Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P29547 (EF1G1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Elongation factor 1-gamma 1

Short name=EF-1-gamma 1
Alternative name(s):
Calcium and membrane-binding protein 1
Calcium phospholipid-binding protein
Short name=CPBP
Eukaryotic elongation factor 1Bgamma 1
Short name=eEF1Bgamma 1
Translation elongation factor 1B gamma 1
Gene names
Name:CAM1
Synonyms:TEF3
Ordered Locus Names:YPL048W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length415 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.8

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.11

Subcellular location

Cytoplasm. Nucleus Ref.6 Ref.8.

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.

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

Initiator methionine11Removed Ref.10
Chain2 – 415414Elongation factor 1-gamma 1
PRO_0000208831

Regions

Domain2 – 7877GST N-terminal
Domain89 – 215127GST C-terminal
Domain254 – 415162EF-1-gamma C-terminal

Amino acid modifications

Modified residue21N-acetylserine Ref.10
Modified residue321Phosphothreonine Ref.9

Experimental info

Sequence conflict1911W → C in AAA16892. Ref.1

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P29547 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 357-373.
[6]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]"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] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TRANSCRIPTIONAL REGULATION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[9]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-32, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[11]"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] [Europe PMC] [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

EMBL
GenBank
DDBJ
L01879 Unassigned DNA. Translation: AAA16892.1.
X67917 Genomic DNA. Translation: CAA48116.1.
U44030 Genomic DNA. Translation: AAB68173.1.
BK006949 Genomic DNA. Translation: DAA11382.1.
PIRS29345.
RefSeqNP_015277.1. NM_001183862.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NHYX-ray3.00A1-219[»]
ProteinModelPortalP29547.
SMRP29547. Positions 1-219, 255-415.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36132. 53 interactions.
DIPDIP-6813N.
IntActP29547. 11 interactions.
MINTMINT-644858.
STRING4932.YPL048W.

Proteomic databases

MaxQBP29547.
PaxDbP29547.
PeptideAtlasP29547.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYPL048W; YPL048W; YPL048W.
GeneID856059.
KEGGsce:YPL048W.

Organism-specific databases

CYGDYPL048w.
SGDS000005969. CAM1.

Phylogenomic databases

eggNOGCOG0625.
GeneTreeENSGT00390000007552.
HOGENOMHOG000201196.
KOK03233.
OMAENYSIWY.
OrthoDBEOG7RBZK2.

Enzyme and pathway databases

BioCycYEAST:G3O-33961-MONOMER.
UniPathwayUPA00345.

Gene expression databases

GenevestigatorP29547.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.30.70.1010. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. 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]
PfamPF00647. EF1G. 1 hit.
PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
SSF89942. SSF89942. 1 hit.
PROSITEPS50040. EF1G_C. 1 hit.
PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP29547.
NextBio981032.

Entry information

Entry nameEF1G1_YEAST
AccessionPrimary (citable) accession number: P29547
Secondary accession number(s): D6W3W6, Q9URC6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: October 1, 1996
Last modified: May 14, 2014
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XVI

Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

Yeast

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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways