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Protein

Protein farnesyltransferase subunit beta

Gene

RAM1

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 moiety from farnesyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins such as a-factor and RAS. The beta subunit is responsible for peptide-binding.

Catalytic activityi

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

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei108Important for selectivity against geranylgeranyl diphosphateBy similarity1
Metal bindingi307Zinc; catalyticBy similarity1
Metal bindingi309Zinc; catalyticBy similarity1
Metal bindingi363Zinc; via tele nitrogen; catalyticBy similarity1

GO - Molecular functioni

  • protein farnesyltransferase activity Source: SGD
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • protein farnesylation Source: SGD
  • regulation of cell proliferation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Prenyltransferase, Transferase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:MONOMER3O-269.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein farnesyltransferase subunit beta (EC:2.5.1.58)
Short name:
FTase-beta
Alternative name(s):
CAAX farnesyltransferase subunit beta
Ras proteins prenyltransferase subunit beta
Gene namesi
Name:RAM1
Synonyms:DPR1, SCG2, STE16
Ordered Locus Names:YDL090C
ORF Names:D2412
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL090C.
SGDiS000002248. RAM1.

Subcellular locationi

GO - Cellular componenti

  • protein farnesyltransferase complex Source: SGD
Complete GO annotation...

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2111393.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001197681 – 431Protein farnesyltransferase subunit betaAdd BLAST431

Proteomic databases

MaxQBiP22007.
PRIDEiP22007.

PTM databases

iPTMnetiP22007.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit.

Binary interactionsi

WithEntry#Exp.IntActNotes
RAM2P297034EBI-14806,EBI-14814

Protein-protein interaction databases

BioGridi31970. 47 interactors.
DIPiDIP-1556N.
IntActiP22007. 10 interactors.
MINTiMINT-396276.

Chemistry databases

BindingDBiP22007.

Structurei

3D structure databases

ProteinModelPortaliP22007.
SMRiP22007.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati130 – 171PFTB 1Add BLAST42
Repeati182 – 224PFTB 2Add BLAST43
Repeati231 – 273PFTB 3Add BLAST43
Repeati280 – 322PFTB 4Add BLAST43
Repeati332 – 375PFTB 5Add BLAST44

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni258 – 261Farnesyl diphosphate bindingBy similarity4
Regioni301 – 304Farnesyl diphosphate bindingBy similarity4
Regioni310 – 313Farnesyl diphosphate bindingBy similarity4

Sequence similaritiesi

Contains 5 PFTB repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00550000075042.
HOGENOMiHOG000190594.
InParanoidiP22007.
KOiK05954.
OMAiNEADKCD.
OrthoDBiEOG092C26Q9.

Family and domain databases

CDDicd02893. FTase. 1 hit.
Gene3Di1.50.10.20. 1 hit.
InterProiIPR026872. FTB.
IPR001330. PFTB_repeat.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
[Graphical view]
PANTHERiPTHR11774:SF6. PTHR11774:SF6. 1 hit.
PfamiPF00432. Prenyltrans. 5 hits.
[Graphical view]
SUPFAMiSSF48239. SSF48239. 1 hit.

Sequencei

Sequence statusi: Complete.

P22007-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRQRVGRSIA RAKFINTALL GRKRPVMERV VDIAHVDSSK AIQPLMKELE
60 70 80 90 100
TDTTEARYKV LQSVLEIYDD EKNIEPALTK EFHKMYLDVA FEISLPPQMT
110 120 130 140 150
ALDASQPWML YWIANSLKVM DRDWLSDDTK RKIVDKLFTI SPSGGPFGGG
160 170 180 190 200
PGQLSHLAST YAAINALSLC DNIDGCWDRI DRKGIYQWLI SLKEPNGGFK
210 220 230 240 250
TCLEVGEVDT RGIYCALSIA TLLNILTEEL TEGVLNYLKN CQNYEGGFGS
260 270 280 290 300
CPHVDEAHGG YTFCATASLA ILRSMDQINV EKLLEWSSAR QLQEERGFCG
310 320 330 340 350
RSNKLVDGCY SFWVGGSAAI LEAFGYGQCF NKHALRDYIL YCCQEKEQPG
360 370 380 390 400
LRDKPGAHSD FYHTNYCLLG LAVAESSYSC TPNDSPHNIK CTPDRLIGSS
410 420 430
KLTDVNPVYG LPIENVRKII HYFKSNLSSP S
Length:431
Mass (Da):48,190
Last modified:November 1, 1997 - v2
Checksum:i2E3B64F30D2FF13A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti47K → R in AAT92990 (PubMed:17322287).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22753 Genomic DNA. Translation: AAA34579.1.
X95644 Genomic DNA. Translation: CAA64921.1.
Z74138 Genomic DNA. Translation: CAA98656.1.
AY692971 Genomic DNA. Translation: AAT92990.1.
BK006938 Genomic DNA. Translation: DAA11768.1.
PIRiS67626. BVBYDP.
RefSeqiNP_010193.1. NM_001180149.1.

Genome annotation databases

EnsemblFungiiYDL090C; YDL090C; YDL090C.
GeneIDi851468.
KEGGisce:YDL090C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22753 Genomic DNA. Translation: AAA34579.1.
X95644 Genomic DNA. Translation: CAA64921.1.
Z74138 Genomic DNA. Translation: CAA98656.1.
AY692971 Genomic DNA. Translation: AAT92990.1.
BK006938 Genomic DNA. Translation: DAA11768.1.
PIRiS67626. BVBYDP.
RefSeqiNP_010193.1. NM_001180149.1.

3D structure databases

ProteinModelPortaliP22007.
SMRiP22007.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31970. 47 interactors.
DIPiDIP-1556N.
IntActiP22007. 10 interactors.
MINTiMINT-396276.

Chemistry databases

BindingDBiP22007.
ChEMBLiCHEMBL2111393.

PTM databases

iPTMnetiP22007.

Proteomic databases

MaxQBiP22007.
PRIDEiP22007.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL090C; YDL090C; YDL090C.
GeneIDi851468.
KEGGisce:YDL090C.

Organism-specific databases

EuPathDBiFungiDB:YDL090C.
SGDiS000002248. RAM1.

Phylogenomic databases

GeneTreeiENSGT00550000075042.
HOGENOMiHOG000190594.
InParanoidiP22007.
KOiK05954.
OMAiNEADKCD.
OrthoDBiEOG092C26Q9.

Enzyme and pathway databases

BioCyciYEAST:MONOMER3O-269.

Miscellaneous databases

PROiP22007.

Family and domain databases

CDDicd02893. FTase. 1 hit.
Gene3Di1.50.10.20. 1 hit.
InterProiIPR026872. FTB.
IPR001330. PFTB_repeat.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
[Graphical view]
PANTHERiPTHR11774:SF6. PTHR11774:SF6. 1 hit.
PfamiPF00432. Prenyltrans. 5 hits.
[Graphical view]
SUPFAMiSSF48239. SSF48239. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiFNTB_YEAST
AccessioniPrimary (citable) accession number: P22007
Secondary accession number(s): D6VRQ8, E9P902, Q12422
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 149 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 3910 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 IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: 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.