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P49356 (FNTB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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.1 Ref.9 Ref.10 Ref.12 Ref.13

Catalytic activity

Farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate. Ref.1 Ref.9 Ref.10 Ref.12 Ref.13

Cofactor

Binds 1 zinc ion per subunit. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13

Subunit structure

Heterodimer of FNTA and FNTB. Ref.1 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13

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 electronic annotation. Source: Ensembl

positive regulation of cell cycle

Inferred from electronic annotation. Source: Ensembl

positive regulation of fibroblast proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of nitric-oxide synthase biosynthetic process

Inferred from electronic annotation. Source: Ensembl

protein farnesylation

Inferred from direct assay Ref.12. Source: UniProtKB

regulation of rhodopsin mediated signaling pathway

Traceable author statement. Source: Reactome

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

rhodopsin mediated signaling pathway

Traceable author statement. Source: Reactome

wound healing

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

microtubule associated complex

Inferred from direct assay PubMed 19228685. Source: BHF-UCL

protein farnesyltransferase complex

Inferred from direct assay Ref.12. Source: UniProtKB

   Molecular_functionfarnesyltranstransferase activity

Inferred from electronic annotation. Source: Ensembl

protein farnesyltransferase activity

Inferred from direct assay Ref.12. Source: UniProtKB

zinc ion binding

Inferred from direct assay Ref.12. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

FNTAP493547EBI-602349,EBI-602336

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 437437Protein farnesyltransferase subunit beta
PRO_0000119761

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

Experimental info

Mutagenesis1021W → T: Removes the steric hindrance that normally precludes geranylgeranyl diphosphate binding. Reduces farnesyltransferase activity and confers geranylgeranyltransferase activity. Ref.12
Mutagenesis2001D → N: Reduced catalytic efficiency. Ref.1
Mutagenesis2491G → V: Reduced catalytic efficiency. Ref.1
Mutagenesis3491G → S: Reduced catalytic efficiency. Ref.1
Sequence conflict2831R → L in AAA86286. Ref.5

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P49356 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 8E8E571846146709

FASTA43748,774
        10         20         30         40         50         60 
MASPSSFTYY CPPSSSPVWS EPLYSLRPEH ARERLQDDSV ETVTSIEQAK VEEKIQEVFS 

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

       130        140        150        160        170        180 
IVATDVCQFL ELCQSPEGGF GGGPGQYPHL APTYAAVNAL CIIGTEEAYD IINREKLLQY 

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

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

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

       370        380        390        400        410        420 
YHTCYCLSGL SIAQHFGSGA MLHDVVLGVP ENALQPTHPV YNIGPDKVIQ ATTYFLQKPV 

