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P29547

- EF1G1_YEAST

UniProt

P29547 - EF1G1_YEAST

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Protein

Elongation factor 1-gamma 1

Gene

CAM1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 MXR1.1 Publication

Pathwayi

GO - Molecular functioni

  1. calcium ion binding Source: SGD
  2. phospholipid binding Source: SGD
  3. transcription coactivator activity Source: SGD
  4. translation elongation factor activity Source: UniProtKB-KW

GO - Biological processi

  1. positive regulation of transcription from RNA polymerase II promoter Source: SGD
  2. ribosome biogenesis Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Elongation factor

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

BioCyciYEAST:G3O-33961-MONOMER.
UniPathwayiUPA00345.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:CAM1
Synonyms:TEF3
Ordered Locus Names:YPL048W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XVI

Organism-specific databases

CYGDiYPL048w.
SGDiS000005969. CAM1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 415414Elongation factor 1-gamma 1PRO_0000208831Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei32 – 321Phosphothreonine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP29547.
PaxDbiP29547.
PeptideAtlasiP29547.

Expressioni

Gene expression databases

GenevestigatoriP29547.

Interactioni

Subunit structurei

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.1 Publication

Protein-protein interaction databases

BioGridi36132. 54 interactions.
DIPiDIP-6813N.
IntActiP29547. 11 interactions.
MINTiMINT-644858.
STRINGi4932.YPL048W.

Structurei

Secondary structure

1
415
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 73
Helixi12 – 2413
Beta strandi29 – 313
Helixi33 – 353
Helixi37 – 437
Beta strandi49 – 535
Helixi55 – 573
Beta strandi59 – 624
Helixi63 – 7311
Helixi77 – 837
Helixi90 – 10415
Turni105 – 1084
Helixi109 – 1135
Helixi115 – 1184
Helixi126 – 14722
Beta strandi151 – 1577
Helixi160 – 17516
Helixi179 – 1846
Helixi186 – 19712
Turni199 – 2013
Helixi202 – 2043

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NHYX-ray3.00A1-219[»]
ProteinModelPortaliP29547.
SMRiP29547. Positions 1-219, 255-415.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29547.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 7877GST N-terminalAdd
BLAST
Domaini89 – 215127GST C-terminalAdd
BLAST
Domaini254 – 415162EF-1-gamma C-terminalPROSITE-ProRule annotationAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 EF-1-gamma C-terminal domain.PROSITE-ProRule annotation
Contains 1 GST C-terminal domain.Curated
Contains 1 GST N-terminal domain.Curated

Phylogenomic databases

eggNOGiCOG0625.
GeneTreeiENSGT00390000007552.
HOGENOMiHOG000201196.
InParanoidiP29547.
KOiK03233.
OMAiENYSIWY.
OrthoDBiEOG7RBZK2.

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.

P29547-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSQGTLYANF RIRTWVPRGL VKALKLDVKV VTPDAAAEQF ARDFPLKKVP
60 70 80 90 100
AFVGPKGYKL TEAMAINYYL VKLSQDDKMK TQLLGADDDL NAQAQIIRWQ
110 120 130 140 150
SLANSDLCIQ IANTIVPLKG GAPYNKKSVD SAMDAVDKIV DIFENRLKNY
160 170 180 190 200
TYLATENISL ADLVAASIFT RYFESLFGTE WRAQHPAIVR WFNTVRASPF
210 220 230 240 250
LKDEYKDFKF ADKPLSPPQK KKEKKAPAAA PAASKKKEEA KPAATETETS
260 270 280 290 300
SKKPKHPLEL LGKSTFVLDD WKRKYSNEDT RPVALPWFWE HYNPEEYSLW
310 320 330 340 350
KVTYKYNDEL TLTFMSNNLV GGFFNRLSAS TKYMFGCLVV YGENNNNGIV
360 370 380 390 400
GAVMVRGQDY VPAFDVAPDW ESYDYAKLDP TNDDDKEFIN NMWAWDKPVS
410
VNGEPKEIVD GKVLK
Length:415
Mass (Da):47,088
Last modified:October 1, 1996 - v2
Checksum:i17BCE60FFB7B2890
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti191 – 1911W → C in AAA16892. (PubMed:8247005)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L01879 Unassigned DNA. Translation: AAA16892.1.
X67917 Genomic DNA. Translation: CAA48116.1.
U44030 Genomic DNA. Translation: AAB68173.1.
BK006949 Genomic DNA. Translation: DAA11382.1.
PIRiS29345.
RefSeqiNP_015277.1. NM_001183862.1.

Genome annotation databases

EnsemblFungiiYPL048W; YPL048W; YPL048W.
GeneIDi856059.
KEGGisce:YPL048W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L01879 Unassigned DNA. Translation: AAA16892.1 .
X67917 Genomic DNA. Translation: CAA48116.1 .
U44030 Genomic DNA. Translation: AAB68173.1 .
BK006949 Genomic DNA. Translation: DAA11382.1 .
PIRi S29345.
RefSeqi NP_015277.1. NM_001183862.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1NHY X-ray 3.00 A 1-219 [» ]
ProteinModelPortali P29547.
SMRi P29547. Positions 1-219, 255-415.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 36132. 54 interactions.
DIPi DIP-6813N.
IntActi P29547. 11 interactions.
MINTi MINT-644858.
STRINGi 4932.YPL048W.

Proteomic databases

MaxQBi P29547.
PaxDbi P29547.
PeptideAtlasi P29547.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YPL048W ; YPL048W ; YPL048W .
GeneIDi 856059.
KEGGi sce:YPL048W.

Organism-specific databases

CYGDi YPL048w.
SGDi S000005969. CAM1.

Phylogenomic databases

eggNOGi COG0625.
GeneTreei ENSGT00390000007552.
HOGENOMi HOG000201196.
InParanoidi P29547.
KOi K03233.
OMAi ENYSIWY.
OrthoDBi EOG7RBZK2.

Enzyme and pathway databases

UniPathwayi UPA00345 .
BioCyci YEAST:G3O-33961-MONOMER.

Miscellaneous databases

EvolutionaryTracei P29547.
NextBioi 981032.

Gene expression databases

Genevestigatori P29547.

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. "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.
    , 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. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. 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. 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.

Entry informationi

Entry nameiEF1G1_YEAST
AccessioniPrimary (citable) accession number: P29547
Secondary accession number(s): D6W3W6, Q9URC6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: October 1, 1996
Last modified: October 29, 2014
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 60865 molecules/cell in log phase SD medium.1 Publication
There are 2 isoforms for eEF1Bgamma in yeast.

Keywords - Technical termi

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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

External Data

Dasty 3