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Reviewed, UniProtKB/Swiss-Prot P29547 (EF1G1_YEAST)

Last modified June 16, 2009. Version 100. 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 · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Elongation factor 1-gamma 1
      Short name=EF-1-gamma 1
Alternative name(s):
    Translation elongation factor 1B gamma 1
    Eukaryotic elongation factor 1Bgamma 1
      Short name=eEF1Bgamma 1
    Calcium and membrane-binding protein 1
    Calcium phospholipid-binding protein
      Short name=CPBP
Gene names
Name: CAM1
Synonyms: TEF3
Ordered Locus Names: YPL048W
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length415 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Subunit of the eukaryotic elongation factor 1 complex (eEF1). Probably plays a role in anchoring the complex to other cellular components. May be involved in transcriptional regulation of MXR1. Ref.7

Pathway

Protein biosynthesis; polypeptide chain elongation.

Subunit structure

The eukaryotic elongation factor 1 complex (eEF1) is probably a heterohexamer. Two trimeric complexes, each composed of eEF1A (TEF1 or TEF2), eEF1Balpha (EFB1) and eEF1Bgamma (CAM1 or TEF4), are probably dimerized via the eF1Bgamma subunits. The eEF1B subcomplex with the GEF activity is formed of eEF1Balpha and eEF1Bgamma. CAM1 interacts with EFB1. Component of a complex bound to MXR1 promoter region. Ref.9

Subcellular location

Cytoplasm. Nucleus. Ref.7 Ref.5

Domain

Ths GST-like domain mediates the interaction to eEFB1 and may be responsible for dimerization of the eEF1 complex.

Miscellaneous

Present with 60865 molecules/cell in log phase SD medium. Ref.6

There are 2 isoforms for eEF1Bgamma in yeast.

Sequence similarities

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

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 415415Elongation factor 1-gamma 1
PRO_0000208831

Regions

Domain1 – 7878GST N-terminal
Domain89 – 215127GST C-terminal
Domain254 – 415162EF-1-gamma C-terminal

Amino acid modifications

Modified residue321Phosphothreonine Ref.8

Experimental info

Sequence conflict1911W → C in AAA16892. Ref.1

Secondary structure

....................................... 415
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P29547-1 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 17BCE60FFB7B2890

FASTA41547,088
        10         20         30         40         50         60 
MSQGTLYANF RIRTWVPRGL VKALKLDVKV VTPDAAAEQF ARDFPLKKVP AFVGPKGYKL 

        70         80         90        100        110        120 
TEAMAINYYL VKLSQDDKMK TQLLGADDDL NAQAQIIRWQ SLANSDLCIQ IANTIVPLKG 

       130        140        150        160        170        180 
GAPYNKKSVD SAMDAVDKIV DIFENRLKNY TYLATENISL ADLVAASIFT RYFESLFGTE 

       190        200        210        220        230        240 
WRAQHPAIVR WFNTVRASPF LKDEYKDFKF ADKPLSPPQK KKEKKAPAAA PAASKKKEEA 

       250        260        270        280        290        300 
KPAATETETS SKKPKHPLEL LGKSTFVLDD WKRKYSNEDT RPVALPWFWE HYNPEEYSLW 

       310        320        330        340        350        360 
KVTYKYNDEL TLTFMSNNLV GGFFNRLSAS TKYMFGCLVV YGENNNNGIV GAVMVRGQDY 

       370        380        390        400        410 
VPAFDVAPDW ESYDYAKLDP TNDDDKEFIN NMWAWDKPVS VNGEPKEIVD GKVLK 

« Hide

References

« Hide 'large scale' references
[1]"DRS1 to DRS7, novel genes required for ribosome assembly and function in Saccharomyces cerevisiae."
Ripmaster T.L., Vaughn G.P., Woolford J.L. Jr.
Mol. Cell. Biol. 13:7901-7912(1993) [PubMed: 8247005] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Cloning and genetic characterization of a calcium- and phospholipid-binding protein from Saccharomyces cerevisiae that is homologous to translation elongation factor-1 gamma."
Kambouris N.G., Burke D.J., Creutz C.E.
Yeast 9:151-163(1993) [PubMed: 8465602] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. expand/collapse author list , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
Nature 387:103-105(1997) [PubMed: 9169875] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[4]"Calcium-dependent secretory vesicle-binding and lipid-binding proteins of Saccharomyces cerevisiae."
Creutz C.E., Snyder S.L., Kambouris N.G.
Yeast 7:229-244(1991) [PubMed: 1882548] [Abstract]
Cited for: PROTEIN SEQUENCE OF 357-373.
[5]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed: 14562095] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[6]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]"A homologue of elongation factor 1 gamma regulates methionine sulfoxide reductase A gene expression in Saccharomyces cerevisiae."
Hanbauer I., Boja E.S., Moskovitz J.
Proc. Natl. Acad. Sci. U.S.A. 100:8199-8204(2003) [PubMed: 12824466] [Abstract]
Cited for: FUNCTION IN TRANSCRIPTIONAL REGULATION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[8]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-32, MASS SPECTROMETRY.
[9]"The crystal structure of the glutathione S-transferase-like domain of elongation factor 1Bgamma from Saccharomyces cerevisiae."
Jeppesen M.G., Ortiz P.A., Shepard W., Kinzy T.G., Nyborg J., Andersen G.R.
J. Biol. Chem. 278:47190-47198(2003) [PubMed: 12972429] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 2-219, INTERACTION WITH EFB1, PUTATIVE STRUCTURE OF THE EEF1 COMPLEX.
+Additional computationally mapped references.

Cross-references

Sequence databases

L01879 Unassigned DNA. Translation: AAA16892.1.
X67917 Genomic DNA. Translation: CAA48116.1.
U44030 Genomic DNA. Translation: AAB68173.1.
PIRS29345.
RefSeqNP_015277.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1NHYX-ray3.00A1-219[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:6813N.
IntActP29547. 11 interactions.

Proteomic databases

PeptideAtlasP29547.
PRIDEP29547.

Genome annotation databases

EnsemblYPL048W. Saccharomyces cerevisiae. [Contig view]
GeneID856059.
GenomeReviewsGene locus YPL048W in contig U00094_GR.
KEGGsce:YPL048W.
NMPDRfig|4932.3.peg.6410.

Organism-specific databases

CYGDYPL048w.
SGDS000005969. CAM1.
Yeast-GFPSearch...

Phylogenomic databases

HOGENOMP29547.
OMAP29547. KSIPYFW.

Gene expression databases

ArrayExpressP29547.
GermOnlineYPL048W. Saccharomyces cerevisiae.

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.
IPR012335. Thioredoxin_fold.
IPR001662. Transl_elong_EF1_G_con.
[Graphical view]
Gene3DG3DSA:1.20.1050.10. GST_C_like. 1 hit.
G3DSA:3.40.30.10. Thioredoxin_fold. 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

NextBio981032.

Entry information

Entry nameEF1G1_YEAST
AccessionPrimary (citable) accession number: P29547
Secondary accession number(s): Q9URC6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: October 1, 1996
Last modified: June 16, 2009
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

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