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Reviewed, UniProtKB/Swiss-Prot Q02293 (FNTB_RAT)

Last modified February 9, 2010. 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

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)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

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

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. 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.

Subunit structure

Heterodimer of an alpha and a beta subunit. Ref.6

Sequence similarities

Belongs to the protein prenyltransferase subunit beta family.

Contains 5 PFTB repeats.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

FntaQ046317EBI-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

Sites

Metal binding2971Zinc
Metal binding2991Zinc
Metal binding3621Zinc

Amino acid modifications

Modified residue3001Phosphotyrosine By similarity

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Q02293-1 [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: 1855253] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[3]Erratum
Park H.-W., Boduluri S.R., Mooomaw J.F., Casey P.J., Beese L.S.
Science 276:21-21(1997)
[4]"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: 9065406] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
[5]"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: 9657673] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS).
[6]"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: 11687658] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH ALPHA SUBUNIT AND GERANYLGERANYL DIPHOSPHATE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M69056 mRNA. Translation: AAA41176.1.
BC087675 mRNA. Translation: AAH87675.1.
IPIIPI00205139.
PIRA40037.
RefSeqNP_742031.1.
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[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-6132N.
IntActQ02293. 1 interaction.
STRINGQ02293.

PTM databases

PhosphoSiteQ02293.

Genome annotation databases

EnsemblENSRNOT00000010588; ENSRNOP00000010588; ENSRNOG00000007660; Rattus norvegicus. [Genome view]
GeneID64511.
KEGGrno:64511.
UCSCNM_172034. rat.

Organism-specific databases

CTD64511.
RGD620119. Fntb.

Phylogenomic databases

eggNOGroNOG14622.
HOVERGENQ02293.
InParanoidQ02293.
OMAELCQSPD.
OrthoDBEOG9CVJTG.
PhylomeDBQ02293.

Enzyme and pathway databases

BRENDA2.5.1.58. 248.

Gene expression databases

ArrayExpressQ02293.
GenevestigatorQ02293.
GermOnlineENSRNOG00000007660. Rattus norvegicus.

Family and domain databases

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

Other Resources

NextBio613294.

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: February 9, 2010
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents