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Q02293 (FNTB_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:Fntb
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length437 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential subunit of the farnesyltransferase complex. Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. Ref.8 Ref.14 Ref.15 Ref.17

Catalytic activity

Farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate. Ref.8 Ref.13 Ref.14 Ref.15 Ref.17

Cofactor

Binds 1 zinc ion per subunit. Ref.5 Ref.6 Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17

Subunit structure

Heterodimer of FNTA and FNTB. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17

Sequence similarities

Belongs to the protein prenyltransferase subunit beta family.

Contains 5 PFTB repeats.

Ontologies

Keywords
   DomainRepeat
   LigandMetal-binding
Zinc
   Molecular functionPrenyltransferase
Transferase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processnegative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell cycle

Inferred from mutant phenotype PubMed 10544242. Source: RGD

positive regulation of cell proliferation

Inferred from mutant phenotype PubMed 10544242. Source: RGD

positive regulation of fibroblast proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of nitric-oxide synthase biosynthetic process

Inferred from mutant phenotype PubMed 9153192. Source: RGD

protein farnesylation

Inferred from sequence or structural similarity. Source: UniProtKB

response to cytokine

Inferred from mutant phenotype PubMed 9153192. Source: RGD

response to inorganic substance

Inferred from mutant phenotype PubMed 18957540. Source: RGD

response to organic cyclic compound

Inferred from mutant phenotype PubMed 16257390. Source: RGD

wound healing

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentmicrotubule associated complex

Inferred from electronic annotation. Source: Ensembl

protein complex

Inferred from direct assay PubMed 15248757. Source: RGD

protein farnesyltransferase complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionfarnesyltranstransferase activity

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 10377218PubMed 12657282PubMed 12657283PubMed 12657284Ref.11PubMed 12699757PubMed 15170324Ref.12. Source: IntAct

protein farnesyltransferase activity

Inferred from direct assay Ref.1. Source: RGD

zinc ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

FntaQ0463114EBI-602454,EBI-602447

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 437437Protein farnesyltransferase subunit beta
PRO_0000119763

Regions

Repeat123 – 16442PFTB 1
Repeat174 – 21542PFTB 2
Repeat222 – 26342PFTB 3
Repeat270 – 31243PFTB 4
Repeat332 – 37443PFTB 5
Region248 – 2514Farnesyl diphosphate binding
Region291 – 2944Farnesyl diphosphate binding
Region300 – 3034Farnesyl diphosphate binding

Sites

Metal binding2971Zinc; catalytic
Metal binding2991Zinc; catalytic
Metal binding3621Zinc; via tele nitrogen; catalytic
Site1021Important for selectivity against geranylgeranyl diphosphate By similarity

Secondary structure

....................................................................... 437
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q02293 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 41A9D6D79CD319A8

FASTA43748,673
        10         20         30         40         50         60 
MASSSSFTYY CPPSSSPVWS EPLYSLRPEH ARERLQDDSV ETVTSIEQAK VEEKIQEVFS 

        70         80         90        100        110        120 
SYKFNHLVPR LVLQREKHFH YLKRGLRQLT DAYECLDASR PWLCYWILHS LELLDEPIPQ 

       130        140        150        160        170        180 
IVATDVCQFL ELCQSPDGGF GGGPGQYPHL APTYAAVNAL CIIGTEEAYN VINREKLLQY 

       190        200        210        220        230        240 
LYSLKQPDGS FLMHVGGEVD VRSAYCAASV ASLTNIITPD LFEGTAEWIA RCQNWEGGIG 

       250        260        270        280        290        300 
GVPGMEAHGG YTFCGLAALV ILKKERSLNL KSLLQWVTSR QMRFEGGFQG RCNKLVDGCY 

       310        320        330        340        350        360 
SFWQAGLLPL LHRALHAQGD PALSMSHWMF HQQALQEYIL MCCQCPAGGL LDKPGKSRDF 

       370        380        390        400        410        420 
YHTCYCLSGL SIAQHFGSGA MLHDVVMGVP ENVLQPTHPV YNIGPDKVIQ ATTHFLQKPV 

