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UniProtKB/Swiss-Prot entry P26641


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

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Entry information
Entry name EF1G_HUMAN
Primary accession number P26641
Secondary accession numbers Q6PJ62 Q6PK31 Q96CU2 Q9P196
Integrated into Swiss-Prot on August 1, 1992
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 106)
Name and origin of the protein
Protein name Elongation factor 1-gamma
Synonyms EF-1-gamma
eEF-1B gamma
Gene name
Name: EEF1G
Synonyms: EF1G
ORFNames: PRO1608
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].
DOI=10.1093/nar/20.22.5907; PubMed=1461723 [NCBI, ExPASy, EBI, Israel, Japan]
Sanders J., Maassen J.A., Moeller 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).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1093/nar/20.10.2598; PubMed=1598220 [NCBI, ExPASy, EBI, Israel, Japan]
Kumabe T., Schma Y., Yamamoto T.;
"Human cDNAs encoding elongation factor 1 gamma and the ribosomal protein L19.";
Nucleic Acids Res. 20:2598-2598(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Bone marrow, Eye, Liver, Lung, Muscle, Testis, and Uterus;
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).
[4]
PROTEIN SEQUENCE OF 2-14.
TISSUE=Platelet;
DOI=10.1038/nbt810; PubMed=12665801 [NCBI, ExPASy, EBI, Israel, Japan]
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[5]
PROTEIN SEQUENCE OF 2-14, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V.;
Submitted (OCT-2004) to UniProtKB.
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 80-437.
TISSUE=Pancreatic carcinoma;
PubMed=1372736 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 121-437.
TISSUE=Fetal liver;
Zhang C., Yu Y., Zhang S., Wei H., Zhang Y., Zhou G., Bi J., Liu M., He F.;
"Functional prediction of the coding sequences of 79 new genes deduced by analysis of cDNA clones from human fetal liver.";
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-43, 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).
[9]
STRUCTURE BY NMR OF 276-437.
DOI=10.1023/A:1023504611632; PubMed=12766415 [NCBI, ExPASy, EBI, Israel, Japan]
Vanwetswinkel S., Kriek J., Andersen G.R., Dijk J., Siegal G.;
"1H, 15N and 13C resonance assignments of the highly conserved 19 kDa C-terminal domain from human elongation factor 1Bgamma.";
J. Biomol. NMR 26:189-190(2003).
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
X63526; CAA45089.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z11531; CAA77630.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000384; AAH00384.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC006509; AAH06509.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC006520; AAH06520.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC007949; AAH07949.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC009865; AAH09865.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC013918; AAH13918.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC015813; AAH15813.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC021974; AAH21974.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC028179; AAH28179.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC031012; AAH31012.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC067738; AAH67738.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M55409; AAC18414.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF119850; AAF69604.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S22655; S22655.
RefSeq NP_001395.1; -.
UniGene Hs.144835
3D structure databases
PDB
1PBU; NMR; -; A=276-437.[ExPASy / RCSB / EBI]
PDBsum 1PBU; -.
ModBase P26641.
Protein-protein interaction databases
IntAct P26641; -.
PTM databases
PhosphoSite P26641; -.
Enzyme and pathway databases
Reactome REACT_71; Gene Expression.
2D gel databases
OGP P26641; -.
Organism-specific databases
H-InvDB HIX0020040; -.
HGNC HGNC:3213; EEF1G.
GenAtlas EEF1G.
HPA CAB004969; -.
MIM 130593; gene. [NCBI / EBI]
PharmGKB PA27649; -.
GeneCards P26641.
Gene expression databases
CleanEx HS_EEF1G; -.
GermOnline ENSG00000186676; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0005853; Cellular component: eukaryotic translation elongation factor 1 complex (inferred from electronic annotation from InterPro).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0003746; Molecular function: translation elongation factor activity (non-traceable author statement from UniProtKB).
GO:0006414; Biological process: translational elongation (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR010987; Glutathione-S-Trfase_C-like.
IPR004046; GST_C.
IPR004045; GST_N.
IPR001662; Transl_elong_EF1_G_con.
Graphical view of domain structure.
Gene3D G3DSA:1.20.1050.10; GST_C_like; 1.
G3DSA:3.30.70.1010; Transl_elong_EF1_G_con; 1.
Pfam PF00647; EF1G; 1.
PF00043; GST_C; 1.
PF02798; GST_N; 1.
Pfam graphical view of domain structure.
ProDom PD006217; EF1_G; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS50040; EF1G_C; 1.
PS50405; GST_CTER; 1.
PS50404; GST_NTER; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P26641.
ProtoNet P26641.
Genome annotation databases
Ensembl ENSG00000186676; Homo sapiens. [Contig view]
GeneID 1937; -.
KEGG hsa:1937; -.
Phylogenomic databases
HOGENOM P26641; -.
HOVERGEN P26641; -.
Other
LinkHub P26641; -.
NextBio 7847; -.
SOURCE EEF1G; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Direct protein sequencing; Elongation factor; Phosphoprotein; Protein biosynthesis.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   437  436     Elongation factor 1-gamma. PRO_0000208813
DOMAIN   2    87  86     GST N-terminal. 
DOMAIN   88   216  129     GST C-terminal. 
DOMAIN   276   437  162     EF-1-gamma C-terminal. 
MOD_RES   2     2        N-acetylalanine. 
MOD_RES   43    43        Phosphothreonine. 
CONFLICT   102   102        A -> V (in Ref. 3; AAH13918). 
HELIX   279   281  3      
HELIX   290   299  10      
HELIX   302   304  3      
HELIX   306   311  6      
TURN   316   318  3      
STRAND   320   324  5      
HELIX   329   331  3      
HELIX   338   348  11      
HELIX   349   351  3      
HELIX   353   355  3      
STRAND   356   358  3      
STRAND   361   364  4      
STRAND   370   381  12      
HELIX   384   386  3      
HELIX   388   390  3      
HELIX   394   396  3      
HELIX   408   418  11      
TURN   424   426  3      
Sequence information
Length: 437 AA [This is the length of the unprocessed precursor] Molecular weight: 50119 Da [This is the MW of the unprocessed precursor] CRC64: A6110663110CF3FC [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAAGTLYTYP ENWRAFKALI AAQYSGAQVR VLSAPPHFHF GQTNRTPEFL RKFPAGKVPA 

        70         80         90        100        110        120 
FEGDDGFCVF ESNAIAYYVS NEELRGSTPE AAAQVVQWVS FADSDIVPPA STWVFPTLGI 

       130        140        150        160        170        180 
MHHNKQATEN AKEEVRRILG LLDAYLKTRT FLVGERVTLA DITVVCTLLW LYKQVLEPSF 

       190        200        210        220        230        240 
RQAFPNTNRW FLTCINQPQF RAVLGEVKLC EKMAQFDAKK FAETQPKKDT PRKEKGSREE 

       250        260        270        280        290        300 
KQKPQAERKE EKKAAAPAPE EEMDECEQAL AAEPKAKDPF AHLPKSTFVL DEFKRKYSNE 

       310        320        330        340        350        360 
DTLSVALPYF WEHFDKDGWS LWYSEYRFPE ELTQTFMSCN LITGMFQRLD KLRKNAFASV 

       370        380        390        400        410        420 
ILFGTNNSSS ISGVWVFRGQ ELAFPLSPDW QVDYESYTWR KLDPGSEETQ TLVREYFSWE 

       430 
GAFQHVGKAF NQGKIFK 

P26641 in FASTA format

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