Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P22007 (FNTB_YEAST)

Last modified November 24, 2009. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Protein farnesyltransferase subunit beta
      Short name=FTase-beta
    EC=2.5.1.58
Alternative name(s):
    CAAX farnesyltransferase subunit beta
    Ras proteins prenyltransferase subunit beta
Gene names
Name: RAM1
Synonyms: DPR1, SCG2, STE16
Ordered Locus Names: YDL090C
ORF Names: D2412
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Hide | Top

Protein attributes

Sequence length431 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Function

Catalyzes the transfer of a farnesyl moiety from farnesyl pyrophosphate 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 activity

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

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Heterodimer of an alpha and a beta subunit.

Miscellaneous

Present with 3910 molecules/cell in log phase SD medium. Ref.4

Sequence similarities

Belongs to the protein prenyltransferase subunit beta family.

Contains 5 PFTB repeats.

Hide | Top

Ontologies

Keywords
   DomainRepeat
   LigandMetal-binding
Zinc
   Molecular functionPrenyltransferase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processprotein amino acid farnesylation

Inferred from direct assay. Source: SGD

   Cellular componentprotein farnesyltransferase complex

Inferred from direct assay. Source: SGD

   Molecular functionprotein binding

Inferred from physical interaction. Source: IntAct

protein farnesyltransferase activity

Inferred from direct assay. Source: SGD

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Hide | Top

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RAM2P297032EBI-14806,EBI-14814

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 431431Protein farnesyltransferase subunit beta
PRO_0000119768

Regions

Repeat130 – 17142PFTB 1
Repeat182 – 22443PFTB 2
Repeat231 – 27343PFTB 3
Repeat280 – 32243PFTB 4
Repeat332 – 37544PFTB 5

Sites

Metal binding3071Zinc By similarity
Metal binding3091Zinc By similarity
Metal binding3631Zinc By similarity

Amino acid modifications

Modified residue171Phosphothreonine Ref.5
Modified residue381Phosphoserine Ref.5

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P22007-1 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 2E3B64F30D2FF13A

FASTA43148,190
        10         20         30         40         50         60 
MRQRVGRSIA RAKFINTALL GRKRPVMERV VDIAHVDSSK AIQPLMKELE TDTTEARYKV 

        70         80         90        100        110        120 
LQSVLEIYDD EKNIEPALTK EFHKMYLDVA FEISLPPQMT ALDASQPWML YWIANSLKVM 

       130        140        150        160        170        180 
DRDWLSDDTK RKIVDKLFTI SPSGGPFGGG PGQLSHLAST YAAINALSLC DNIDGCWDRI 

       190        200        210        220        230        240 
DRKGIYQWLI SLKEPNGGFK TCLEVGEVDT RGIYCALSIA TLLNILTEEL TEGVLNYLKN 

       250        260        270        280        290        300 
CQNYEGGFGS CPHVDEAHGG YTFCATASLA ILRSMDQINV EKLLEWSSAR QLQEERGFCG 

       310        320        330        340        350        360 
RSNKLVDGCY SFWVGGSAAI LEAFGYGQCF NKHALRDYIL YCCQEKEQPG LRDKPGAHSD 

       370        380        390        400        410        420 
FYHTNYCLLG LAVAESSYSC TPNDSPHNIK CTPDRLIGSS KLTDVNPVYG LPIENVRKII 

       430 
HYFKSNLSSP S

« Hide

Hide | Top

References

« Hide 'large scale' references
[1]"Structure and expression of yeast DPR1, a gene essential for the processing and intracellular localization of ras proteins."
Goodman L.E., Perou C.M., Fujiyama A., Tamanoi F.
Yeast 4:271-281(1988) [PubMed: 3064491] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The sequence of a 16,691 bp segment of Saccharomyces cerevisiae chromosome IV identifies the DUN1, PMT1, PMT5, SRP14 and DPR1 genes, and five new open reading frames."
Boskovic J., Soler-Mira A., Garcia-Cantalejo J.M., Ballesta J.P.G., Jimenez A., Remacha M.A.
Yeast 12:1377-1384(1996) [PubMed: 8923743] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed: 9169867] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"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].
[5]"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-17 AND SER-38, MASS SPECTROMETRY.
+Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

M22753 Genomic DNA. Translation: AAA34579.1.
X95644 Genomic DNA. Translation: CAA64921.1.
Z74138 Genomic DNA. Translation: CAA98656.1.
PIRBVBYDP. S67626.
RefSeqNP_010193.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP:1556N.
IntActP22007. 20 interactions.
STRINGP22007.

Genome annotation databases

EnsemblYDL090C; YDL090C; YDL090C; Saccharomyces cerevisiae. [Genome view]
GeneID851468.
KEGGsce:YDL090C.
NMPDRfig|4932.3.peg.931.

Organism-specific databases

CYGDYDL090c.
SGDS000002248. RAM1.

Phylogenomic databases

HOGENOMP22007.
OMAYWIANSL
OrthoDBEOG9KWM9K

Enzyme and pathway databases

BRENDA2.5.1.58. 250.

Gene expression databases

ArrayExpressP22007.
GenevestigatorP22007.
GermOnlineYDL090C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR001330. Prenyltrans.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
[Graphical view]
PfamPF00432. Prenyltrans. 5 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio968756.

Hide | Top

Entry information

Entry nameFNTB_YEAST
AccessionPrimary (citable) accession number: P22007
Secondary accession number(s): Q12422
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: November 1, 1997
Last modified: November 24, 2009
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Hide | Top

Relevant documents

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 · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents