Elongation factor 1-gamma - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P26641 (EF1G_HUMAN)

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

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

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Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	437 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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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.

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Ontologies

Keywords
Biological process	Protein biosynthesis
Molecular function	Elongation factor
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	translational elongation Non-traceable author statement. Source: UniProtKB
Cellular component	cytosol Inferred from Experiment. Source: Reactome eukaryotic translation elongation factor 1 complex Inferred from electronic annotation. Source: InterPro
Molecular function	protein binding Inferred from physical interaction. Source: UniProtKB translation elongation factor activity Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
EEF1B2	P24534	2	EBI-351467,EBI-354334
EEF1D	P29692	2	EBI-351467,EBI-358607
NDRG1	Q92597	1	EBI-351467,EBI-716486

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.4 Ref.5

Chain

2 – 437

436

Elongation factor 1-gamma

PRO_0000208813

Regions

Domain

2 – 87

GST N-terminal

Domain

88 – 216

129

GST C-terminal

Domain

276 – 437

162

EF-1-gamma C-terminal

Amino acid modifications

Modified residue

N-acetylalanine Ref.5

Modified residue

Phosphothreonine Ref.8

Modified residue

Phosphothreonine Ref.9

Modified residue

132

N6-acetyllysine Ref.11

Modified residue

147

N6-acetyllysine Ref.11

Modified residue

434

N6-acetyllysine Ref.11

Experimental info

Sequence conflict

102

A → V in AAH13918. Ref.3

Secondary structure

437

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P26641-1 [UniParc].

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

437

50,119

        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

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References

	« Hide 'large scale' referencesShow '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.

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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.

IPI

IPI00937615.

PIR

S22655.

RefSeq

NP_001395.1.

UniGene

Hs.144835

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PBU	NMR	-	A	276-437	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P26641. 64 interactions.

STRING

P26641.

PTM databases

PhosphoSite

P26641.

2-D gel databases

OGP

P26641.

Proteomic databases

PRIDE

P26641.

Genome annotation databases

Ensembl

ENST00000278279; 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]

GeneID

1937.

KEGG

hsa:1937.

UCSC

uc001ntm.1. human.

Organism-specific databases

CTD

1937.

GeneCards

GC11M062083.

H-InvDB

HIX0020040.

HGNC

HGNC:3213. EEF1G.

HPA

CAB004969.

MIM

130593. gene.

PharmGKB

PA27649.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P26641.

HOVERGEN

P26641.

Enzyme and pathway databases

Reactome

REACT_17015. Metabolism of proteins.
REACT_71. Gene Expression.

Gene expression databases

Bgee

P26641.

CleanEx

HS_EEF1G.

Genevestigator

P26641.

GermOnline

ENSG00000186676. Homo sapiens.

Family and domain databases

InterPro

IPR010987. 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]

Gene3D

G3DSA:1.20.1050.10. GST_C_like. 1 hit.
G3DSA:3.30.70.1010. Transl_elong_EF1_G_con. 1 hit.

Pfam

PF00647. EF1G. 1 hit.
PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]

ProDom

PD006217. EF1_G. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

PS50040. EF1G_C. 1 hit.
PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

7847.

SOURCE

Search...

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Entry information

Entry name

EF1G_HUMAN

Accession

Primary (citable) accession number: P26641
Secondary accession number(s): Q6PJ62

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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.

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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

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents