Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Farnesyl pyrophosphate synthase  

UniProtKB / Swiss-Prot ID :  FPPS_HUMAN

Gene Name (Synonyms) : 
FDPS, FPS, KIAA1293  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. 

Protein Function :  Key enzyme in isoprenoid biosynthesis which catalyzes the formation of farnesyl diphosphate (FPP), a precursor for several classes of essential metabolites including sterols, dolichols, carotenoids, and ubiquinones. FPP also serves as substrate for protein farnesylation and geranylgeranylation. 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. 

Protein Sequence MPLSRWLRSVGVFLLPAPYWAPRERWLGSLRRPSLVHGYPVLAWHSARCWCQAWTEEPRALCSSLRMNGD...
Predicted Secondary Structure CCCCCCCCHHHHHHHHHHHHHHHHHHHHHHHHHCCCCCCHHHHHHHHHHHHCCCCCHHHHHHHHHHHHHH...
Protein Variant
LocationDescription
364V -> A (in dbSNP:rs41314549). VAR_061274
391I -> V (in dbSNP:rs17456). VAR_049644
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
112Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)IARLKEVLE
CCCCCCCCC
39.98Phosphositeplus
Link
123Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AIGGKYNRG
EECCCCCHH
33.85Phosphositeplus
Link
123N6-acetyllysineAIGGKYNRG
EECCCCCHH
33.85HPRD
Link
123N6-acetyllysineAIGGKYNRG
EECCCCCHH
33.85Phosphositeplus
Link
123N6-acetyllysine.AIGGKYNRG
EECCCCCHH
33.85UniProtKB
Link
142Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VEPRKQDAD
HHHHHHHHH
64.34Phosphositeplus
Link
210Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YRLLKLYCR
HHHHHHHHH
41.84Phosphositeplus
Link
332Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)IQDNKCSWL
HHHHCCCCC
37.62Phosphositeplus
Link
353Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YQILKENYG
HHCCC
45.61Phosphositeplus
Link-
353N6-acetyllysineYQILKENYG
HHCCC
45.61HPRD
Link-
353N6-acetyllysineYQILKENYG
HHCCC
45.61Phosphositeplus
Link-
353N6-acetyllysine.YQILKENYG
HHCCC
45.61UniProtKB
Link-
359Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NYGQKEAEK
55.30Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
ATX1_HUMANphysical interactionMINT-2858967MINT16713569
ATX1_HUMANyeast 2-hybridHPRD:00606HPRD16713569
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
DrugBank
DB00630Alendronate
DB00710Ibandronate
DB00282Pamidronate
DB00884Risedronate
DB00399Zoledronate
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123 AND LYS-353, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures