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P26641

- EF1G_HUMAN

UniProt

P26641 - EF1G_HUMAN

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Protein

Elongation factor 1-gamma

Gene
EEF1G, EF1G, PRO1608
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  1. protein binding Source: UniProtKB
  2. translation elongation factor activity Source: UniProtKB-KW

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. gene expression Source: Reactome
  3. response to virus Source: UniProtKB
  4. translation Source: Reactome
  5. translational elongation Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Elongation factor

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

ReactomeiREACT_1477. Eukaryotic Translation Elongation.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor 1-gamma
Short name:
EF-1-gamma
Alternative name(s):
eEF-1B gamma
Gene namesi
Name:EEF1G
Synonyms:EF1G
ORF Names:PRO1608
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:3213. EEF1G.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProt
  3. nucleus Source: UniProt
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27649.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 437436Elongation factor 1-gammaPRO_0000208813Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine4 Publications
Modified residuei147 – 1471N6-acetyllysine1 Publication
Modified residuei212 – 2121N6-acetyllysine By similarity
Modified residuei401 – 4011N6-acetyllysine By similarity
Modified residuei434 – 4341N6-acetyllysine; alternate1 Publication
Modified residuei434 – 4341N6-malonyllysine; alternate1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP26641.
PaxDbiP26641.
PRIDEiP26641.

2D gel databases

OGPiP26641.

PTM databases

PhosphoSiteiP26641.

Expressioni

Tissue specificityi

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

Inductioni

Down-regulated in response to enterovirus 71 (EV71) infection.1 Publication

Gene expression databases

CleanExiHS_EEF1G.
GenevestigatoriP26641.

Organism-specific databases

HPAiHPA040688.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
EEF1B2P245343EBI-351467,EBI-354334
EEF1DP296923EBI-351467,EBI-358607
TRIM63Q969Q12EBI-351467,EBI-5661333

Protein-protein interaction databases

BioGridi108257. 123 interactions.
DIPiDIP-32516N.
IntActiP26641. 113 interactions.
MINTiMINT-1191315.

Structurei

Secondary structure

1
437
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi279 – 2813
Helixi290 – 29910
Helixi302 – 3043
Helixi306 – 3116
Turni316 – 3183
Beta strandi320 – 3245
Helixi329 – 3313
Helixi338 – 34811
Helixi349 – 3513
Helixi353 – 3553
Beta strandi356 – 3583
Beta strandi361 – 3644
Beta strandi370 – 38112
Helixi384 – 3863
Helixi388 – 3903
Helixi394 – 3963
Helixi408 – 41811
Turni424 – 4263

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PBUNMR-A276-437[»]
ProteinModelPortaliP26641.
SMRiP26641. Positions 1-202, 276-437.

Miscellaneous databases

EvolutionaryTraceiP26641.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 8786GST N-terminalAdd
BLAST
Domaini88 – 216129GST C-terminalAdd
BLAST
Domaini276 – 437162EF-1-gamma C-terminalAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0625.
HOGENOMiHOG000235245.
HOVERGENiHBG051444.
InParanoidiP26641.
KOiK03233.
OrthoDBiEOG72G177.
PhylomeDBiP26641.
TreeFamiTF314343.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.30.70.1010. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. 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]
PfamiPF00647. EF1G. 1 hit.
PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
SSF89942. SSF89942. 1 hit.
PROSITEiPS50040. EF1G_C. 1 hit.
PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P26641-1 [UniParc]FASTAAdd to Basket

« Hide

MAAGTLYTYP ENWRAFKALI AAQYSGAQVR VLSAPPHFHF GQTNRTPEFL    50
RKFPAGKVPA FEGDDGFCVF ESNAIAYYVS NEELRGSTPE AAAQVVQWVS 100
FADSDIVPPA STWVFPTLGI MHHNKQATEN AKEEVRRILG LLDAYLKTRT 150
FLVGERVTLA DITVVCTLLW LYKQVLEPSF RQAFPNTNRW FLTCINQPQF 200
RAVLGEVKLC EKMAQFDAKK FAETQPKKDT PRKEKGSREE KQKPQAERKE 250
EKKAAAPAPE EEMDECEQAL AAEPKAKDPF AHLPKSTFVL DEFKRKYSNE 300
DTLSVALPYF WEHFDKDGWS LWYSEYRFPE ELTQTFMSCN LITGMFQRLD 350
KLRKNAFASV ILFGTNNSSS ISGVWVFRGQ ELAFPLSPDW QVDYESYTWR 400
KLDPGSEETQ TLVREYFSWE GAFQHVGKAF NQGKIFK 437
Length:437
Mass (Da):50,119
Last modified:January 23, 2007 - v3
Checksum:iA6110663110CF3FC
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti102 – 1021A → V in AAH13918. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS44626.1.
PIRiS22655.
RefSeqiNP_001395.1. NM_001404.4.
UniGeneiHs.144835.
Hs.444467.

Genome annotation databases

EnsembliENST00000329251; ENSP00000331901; ENSG00000254772.
GeneIDi1937.
KEGGihsa:1937.
UCSCiuc001ntm.1. human.

Polymorphism databases

DMDMi119165.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS44626.1.
PIRi S22655.
RefSeqi NP_001395.1. NM_001404.4.
UniGenei Hs.144835.
Hs.444467.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1PBU NMR - A 276-437 [» ]
ProteinModelPortali P26641.
SMRi P26641. Positions 1-202, 276-437.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108257. 123 interactions.
DIPi DIP-32516N.
IntActi P26641. 113 interactions.
MINTi MINT-1191315.

PTM databases

PhosphoSitei P26641.

Polymorphism databases

DMDMi 119165.

2D gel databases

OGPi P26641.

Proteomic databases

MaxQBi P26641.
PaxDbi P26641.
PRIDEi P26641.

Protocols and materials databases

DNASUi 1937.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000329251 ; ENSP00000331901 ; ENSG00000254772 .
GeneIDi 1937.
KEGGi hsa:1937.
UCSCi uc001ntm.1. human.

Organism-specific databases

CTDi 1937.
GeneCardsi GC11M062332.
HGNCi HGNC:3213. EEF1G.
HPAi HPA040688.
MIMi 130593. gene.
neXtProti NX_P26641.
PharmGKBi PA27649.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0625.
HOGENOMi HOG000235245.
HOVERGENi HBG051444.
InParanoidi P26641.
KOi K03233.
OrthoDBi EOG72G177.
PhylomeDBi P26641.
TreeFami TF314343.

Enzyme and pathway databases

Reactomei REACT_1477. Eukaryotic Translation Elongation.

Miscellaneous databases

ChiTaRSi EEF1G. human.
EvolutionaryTracei P26641.
GeneWikii EEF1G.
GenomeRNAii 1937.
NextBioi 7847.
PROi P26641.
SOURCEi Search...

Gene expression databases

CleanExi HS_EEF1G.
Genevestigatori P26641.

Family and domain databases

Gene3Di 1.20.1050.10. 1 hit.
3.30.70.1010. 1 hit.
3.40.30.10. 1 hit.
InterProi IPR010987. 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 ]
Pfami PF00647. EF1G. 1 hit.
PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view ]
SUPFAMi SSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
SSF89942. SSF89942. 1 hit.
PROSITEi PS50040. EF1G_C. 1 hit.
PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. 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. 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.

Entry informationi

Entry nameiEF1G_HUMAN
AccessioniPrimary (citable) accession number: P26641
Secondary accession number(s): Q6PJ62
, Q6PK31, Q96CU2, Q9P196
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 163 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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