GGPPS_HUMAN - dbPTM
GGPPS_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GGPPS_HUMAN
UniProt AC O95749
Protein Name Geranylgeranyl pyrophosphate synthase
Gene Name GGPS1
Organism Homo sapiens (Human).
Sequence Length 300
Subcellular Localization Cytoplasm.
Protein Description Catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate, an important precursor of carotenoids and geranylated proteins..
Protein Sequence MEKTQETVQRILLEPYKYLLQLPGKQVRTKLSQAFNHWLKVPEDKLQIIIEVTEMLHNASLLIDDIEDNSKLRRGFPVAHSIYGIPSVINSANYVYFLGLEKVLTLDHPDAVKLFTRQLLELHQGQGLDIYWRDNYTCPTEEEYKAMVLQKTGGLFGLAVGLMQLFSDYKEDLKPLLNTLGLFFQIRDDYANLHSKEYSENKSFCEDLTEGKFSFPTIHAIWSRPESTQVQNILRQRTENIDIKKYCVHYLEDVGSFEYTRNTLKELEAKAYKQIDARGGNPELVALVKHLSKMFKEENE
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
1Acetylation-------MEKTQETV
-------CCHHHHHH
12.2922814378
3Ubiquitination-----MEKTQETVQR
-----CCHHHHHHHH
54.96-
16PhosphorylationQRILLEPYKYLLQLP
HHHHHHHHHHHHCCC
11.6825884760
17UbiquitinationRILLEPYKYLLQLPG
HHHHHHHHHHHCCCC
39.8921890473
17UbiquitinationRILLEPYKYLLQLPG
HHHHHHHHHHHCCCC
39.89-
25AcetylationYLLQLPGKQVRTKLS
HHHCCCCHHHHHHHH
43.6219608861
25MalonylationYLLQLPGKQVRTKLS
HHHCCCCHHHHHHHH
43.6226320211
30AcetylationPGKQVRTKLSQAFNH
CCHHHHHHHHHHHHH
35.2625953088
59UbiquitinationVTEMLHNASLLIDDI
HHHHHHHCHHEECCC
7.2721890473
60PhosphorylationTEMLHNASLLIDDIE
HHHHHHCHHEECCCC
29.0920363803
70PhosphorylationIDDIEDNSKLRRGFP
ECCCCCCCHHCCCCC
45.4420363803
71UbiquitinationDDIEDNSKLRRGFPV
CCCCCCCHHCCCCCC
52.87-
87PhosphorylationHSIYGIPSVINSANY
HHHHCCCHHHCCCCE
33.4419835603
91PhosphorylationGIPSVINSANYVYFL
CCCHHHCCCCEEEEE
13.5319835603
94PhosphorylationSVINSANYVYFLGLE
HHHCCCCEEEEECCE
9.0219835603
113UbiquitinationLDHPDAVKLFTRQLL
CCCHHHHHHHHHHHH
39.3321890473
142UbiquitinationNYTCPTEEEYKAMVL
CCCCCCHHHHHHHHH
69.93-
196UbiquitinationDYANLHSKEYSENKS
HHHHCCCCCCCCCCC
50.3421890473
202UbiquitinationSKEYSENKSFCEDLT
CCCCCCCCCCCCHHH
40.64-
203PhosphorylationKEYSENKSFCEDLTE
CCCCCCCCCCCHHHC
46.8721815630
219UbiquitinationKFSFPTIHAIWSRPE
CCCCCCHHHHHCCCC
17.40-
263PhosphorylationSFEYTRNTLKELEAK
CCCCCHHHHHHHHHH
35.6029759185
265UbiquitinationEYTRNTLKELEAKAY
CCCHHHHHHHHHHHH
59.21-
265AcetylationEYTRNTLKELEAKAY
CCCHHHHHHHHHHHH
59.2125953088
270AcetylationTLKELEAKAYKQIDA
HHHHHHHHHHHHHHC
42.7625953088
272PhosphorylationKELEAKAYKQIDARG
HHHHHHHHHHHHCCC
11.6122817900
273UbiquitinationELEAKAYKQIDARGG
HHHHHHHHHHHCCCC
45.71-
273AcetylationELEAKAYKQIDARGG
HHHHHHHHHHHCCCC
45.7125953088
278MethylationAYKQIDARGGNPELV
HHHHHHCCCCCHHHH
50.21-
289AcetylationPELVALVKHLSKMFK
HHHHHHHHHHHHHHH
39.4125953088
293AcetylationALVKHLSKMFKEENE
HHHHHHHHHHHHHCC
55.5025953088

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 GGPPS_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GGPPS_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 GGPPS_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GGPPS_HUMANGGPS1physical
25416956
F120A_HUMANFAM120Aphysical
26186194
ZN696_HUMANZNF696physical
26186194
IQGA1_HUMANIQGAP1physical
26186194
CC85C_HUMANCCDC85Cphysical
26186194
HXA5_HUMANHOXA5physical
26186194
SLTM_HUMANSLTMphysical
26186194
TUSC1_HUMANTUSC1physical
26186194
RS14_HUMANRPS14physical
26344197
RUXE_HUMANSNRPEphysical
26344197
TUSC1_HUMANTUSC1physical
28514442
IQGA1_HUMANIQGAP1physical
28514442
SLTM_HUMANSLTMphysical
28514442
F120A_HUMANFAM120Aphysical
28514442
CC85C_HUMANCCDC85Cphysical
28514442
ZN696_HUMANZNF696physical
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
DB00399Zoledronate
Regulatory Network of GGPPS_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-25, AND MASS SPECTROMETRY.

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