       430 
PGFEECEDAV TSDPATD 

« Hide

References

« Hide 'large scale' references
[1]"cDNA cloning and expression of the peptide-binding beta subunit of rat p21ras farnesyltransferase, the counterpart of yeast DPR1/RAM1."
Chen W.-J., Andres D.A., Goldstein J.L., Russell D.W., Brown M.S.
Cell 66:327-334(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Brain.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[3]"Crystal structure of protein farnesyltransferase at 2.25-A resolution."
Park H.-W., Boduluri S.R., Mooomaw J.F., Casey P.J., Beese L.S.
Science 275:1800-1804(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH ZINC.
[4]Erratum
Park H.-W., Boduluri S.R., Mooomaw J.F., Casey P.J., Beese L.S.
Science 276:21-21(1997)
[5]"Protein farnesyltransferase: structure and implications for substrate binding."
Dunten P., Kammlott U., Crowther R., Weber D., Palermo R., Birktoft J.
Biochemistry 37:7907-7912(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH FNTA; FARNESYL DIPHOSPHATE AND ZINC IONS, SUBUNIT, COFACTOR.
[6]"Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate."
Long S.B., Casey P.J., Beese L.S.
Biochemistry 37:9612-9618(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) IN COMPLEX WITH FNTA; FARNESYL DIPHOSPHATE AND ZINC IONS, COFACTOR, SUBUNIT.
[7]"Crystal structure of farnesyl protein transferase complexed with a CaaX peptide and farnesyl diphosphate analogue."
Strickland C.L., Windsor W.T., Syto R., Wang L., Bond R., Wu Z., Schwartz J., Le H.V., Beese L.S., Weber P.C.
Biochemistry 37:16601-16611(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH FNTA; ZINC IONS AND FARNESYL DIPHOSPHATE ANALOG, COFACTOR, SUBUNIT.
[8]"The basis for K-Ras4B binding specificity to protein farnesyltransferase revealed by 2 A resolution ternary complex structures."
Long S.B., Casey P.J., Beese L.S.
Structure 8:209-222(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ZINC IONS; FNTA AND KRAS, INTERACTION WITH KRAS, CATALYTIC ACTIVITY, COFACTOR, FUNCTION, SUBUNIT.
[9]"The crystal structure of human protein farnesyltransferase reveals the basis for inhibition by CaaX tetrapeptides and their mimetics."
Long S.B., Hancock P.J., Kral A.M., Hellinga H.W., Beese L.S.
Proc. Natl. Acad. Sci. U.S.A. 98:12948-12953(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH FNTA AND GERANYLGERANYL DIPHOSPHATE, SUBUNIT.
[10]"Reaction path of protein farnesyltransferase at atomic resolution."
Long S.B., Casey P.J., Beese L.S.
Nature 419:645-650(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH FNTA; FARNESYL DIPHOSPHATE AND ZINC IONS, SUBUNIT, COFACTOR.
[11]"Biochemical and structural studies with prenyl diphosphate analogues provide insights into isoprenoid recognition by protein farnesyl transferase."
Turek-Etienne T.C., Strickland C.L., Distefano M.D.
Biochemistry 42:3716-3724(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-427 IN COMPLEX WITH FNTA; GERANYLGERANYL DIPHOSPHATE AND ZINC IONS, COFACTOR, SUBUNIT.
[12]"Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity."
Reid T.S., Terry K.L., Casey P.J., Beese L.S.
J. Mol. Biol. 343:417-433(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH FNTA AND ZINC IONS, COFACTOR, SUBUNIT.
[13]"Caged protein prenyltransferase substrates: tools for understanding protein prenylation."
DeGraw A.J., Hast M.A., Xu J., Mullen D., Beese L.S., Barany G., Distefano M.D.
Chem. Biol. Drug Des. 72:171-181(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH FNTA; FARNESYL DIPHOSPHATE AND ZINC, COFACTOR, CATALYTIC ACTIVITY, SUBUNIT.
[14]"Structural basis for binding and selectivity of antimalarial and anticancer ethylenediamine inhibitors to protein farnesyltransferase."
Hast M.A., Fletcher S., Cummings C.G., Pusateri E.E., Blaskovich M.A., Rivas K., Gelb M.H., Van Voorhis W.C., Sebti S.M., Hamilton A.D., Beese L.S.
Chem. Biol. 16:181-192(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH FNTA; FARNESYL DIPHOSPHATE AND ZINC IONS, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, SUBUNIT.
[15]"Analysis of the eukaryotic prenylome by isoprenoid affinity tagging."
Nguyen U.T., Guo Z., Delon C., Wu Y., Deraeve C., Franzel B., Bon R.S., Blankenfeldt W., Goody R.S., Waldmann H., Wolters D., Alexandrov K.
Nat. Chem. Biol. 5:227-235(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 1-427 IN COMPLEX WITH FNTA AND ZINC IONS, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, FUNCTION.
[16]"Discovery of C-imidazole azaheptapyridine FPT inhibitors."
Zhu H.Y., Cooper A.B., Desai J., Njoroge G., Kirschmeier P., Bishop W.R., Strickland C., Hruza A., Doll R.J., Girijavallabhan V.M.
Bioorg. Med. Chem. Lett. 20:1134-1136(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH FNTA; FARNESYL DIPHOSPHATE AND ZINC, SUBUNIT, COFACTOR.
[17]"Development of selective, potent RabGGTase inhibitors."
Stigter E.A., Guo Z., Bon R.S., Wu Y.W., Choidas A., Wolf A., Menninger S., Waldmann H., Blankenfeldt W., Goody R.S.
J. Med. Chem. 55:8330-8340(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1-427 IN COMPLEX WITH FNTA; FARNESYL DIPHOSPHATE AND ZINC IONS, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M69056 mRNA. Translation: AAA41176.1.
BC087675 mRNA. Translation: AAH87675.1.
PIRA40037.
RefSeqNP_742031.1. NM_172034.2.
UniGeneRn.8873.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1D8DX-ray2.00B1-437[»]
1D8EX-ray3.00B1-437[»]
1FPPX-ray2.75B1-437[»]
1FT1X-ray2.25B1-437[»]
1FT2X-ray3.40B22-422[»]
1FTImodel-B22-422[»]
1HZ7model-B41-406[»]
1JCRX-ray2.00B1-437[»]
1JCSX-ray2.20B1-437[»]
1KZOX-ray2.20B1-437[»]
1KZPX-ray2.10B1-437[»]
1KZRmodel-B17-423[»]
1N94X-ray3.50B22-418[»]
1N95X-ray2.30B22-423[»]
1N9AX-ray3.20B22-423[»]
1NI1X-ray2.30B22-423[»]
1NL4X-ray2.70B23-423[»]
1O1RX-ray2.30B1-427[»]
1O1SX-ray2.30B1-427[»]
1O1TX-ray2.10B1-427[»]
1O5MX-ray2.30B1-437[»]
1QBQX-ray2.40B1-437[»]
1QE2model-B41-406[»]
1SA5X-ray2.60B1-437[»]
1TN7X-ray2.30B1-437[»]
1TN8X-ray2.25B1-437[»]
1X81X-ray3.50B22-418[»]
2BEDX-ray2.70B23-423[»]
2FTImodel-B22-422[»]
2R2LX-ray2.23B23-423[»]
2ZIRX-ray2.40B1-437[»]
2ZISX-ray2.60B1-437[»]
3DPYX-ray2.70B1-437[»]
3E30X-ray2.45B1-437[»]
3E32X-ray2.45B1-437[»]
3E33X-ray1.90B1-437[»]
3E34X-ray2.05B1-437[»]
3EU5X-ray2.80B1-427[»]
3EUVX-ray2.75B1-427[»]
3FTImodel-B22-422[»]
3KSLX-ray2.05B1-437[»]
3KSQX-ray2.10B1-437[»]
4GTMX-ray2.20B1-427[»]
4GTOX-ray2.15B1-427[»]
4GTPX-ray2.75B1-427[»]
4GTQX-ray2.60B1-427[»]
4GTRX-ray2.20B1-427[»]
ProteinModelPortalQ02293.
SMRQ02293. Positions 22-437.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-6132N.
IntActQ02293. 1 interaction.
MINTMINT-121917.
STRING10116.ENSRNOP00000010588.

Chemistry

BindingDBQ02293.
ChEMBLCHEMBL2095197.

PTM databases

PhosphoSiteQ02293.

Proteomic databases

PaxDbQ02293.
PRIDEQ02293.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000010588; ENSRNOP00000010588; ENSRNOG00000007660.
GeneID64511.
KEGGrno:64511.
UCSCRGD:620119. rat.

Organism-specific databases

CTD2342.
RGD620119. Fntb.

Phylogenomic databases

eggNOGCOG5029.
GeneTreeENSGT00550000075042.
HOGENOMHOG000190594.
HOVERGENHBG008173.
InParanoidQ02293.
KOK05954.
OMAKLLDFLW.
OrthoDBEOG7P02HV.
PhylomeDBQ02293.
TreeFamTF353162.

Enzyme and pathway databases

SABIO-RKQ02293.

Gene expression databases

GenevestigatorQ02293.

Family and domain databases

Gene3D1.50.10.20. 1 hit.
InterProIPR026872. FTB.
IPR001330. Prenyltrans.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
[Graphical view]
PANTHERPTHR11774:SF6. PTHR11774:SF6. 1 hit.
PfamPF00432. Prenyltrans. 2 hits.
[Graphical view]
SUPFAMSSF48239. SSF48239. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ02293.
NextBio613294.
PROQ02293.

Entry information

Entry nameFNTB_RAT
AccessionPrimary (citable) accession number: Q02293
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: June 11, 2014
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references