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Human Metabolome Database Version 2.5

 

Showing metabocard for Farnesyl pyrophosphate (HMDB00961)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:24
Accession Number HMDB00961
Secondary Accession Numbers HMDB04201
Common Name Farnesyl pyrophosphate
Description Farnesyl pyrophosphate is an intermediate in the HMG-CoA reductase pathway used by organisms in the biosynthesis of terpenes and terpenoids. -- Wikipedia
Synonyms
  1. (2E,6E)-Farnesyl diphosphate
  2. (2E,6E)-Farnesyl pyrophosphate
  3. (E,E)-Farnesyl diphosphate
  4. (E,E)-Farnesyl pyrophosphate
  5. (all-E)-Farnesyl diphosphate
  6. 2-trans,6-trans-Farnesyl diphosphate
  7. 2-trans,6-trans-Farnesyl pyrophosphate
  8. Farnesyl diphosphate
  9. Farnesyl pyrophosphate
  10. Farnesyl pyrophosphic acid
  11. Farnesyl-PP
  12. all-trans-Farnesyl pyrophosphate
  13. trans-trans-Farnesyl diphosphate
  14. trans-trans-Farnesyl pyrophosphate
  15. trans-Farnesyl pyrophosphate
Chemical IUPAC Name [hydroxy-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trienoxy]phosphoryl]oxyphosphonic acid
Chemical Formula C15H28O7P2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Miscellaneous
Class
  • Acyl Phosphates
Sub Class
  • Medium chain acyl phosphates
Family
  • Mammalian Metabolite
Species
  • phosphoric acid ester
  • alkene
Biofunction
  • Component of Terpenoid biosynthesis
Application
—
Source
  • Endogenous
Average Molecular Weight 382.326
Monoisotopic Molecular Weight 382.131012
Isomeric SMILES CC(C)=CCCC(C)=CCCC(C)=CCOP(O)(=O)OP(O)(O)=O
Canonical SMILES CC(C)=CCCC(C)=CCCC(C)=CCOP(O)(=O)OP(O)(O)=O
KEGG Compound ID C00448 Link Image
BioCyc ID FARNESYL-PP Link Image
BiGG ID 35006 Link Image
Wikipedia Link Farnesyl pyrophosphate Link Image
NuGOwiki Link HMDB00961 Link Image
Metagene Link HMDB00961 Link Image
METLIN ID 403 Link Image
PubChem Compound 445713 Link Image
PubChem Substance 2699 Link Image
ChEBI ID 17407 Link Image
CAS Registry Number 13058-04-3
InChI Identifier InChI=1/C15H28O7P2/c1-13(2)7-5-8-14(3)9-6-10-15(4)11-12-21-24(19,20)22-23(16,17)18/h7,9,11H,5-6,8,10,12H2,1-4H3,(H,19,20)(H2,16,17,18)/b14-9+,15-11+
Synthesis Reference Castillo-Bocanegra, Rafael. Synthesis and biological activity of farnesyl pyrophosphate analogs. (1977), 193 pp.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 0.080699995 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -3
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 2.40 [Predicted by ALOGPS]; 0.6 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID 1T0A Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm
  • endoplasmic reticulum
  • peroxisome
Biofluid Location
  • Blood
Tissue Location
Tissue References
Neuron —
Testes —
Concentrations (Normal)
Biofluid Blood
Value 0.0086 (0.0000-0.0170) uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Saisho Y, Morimoto A, Umeda T: Determination of farnesyl pyrophosphate in dog and human plasma by high-performance liquid chromatography with fluorescence detection. Anal Biochem. 1997 Oct 1;252(1):89-95. [PubMed Link Image]
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Porphyrin Metabolism SMP00024 Link Image map00860 Link Image
Steroid Biosynthesis SMP00023 Link Image map00100 Link Image
General References
  1. Shellman YG, Ribble D, Miller L, Gendall J, Vanbuskirk K, Kelly D, Norris DA, Dellavalle RP: Lovastatin-induced apoptosis in human melanoma cell lines. Melanoma Res. 2005 Apr;15(2):83-9. [PubMed Link Image]
  2. Argmann CA, Edwards JY, Sawyez CG, O'Neil CH, Hegele RA, Pickering JG, Huff MW: Regulation of macrophage cholesterol efflux through hydroxymethylglutaryl-CoA reductase inhibition: a role for RhoA in ABCA1-mediated cholesterol efflux. J Biol Chem. 2005 Jun 10;280(23):22212-21. Epub 2005 Apr 6. [PubMed Link Image]
  3. Reigard SA, Zahn TJ, Haworth KB, Hicks KA, Fierke CA, Gibbs RA: Interplay of isoprenoid and peptide substrate specificity in protein farnesyltransferase. Biochemistry. 2005 Aug 23;44(33):11214-23. [PubMed Link Image]
  4. Tacer KF, Haugen TB, Baltsen M, Debeljak N, Rozman D: Tissue-specific transcriptional regulation of the cholesterol biosynthetic pathway leads to accumulation of testis meiosis-activating sterol (T-MAS). J Lipid Res. 2002 Jan;43(1):82-9. [PubMed Link Image]
  5. Saisho Y, Morimoto A, Umeda T: Determination of farnesyl pyrophosphate in dog and human plasma by high-performance liquid chromatography with fluorescence detection. Anal Biochem. 1997 Oct 1;252(1):89-95. [PubMed Link Image]
  6. Sanders JM, Song Y, Chan JM, Zhang Y, Jennings S, Kosztowski T, Odeh S, Flessner R, Schwerdtfeger C, Kotsikorou E, Meints GA, Gomez AO, Gonzalez-Pacanowska D, Raker AM, Wang H, van Beek ER, Papapoulos SE, Morita CT, Oldfield E: Pyridinium-1-yl bisphosphonates are potent inhibitors of farnesyl diphosphate synthase and bone resorption. J Med Chem. 2005 Apr 21;48(8):2957-63. [PubMed Link Image]
  7. Notarnicola M, Messa C, Cavallini A, Bifulco M, Tecce MF, Eletto D, Di Leo A, Montemurro S, Laezza C, Caruso MG: Higher farnesyl diphosphate synthase activity in human colorectal cancer inhibition of cellular apoptosis. Oncology. 2004;67(5-6):351-8. [PubMed Link Image]
  8. Fukuchi J, Song C, Ko AL, Liao S: Transcriptional regulation of farnesyl pyrophosphate synthase by liver X receptors. Steroids. 2003 Sep;68(7-8):685-91. [PubMed Link Image]
  9. Wikipedia Link Image
Metabolic Enzymes
  1. Squalene synthetase
  2. Geranylgeranyl pyrophosphate synthetase
  3. Farnesyl pyrophosphate synthetase
  4. Protein farnesyltransferase/geranylgeranyltransferase type I alpha subunit
  5. Farnesyl diphosphate synthase
  6. Protein farnesyltransferase subunit beta
Enzyme 1 [top]
Enzyme 1 ID 5492
Enzyme 1 Name Squalene synthetase
Enzyme 1 Synonyms
  1. SQS
  2. SS
  3. Farnesyl-diphosphate farnesyltransferase
  4. FPP:FPP farnesyltransferase
Enzyme 1 Gene Name FDFT1
Enzyme 1 Protein Sequence >Squalene synthetase 
MEFVKCLGHPEEFYNLVRFRIGGKRKVMPKMDQDSLSSSLKTCYKYLNQTSRSFAAVIQA
LDGEMRNAVCIFYLVLRALDTLEDDMTISVEKKVPLLHNFHSFLYQPDWRFMESKEKDRQ
VLEDFPTISLEFRNLAEKYQTVIADICRRMGIGMAEFLDKHVTSEQEWDKYCHYVAGLVG
IGLSRLFSASEFEDPLVGEDTERANSMGLFLQKTNIIRDYLEDQQGGREFWPQEVWSRYV
KKLGDFAKPENIDLAVQCLNELITNALHHIPDVITYLSRLRNQSVFNFCAIPQVMAIATL
AACYNNQQVFKGAVKIRKGQAVTLMMDATNMPAVKAIIYQYMEEIYHRIPDSDPSSSKTR
QIISTIRTQNLPNCQLISRSHYSPIYLSFVMLLAALSWQYLTTLSQVTEDYVQTGEH
Enzyme 1 Number of Residues 417
Enzyme 1 Molecular Weight 48116
Enzyme 1 Theoretical pI 6.51
Enzyme 1 GO Classification
Function
  • catalytic activity
  • farnesyl-diphosphate farnesyltransferase activity
  • farnesyltranstransferase activity
  • prenyltransferase activity
  • transferase activity
  • transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
  • biosynthesis
  • lipid biosynthesis
  • metabolism
  • physiological process
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 1 General Function Lipid transport and metabolism
Enzyme 1 Specific Function 2 farnesyl diphosphate = diphosphate + presqualene diphosphate
Enzyme 1 Pathways
Enzyme 1 Reactions
  • 2 farnesyl diphosphate = diphosphate + presqualene diphosphate
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • 284-304 384-404
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 292510 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P37268 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name FDFT_HUMAN Link Image
Enzyme 1 PDB ID 1EZF Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1254 bp 
ATGGAGTTCGTGAAATGCCTTGGCCACCCCGAAGAGTTCTACAACCTGGTGCGCTTCCGG
ATCGGGGGCAAGCGGAAGGTGATGCCCAAGATGGACCAGGACTCGCTCAGCAGCAGCCTG
AAAACTTGCTACAAGTATCTCAATCAGACCAGTCGCAGTTTCGCAGCTGTTATCCAGGCG
CTGGATGGGGAAATGCGCAACGCAGTGTGCATATTTTATCTGGTTCTCCGAGCTCTGGAC
ACACTGGAAGATGACATGACCATCAGTGTGGAAAAGAAGGTCCCGCTGTTACACAACTTT
CACTCTTTCCTTTACCAACCAGACTGGCGGTTCATGGAGAGCAAGGAGAAGGATCGCCAG
GTGCTGGAGGACTTCCCAACGATCTCCCTTGAGTTTAGAAATCTGGCTGAGAAATACCAA
ACAGTGATTGCCGACATTTGCCGGAGAATGGGCATTGGGATGGCAGAGTTTTTGGATAAG
CATGTGACCTCTGAACAGGAGTGGGACAAGTACTGCCACTATGTTGCTGGGCTGGTCGGA
ATTGGCCTTTCCCGTCTTTTCTCAGCCTCAGAGTTTGAAGACCCCTTAGTTGGTGAAGAT
ACAGAACGTGCCAACTCTATGGGCCTGTTTCTGCAGAAAACAAACATCATCCGTGACTAT
CTGGAAGACCAGCAAGGAGGAAGAGAGTTCTGGCCTCAAGAGGTTTGGAGCAGGTATGTT
AAGAAGTTAGGGGATTTTGCTAAGCCGGAGAATATTGACTTGGCCGTGCAGTGCCTGAAT
GAACTTATAACCAATGCACTGCACCACATCCCAGATGTCATCACCTACCTTTCGAGACTC
AGAAACCAGAGTGTGTTTAACTTCTGCGCTATTCCACAGGTGATGGCCATTGCCACTTTG
GCTGCCTGTTATAATAACCAGCAGGTGTTCAAAGGGGCAGTGAAGATTCGGAAAGGGCAA
GCAGTGACCCTGATGATGGATGCCACCAATATGCCAGCTGTCAAAGCCATCATATATCAG
TATATGGAAGAGATTTATCATAGAATCCCCGACTCAGACCCATCTTCTAGCAAAACAAGG
CAGATCATCTCCACCATCCGGACGCAGAATCTTCCCAACTGTCAGCTGATTTCCCGAAGC
CACTACTCCCCCATCTACCTGTCGTTTGTCATGCTTTTGGCTGCCCTGAGCTGGCAGTAC
CTGACCACTCTCTCCCAGGTAACAGAAGACTATGTTCAGACTGGAGAACACTGA
Enzyme 1 GenBank Gene ID L06070 Link Image
Enzyme 1 GeneCard ID FDFT1 Link Image
Enzyme 1 GenAtlas ID FDFT1 Link Image
Enzyme 1 HGNC ID HGNC:3629 Link Image
Enzyme 1 Chromosome Location 8
Enzyme 1 Locus 8p23.1-p22
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Robinson GW, Tsay YH, Kienzle BK, Smith-Monroy CA, Bishop RW: Conservation between human and fungal squalene synthetases: similarities in structure, function, and regulation. Mol Cell Biol. 1993 May;13(5):2706-17. [PubMed Link Image]
  2. Jiang G, McKenzie TL, Conrad DG, Shechter I: Transcriptional regulation by lovastatin and 25-hydroxycholesterol in HepG2 cells and molecular cloning and expression of the cDNA for the human hepatic squalene synthase. J Biol Chem. 1993 Jun 15;268(17):12818-24. [PubMed Link Image]
  3. Summers C, Karst F, Charles AD: Cloning, expression and characterisation of the cDNA encoding human hepatic squalene synthase, and its relationship to phytoene synthase. Gene. 1993 Dec 22;136(1-2Che):185-92. [PubMed Link Image]
