CPLM-012221

Genbank Nucleotide ID

Isopentenyl-diphosphate Delta-isomerase 1

Protein Synonyms/Alias

Isopentenyl pyrophosphate isomerase 1; IPP isomerase 1; IPPI1

Homo sapiens (Human)

Position	Peptide	Type	References
36	NKIGAETKKNCHLNE	ubiquitination	[1]
47	HLNENIEKGLLHRAF	ubiquitination	[2]
113	RAAQRRLKAELGIPL	ubiquitination	[1, 2, 3, 4, 5, 6]
157	DYILLVRKNVTLNPD	ubiquitination	[6]
169	NPDPNEIKSYCYVSK	ubiquitination	[2]
176	KSYCYVSKEELKELL	acetylation	[7]
176	KSYCYVSKEELKELL	ubiquitination	[6, 8]
180	YVSKEELKELLKKAA	acetylation	[9]
180	YVSKEELKELLKKAA	ubiquitination	[2]
192	KAASGEIKITPWFKI	ubiquitination	[2, 6]
223	NQFVDHEKIYRM***	ubiquitination	[2, 6]

[1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[3] Global identification of modular cullin-RING ligase substrates.
Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
[4] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
[5] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
[6] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[7] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
[8] Integrated proteomic analysis of post-translational modifications by serial enrichment.
Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
[9] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
PLoS One. 2012;7(12):e50545. [PMID: 23236377]

Functional Description

Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).

DOMAIN 49 199 Nudix hydrolase.
MOTIF 225 227 Microbody targeting signal.
ACT_SITE 86 86
ACT_SITE 148 148
METAL 40 40 Magnesium.
METAL 51 51 Magnesium.
METAL 146 146 Magnesium.
METAL 148 148 Magnesium.
BINDING 36 36 Substrate.
BINDING 70 70 Substrate.
BINDING 74 74 Substrate.
BINDING 87 87 Substrate.
MOD_RES 176 176 N6-acetyllysine.

3D-structure; Acetylation; Alternative splicing; Cholesterol biosynthesis; Cholesterol metabolism; Complete proteome; Isomerase; Isoprene biosynthesis; Lipid biosynthesis; Lipid metabolism; Magnesium; Metal-binding; Peroxisome; Reference proteome; Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis; Sterol metabolism.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005829; C:cytosol; TAS:Reactome.
GO:0005739; C:mitochondrion; IEA:Compara.
GO:0005777; C:peroxisome; IDA:UniProtKB.
GO:0016787; F:hydrolase activity; IEA:InterPro.
GO:0004452; F:isopentenyl-diphosphate delta-isomerase activity; IDA:UniProtKB.
GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO:0030145; F:manganese ion binding; IDA:UniProtKB.
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO:0006695; P:cholesterol biosynthetic process; TAS:Reactome.
GO:0050992; P:dimethylallyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
GO:0008299; P:isoprenoid biosynthetic process; IDA:UniProtKB.
GO:0035634; P:response to stilbenoid; IEA:Compara.

IPR011876; IsopentenylPP_isomerase_typ1.
IPR000086; NUDIX_hydrolase_dom.
IPR015797; NUDIX_hydrolase_dom-like.