Tandem mass spectrometry [1].

Copyright
Data from Dr. Claude P. Muller, Centre de Recherche Public de la Sante / National Public Health Laboratory, Luxembourg
Cross-references
UniProtKB/Swiss-ProtP13639; EF2_HUMAN.



2D PAGE maps for identified proteins
  • How to interpret a protein map
  • You may obtain an estimated location of the protein on various 2D PAGE maps, provided the whole amino acid sequence is known. The estimation is obtained according to the computed protein's pI and Mw.
  • Warning 1: the displayed region reflects an area around the theoretical pI and molecular weight of the protein and is only provided for the user's information. It should be used with caution, as the experimental and theoretical positions of a protein may differ significantly.
  • Warning 2: the 2D PAGE map is built on demand. This may take some few seconds to be computed.



External data extracted from UniProtKB/Swiss-Prot
Extracted from UniProtKB/Swiss-Prot, release: 0.0
Entry nameEF2_HUMAN
Primary accession numberP13639
Secondary accession number(s) B2RMP5 D6W618 Q58J86
Sequence was last modified on January 23, 2007 (version 4)
Annotations were last modified on October 1, 2014 (version 163)
Name and origin of the protein
DescriptionRecName: Full=Elongation factor 2; Short=EF-2;
Gene nameName=EEF2
Synonyms=EF2
Encoded onName=EEF2; Synonyms=EF2
Keywords3D-structure; Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Disease mutation; Elongation factor; GTP-binding; Neurodegeneration; Nucleotide-binding; Phosphoprotein; Protein biosynthesis; Reference proteome; Spinocerebellar ataxia; Ubl conjugation.
Copyright
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License
Cross-references
EMBLX51466; CAA35829.1; -; mRNA
EMBLZ11692; CAA77750.1; -; mRNA
EMBLAY942181; AAX34409.1; -; mRNA
EMBLCH471139; EAW69274.1; -; Genomic_DNA
EMBLCH471139; EAW69275.1; -; Genomic_DNA
EMBLBC126259; AAI26260.1; -; mRNA
EMBLBC136313; AAI36314.1; -; mRNA
EMBLM19997; AAA50388.1; -; mRNA
CCDSCCDS12117.1; -; .
PIRS18294; EFHU2; .
RefSeqNP_001952.1; NM_001961.3; .
UniGeneHs.515070; -; .
PDB3J3A; EM; 5.00 A; z=1-858
PDBsum3J3A; -; .
ProteinModelPortalP13639; -; .
SMRP13639; 3-858; .
BioGrid108258; 122; .
IntActP13639; 47; .
MINTMINT-4999025; -; .
STRING9606.ENSP00000307940; -; .
ChEMBLCHEMBL1795108; -; .
PhosphoSiteP13639; -; .
DMDM119172; -; .
REPRODUCTION-2DPAGEIPI00186290; -; .
MaxQBP13639; -; .
PaxDbP13639; -; .
PeptideAtlasP13639; -; .
PRIDEP13639; -; .
DNASU1938; -; .
EnsemblENST00000309311; ENSP00000307940; ENSG00000167658; .
GeneID1938; -; .
KEGGhsa:1938; -; .
UCSCuc002lze.3; human; .
CTD1938; -; .
GeneCardsGC19M003976; -; .
HGNCHGNC:3214; EEF2; .
HPACAB007795; -; .
MIM130610; gene; .
MIM609306; phenotype; .
neXtProtNX_P13639; -; .
Orphanet101112; Spinocerebellar ataxia type 26; .
PharmGKBPA27650; -; .
eggNOGCOG0480; -; .
HOGENOMHOG000231589; -; .
HOVERGENHBG001838; -; .
InParanoidP13639; -; .
KOK03234; -; .
OMARWAPVPE; -; .
OrthoDBEOG7WDN1S; -; .
PhylomeDBP13639; -; .
TreeFamTF300575; -; .
ReactomeREACT_1404; Peptide chain elongation; .
ChiTaRSEEF2; human; .
GeneWikiEEF2; -; .
GenomeRNAi1938; -; .
NextBio7853; -; .
PROPR:P13639; -; .
ArrayExpressP13639; -; .
BgeeP13639; -; .
CleanExHS_EEF2; -; .
GenevestigatorP13639; -; .
GOGO:0005829; C:cytosol; TAS:Reactome; .
GOGO:0070062; C:extracellular vesicular exosome; IDA:UniProt; .
GOGO:0016020; C:membrane; IDA:UniProtKB; .
GOGO:0005634; C:nucleus; IDA:UniProt; .
GOGO:0005844; C:polysome; IEA:Ensembl; .
GOGO:0030529; C:ribonucleoprotein complex; IDA:MGI; .
GOGO:0005525; F:GTP binding; IEA:UniProtKB-KW; .
GOGO:0003924; F:GTPase activity; IEA:Ensembl; .
GOGO:0044822; F:poly(A) RNA binding; IDA:UniProtKB; .
GOGO:0019901; F:protein kinase binding; IPI:UniProt; .
GOGO:0008494; F:translation activator activity; IGI:UniProt; .
GOGO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW; .
GOGO:0008219; P:cell death; IEA:UniProtKB-KW; .
GOGO:0044267; P:cellular protein metabolic process; TAS:Reactome; .
GOGO:0010467; P:gene expression; TAS:Reactome; .
GOGO:0010628; P:positive regulation of gene expression; IGI:UniProt; .
GOGO:0045727; P:positive regulation of translation; IGI:UniProt; .
GOGO:0006412; P:translation; TAS:Reactome; .
GOGO:0006414; P:translational elongation; TAS:Reactome; .
Gene3D3.30.230.10; -; 1; .
Gene3D3.30.70.240; -; 1; .
Gene3D3.40.50.300; -; 1; .
InterProIPR000795; EF_GTP-bd_dom; .
InterProIPR009022; EFG_III-V; .
InterProIPR000640; EFG_V; .
InterProIPR027417; P-loop_NTPase; .
InterProIPR020568; Ribosomal_S5_D2-typ_fold; .
InterProIPR014721; Ribosomal_S5_D2-typ_fold_subgr; .
InterProIPR005225; Small_GTP-bd_dom; .
InterProIPR009000; Transl_B-barrel; .
InterProIPR005517; Transl_elong_EFG/EF2_IV; .
InterProIPR004161; Transl_elong_EFTu/EF1A_2; .
PfamPF00679; EFG_C; 1; .
PfamPF14492; EFG_II; 1; .
PfamPF03764; EFG_IV; 1; .
PfamPF00009; GTP_EFTU; 1; .
PfamPF03144; GTP_EFTU_D2; 1; .
PRINTSPR00315; ELONGATNFCT; .
SMARTSM00838; EFG_C; 1; .
SMARTSM00889; EFG_IV; 1; .
SUPFAMSSF50447; SSF50447; 1; .
SUPFAMSSF52540; SSF52540; 1; .
SUPFAMSSF54211; SSF54211; 1; .
SUPFAMSSF54980; SSF54980; 2; .
TIGRFAMsTIGR00231; small_GTP; 1; .
PROSITEPS00301; G_TR_1; 1; .
PROSITEPS51722; G_TR_2; 1; .



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Database constructed and maintained by SIB, using the Make2D-DB II package (ver. 3.10.2) from the World-2DPAGE Constellation of the Expasy web server