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Reviewed, UniProtKB/Swiss-Prot P26641 (EF1G_HUMAN)

Last modified November 3, 2009. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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) [Complete 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.

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
Modified residue431Phosphothreonine Ref.8
Modified residue461Phosphothreonine Ref.9
Modified residue1321N6-acetyllysine Ref.11
Modified residue1471N6-acetyllysine Ref.11
Modified residue4341N6-acetyllysine Ref.11

Experimental info

Sequence conflict1021A → V in AAH13918. Ref.3

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P26641-1 [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: 1461723] [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: 1598220] [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: 15489334] [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: 12665801] [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, 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: 1372736] [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]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-43, MASS SPECTROMETRY.
Tissue: Epithelium.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-46, MASS SPECTROMETRY.
[10]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[11]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-132; LYS-147 AND LYS-434, MASS SPECTROMETRY.
[12]"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: 12766415] [Abstract]
Cited for: STRUCTURE BY NMR OF 276-437.

Cross-references

Sequence databases

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.
IPIIPI00937615.
PIRS22655.
RefSeqNP_001395.1.
UniGeneHs.144835

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1PBUNMR-A276-437[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP26641. 64 interactions.
STRINGP26641.

PTM databases

PhosphoSiteP26641.

2-D gel databases

OGPP26641.

Proteomic databases

PRIDEP26641.

Genome annotation databases

EnsemblENST00000278279; ENSP00000278279; ENSG00000149016; Homo sapiens. [Genome view]
ENST00000308436; ENSP00000308000; ENSG00000149016; Homo sapiens. [Genome view]
ENST00000329251; ENSP00000331901; ENSG00000149016; Homo sapiens. [Genome view]
ENST00000378019; ENSP00000367258; ENSG00000149016; Homo sapiens. [Genome view]
ENST00000422402; ENSP00000413374; ENSG00000149016; Homo sapiens. [Genome view]
ENST00000424909; ENSP00000403989; ENSG00000149016; Homo sapiens. [Genome view]
GeneID1937.
KEGGhsa:1937.
UCSCuc001ntm.1. human.

Organism-specific databases

CTD1937.
GeneCardsGC11M062083.
H-InvDBHIX0020040.
HGNCHGNC:3213. EEF1G.
HPACAB004969.
MIM130593. gene.
PharmGKBPA27649.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP26641.
HOVERGENP26641.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
REACT_71. Gene Expression.

Gene expression databases

BgeeP26641.
CleanExHS_EEF1G.
GenevestigatorP26641.
GermOnlineENSG00000186676. Homo sapiens.

Family and domain databases

InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR017933. Glutathione_S_Trfase/Cl_chnl_C.
IPR004046. GST_C.
IPR001662. Transl_elong_EF1_G_con.
[Graphical view]
Gene3DG3DSA:1.20.1050.10. GST_C_like. 1 hit.
G3DSA:3.30.70.1010. Transl_elong_EF1_G_con. 1 hit.
PfamPF00647. EF1G. 1 hit.
PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
ProDomPD006217. EF1_G. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS50040. EF1G_C. 1 hit.
PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio7847.
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: November 3, 2009
This is version 117 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 11

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

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents