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P26641 (EF1G_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 159. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Elongation factor 1-gamma

Short name=EF-1-gamma
Alternative name(s):
eEF-1B gamma
Gene names
Name:EEF1G
Synonyms:EF1G
ORF Names:PRO1608
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length437 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probably plays a role in anchoring the complex to other cellular components.

Subunit structure

EF-1 is composed of four subunits: alpha, beta, delta, and gamma.

Tissue specificity

Highly expressed in pancreatic tumor tissue and to a lesser extent in normal kidney, intestine, pancreas, stomach, lung, brain, spleen and liver.

Induction

Down-regulated in response to enterovirus 71 (EV71) infection. Ref.8

Sequence similarities

Contains 1 EF-1-gamma C-terminal domain.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4 Ref.5
Chain2 – 437436Elongation factor 1-gamma
PRO_0000208813

Regions

Domain2 – 8786GST N-terminal
Domain88 – 216129GST C-terminal
Domain276 – 437162EF-1-gamma C-terminal

Amino acid modifications

Modified residue21N-acetylalanine Ref.5 Ref.9 Ref.13 Ref.14
Modified residue1471N6-acetyllysine Ref.10
Modified residue2121N6-acetyllysine By similarity
Modified residue4011N6-acetyllysine By similarity
Modified residue4341N6-acetyllysine; alternate Ref.10
Modified residue4341N6-malonyllysine; alternate Ref.12

Experimental info

Sequence conflict1021A → V in AAH13918. Ref.3

Secondary structure

................................... 437
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P26641 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: A6110663110CF3FC

FASTA43750,119
        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 

« Hide

References

« Hide 'large scale' references
[1]"Elongation factor-1 messenger-RNA levels in cultured cells are high compared to tissue and are not drastically affected further by oncogenic transformation."
Sanders J., Maassen J.A., Moeller W.
Nucleic Acids Res. 20:5907-5910(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Human cDNAs encoding elongation factor 1 gamma and the ribosomal protein L19."
Kumabe T., Schma Y., Yamamoto T.
Nucleic Acids Res. 20:2598-2598(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Bone marrow, Eye, Liver, Lung, Muscle, Testis and Uterus.
[4]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-14.
Tissue: Platelet.
[5]Bienvenut W.V.
Submitted (OCT-2004) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-14, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[6]"Expression of elongation factor-1 gamma-related sequence in human pancreatic cancer."
Lew Y., Jones D.V., Mars W.M., Evans D., Byrd D., Frazier M.L.
Pancreas 7:144-152(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 80-437.
Tissue: Pancreatic carcinoma.
[7]"Functional prediction of the coding sequences of 79 new genes deduced by analysis of cDNA clones from human fetal liver."
Zhang C., Yu Y., Zhang S., Wei H., Zhang Y., Zhou G., Bi J., Liu M., He F.
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 121-437.
Tissue: Fetal liver.
[8]"Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection."
Leong W.F., Chow V.T.
Cell. Microbiol. 8:565-580(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.
[9]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-147 AND LYS-434, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"The first identification of lysine malonylation substrates and its regulatory enzyme."
Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y., He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C., Dai J., Verdin E., Ye Y., Zhao Y.
Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: MALONYLATION AT LYS-434.
[13]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"1H, 15N and 13C resonance assignments of the highly conserved 19 kDa C-terminal domain from human elongation factor 1Bgamma."
Vanwetswinkel S., Kriek J., Andersen G.R., Dijk J., Siegal G.
J. Biomol. NMR 26:189-190(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 276-437.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X63526 mRNA. Translation: CAA45089.1.
Z11531 mRNA. Translation: CAA77630.1.
BC000384 mRNA. Translation: AAH00384.1.
BC006509 mRNA. Translation: AAH06509.1.
BC006520 mRNA. Translation: AAH06520.1.
BC007949 mRNA. Translation: AAH07949.2.
BC009865 mRNA. Translation: AAH09865.1.
BC013918 mRNA. Translation: AAH13918.1.
BC015813 mRNA. Translation: AAH15813.1.
BC021974 mRNA. Translation: AAH21974.2.
BC028179 mRNA. Translation: AAH28179.1.
BC031012 mRNA. Translation: AAH31012.1.
BC067738 mRNA. Translation: AAH67738.1.
M55409 mRNA. Translation: AAC18414.1.
AF119850 mRNA. Translation: AAF69604.1.
PIRS22655.
RefSeqNP_001395.1. NM_001404.4.
UniGeneHs.144835.
Hs.444467.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PBUNMR-A276-437[»]
ProteinModelPortalP26641.
SMRP26641. Positions 6-202, 276-437.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108257. 126 interactions.
DIPDIP-32516N.
IntActP26641. 111 interactions.
MINTMINT-1191315.

PTM databases

PhosphoSiteP26641.

Polymorphism databases

DMDM119165.

2D gel databases

OGPP26641.

Proteomic databases

PaxDbP26641.
PRIDEP26641.

Protocols and materials databases

DNASU1937.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000329251; ENSP00000331901; ENSG00000254772.
GeneID1937.
KEGGhsa:1937.
UCSCuc001ntm.1. human.

Organism-specific databases

CTD1937.
GeneCardsGC11M062332.
HGNCHGNC:3213. EEF1G.
HPAHPA040688.
MIM130593. gene.
neXtProtNX_P26641.
PharmGKBPA27649.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0625.
HOGENOMHOG000235245.
HOVERGENHBG051444.
InParanoidP26641.
KOK03233.
OrthoDBEOG72G177.
PhylomeDBP26641.
TreeFamTF314343.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
REACT_71. Gene Expression.

Gene expression databases

CleanExHS_EEF1G.
GenevestigatorP26641.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.30.70.1010. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
IPR001662. Transl_elong_EF1_G_con.
[Graphical view]
PfamPF00647. EF1G. 1 hit.
PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
SSF89942. SSF89942. 1 hit.
PROSITEPS50040. EF1G_C. 1 hit.
PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEEF1G. human.
EvolutionaryTraceP26641.
GeneWikiEEF1G.
GenomeRNAi1937.
NextBio7847.
PROP26641.
SOURCESearch...

Entry information

Entry nameEF1G_HUMAN
AccessionPrimary (citable) accession number: P26641
Secondary accession number(s): Q6PJ62 expand/collapse secondary AC list , Q6PK31, Q96CU2, Q9P196
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 159 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM