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Q9BXS1 (IDI2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Isopentenyl-diphosphate delta-isomerase 2

EC=5.3.3.2
Alternative name(s):
Isopentenyl pyrophosphate isomerase 2
Short name=IPP isomerase 2
Short name=IPPI2
Gene names
Name:IDI2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length227 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

Isopentenyl diphosphate = dimethylallyl diphosphate.

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Pathway

Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate: step 1/1.

Subcellular location

Peroxisome Ref.1.

Tissue specificity

Detected in skeletal muscle. Ref.1

Sequence similarities

Belongs to the IPP isomerase type 1 family.

Contains 1 nudix hydrolase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 227227Isopentenyl-diphosphate delta-isomerase 2
PRO_0000205228

Regions

Domain49 – 199151Nudix hydrolase
Motif225 – 2273Microbody targeting signal Potential

Sites

Active site861 By similarity
Active site1481 By similarity
Metal binding401Magnesium By similarity
Metal binding511Magnesium By similarity
Metal binding1461Magnesium By similarity
Metal binding1481Magnesium By similarity
Binding site361Substrate By similarity
Binding site701Substrate By similarity
Binding site741Substrate By similarity
Binding site871Substrate By similarity

Secondary structure

........................................... 227
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9BXS1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 2FD79B076D94A7D0

FASTA22726,753
        10         20         30         40         50         60 
MSDINLDWVD RRQLQRLEEM LIVVDENDKV IGADTKRNCH LNENIEKGLL HRAFSVVLFN 

        70         80         90        100        110        120 
TKNRILIQQR SDTKVTFPGY FTDSCSSHPL YNPAELEEKD AIGVRRAAQR RLQAELGIPG 

       130        140        150        160        170        180 
EQISPEDIVF MTIYHHKAKS DRIWGEHEIC YLLLVRKNVT LNPDPSETKS ILYLSQEELW 

       190        200        210        220 
ELLEREARGE VKVTPWLRTI AERFLYRWWP HLDDVTPFVE LHKIHRV 

« Hide

References

« Hide 'large scale' references
[1]"IDI2, a second isopentenyl diphosphate isomerase in mammals."
Clizbe D.B., Owens M.L., Masuda K.R., Shackelford J.E., Krisans S.K.
J. Biol. Chem. 282:6668-6676(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Skeletal muscle.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Skeletal muscle.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF291755 Genomic DNA. Translation: AAK29358.1.
AF271729 expand/collapse EMBL AC list , AF271726, AF271727, AF271728 Genomic DNA. Translation: AAK49436.1.
AF271725 mRNA. Translation: AAK49437.1.
AK056950 mRNA. Translation: BAB71322.1.
BC017778 mRNA. Translation: AAH17778.1.
RefSeqNP_150286.1. NM_033261.2.
UniGeneHs.591325.
Hs.9270.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2PNYX-ray1.81A1-227[»]
ProteinModelPortalQ9BXS1.
SMRQ9BXS1. Positions 1-227.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124870. 2 interactions.
IntActQ9BXS1. 1 interaction.
STRING9606.ENSP00000277517.

PTM databases

PhosphoSiteQ9BXS1.

Polymorphism databases

DMDM20978506.

Proteomic databases

PaxDbQ9BXS1.
PRIDEQ9BXS1.

Protocols and materials databases

DNASU91734.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000277517; ENSP00000277517; ENSG00000148377.
GeneID91734.
KEGGhsa:91734.
UCSCuc001ifv.1. human.

Organism-specific databases

CTD91734.
GeneCardsGC10M001064.
H-InvDBHIX0127248.
HGNCHGNC:23487. IDI2.
HPAHPA041254.
MIM615389. gene.
neXtProtNX_Q9BXS1.
PharmGKBPA134935136.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1443.
HOGENOMHOG000274106.
HOVERGENHBG002995.
InParanoidQ9BXS1.
KOK01823.
OMAYILIANT.
OrthoDBEOG7H4DVK.
PhylomeDBQ9BXS1.
TreeFamTF300129.

Enzyme and pathway databases

BioCycMetaCyc:HS07522-MONOMER.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00059; UER00104.

Gene expression databases

BgeeQ9BXS1.
CleanExHS_IDI2.
GenevestigatorQ9BXS1.

Family and domain databases

Gene3D3.90.79.10. 1 hit.
InterProIPR011876. IsopentenylPP_isomerase_typ1.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
PANTHERPTHR10885. PTHR10885. 1 hit.
PfamPF00293. NUDIX. 1 hit.
[Graphical view]
PIRSFPIRSF018427. Isopntndiph_ism. 1 hit.
SUPFAMSSF55811. SSF55811. 1 hit.
TIGRFAMsTIGR02150. IPP_isom_1. 1 hit.
PROSITEPS51462. NUDIX. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9BXS1.
GenomeRNAi91734.
NextBio77415.
PROQ9BXS1.
SOURCESearch...

Entry information

Entry nameIDI2_HUMAN
AccessionPrimary (citable) accession number: Q9BXS1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2002
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM