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Protein

Protein farnesyltransferase subunit beta

Gene

cpp1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission 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. The beta subunit is responsible for peptide-binding.1 Publication

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)LengthDescriptionGraphical viewFeature identifierActions
Sitei58 – 581Important for selectivity against geranylgeranyl diphosphateBy similarity
Metal bindingi253 – 2531Zinc; catalyticBy similarity
Metal bindingi255 – 2551Zinc; catalyticBy similarity
Metal bindingi316 – 3161Zinc; via tele nitrogen; catalyticBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. protein farnesylation Source: PomBase
  2. protein targeting to plasma membrane Source: PomBase
  3. regulation of cell proliferation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Prenyltransferase, Transferase

Keywords - Ligandi

Metal-binding, Zinc

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:cpp1
ORF Names:SPAC17G6.04c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485: Chromosome I

Organism-specific databases

PomBaseiSPAC17G6.04c.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: PomBase
  2. nucleus Source: PomBase
  3. protein farnesyltransferase complex Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 382382Protein farnesyltransferase subunit betaPRO_0000119767Add
BLAST

Proteomic databases

MaxQBiO13782.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit.1 Publication

Protein-protein interaction databases

BioGridi278844. 11 interactions.
MINTiMINT-4667919.
STRINGi4896.SPAC17G6.04c-1.

Structurei

3D structure databases

ProteinModelPortaliO13782.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati78 – 11942PFTB 1Add
BLAST
Repeati129 – 17042PFTB 2Add
BLAST
Repeati178 – 21942PFTB 3Add
BLAST
Repeati226 – 26843PFTB 4Add
BLAST
Repeati286 – 32843PFTB 5Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni204 – 2074Farnesyl diphosphate bindingBy similarity
Regioni247 – 2504Farnesyl diphosphate bindingBy similarity
Regioni256 – 2594Farnesyl diphosphate bindingBy similarity

Sequence similaritiesi

Contains 5 PFTB repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5029.
HOGENOMiHOG000190594.
InParanoidiO13782.
KOiK05954.
OMAiEYILTCC.
OrthoDBiEOG7XSTQC.
PhylomeDBiO13782.

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. 1 hit.
[Graphical view]
SUPFAMiSSF48239. SSF48239. 1 hit.

Sequencei

Sequence statusi: Complete.

O13782-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDELSETQVM QNETATAVLP LLNGESQSFN LQKHLKYLTK MLDPLPSPFT
60 70 80 90 100
VLDASRAWMV YWELSSLAIL GKLDSSVCER AISSVRQLKG PSGGFCGGNG
110 120 130 140 150
QDEHLLSTYA SILSICLCDS TDAYSLIERD RLYDWLFSLK NPDGSFRVNN
160 170 180 190 200
EGESDARSVY AAVCVSSLVG ISMDDPLFEG TLQWLCKCQT YEGGLSGVPY
210 220 230 240 250
AEAHGGYTFC ALAAIALLGG LDNLNEIKLS TWLVQRQDPA LYGFSGRSNK
260 270 280 290 300
LVDGCYSWWV GASHVIVASG YGSASHKSLP NLFYNPEKLL GYILQCCQST
310 320 330 340 350
SGGLRDKPPK RPDQYHTCYC LLGLSSIAYD YRYHTSDGWS YKPSILHSSL
360 370 380
SSLLPAHPIY CVPFGFEERI KSYFLSQESS KF
Length:382
Mass (Da):42,189
Last modified:January 1, 1998 - v1
Checksum:iC3F2705D93F84203
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB16215.1.
PIRiT37836.
RefSeqiNP_594251.1. NM_001019674.2.

Genome annotation databases

EnsemblFungiiSPAC17G6.04c.1; SPAC17G6.04c.1:pep; SPAC17G6.04c.
GeneIDi2542380.
KEGGispo:SPAC17G6.04c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB16215.1.
PIRiT37836.
RefSeqiNP_594251.1. NM_001019674.2.

3D structure databases

ProteinModelPortaliO13782.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278844. 11 interactions.
MINTiMINT-4667919.
STRINGi4896.SPAC17G6.04c-1.

Proteomic databases

MaxQBiO13782.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC17G6.04c.1; SPAC17G6.04c.1:pep; SPAC17G6.04c.
GeneIDi2542380.
KEGGispo:SPAC17G6.04c.

Organism-specific databases

PomBaseiSPAC17G6.04c.

Phylogenomic databases

eggNOGiCOG5029.
HOGENOMiHOG000190594.
InParanoidiO13782.
KOiK05954.
OMAiEYILTCC.
OrthoDBiEOG7XSTQC.
PhylomeDBiO13782.

Miscellaneous databases

NextBioi20803439.
PROiO13782.

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. 1 hit.
[Graphical view]
SUPFAMiSSF48239. SSF48239. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Protein farnesylation is critical for maintaining normal cell morphology and canavanine resistance in Schizosaccharomyces pombe."
    Yang W., Urano J., Tamanoi F.
    J. Biol. Chem. 275:429-438(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT.
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.

Entry informationi

Entry nameiFNTB_SCHPO
AccessioniPrimary (citable) accession number: O13782
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: January 1, 1998
Last modified: January 7, 2015
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.