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Protein

Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha

Gene

RAM2

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

Functioni

Catalyzes the transfer of a farnesyl or geranyl-geranyl moiety from farnesyl or geranyl-geranyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. The alpha subunit is thought to participate in a stable complex with the substrate. The beta subunit binds the peptide substrate.

Catalytic activityi

Farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate.
Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate.

GO - Molecular functioni

  • CAAX-protein geranylgeranyltransferase activity Source: SGD
  • protein farnesyltransferase activity Source: SGD
  • protein geranylgeranyltransferase activity Source: SGD

GO - Biological processi

  • peptide pheromone maturation Source: SGD
  • protein farnesylation Source: SGD
  • protein geranylgeranylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Prenyltransferase, Transferase

Enzyme and pathway databases

BioCyciYEAST:MONOMER3O-38.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha (EC:2.5.1.58, EC:2.5.1.59)
Alternative name(s):
CAAX farnesyltransferase subunit alpha
FTase-alpha
Ras proteins prenyltransferase subunit alpha
Type I protein geranyl-geranyltransferase subunit alpha
Short name:
GGTase-I-alpha
Gene namesi
Name:RAM2
Ordered Locus Names:YKL019W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XI

Organism-specific databases

EuPathDBiFungiDB:YKL019W.
SGDiS000001502. RAM2.

Subcellular locationi

GO - Cellular componenti

  • CAAX-protein geranylgeranyltransferase complex Source: SGD
  • protein farnesyltransferase complex Source: SGD
Complete GO annotation...

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2111393.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 316316Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alphaPRO_0000119754Add
BLAST

Proteomic databases

MaxQBiP29703.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit.

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC43P188983EBI-14814,EBI-3961
RAM1P220074EBI-14814,EBI-14806

Protein-protein interaction databases

BioGridi34112. 23 interactions.
DIPiDIP-1233N.
IntActiP29703. 6 interactions.
MINTiMINT-396243.

Chemistry

BindingDBiP29703.

Structurei

3D structure databases

ProteinModelPortaliP29703.
SMRiP29703. Positions 3-315.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati47 – 8135PFTA 1Add
BLAST
Repeati89 – 12335PFTA 2Add
BLAST
Repeati125 – 15935PFTA 3Add
BLAST
Repeati160 – 19334PFTA 4Add
BLAST
Repeati199 – 23335PFTA 5Add
BLAST

Sequence similaritiesi

Contains 5 PFTA repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00550000074935.
HOGENOMiHOG000188957.
InParanoidiP29703.
KOiK05955.
OMAiFRIREAM.
OrthoDBiEOG7008JT.

Family and domain databases

InterProiIPR002088. Prenyl_trans_a.
[Graphical view]
PfamiPF01239. PPTA. 4 hits.
[Graphical view]
PROSITEiPS51147. PFTA. 5 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P29703-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEEYDYSDVK PLPIETDLQD ELCRIMYTED YKRLMGLARA LISLNELSPR
60 70 80 90 100
ALQLTAEIID VAPAFYTIWN YRFNIVRHMM SESEDTVLYL NKELDWLDEV
110 120 130 140 150
TLNNPKNYQI WSYRQSLLKL HPSPSFKREL PILKLMIDDD SKNYHVWSYR
160 170 180 190 200
KWCCLFFSDF QHELAYASDL IETDIYNNSA WTHRMFYWVN AKDVISKVEL
210 220 230 240 250
ADELQFIMDK IQLVPQNISP WTYLRGFQEL FHDRLQWDSK VVDFATTFIG
260 270 280 290 300
DVLSLPIGSP EDLPEIESSY ALEFLAYHWG ADPCTRDNAV KAYSLLAIKY
310
DPIRKNLWHH KINNLN
Length:316
Mass (Da):37,508
Last modified:April 1, 1993 - v1
Checksum:iD828519BB9914608
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M88584 Genomic DNA. Translation: AAA34957.1.
Z28019 Genomic DNA. Translation: CAA81854.1.
L24760 Genomic DNA. Translation: AAA20574.1.
BK006944 Genomic DNA. Translation: DAA09136.1.
PIRiA41626.
RefSeqiNP_012906.3. NM_001179585.3.

Genome annotation databases

EnsemblFungiiYKL019W; YKL019W; YKL019W.
GeneIDi853849.
KEGGisce:YKL019W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M88584 Genomic DNA. Translation: AAA34957.1.
Z28019 Genomic DNA. Translation: CAA81854.1.
L24760 Genomic DNA. Translation: AAA20574.1.
BK006944 Genomic DNA. Translation: DAA09136.1.
PIRiA41626.
RefSeqiNP_012906.3. NM_001179585.3.

3D structure databases

ProteinModelPortaliP29703.
SMRiP29703. Positions 3-315.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34112. 23 interactions.
DIPiDIP-1233N.
IntActiP29703. 6 interactions.
MINTiMINT-396243.

Chemistry

BindingDBiP29703.
ChEMBLiCHEMBL2111393.

Proteomic databases

MaxQBiP29703.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYKL019W; YKL019W; YKL019W.
GeneIDi853849.
KEGGisce:YKL019W.

Organism-specific databases

EuPathDBiFungiDB:YKL019W.
SGDiS000001502. RAM2.

Phylogenomic databases

GeneTreeiENSGT00550000074935.
HOGENOMiHOG000188957.
InParanoidiP29703.
KOiK05955.
OMAiFRIREAM.
OrthoDBiEOG7008JT.

Enzyme and pathway databases

BioCyciYEAST:MONOMER3O-38.

Miscellaneous databases

PROiP29703.

Family and domain databases

InterProiIPR002088. Prenyl_trans_a.
[Graphical view]
PfamiPF01239. PPTA. 4 hits.
[Graphical view]
PROSITEiPS51147. PFTA. 5 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "RAM2, an essential gene of yeast, and RAM1 encode the two polypeptide components of the farnesyltransferase that prenylates a-factor and Ras proteins."
    He B., Chen P., Chen S.-Y., Vancura K.L., Michaelis S., Powers S.
    Proc. Natl. Acad. Sci. U.S.A. 88:11373-11377(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Complete DNA sequence of yeast chromosome XI."
    Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
    , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
    Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Molecular characterization of the SPT23 gene: a dosage-dependent suppressor of Ty-induced promoter mutations from Saccharomyces cerevisiae."
    Burkett T.J., Garfinkel D.J.
    Yeast 10:81-92(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-110.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiFNTA_YEAST
AccessioniPrimary (citable) accession number: P29703
Secondary accession number(s): D6VXR6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: June 8, 2016
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 396 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.