  4. Soltis DA, McMahon G, Caplan SL, Dudas DA, Chamberlin HA, Vattay A, Dottavio D, Rucker ML, Engstrom RG, Cornell-Kennon SA, et al.: Expression, purification, and characterization of the human squalene synthase: use of yeast and baculoviral systems. Arch Biochem Biophys. 1995 Feb 1;316(2):713-23. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 6219
Enzyme 2 Name Geranylgeranyl pyrophosphate synthetase
Enzyme 2 Synonyms
  1. GGPP synthetase
  2. GGPPSase
  3. Geranylgeranyl diphosphate synthase[Includes: Dimethylallyltranstransferase
Enzyme 2 Gene Name GGPS1
Enzyme 2 Protein Sequence >Geranylgeranyl pyrophosphate synthetase 
MEKTQETVQRILLEPYKYLLQLPGKQVRTKLSQAFNHWLKVPEDKLQIIIEVTEMLHNAS
LLIDDIEDNSKLRRGFPVAHSIYGIPSVINSANYVYFLGLEKVLTLDHPDAVKLFTRQLL
ELHQGQGLDIYWRDNYTCPTEEEYKAMVLQKTGGLFGLAVGLMQLFSDYKEDLKPLLNTL
GLFFQIRDDYANLHSKEYSENKSFCEDLTEGKFSFPTIHAIWSRPESTQVQNILRQRTEN
IDIKKYCVHYLEDVGSFEYTRNTLKELEAKAYKQIDARGGNPELVALVKHLSKMFKEENE
Enzyme 2 Number of Residues 300
Enzyme 2 Molecular Weight 34871
Enzyme 2 Theoretical pI 6.06
Enzyme 2 GO Classification
Function
—
Process
  • cellular lipid metabolism
  • isoprenoid biosynthesis
  • isoprenoid metabolism
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
—
Enzyme 2 General Function Coenzyme transport and metabolism
Enzyme 2 Specific Function Catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate, an important precursor of carotenoids and geranylated proteins
Enzyme 2 Pathways
Enzyme 2 Reactions
  • trans,trans-farnesyl diphosphate + isopentenyl diphosphate = diphosphate + geranylgeranyl diphosphate
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 4520350 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID O95749 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name GGPPS_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >903 bp 
ATGGAGAAGACTCAAGAAACAGTCCAAAGAATTCTTCTAGAACCCTATAAATACTTACTT
CAGTTACCAGGTAAACAAGTGAGAACCAAACTTTCACAGGCATTTAATCATTGGCTGAAA
GTTCCAGAGGACAAGCTACAGATTATTATTGAAGTGACAGAAATGTTGCATAATGCCAGT
TTACTCATCGATGATATTGAAGACAACTCAAAACTCCGACGTGGCTTTCCAGTGGCCCAC
AGCATCTATGGAATCCCATCTGTCATCAATTCTGCCAATTACGTGTATTTCCTTGGCTTG
GAGAAAGTCTTAACCCTTGATCACCCAGATGCAGTGAAGCTTTTTACCCGCCAGCTTTTG
GAACTCCATCAGGGACAAGGCCTAGATATTTACTGGAGGGATAATTACACTTGTCCCACT
GAAGAAGAATATAAAGCTATGGTGCTGCAGAAAACAGGTGGACTGTTTGGATTAGCAGTA
GGTCTCATGCAGTTGTTCTCTGATTACAAAGAAGATTTAAAACCGCTACTTAATACACTT
GGGCTCTTTTTCCAAATTAGGGATGATTATGCTAATCTACACTCCAAAGAATATAGTGAA
AACAAAAGTTTTTGTGAAGATCTGACAGAGGGAAAGTTCTCATTTCCTACTATTCATGCT
ATTTGGTCAAGGCCTGAAAGCACCCAGGTGCAGAATATCTTGCGCCAGAGAACAGAAAAC
ATAGATATAAAAAAATACTGTGTACATTATCTTGAGGATGTAGGTTCTTTTGAATACACT
CGTAATACCCTTAAAGAGCTTGAAGCTAAAGCCTATAAACAGATTGATGCACGTGGTGGG
AACCCTGAGCTAGTAGCCTTAGTAAAACACTTAAGTAAGATGTTCAAAGAAGAAAATGAA
TAA
Enzyme 2 GenBank Gene ID AB017971 Link Image
Enzyme 2 GeneCard ID GGPS1 Link Image
Enzyme 2 GenAtlas ID GGPS1 Link Image
Enzyme 2 HGNC ID HGNC:4249 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 1q43
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Ericsson J, Greene JM, Carter KC, Shell BK, Duan DR, Florence C, Edwards PA: Human geranylgeranyl diphosphate synthase: isolation of the cDNA, chromosomal mapping and tissue expression. J Lipid Res. 1998 Sep;39(9):1731-9. [PubMed Link Image]
  2. Kuzuguchi T, Morita Y, Sagami I, Sagami H, Ogura K: Human geranylgeranyl diphosphate synthase. cDNA cloning and expression. J Biol Chem. 1999 Feb 26;274(9):5888-94. [PubMed Link Image]
  3. Hu RM, Han ZG, Song HD, Peng YD, Huang QH, Ren SX, Gu YJ, Huang CH, Li YB, Jiang CL, Fu G, Zhang QH, Gu BW, Dai M, Mao YF, Gao GF, Rong R, Ye M, Zhou J, Xu SH, Gu J, Shi JX, Jin WR, Zhang CK, Wu TM, Huang GY, Chen Z, Chen MD, Chen JL: Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning. Proc Natl Acad Sci U S A. 2000 Aug 15;97(17):9543-8. [PubMed Link Image]
  4. Kainou T, Kawamura K, Tanaka K, Matsuda H, Kawamukai M: Identification of the GGPS1 genes encoding geranylgeranyl diphosphate synthases from mouse and human. Biochim Biophys Acta. 1999 Mar 25;1437(3):333-40. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 6220
Enzyme 3 Name Farnesyl pyrophosphate synthetase
Enzyme 3 Synonyms
  1. FPP synthetase
  2. FPS
  3. Farnesyl diphosphate synthetase[Includes: Dimethylallyltranstransferase
Enzyme 3 Gene Name FDPS
Enzyme 3 Protein Sequence >Farnesyl pyrophosphate synthetase 
MNGDQNSDVYAQEKQDFVQHFSQIVRVLTEDEMGHPEIGDAIARLKEVLEYNAIGGKYNR
GLTVVVAFRELVEPRKQDADSLQRAWTVGWCVELLQAFFLVADDIMDSSLTRRGQICWYQ
KPGVGLDAINDANLLEACIYRLLKLYCREQPYYLNLIELFLQSSYQTEIGQTLDLLTAPQ
GNVDLVRFTEKRYKSIVKYKTAFYSFYLPIAAAMYMAGIDGEKEHANAKKILLEMGEFFQ
IQDDYLDLFGDPSVTGKIGTDIQDNKCSWLVVQCLQRATPEQYQILKENYGQKEAEKVAR
VKALYEELDLPAVFLQYEEDSYSHIMALIEQYAAPLPPAVFLGLARKIYKRRK
Enzyme 3 Number of Residues 353
Enzyme 3 Molecular Weight 40533
Enzyme 3 Theoretical pI 4.80
Enzyme 3 GO Classification
Function
—
Process
  • cellular lipid metabolism
  • isoprenoid biosynthesis
  • isoprenoid metabolism
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
—
Enzyme 3 General Function Coenzyme transport and metabolism
Enzyme 3 Specific Function Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate
Enzyme 3 Pathways
Enzyme 3 Reactions
  • geranyl diphosphate + isopentenyl diphosphate = diphosphate + trans,trans-farnesyl diphosphate
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • 202-219
  • 322-344
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 182399 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P14324 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name FPPS_HUMAN Link Image
Enzyme 3 PDB ID 1YV5 Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1062 bp 
ATGAACGGAGACCAGAATTCAGATGTTTATGCCCAAGAAAAGCAGGATTTCGTTCAGCAC
TTCTCCCAGATCGTTAGGGTGCTGACTGAGGATGAGATGGGGCACCCAGAGATAGGAGAT
GCTATTGCCCGGCTCAAGGAGGTCCTGGAGTACAATGCCATTGGAGGCAAGTATAACCGG
GGTTTGACGGTGGTAGTAGCATTCCGGGAGCTGGTGGAGCCAAGGAAACAGGATGCTGAT
AGTCTCCAGCGGGCCTGGACTGTGGGCTGGTGTGTGGAACTGCTGCAAGCTTTCTTCCTG
GTGGCAGATGACATCATGGATTCATCCCTTACCCGCCGGGGACAGACCTGCTGGTATCAG
AAGCCGGGCGTGGGTTTGGATGCCATCAATGATGCTAACCTCCTGGAAGCATGTATCTAC
CGCCTGCTGAAGCTCTATTGCCGGGAGCAGCCCTATTACCTGAACCTGATCGAGCTCTTC
CTGCAGAGTTCCTATCAGACTGAGATTGGGCAGACCCTGGACCTCCTCACAGCCCCCCAG
GGCAATGTGGATCTTGTCAGATTCACTGAAAAGAGGTACAAATCTATTGTCAAGTACAAG
ACAGCTTTCTACTCCTTCTACCTTCCTATAGCTGCAGCCATGTACATGGCAGGAATTGAT
GGCGAGAAGGAGCACGCCAATGCCAAGAAGATCCTGCTGGAGATGGGGGAGTTCTTTCAG
ATTCAGGATGATTACCTTGACCTCTTTGGGGACCCCAGTGTGACCGGCAAAATTGGCACT
GACATCCAGGACAACAAATGCAGCTGGCTGGTGGTTCAGTGTCTGCAACGGGCCACTCCA
GAACAGTACCAGATCCTGAAGGAAAATTACGGGCAGAAGGAGGCTGAGAAAGTGGCCCGG
GTGAAGGCGCTATATGAGGAGCTGGATCTGCCAGCAGTGTTCTTGCAATATGAGGAAGAC
AGTTACAGCCACATTATGGCTCTCATTGAACAGTACGCAGCACCCCTGCCCCCAGCCGTC
TTTCTGGGGCTTGCGCGCAAAATCTACAAGCGGAGAAAGTGA
Enzyme 3 GenBank Gene ID J05262 Link Image
Enzyme 3 GeneCard ID FDPS Link Image
Enzyme 3 GenAtlas ID FDPS Link Image
Enzyme 3 HGNC ID HGNC:3631 Link Image
Enzyme 3 Chromosome Location 1
Enzyme 3 Locus 1q22
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Wilkin DJ, Kutsunai SY, Edwards PA: Isolation and sequence of the human farnesyl pyrophosphate synthetase cDNA. Coordinate regulation of the mRNAs for farnesyl pyrophosphate synthetase, 3-hydroxy-3-methylglutaryl coenzyme A reductase, and 3-hydroxy-3-methylglutaryl coenzyme A synthase by phorbol ester. J Biol Chem. 1990 Mar 15;265(8):4607-14. [PubMed Link Image]
  2. Nomura N, Miyajima N, Sazuka T, Tanaka A, Kawarabayasi Y, Sato S, Nagase T, Seki N, Ishikawa K, Tabata S: Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1. DNA Res. 1994;1(1):27-35. [PubMed Link Image]
  3. Sheares BT, White SS, Molowa DT, Chan K, Ding VD, Kroon PA, Bostedor RG, Karkas JD: Cloning, analysis, and bacterial expression of human farnesyl pyrophosphate synthetase and its regulation in Hep G2 cells. Biochemistry. 1989 Oct 3;28(20):8129-35. [PubMed Link Image]
  4. Lefebvre L, Vanderplasschen A, Ciminale V, Heremans H, Dangoisse O, Jauniaux JC, Toussaint JF, Zelnik V, Burny A, Kettmann R, Willems L: Oncoviral bovine leukemia virus G4 and human T-cell leukemia virus type 1 p13(II) accessory proteins interact with farnesyl pyrophosphate synthetase. J Virol. 2002 Feb;76(3):1400-14. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 7185
Enzyme 4 Name Protein farnesyltransferase/geranylgeranyltransferase type I alpha subunit
Enzyme 4 Synonyms
  1. CAAX farnesyltransferase alpha subunit
  2. Ras proteins prenyltransferase alpha
  3. FTase-alpha
  4. Type I protein geranyl-geranyltransferase alpha subunit
  5. GGTase-I-alpha
Enzyme 4 Gene Name FNTA
Enzyme 4 Protein Sequence >Protein farnesyltransferase/geranylgeranyltransferase type I alpha subunit 
MAATEGVGEAAQGGEPGQPAQPPPQPHPPPPQQQHKEEMAAEAGEAVASPMDDGFVSLDS
PSYVLYRDRAEWADIDPVPQNDGPNPVVQIIYSDKFRDVYDYFRAVLQRDERSERAFKLT
RDAIELNAANYTVWHFRRVLLKSLQKDLHEEMNYITAIIEEQPKNYQVWHHRRVLVEWLR
DPSQELEFIADILNQDAKNYHAWQHRQWVIQEFKLWDNELQYVDQLLKEDVRNNSVWNQR
YFVISNTTGYNDRAVLEREVQYTLEMIKLVPHNESAWNYLKGILQDRGLSKYPNLLNQLL
DLQPSHSSPYLIAFLVDIYEDMLENQCDNKEDILNKALELCEILAKEKDTIRKEYWRYIG
RSLQSKHSTENDSPTNVQQ
Enzyme 4 Number of Residues 379
Enzyme 4 Molecular Weight 44409
Enzyme 4 Theoretical pI 4.72
Enzyme 4 GO Classification
Function
  • catalytic activity
  • prenyltransferase activity
  • protein prenyltransferase activity
  • transferase activity
  • transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid lipidation
  • protein amino acid prenylation
  • protein modification
  • protein prenylation
Component
—
Enzyme 4 General Function Translation, ribosomal structure and biogenesis
Enzyme 4 Specific Function Catalyzes the transfer of a farnesyl or geranyl-geranyl moiety from farnesyl or geranyl-geranyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. The alpha subunit is thought to participate in a stable complex with the substrate. The beta subunit binds the peptide substrate
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions
  • geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 388756 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P49354 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name PFTA_HUMAN Link Image
Enzyme 4 PDB ID 1S63 Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1140 bp 
ATGGCGGCCACCGAGGGGGTCGGGGAGGCTGCGCAAGGGGGCGAGCCCGGGCAGCCGGCG
CAACCCCCGCCCCAGCCGCACCCACCGCCGCCCCAGCAGCAGCACAAGGAAGAGATGGCG
GCCGAGGCTGGGGAAGCCGTGGCGTCCCCCATGGACGACGGGTTTGTGAGCCTGGACTCG
CCCTCCTATGTCCTGTACAGGGACAGAGCAGAATGGGCTGATATAGATCCGGTGCCGCAG
AATGATGGCCCCAATCCCGTGGTCCAGATCATTTATAGTGACAAATTTAGAGATGTTTAT
GATTACTTCCGAGCTGTCCTGCAGCGTGATGAAAGAAGTGAACGAGCTTTTAAGCTAACC
CGGGATGCTATTGAGTTAAATGCAGCCAATTATACAGTGTGGCATTTCCGGAGAGTTCTT
TTGAAGTCACTTCAGAAGGATCTACATGAGGAAATGAACTACATCACTGCAATAATTGAG
GAGCAGCCCAAAAACTATCAAGTTTGGCATCATAGGCGAGTATTAGTGGAATGGCTAAGA
GATCCATCTCAGGAGCTTGAATTTATTGCTGATATTCTTAATCAGGATGCAAAGAATTAT
CATGCCTGGCAGCATCGACAATGGGTTATTCAGGAATTTAAACTTTGGGATAATGAGCTG
CAGTATGTGGACCAACTTCTGAAAGAGGATGTGAGAAATAACTCTGTCTGGAACCAAAGA
TACTTCGTTATTTCTAACACCACTGGCTACAATGATCGTGCTGTATTGGAGAGAGAAGTC
CAATACACTCTGGAAATGATTAAACTAGTACCACATAATGAAAGTGCATGGAACTATTTG
AAAGGGATTTTGCAGGATCGTGGTCTTTCCAAATATCCTAATCTGTTAAATCAATTACTT
GATTTACAACCAAGTCATAGTTCCCCCTACCTAATTGCCTTTCTTGTGGATATCTATGAA
GACATGCTAGAAAATCAGTGTGACAATAAGGAAGACATTCTTAATAAAGCATTAGAGTTA
TGTGAAATCCTAGCTAAAGAAAAGGACACTATAAGAAAGGAATATTGGAGATACATTGGA
AGATCCCTTCAAAGCAAACACAGCACAGAAAATGACTCACCAACAAATGTACAGCAATAA
Enzyme 4 GenBank Gene ID L10413 Link Image
Enzyme 4 GeneCard ID FNTA Link Image
Enzyme 4 GenAtlas ID FNTA Link Image
Enzyme 4 HGNC ID HGNC:3782 Link Image
Enzyme 4 Chromosome Location 8
Enzyme 4 Locus 8p22-q11
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Andres DA, Milatovich A, Ozcelik T, Wenzlau JM, Brown MS, Goldstein JL, Francke U: cDNA cloning of the two subunits of human CAAX farnesyltransferase and chromosomal mapping of FNTA and FNTB loci and related sequences. Genomics. 1993 Oct;18(1):105-12. [PubMed Link Image]
  2. Andres DA, Goldstein JL, Ho YK, Brown MS: Mutational analysis of alpha-subunit of protein farnesyltransferase. Evidence for a catalytic role. J Biol Chem. 1993 Jan 15;268(2):1383-90. [PubMed Link Image]
  3. Omer CA, Kral AM, Diehl RE, Prendergast GC, Powers S, Allen CM, Gibbs JB, Kohl NE: Characterization of recombinant human farnesyl-protein transferase: cloning, expression, farnesyl diphosphate binding, and functional homology with yeast prenyl-protein transferases. Biochemistry. 1993 May 18;32(19):5167-76. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 13006
Enzyme 5 Name Farnesyl diphosphate synthase
Enzyme 5 Synonyms
  1. Farnesyl pyrophosphate synthetase, dimethylallyltranstransferase, geranyltranstransferase
  2. Farnesyl diphosphate synthase
  3. Farnesyl pyrophosphate synthetase, dimethylallyltranstransferase, geranyltranstransferase, isoform CRA_b
  4. cDNA FLJ76177, highly similar to Homo sapiens farnesyl diphosphate synthase
  5. farnesyl pyrophosphate synthetase, dimethylallyltranstransferase, geranyltranstransferase
  6. FDPS, mRNA
Enzyme 5 Gene Name FDPS
Enzyme 5 Protein Sequence >Farnesyl diphosphate synthase 
MPLSRWLRSVGVFLLPAPYWAPRERWLGSLRRPSLVHGYPVLAWHSARCWCQAWTEEPRA
LCSSLRMNGDQNSDVYAQEKQDFVQHFSQIVRVLTEDEMGHPEIGDAIARLKEVLEYNAI
GGKYNRGLTVVVAFRELVEPRKQDADSLQRAWTVGWCVELLQAFFLVADDIMDSSLTRRG
QICWYQKPGVGLDAINDANLLEACIYRLLKLYCREQPYYLNLIELFLQSSYQTEIGQTLD
LLTAPQGNVDLVRFTEKRYKSIVKYKTAFYSFYLPIAAAMYMAGIDGEKEHANAKKILLE
MGEFFQIQDDYLDLFGDPSVTGKIGTDIQDNKCSWLVVQCLQRATPEQYQILKENYGQKE
AEKVARVKALYEELDLPAVFLQYEEDSYSHIMALIEQYAAPLPPAVFLGLARKIYKRRK
Enzyme 5 Number of Residues 419
Enzyme 5 Molecular Weight 48276
Enzyme 5 Theoretical pI 6.02
Enzyme 5 GO Classification
Function
—
Process
  • cellular lipid metabolism
  • isoprenoid biosynthesis
  • isoprenoid metabolism
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
—
Enzyme 5 General Function Coenzyme transport and metabolism
Enzyme 5 Specific Function Not Available
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 14603061 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q96G29 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name Q96G29_HUMAN Link Image
Enzyme 5 PDB ID 1YV5 Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence Not Available
Enzyme 5 GenBank Gene ID BC010004 Link Image
Enzyme 5 GeneCard ID Q96G29 Link Image
Enzyme 5 GenAtlas ID FDPS Link Image
Enzyme 5 HGNC ID HGNC:3631 Link Image
Enzyme 5 Chromosome Location Not Available
Enzyme 5 Locus Not Available
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 16866
Enzyme 6 Name Protein farnesyltransferase subunit beta
Enzyme 6 Synonyms
  1. FTase-beta
  2. CAAX farnesyltransferase subunit beta
  3. RAS proteins prenyltransferase beta
Enzyme 6 Gene Name FNTB
Enzyme 6 Protein Sequence >Protein farnesyltransferase subunit beta 
MASPSSFTYYCPPSSSPVWSEPLYSLRPEHARERLQDDSVETVTSIEQAKVEEKIQEVFS
SYKFNHLVPRLVLQREKHFHYLKRGLRQLTDAYECLDASRPWLCYWILHSLELLDEPIPQ
IVATDVCQFLELCQSPEGGFGGGPGQYPHLAPTYAAVNALCIIGTEEAYDIINREKLLQY
LYSLKQPDGSFLMHVGGEVDVRSAYCAASVASLTNIITPDLFEGTAEWIARCQNWEGGIG
GVPGMEAHGGYTFCGLAALVILKRERSLNLKSLLQWVTSRQMRFEGGFQGRCNKLVDGCY
SFWQAGLLPLLHRALHAQGDPALSMSHWMFHQQALQEYILMCCQCPAGGLLDKPGKSRDF
YHTCYCLSGLSIAQHFGSGAMLHDVVLGVPENALQPTHPVYNIGPDKVIQATTYFLQKPV
PGFEELKDETSAEPATD
Enzyme 6 Number of Residues 437
Enzyme 6 Molecular Weight 48774
Enzyme 6 Theoretical pI 5.67
Enzyme 6 GO Classification
Function
  • catalytic activity
Process
—
Component
—
Enzyme 6 General Function Not Available
Enzyme 6 Specific 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
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein Not Available
Enzyme 6 UniProtKB/Swiss-Prot ID P49356 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name FNTB_HUMAN Link Image
Enzyme 6 PDB ID 1S63 Link Image
Enzyme 6 PDB File Show
Enzyme 6 3D Structure
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence Not Available
Enzyme 6 GenBank Gene ID L00635 Link Image
Enzyme 6 GeneCard ID P49356 Link Image
Enzyme 6 GenAtlas ID FNTB Link Image
Enzyme 6 HGNC ID HGNC:3785 Link Image
Enzyme 6 Chromosome Location 14
Enzyme 6 Locus 14q23-q24
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Omer CA, Kral AM, Diehl RE, Prendergast GC, Powers S, Allen CM, Gibbs JB, Kohl NE: Characterization of recombinant human farnesyl-protein transferase: cloning, expression, farnesyl diphosphate binding, and functional homology with yeast prenyl-protein transferases. Biochemistry. 1993 May 18;32(19):5167-76. [PubMed Link Image]
  2. Andres DA, Milatovich A, Ozcelik T, Wenzlau JM, Brown MS, Goldstein JL, Francke U: cDNA cloning of the two subunits of human CAAX farnesyltransferase and chromosomal mapping of FNTA and FNTB loci and related sequences. Genomics. 1993 Oct;18(1):105-12. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available