       430 
PGFEELKDET SAEPATD 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of recombinant human farnesyl-protein transferase: cloning, expression, farnesyl diphosphate binding, and functional homology with yeast prenyl-protein transferases."
Omer C.A., Kral A.M., Diehl R.E., Prendergast G.C., Powers S., Allen C.M., Gibbs J.B., Kohl N.E.
Biochemistry 32:5167-5176(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF ASP-200; GLY-249 AND GLY-349, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT.
Tissue: Placenta.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: Placenta.
[5]"cDNA cloning of the two subunits of human CAAX farnesyltransferase and chromosomal mapping of FNTA and FNTB loci and related sequences."
Andres D.A., Milatovich A., Ozcelik T., Wenzlau J.M., Brown M.S., Goldstein J.L., Francke U.
Genomics 18:105-112(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 51-437.
Tissue: Retina.
[6]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"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 ZINC IONS; FNTA; FARNESYL DIPHOSPHATE AND INHIBITOR L-739,750, SUBUNIT, COFACTOR.
[9]"3-aminopyrrolidinone farnesyltransferase inhibitors: design of macrocyclic compounds with improved pharmacokinetics and excellent cell potency."
Bell I.M., Gallicchio S.N., Abrams M., Beese L.S., Beshore D.C., Bhimnathwala H., Bogusky M.J., Buser C.A., Culberson J.C., Davide J., Ellis-Hutchings M., Fernandes C., Gibbs J.B., Graham S.L., Hamilton K.A., Hartman G.D., Heimbrook D.C., Homnick C.F. expand/collapse author list , Huber H.E., Huff J.R., Kassahun K., Koblan K.S., Kohl N.E., Lobell R.B., Lynch J.J. Jr., Robinson R., Rodrigues A.D., Taylor J.S., Walsh E.S., Williams T.M., Zartman C.B.
J. Med. Chem. 45:2388-2409(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ZINC IONS; FNTA; FARNESYL DIPHOSPHATE AND INHIBITORS, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, FUNCTION.
[10]"Dual protein farnesyltransferase-geranylgeranyltransferase-I inhibitors as potential cancer chemotherapeutic agents."
deSolms S.J., Ciccarone T.M., MacTough S.C., Shaw A.W., Buser C.A., Ellis-Hutchings M., Fernandes C., Hamilton K.A., Huber H.E., Kohl N.E., Lobell R.B., Robinson R.G., Tsou N.N., Walsh E.S., Graham S.L., Beese L.S., Taylor J.S.
J. Med. Chem. 46:2973-2984(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ZINC IONS; FNTA; FARNESYL DIPHOSPHATE AND INHIBITOR, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, FUNCTION.
[11]"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 (1.80 ANGSTROMS) IN COMPLEX WITH ZINC IONS; FNTA AND FARNESYL DIPHOSPHATE ANALOG, COFACTOR, SUBUNIT.
[12]"Conversion of protein farnesyltransferase to a geranylgeranyltransferase."
Terry K.L., Casey P.J., Beese L.S.
Biochemistry 45:9746-9755(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH ZINC IONS; FNTA AND FARNESYL DIPHOSPHATE ANALOG, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, FUNCTION, MUTAGENESIS OF TRP-102.
[13]"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 (1.80 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND FNTA, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L00635 mRNA. Translation: AAA35854.1.
AK315714 mRNA. Translation: BAG38073.1.
CH471061 Genomic DNA. Translation: EAW80897.1.
BC020232 mRNA. Translation: AAH20232.1.
L10414 mRNA. Translation: AAA86286.1.
PIRB49274.
RefSeqNP_002019.1. NM_002028.3.
UniGeneHs.325531.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JCQX-ray2.30B1-437[»]
1LD7X-ray2.00B1-437[»]
1LD8X-ray1.80B1-437[»]
1MZCX-ray2.00B1-437[»]
1S63X-ray1.90B1-437[»]
1SA4X-ray2.10B1-437[»]
1TN6X-ray1.80B1-437[»]
2F0YX-ray2.70B1-437[»]
2H6FX-ray1.50B1-437[»]
2H6GX-ray1.85B1-437[»]
2H6HX-ray1.80B1-437[»]
2H6IX-ray3.00B1-437[»]
2IEJX-ray1.80B1-437[»]
3E37X-ray1.80B1-437[»]
ProteinModelPortalP49356.
SMRP49356. Positions 15-424.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108627. 7 interactions.
IntActP49356. 2 interactions.
MINTMINT-238879.
STRING9606.ENSP00000246166.

Chemistry

BindingDBP49356.
ChEMBLCHEMBL2096991.

PTM databases

PhosphoSiteP49356.

Polymorphism databases

DMDM1346696.

Proteomic databases

PeptideAtlasP49356.
PRIDEP49356.

Protocols and materials databases

DNASU2342.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000246166; ENSP00000246166; ENSG00000257365.
GeneID2342.
KEGGhsa:2342.
UCSCuc001xia.3. human.

Organism-specific databases

CTD2342.
GeneCardsGC14P065454.
HGNCHGNC:3785. FNTB.
MIM134636. gene.
neXtProtNX_P49356.
PharmGKBPA28202.
GenAtlasSearch...

Phylogenomic databases

HOVERGENHBG008173.
InParanoidP49356.
KOK05954.
OMARGAYCAI.
OrthoDBEOG7P02HV.
PhylomeDBP49356.
TreeFamTF353162.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.

Gene expression databases

ArrayExpressP49356.
BgeeP49356.
CleanExHS_FNTB.
GenevestigatorP49356.

Family and domain databases

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

EvolutionaryTraceP49356.
GeneWikiFNTB.
GenomeRNAi2342.
NextBio9505.
PROP49356.
SOURCESearch...

Entry information

Entry nameFNTB_HUMAN
AccessionPrimary (citable) accession number: P49356
Secondary accession number(s): B2RDX6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: March 19, 2014
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM