FPPS_HUMAN - dbPTM
FPPS_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FPPS_HUMAN
UniProt AC P14324
Protein Name Farnesyl pyrophosphate synthase
Gene Name FDPS
Organism Homo sapiens (Human).
Sequence Length 419
Subcellular Localization Cytoplasm.
Protein Description 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 MPLSRWLRSVGVFLLPAPYWAPRERWLGSLRRPSLVHGYPVLAWHSARCWCQAWTEEPRALCSSLRMNGDQNSDVYAQEKQDFVQHFSQIVRVLTEDEMGHPEIGDAIARLKEVLEYNAIGGKYNRGLTVVVAFRELVEPRKQDADSLQRAWTVGWCVELLQAFFLVADDIMDSSLTRRGQICWYQKPGVGLDAINDANLLEACIYRLLKLYCREQPYYLNLIELFLQSSYQTEIGQTLDLLTAPQGNVDLVRFTEKRYKSIVKYKTAFYSFYLPIAAAMYMAGIDGEKEHANAKKILLEMGEFFQIQDDYLDLFGDPSVTGKIGTDIQDNKCSWLVVQCLQRATPEQYQILKENYGQKEAEKVARVKALYEELDLPAVFLQYEEDSYSHIMALIEQYAAPLPPAVFLGLARKIYKRRK
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
1 (in isoform 2)Acetylation-7.32-
29PhosphorylationPRERWLGSLRRPSLV
CHHHHCCCCCCCHHH		19.2824719451
34PhosphorylationLGSLRRPSLVHGYPV
CCCCCCCHHHCCCCH		41.0128348404
57UbiquitinationWCQAWTEEPRALCSS
HHHHHCCCHHHHHHH		32.4819608861
57AcetylationWCQAWTEEPRALCSS
HHHHHCCCHHHHHHH		32.4819608861
63PhosphorylationEEPRALCSSLRMNGD
CCHHHHHHHCCCCCC		33.0026270265
64PhosphorylationEPRALCSSLRMNGDQ
CHHHHHHHCCCCCCC		20.9926270265
76PhosphorylationGDQNSDVYAQEKQDF
CCCCCCCHHHHHHHH		13.9327642862
80AcetylationSDVYAQEKQDFVQHF
CCCHHHHHHHHHHHH		42.9923236377
80UbiquitinationSDVYAQEKQDFVQHF
CCCHHHHHHHHHHHH		42.99-
88PhosphorylationQDFVQHFSQIVRVLT
HHHHHHHHHHHHHHC		19.5124275569
95PhosphorylationSQIVRVLTEDEMGHP
HHHHHHHCCCCCCCH		38.2329449344
99SulfoxidationRVLTEDEMGHPEIGD
HHHCCCCCCCHHHHH		10.3921406390
112UbiquitinationGDAIARLKEVLEYNA
HHHHHHHHHHHHHHC		39.9821906983
112AcetylationGDAIARLKEVLEYNA
HHHHHHHHHHHHHHC		39.9826051181
117PhosphorylationRLKEVLEYNAIGGKY
HHHHHHHHHCCCCCC		13.0128152594
1232-HydroxyisobutyrylationEYNAIGGKYNRGLTV
HHHCCCCCCCCCCEE		33.85-
123AcetylationEYNAIGGKYNRGLTV
HHHCCCCCCCCCCEE		33.8519608861
123UbiquitinationEYNAIGGKYNRGLTV
HHHCCCCCCCCCCEE		33.8521890473
123MalonylationEYNAIGGKYNRGLTV
HHHCCCCCCCCCCEE		33.8526320211
124PhosphorylationYNAIGGKYNRGLTVV
HHCCCCCCCCCCEEE		17.23-
142UbiquitinationRELVEPRKQDADSLQ
HHHHCCCCCCHHHHH		64.3421890473
187UbiquitinationGQICWYQKPGVGLDA
CEEEEECCCCCCCCC		28.22-
210AcetylationACIYRLLKLYCREQP
HHHHHHHHHHHHCCC		41.8425953088
210UbiquitinationACIYRLLKLYCREQP
HHHHHHHHHHHHCCC		41.8421906983
259PhosphorylationVRFTEKRYKSIVKYK
EEEEHHHHHHHHCHH		21.8328270605
260UbiquitinationRFTEKRYKSIVKYKT
EEEHHHHHHHHCHHH		37.43-
261PhosphorylationFTEKRYKSIVKYKTA
EEHHHHHHHHCHHHH		24.5528270605
264UbiquitinationKRYKSIVKYKTAFYS
HHHHHHHCHHHHHHH		39.08-
265PhosphorylationRYKSIVKYKTAFYSF
HHHHHHCHHHHHHHC		11.5930576142
271PhosphorylationKYKTAFYSFYLPIAA
CHHHHHHHCHHHHHH		10.8530576142
273PhosphorylationKTAFYSFYLPIAAAM
HHHHHHCHHHHHHHH		12.96-
281PhosphorylationLPIAAAMYMAGIDGE
HHHHHHHHHHCCCCH		4.5130576142
287AcetylationMYMAGIDGEKEHANA
HHHHCCCCHHHHHCH		46.0519608861
287UbiquitinationMYMAGIDGEKEHANA
HHHHCCCCHHHHHCH		46.0519608861
301SulfoxidationAKKILLEMGEFFQIQ
HHHHHHHHHHHHEEC		6.6828183972
332UbiquitinationGTDIQDNKCSWLVVQ
CCCCCCCCCEEHHHH		37.6221890473
334PhosphorylationDIQDNKCSWLVVQCL
CCCCCCCEEHHHHHH		25.6725599653
345PhosphorylationVQCLQRATPEQYQIL
HHHHHHCCHHHHHHH		29.5528348404
349PhosphorylationQRATPEQYQILKENY
HHCCHHHHHHHHHHC		8.8928796482
353AcetylationPEQYQILKENYGQKE
HHHHHHHHHHCCHHH		45.6119608861
353UbiquitinationPEQYQILKENYGQKE
HHHHHHHHHHCCHHH		45.6121890473
359UbiquitinationLKENYGQKEAEKVAR
HHHHCCHHHHHHHHH		55.302190698
363UbiquitinationYGQKEAEKVARVKAL
CCHHHHHHHHHHHHH		48.52-
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of FPPS_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FPPS_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of FPPS_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IDHC_HUMANIDH1physical
22863883
NDKA_HUMANNME1physical
22863883
PLST_HUMANPLS3physical
22863883
TALDO_HUMANTALDO1physical
22863883
BASP1_HUMANBASP1physical
26344197
CLIC4_HUMANCLIC4physical
26344197
DPH2_HUMANDPH2physical
26344197
GARS_HUMANGARSphysical
26344197
SPS1_HUMANSEPHS1physical
26344197
TTC38_HUMANTTC38physical
26344197
DLP1_HUMANPDSS2physical
28514442
PCYOX_HUMANPCYOX1physical
28514442
CLPP_HUMANCLPPphysical
28514442
FACE1_HUMANZMPSTE24physical
28514442
CDC27_HUMANCDC27physical
28514442
TTC19_HUMANTTC19physical
28514442
DPS1_HUMANPDSS1physical
28514442
HEM1_HUMANALAS1physical
28514442
PSME4_HUMANPSME4physical
28514442
MMAB_HUMANMMABphysical
28514442
ATPF2_HUMANATPAF2physical
28514442
GCSP_HUMANGLDCphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00630Alendronate
DB00710Ibandronate
DB00282Pamidronate
DB00884Risedronate
DB00399Zoledronate
Regulatory Network of FPPS_HUMAN

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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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