IDI1_HUMAN - dbPTM
IDI1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IDI1_HUMAN
UniProt AC Q13907
Protein Name Isopentenyl-diphosphate Delta-isomerase 1
Gene Name IDI1
Organism Homo sapiens (Human).
Sequence Length 227
Subcellular Localization Peroxisome.
Protein Description Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP)..
Protein Sequence MPEINTNHLDKQQVQLLAEMCILIDENDNKIGAETKKNCHLNENIEKGLLHRAFSVFLFNTENKLLLQQRSDAKITFPGCFTNTCCSHPLSNPAELEESDALGVRRAAQRRLKAELGIPLEEVPPEEINYLTRIHYKAQSDGIWGEHEIDYILLVRKNVTLNPDPNEIKSYCYVSKEELKELLKKAASGEIKITPWFKIIAATFLFKWWDNLNHLNQFVDHEKIYRM
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
36UbiquitinationNKIGAETKKNCHLNE
CCCCCCHHCCCCCCC		33.23-
37UbiquitinationKIGAETKKNCHLNEN
CCCCCHHCCCCCCCC		72.7027667366
38UbiquitinationIGAETKKNCHLNENI
CCCCHHCCCCCCCCH		21.7227667366
45UbiquitinationNCHLNENIEKGLLHR
CCCCCCCHHHCHHHH		4.7621963094
47UbiquitinationHLNENIEKGLLHRAF
CCCCCHHHCHHHHHH		51.5721890473
47 (in isoform 2)Phosphorylation-51.5727542207
472-HydroxyisobutyrylationHLNENIEKGLLHRAF
CCCCCHHHCHHHHHH		51.57-
47 (in isoform 1)Ubiquitination-51.5721890473
48UbiquitinationLNENIEKGLLHRAFS
CCCCHHHCHHHHHHE		22.2333845483
55PhosphorylationGLLHRAFSVFLFNTE
CHHHHHHEEEEEECC		15.8129514088
62UbiquitinationSVFLFNTENKLLLQQ
EEEEEECCCCCCEEC		54.1721963094
75UbiquitinationQQRSDAKITFPGCFT
ECCCCCCEECCCCCC		5.2821963094
76PhosphorylationQRSDAKITFPGCFTN
CCCCCCEECCCCCCC		24.07-
82PhosphorylationITFPGCFTNTCCSHP
EECCCCCCCCCCCCC		33.4226091039
84UbiquitinationFPGCFTNTCCSHPLS
CCCCCCCCCCCCCCC		16.3021963094
84PhosphorylationFPGCFTNTCCSHPLS
CCCCCCCCCCCCCCC		16.3026091039
87PhosphorylationCFTNTCCSHPLSNPA
CCCCCCCCCCCCCHH		30.2226091039
91PhosphorylationTCCSHPLSNPAELEE
CCCCCCCCCHHHHHH		45.26-
93UbiquitinationCSHPLSNPAELEESD
CCCCCCCHHHHHHHH		24.6027667366
94UbiquitinationSHPLSNPAELEESDA
CCCCCCHHHHHHHHH		37.9527667366
94 (in isoform 2)Ubiquitination-37.95-
99PhosphorylationNPAELEESDALGVRR
CHHHHHHHHHHHHHH		20.86-
101UbiquitinationAELEESDALGVRRAA
HHHHHHHHHHHHHHH		18.5921963094
104 (in isoform 2)Ubiquitination-3.7821890473
104UbiquitinationEESDALGVRRAAQRR
HHHHHHHHHHHHHHH		3.7833845483
112PhosphorylationRRAAQRRLKAELGIP
HHHHHHHHHHHHCCC		7.21-
113UbiquitinationRAAQRRLKAELGIPL
HHHHHHHHHHHCCCH		37.6921890473
113 (in isoform 1)Ubiquitination-37.6921890473
114UbiquitinationAAQRRLKAELGIPLE
HHHHHHHHHHCCCHH		23.1021963094
121UbiquitinationAELGIPLEEVPPEEI
HHHCCCHHHCCHHHH		52.15-
128UbiquitinationEEVPPEEINYLTRIH
HHCCHHHHHHHEEEE		3.8129967540
130PhosphorylationVPPEEINYLTRIHYK
CCHHHHHHHEEEEEE		18.34-
131UbiquitinationPPEEINYLTRIHYKA
CHHHHHHHEEEEEEE		1.9321963094
131 (in isoform 2)Ubiquitination-1.93-
132PhosphorylationPEEINYLTRIHYKAQ
HHHHHHHEEEEEEEC		19.74-
133PhosphorylationEEINYLTRIHYKAQS
HHHHHHEEEEEEECC		15.87-
140UbiquitinationRIHYKAQSDGIWGEH
EEEEEECCCCCCCCC		42.5421890473
147UbiquitinationSDGIWGEHEIDYILL
CCCCCCCCCCCEEEE		33.1232015554
151UbiquitinationWGEHEIDYILLVRKN
CCCCCCCEEEEEEEC		10.1021890473
155UbiquitinationEIDYILLVRKNVTLN
CCCEEEEEEECEECC		7.9922817900
156UbiquitinationIDYILLVRKNVTLNP
CCEEEEEEECEECCC		25.4622817900
157UbiquitinationDYILLVRKNVTLNPD
CEEEEEEECEECCCC		48.5721890473
158UbiquitinationYILLVRKNVTLNPDP
EEEEEEECEECCCCH		22.8029967540
160PhosphorylationLLVRKNVTLNPDPNE
EEEEECEECCCCHHH		30.16-
163UbiquitinationRKNVTLNPDPNEIKS
EECEECCCCHHHHHH		62.6421890473
164UbiquitinationKNVTLNPDPNEIKSY
ECEECCCCHHHHHHH		58.5522817900
168UbiquitinationLNPDPNEIKSYCYVS
CCCCHHHHHHHEEEC		4.5821890473
169UbiquitinationNPDPNEIKSYCYVSK
CCCHHHHHHHEEECH		29.2421890473
169AcetylationNPDPNEIKSYCYVSK
CCCHHHHHHHEEECH		29.2426051181
169 (in isoform 1)Ubiquitination-29.2421890473
170 (in isoform 2)Ubiquitination-26.5421890473
170SumoylationPDPNEIKSYCYVSKE
CCHHHHHHHEEECHH		26.54-
170UbiquitinationPDPNEIKSYCYVSKE
CCHHHHHHHEEECHH		26.5421906983
170PhosphorylationPDPNEIKSYCYVSKE
CCHHHHHHHEEECHH		26.5429083192
171PhosphorylationDPNEIKSYCYVSKEE
CHHHHHHHEEECHHH		5.2529083192
172S-nitrosocysteinePNEIKSYCYVSKEEL
HHHHHHHEEECHHHH		3.31-
172UbiquitinationPNEIKSYCYVSKEEL
HHHHHHHEEECHHHH		3.3122817900
172S-nitrosylationPNEIKSYCYVSKEEL
HHHHHHHEEECHHHH		3.3119483679
173UbiquitinationNEIKSYCYVSKEELK
HHHHHHEEECHHHHH		10.2622817900
173PhosphorylationNEIKSYCYVSKEELK
HHHHHHEEECHHHHH		10.2629083192
175PhosphorylationIKSYCYVSKEELKEL
HHHHEEECHHHHHHH		14.1029083192
176AcetylationKSYCYVSKEELKELL
HHHEEECHHHHHHHH		45.2019608861
176UbiquitinationKSYCYVSKEELKELL
HHHEEECHHHHHHHH		45.20-
176SuccinylationKSYCYVSKEELKELL
HHHEEECHHHHHHHH		45.2023954790
177UbiquitinationSYCYVSKEELKELLK
HHEEECHHHHHHHHH		62.1432015554
180UbiquitinationYVSKEELKELLKKAA
EECHHHHHHHHHHHH		49.9821890473
180AcetylationYVSKEELKELLKKAA
EECHHHHHHHHHHHH		49.9825038526
180SuccinylationYVSKEELKELLKKAA
EECHHHHHHHHHHHH		49.9823954790
180 (in isoform 1)Ubiquitination-49.9821890473
181UbiquitinationVSKEELKELLKKAAS
ECHHHHHHHHHHHHC		72.4621890473
185UbiquitinationELKELLKKAASGEIK
HHHHHHHHHHCCCCC		49.5122817900
186UbiquitinationLKELLKKAASGEIKI
HHHHHHHHHCCCCCC		12.7922817900
187PhosphorylationKELLKKAASGEIKIT
HHHHHHHHCCCCCCC		27.27-
188PhosphorylationELLKKAASGEIKITP
HHHHHHHCCCCCCCH		41.6429396449
189PhosphorylationLLKKAASGEIKITPW
HHHHHHCCCCCCCHH		35.60-
192UbiquitinationKAASGEIKITPWFKI
HHHCCCCCCCHHHHH		35.902189047
192 (in isoform 1)Ubiquitination-35.9021890473
193UbiquitinationAASGEIKITPWFKII
HHCCCCCCCHHHHHH		7.4121890473
194UbiquitinationASGEIKITPWFKIIA
HCCCCCCCHHHHHHH		14.9521890473
203PhosphorylationWFKIIAATFLFKWWD
HHHHHHHHHHHHHHH		16.3221406692
208 (in isoform 2)Phosphorylation-10.5827642862
211UbiquitinationFLFKWWDNLNHLNQF
HHHHHHHHHHHHHHH		29.0821890473
214UbiquitinationKWWDNLNHLNQFVDH
HHHHHHHHHHHHCCH		29.3529967540
214 (in isoform 2)Ubiquitination-29.35-
223UbiquitinationNQFVDHEKIYRM---
HHHCCHHHHHCC---		41.43-
223 (in isoform 1)Ubiquitination-41.4321890473
224UbiquitinationQFVDHEKIYRM----
HHCCHHHHHCC----		2.1021890473
226 (in isoform 2)Ubiquitination-28.0121890473
226UbiquitinationVDHEKIYRM------
CCHHHHHCC------		28.0121890473
228 (in isoform 2)Phosphorylation-27642862
230 (in isoform 2)Phosphorylation-27642862
233UbiquitinationRM-------------
CC-------------		33845483
233AcetylationRM-------------
CC-------------		19608861
233 (in isoform 2)Ubiquitination--
233 (in isoform 2)Malonylation-32601280
237 (in isoform 2)Ubiquitination-21890473
237Ubiquitination-----------------
-----------------		21890473
241Ubiquitination---------------------
---------------------		22817900
242Ubiquitination----------------------
----------------------		22817900
249 (in isoform 2)Ubiquitination-21890473
249Ubiquitination-----------------------------
-----------------------------		21890473
260Phosphorylation----------------------------------------
----------------------------------------		-
280 (in isoform 2)Ubiquitination-21890473
280Ubiquitination------------------------------------------------------------
------------------------------------------------------------		21890473
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
55SPhosphorylationKinaseCHEK1O14757
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IDI1_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 IDI1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VWA8_HUMANVWA8physical
26186194
VWA8_HUMANVWA8physical
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
There are no disease associations of PTM sites.
Regulatory Network of IDI1_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-176, AND MASS SPECTROMETRY.

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