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P22007

- FNTB_YEAST

UniProt

P22007 - FNTB_YEAST

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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: 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

Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei108 – 1081Important for selectivity against geranylgeranyl diphosphateBy similarity
Metal bindingi307 – 3071Zinc; catalyticBy similarity
Metal bindingi309 – 3091Zinc; catalyticBy similarity
Metal bindingi363 – 3631Zinc; via tele nitrogen; catalyticBy similarity

GO - Molecular functioni

  1. protein farnesyltransferase activity Source: SGD
  2. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. protein farnesylation Source: SGD
  2. 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
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

CYGDiYDL090c.
SGDiS000002248. RAM1.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 431431Protein farnesyltransferase subunit betaPRO_0000119768Add
BLAST

Proteomic databases

MaxQBiP22007.
PaxDbiP22007.

Expressioni

Gene expression databases

GenevestigatoriP22007.

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 interactions.
DIPiDIP-1556N.
IntActiP22007. 10 interactions.
MINTiMINT-396276.

Structurei

3D structure databases

ProteinModelPortaliP22007.
SMRiP22007. Positions 49-408.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati130 – 17142PFTB 1Add
BLAST
Repeati182 – 22443PFTB 2Add
BLAST
Repeati231 – 27343PFTB 3Add
BLAST
Repeati280 – 32243PFTB 4Add
BLAST
Repeati332 – 37544PFTB 5Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni258 – 2614Farnesyl diphosphate bindingBy similarity
Regioni301 – 3044Farnesyl diphosphate bindingBy similarity
Regioni310 – 3134Farnesyl diphosphate bindingBy similarity

Sequence similaritiesi

Contains 5 PFTB repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5029.
GeneTreeiENSGT00550000075042.
HOGENOMiHOG000190594.
InParanoidiP22007.
KOiK05954.
OMAiDEAHGGY.
OrthoDBiEOG7XSTQC.

Family and domain databases

Gene3Di1.50.10.20. 1 hit.
InterProiIPR026872. FTB.
IPR001330. Prenyltrans.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti47 – 471K → R in AAT92990. (PubMed:17322287)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi S67626. BVBYDP.
RefSeqi NP_010193.1. NM_001180149.1.

3D structure databases

ProteinModelPortali P22007.
SMRi P22007. Positions 49-408.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 31970. 47 interactions.
DIPi DIP-1556N.
IntActi P22007. 10 interactions.
MINTi MINT-396276.

Chemistry

BindingDBi P22007.
ChEMBLi CHEMBL2111393.

Proteomic databases

MaxQBi P22007.
PaxDbi P22007.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YDL090C ; YDL090C ; YDL090C .
GeneIDi 851468.
KEGGi sce:YDL090C.

Organism-specific databases

CYGDi YDL090c.
SGDi S000002248. RAM1.

Phylogenomic databases

eggNOGi COG5029.
GeneTreei ENSGT00550000075042.
HOGENOMi HOG000190594.
InParanoidi P22007.
KOi K05954.
OMAi DEAHGGY.
OrthoDBi EOG7XSTQC.

Enzyme and pathway databases

BioCyci YEAST:MONOMER3O-269.

Miscellaneous databases

NextBioi 968756.
PROi P22007.

Gene expression databases

Genevestigatori P22007.

Family and domain databases

Gene3Di 1.50.10.20. 1 hit.
InterProi IPR026872. FTB.
IPR001330. Prenyltrans.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
[Graphical view ]
PANTHERi PTHR11774:SF6. PTHR11774:SF6. 1 hit.
Pfami PF00432. Prenyltrans. 5 hits.
[Graphical view ]
SUPFAMi SSF48239. SSF48239. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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.
    , 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] [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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

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: October 29, 2014
This is version 136 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

External Data

Dasty 3