P26641 (EF1G_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

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

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.

Ontologies

Keywords
Biological process	Protein biosynthesis
Molecular function	Elongation factor
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	response to virus Inferred from expression pattern Ref.8. Source: UniProtKB
Cellular_component	cytosol Traceable author statement. Source: Reactome eukaryotic translation elongation factor 1 complex Inferred from electronic annotation. Source: InterPro
Molecular_function	translation elongation factor activity Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EEF1B2	P24534	3	EBI-351467,EBI-354334
EEF1D	P29692	3	EBI-351467,EBI-358607

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.4 Ref.5

Chain

2 – 437

436

Elongation factor 1-gamma

PRO_0000208813

Regions

Domain

2 – 87

86

GST N-terminal

Domain

88 – 216

129

GST C-terminal

Domain

276 – 437

162

EF-1-gamma C-terminal

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.5

Modified residue

434

1

N6-acetyllysine; alternate Ref.9

Modified residue

434

1

N6-malonyllysine; alternate Ref.11

Experimental info

Sequence conflict

102

1

A → V in AAH13918. Ref.3

Secondary structure

1

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437

Helix Strand Turn

Details...

Helix

279 – 281

3

Helix

290 – 299

10

Helix

302 – 304

3

Helix

306 – 311

6

Turn

316 – 318

3

Beta strand

320 – 324

5

Helix

329 – 331

3

Helix

338 – 348

11

Helix

349 – 351

3

Helix

353 – 355

3

Beta strand

356 – 358

3

Beta strand

361 – 364

4

Beta strand

370 – 381

12

Helix

384 – 386

3

Helix

388 – 390

3

Helix

394 – 396

3

Helix

408 – 418

11

Turn

424 – 426

3

Sequences

	Sequence		Length	Mass (Da)
	P26641 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: A6110663110CF3FC	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

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] [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, 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, MASS SPECTROMETRY.
[9]	"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-434, MASS SPECTROMETRY.
[10]	"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].
[11]	"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.
[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] [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.

IPI

IPI00937615.

PIR

S22655.

RefSeq

NP_001395.1. NM_001404.4.

UniGene

Hs.144835.
Hs.444467.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

P26641.

ModBase

Search...

Protein-protein interaction databases

IntAct

P26641. 92 interactions.

MINT

MINT-1191315.

PTM databases

PhosphoSite

P26641.

Polymorphism databases

DMDM

119165.

2D gel databases

OGP

P26641.

Proteomic databases

PaxDb

P26641.

PRIDE

P26641.

Protocols and materials databases

DNASU

1937.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000329251; ENSP00000331901; ENSG00000254772.

GeneID

1937.

KEGG

hsa:1937.

UCSC

uc001ntm.1. human.

Organism-specific databases

CTD

1937.

GeneCards

GC11M062332.

HGNC

HGNC:3213. EEF1G.

HPA

HPA040688.

MIM

130593. gene.

neXtProt

NX_P26641.

PharmGKB

PA27649.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0625.

HOGENOM

HOG000235245.

HOVERGEN

HBG051444.

InParanoid

P26641.

KO

K03233.

PhylomeDB

P26641.

Enzyme and pathway databases

Reactome

REACT_17015. Metabolism of proteins.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P26641.

CleanEx

HS_EEF1G.

Genevestigator

P26641.

GermOnline

ENSG00000186676. Homo sapiens.

Family and domain databases

Gene3D

1.20.1050.10. 1 hit.
3.30.70.1010. 1 hit.
3.40.30.10. 1 hit.

InterPro

IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR017933. Glutathione_S_Trfase/Cl_chnl_C.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
IPR001662. Transl_elong_EF1_G_con.
[Graphical view]

Pfam

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

SUPFAM

SSF47616. GST_C_like. 1 hit.
SSF52833. Thiordxn-like_fd. 1 hit.
SSF89942. Transl_elong_EF1_G_con. 1 hit.

PROSITE

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

ProtoNet

Search...

Other

ChiTaRS

EEF1G. human.

EvolutionaryTrace

P26641.

GenomeRNAi

1937.

NextBio

7847.

SOURCE

Search...

Entry information

Entry name

EF1G_HUMAN

Accession

Primary (citable) accession number: P26641
Secondary accession number(s): Q6PJ62 , Q6PK31, Q96CU2, Q9P196

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 152 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.