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Q8K2I1 (FNTB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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.2

Catalytic activity

Farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate. Ref.2

Cofactor

Binds 1 zinc ion per subunit. Ref.2

Subunit structure

Heterodimer of FNTA and FNTB. Ref.2

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
Reference proteome
Gene Ontology (GO)
   Biological_processnegative regulation of cell proliferation

Inferred from mutant phenotype PubMed 15837621. Source: MGI

positive regulation of cell cycle

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from mutant phenotype PubMed 15837621. Source: MGI

positive regulation of fibroblast proliferation

Inferred from mutant phenotype PubMed 15837621. Source: MGI

positive regulation of nitric-oxide synthase biosynthetic process

Inferred from electronic annotation. Source: Ensembl

protein farnesylation

Inferred from sequence or structural similarity. Source: UniProtKB

response to cytokine

Inferred from electronic annotation. Source: Ensembl

response to inorganic substance

Inferred from electronic annotation. Source: Ensembl

response to organic cyclic compound

Inferred from electronic annotation. Source: Ensembl

wound healing

Inferred from mutant phenotype PubMed 15837621. Source: MGI

   Cellular_componentmicrotubule associated complex

Inferred from electronic annotation. Source: Ensembl

protein farnesyltransferase complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionfarnesyltranstransferase activity

Inferred from mutant phenotype PubMed 15837621. Source: MGI

protein farnesyltransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 437437Protein farnesyltransferase subunit beta
PRO_0000119762

Regions

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

Sites

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

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8K2I1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 42B780B356136950

FASTA43748,820
        10         20         30         40         50         60 
MASSSSFTYY CPPSSSPVWS EPLYSLRPEH VRERLQDDSV ETVTSIEQAK VEEKIQEVFS 

        70         80         90        100        110        120 
SYKFNHLVPR LILQREKHFH 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 MLHDMVMGVP ENVLQPTHPV YNIGPEKVIQ ATTHFLQKPV 

       430 
PGFEECEDEV TSDPATD 

« Hide

References

« Hide 'large scale' references
[1]"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].
Strain: 129.
Tissue: Mammary tumor.
[2]"Structure-guided development of selective RabGGTase inhibitors."
Bon R.S., Guo Z., Stigter E.A., Wetzel S., Menninger S., Wolf A., Choidas A., Alexandrov K., Blankenfeldt W., Goody R.S., Waldmann H.
Angew. Chem. Int. Ed. Engl. 50:4957-4961(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 2-427 IN COMPLEX WITH FNTA AND ZINC IONS, SUBUNIT, CATALYTIC ACTIVITY, FUNCTION, COFACTOR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC031417 mRNA. Translation: AAH31417.1.
RefSeqNP_666039.1. NM_145927.2.
UniGeneMm.151174.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3PZ4X-ray2.10B2-427[»]
ProteinModelPortalQ8K2I1.
SMRQ8K2I1. Positions 17-423.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBQ8K2I1.
ChEMBLCHEMBL2096912.

PTM databases

PhosphoSiteQ8K2I1.

Proteomic databases

PRIDEQ8K2I1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000041008; ENSMUSP00000035498; ENSMUSG00000033373.
GeneID110606.
KEGGmmu:110606.
UCSCuc007nyu.1. mouse.

Organism-specific databases

CTD2342.
MGIMGI:1861305. Fntb.

Phylogenomic databases

GeneTreeENSGT00550000075042.
HOGENOMHOG000190594.
HOVERGENHBG008173.
InParanoidQ8K2I1.
KOK05954.
OMARGAYCAI.
PhylomeDBQ8K2I1.
TreeFamTF353162.

Gene expression databases

ArrayExpressQ8K2I1.
BgeeQ8K2I1.
CleanExMM_FNTB.
GenevestigatorQ8K2I1.

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

ChiTaRSFNTB. mouse.
NextBio364317.
PROQ8K2I1.
SOURCESearch...

Entry information

Entry nameFNTB_MOUSE
AccessionPrimary (citable) accession number: Q8K2I1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 1, 2002
Last modified: April 16, 2014
This is version 91 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot