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Q13907

- IDI1_HUMAN

UniProt

Q13907 - IDI1_HUMAN

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Protein

Isopentenyl-diphosphate Delta-isomerase 1

Gene

IDI1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

Isopentenyl diphosphate = dimethylallyl diphosphate.

Cofactori

Mg2+1 PublicationNote: Binds 1 Mg(2+) ion per subunit.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei36 – 361Substrate1 Publication
Metal bindingi40 – 401Magnesium
Metal bindingi51 – 511Magnesium
Binding sitei70 – 701Substrate1 Publication
Binding sitei74 – 741Substrate1 Publication
Active sitei86 – 861
Binding sitei87 – 871Substrate1 Publication
Metal bindingi146 – 1461Magnesium
Active sitei148 – 1481
Metal bindingi148 – 1481Magnesium

GO - Molecular functioni

  1. hydrolase activity Source: InterPro
  2. isopentenyl-diphosphate delta-isomerase activity Source: UniProtKB
  3. magnesium ion binding Source: UniProtKB
  4. manganese ion binding Source: UniProtKB
  5. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. cholesterol biosynthetic process Source: Reactome
  2. dimethylallyl diphosphate biosynthetic process Source: UniProtKB-UniPathway
  3. isoprenoid biosynthetic process Source: UniProtKB
  4. response to stilbenoid Source: Ensembl
  5. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Cholesterol biosynthesis, Cholesterol metabolism, Isoprene biosynthesis, Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS00895-MONOMER.
BRENDAi5.3.3.2. 2681.
ReactomeiREACT_147904. Activation of gene expression by SREBF (SREBP).
REACT_9405. Cholesterol biosynthesis.
SABIO-RKQ13907.
UniPathwayiUPA00059; UER00104.

Names & Taxonomyi

Protein namesi
Recommended name:
Isopentenyl-diphosphate Delta-isomerase 1 (EC:5.3.3.2)
Alternative name(s):
Isopentenyl pyrophosphate isomerase 1
Short name:
IPP isomerase 1
Short name:
IPPI1
Gene namesi
Name:IDI1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:5387. IDI1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. mitochondrion Source: Ensembl
  3. peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29635.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 227227Isopentenyl-diphosphate Delta-isomerase 1PRO_0000205222Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei176 – 1761N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ13907.
PaxDbiQ13907.
PRIDEiQ13907.

PTM databases

PhosphoSiteiQ13907.

Expressioni

Gene expression databases

BgeeiQ13907.
CleanExiHS_IDI1.
ExpressionAtlasiQ13907. baseline and differential.
GenevestigatoriQ13907.

Organism-specific databases

HPAiHPA039169.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi109648. 4 interactions.
IntActiQ13907. 1 interaction.
MINTiMINT-3028956.
STRINGi9606.ENSP00000370748.

Structurei

Secondary structure

1
227
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 83Combined sources
Helixi11 – 166Combined sources
Beta strandi20 – 245Combined sources
Beta strandi30 – 356Combined sources
Helixi36 – 394Combined sources
Helixi42 – 454Combined sources
Turni46 – 483Combined sources
Beta strandi51 – 599Combined sources
Beta strandi65 – 706Combined sources
Beta strandi75 – 773Combined sources
Beta strandi81 – 877Combined sources
Beta strandi90 – 923Combined sources
Helixi93 – 964Combined sources
Helixi99 – 1013Combined sources
Helixi102 – 11615Combined sources
Helixi120 – 1223Combined sources
Helixi125 – 1273Combined sources
Beta strandi128 – 13912Combined sources
Beta strandi141 – 15616Combined sources
Turni165 – 1673Combined sources
Beta strandi168 – 1747Combined sources
Helixi176 – 18712Combined sources
Helixi195 – 2039Combined sources
Helixi205 – 2095Combined sources
Turni210 – 2134Combined sources
Helixi216 – 2183Combined sources
Beta strandi224 – 2263Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DHOX-ray1.60A1-227[»]
2I6KX-ray2.00A/B1-227[»]
2ICJX-ray1.70A1-227[»]
2ICKX-ray1.93A1-227[»]
ProteinModelPortaliQ13907.
SMRiQ13907. Positions 9-227.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13907.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini49 – 199151Nudix hydrolasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi225 – 2273Microbody targeting signal

Sequence similaritiesi

Belongs to the IPP isomerase type 1 family.Curated
Contains 1 nudix hydrolase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG1443.
GeneTreeiENSGT00390000008527.
HOVERGENiHBG002995.
InParanoidiQ13907.
KOiK01823.
OMAiRLMDERC.
OrthoDBiEOG7H4DVK.
PhylomeDBiQ13907.
TreeFamiTF300129.

Family and domain databases

Gene3Di3.90.79.10. 1 hit.
InterProiIPR011876. IsopentenylPP_isomerase_typ1.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
PANTHERiPTHR10885. PTHR10885. 1 hit.
PfamiPF00293. NUDIX. 1 hit.
[Graphical view]
PIRSFiPIRSF018427. Isopntndiph_ism. 1 hit.
SUPFAMiSSF55811. SSF55811. 1 hit.
TIGRFAMsiTIGR02150. IPP_isom_1. 1 hit.
PROSITEiPS51462. NUDIX. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q13907-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPEINTNHLD KQQVQLLAEM CILIDENDNK IGAETKKNCH LNENIEKGLL
60 70 80 90 100
HRAFSVFLFN TENKLLLQQR SDAKITFPGC FTNTCCSHPL SNPAELEESD
110 120 130 140 150
ALGVRRAAQR RLKAELGIPL EEVPPEEINY LTRIHYKAQS DGIWGEHEID
160 170 180 190 200
YILLVRKNVT LNPDPNEIKS YCYVSKEELK ELLKKAASGE IKITPWFKII
210 220
AATFLFKWWD NLNHLNQFVD HEKIYRM
Length:227
Mass (Da):26,319
Last modified:May 30, 2000 - v2
Checksum:i1255ACC2C4D1E8D1
GO
Isoform 2 (identifier: Q13907-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MWRGLALARAIGCAARGRGQWAVRAADCAQSGRHPGPAVVCGRRLISVLEQIRHFVMM

Show »
Length:284
Mass (Da):32,485
Checksum:i80478664FEBD5978
GO

Sequence cautioni

The sequence AAH57827.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAK29357.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAK49434.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAK49435.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAP35407.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA34890.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 451I → V in BAD96595. 1 PublicationCurated
Sequence conflicti101 – 1011A → T in AAH19227. (PubMed:15489334)Curated
Sequence conflicti156 – 1561R → G in BAD96595. 1 PublicationCurated
Sequence conflicti173 – 1731Y → H in AAH06999. (PubMed:15489334)Curated
Isoform 2 (identifier: Q13907-2)
Sequence conflicti39 – 391V → G in AAI07894. (PubMed:15489334)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MWRGLALARAIGCAARGRGQ WAVRAADCAQSGRHPGPAVV CGRRLISVLEQIRHFVMM in isoform 2. 2 PublicationsVSP_037889

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17025 mRNA. Translation: CAA34890.1. Different initiation.
AF291755 Genomic DNA. Translation: AAK29357.1. Different initiation.
AF271720 mRNA. Translation: AAK49435.1. Different initiation.
AF271724
, AF271721, AF271722, AF271723 Genomic DNA. Translation: AAK49434.1. Different initiation.
BT006761 mRNA. Translation: AAP35407.1. Different initiation.
AK303669 mRNA. Translation: BAG64667.1.
AC022536 Genomic DNA. No translation available.
CH471072 Genomic DNA. Translation: EAW86521.1.
BC005247 mRNA. Translation: AAH05247.2.
BC006999 mRNA. Translation: AAH06999.2.
BC019227 mRNA. Translation: AAH19227.2.
BC022418 mRNA. Translation: AAH22418.2.
BC025375 mRNA. Translation: AAH25375.2.
BC057827 mRNA. Translation: AAH57827.1. Different initiation.
BC107893 mRNA. Translation: AAI07894.1.
AK222875 mRNA. Translation: BAD96595.1.
CCDSiCCDS7056.1. [Q13907-2]
RefSeqiNP_004499.2. NM_004508.2. [Q13907-2]
XP_005252502.1. XM_005252445.1.
UniGeneiHs.283652.

Genome annotation databases

EnsembliENST00000381344; ENSP00000370748; ENSG00000067064. [Q13907-2]
GeneIDi3422.
KEGGihsa:3422.
UCSCiuc001ifz.3. human. [Q13907-2]

Polymorphism databases

DMDMi6225527.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17025 mRNA. Translation: CAA34890.1 . Different initiation.
AF291755 Genomic DNA. Translation: AAK29357.1 . Different initiation.
AF271720 mRNA. Translation: AAK49435.1 . Different initiation.
AF271724
, AF271721 , AF271722 , AF271723 Genomic DNA. Translation: AAK49434.1 . Different initiation.
BT006761 mRNA. Translation: AAP35407.1 . Different initiation.
AK303669 mRNA. Translation: BAG64667.1 .
AC022536 Genomic DNA. No translation available.
CH471072 Genomic DNA. Translation: EAW86521.1 .
BC005247 mRNA. Translation: AAH05247.2 .
BC006999 mRNA. Translation: AAH06999.2 .
BC019227 mRNA. Translation: AAH19227.2 .
BC022418 mRNA. Translation: AAH22418.2 .
BC025375 mRNA. Translation: AAH25375.2 .
BC057827 mRNA. Translation: AAH57827.1 . Different initiation.
BC107893 mRNA. Translation: AAI07894.1 .
AK222875 mRNA. Translation: BAD96595.1 .
CCDSi CCDS7056.1. [Q13907-2 ]
RefSeqi NP_004499.2. NM_004508.2. [Q13907-2 ]
XP_005252502.1. XM_005252445.1.
UniGenei Hs.283652.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DHO X-ray 1.60 A 1-227 [» ]
2I6K X-ray 2.00 A/B 1-227 [» ]
2ICJ X-ray 1.70 A 1-227 [» ]
2ICK X-ray 1.93 A 1-227 [» ]
ProteinModelPortali Q13907.
SMRi Q13907. Positions 9-227.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109648. 4 interactions.
IntActi Q13907. 1 interaction.
MINTi MINT-3028956.
STRINGi 9606.ENSP00000370748.

Chemistry

GuidetoPHARMACOLOGYi 646.

PTM databases

PhosphoSitei Q13907.

Polymorphism databases

DMDMi 6225527.

Proteomic databases

MaxQBi Q13907.
PaxDbi Q13907.
PRIDEi Q13907.

Protocols and materials databases

DNASUi 3422.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000381344 ; ENSP00000370748 ; ENSG00000067064 . [Q13907-2 ]
GeneIDi 3422.
KEGGi hsa:3422.
UCSCi uc001ifz.3. human. [Q13907-2 ]

Organism-specific databases

CTDi 3422.
GeneCardsi GC10M001075.
H-InvDB HIX0008588.
HGNCi HGNC:5387. IDI1.
HPAi HPA039169.
MIMi 604055. gene.
neXtProti NX_Q13907.
PharmGKBi PA29635.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1443.
GeneTreei ENSGT00390000008527.
HOVERGENi HBG002995.
InParanoidi Q13907.
KOi K01823.
OMAi RLMDERC.
OrthoDBi EOG7H4DVK.
PhylomeDBi Q13907.
TreeFami TF300129.

Enzyme and pathway databases

UniPathwayi UPA00059 ; UER00104 .
BioCyci MetaCyc:HS00895-MONOMER.
BRENDAi 5.3.3.2. 2681.
Reactomei REACT_147904. Activation of gene expression by SREBF (SREBP).
REACT_9405. Cholesterol biosynthesis.
SABIO-RK Q13907.

Miscellaneous databases

ChiTaRSi IDI1. human.
EvolutionaryTracei Q13907.
GenomeRNAii 3422.
NextBioi 13496.
PROi Q13907.
SOURCEi Search...

Gene expression databases

Bgeei Q13907.
CleanExi HS_IDI1.
ExpressionAtlasi Q13907. baseline and differential.
Genevestigatori Q13907.

Family and domain databases

Gene3Di 3.90.79.10. 1 hit.
InterProi IPR011876. IsopentenylPP_isomerase_typ1.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view ]
PANTHERi PTHR10885. PTHR10885. 1 hit.
Pfami PF00293. NUDIX. 1 hit.
[Graphical view ]
PIRSFi PIRSF018427. Isopntndiph_ism. 1 hit.
SUPFAMi SSF55811. SSF55811. 1 hit.
TIGRFAMsi TIGR02150. IPP_isom_1. 1 hit.
PROSITEi PS51462. NUDIX. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A human promyelocyte mRNA transiently induced by TPA is homologous to yeast IPP isomerase."
    Xuan J.W., Kowalski J., Chambers A.F., Denhardt D.T.
    Genomics 20:129-131(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Two genes for isopentenyl diphosphate isomerase in human."
    Masuda K., Breitling R., Krisans S.K., Keller B., Moeller G., Adamski J.
    Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Characterisation of a human gene for isopentenyl diphosphate dimethylally diphosphate isomerase 1 (IDI1)."
    Masuda K., Krisans S.K., Keller B., Moeller G., Adamski J.
    Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. "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.
    , 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] (ISOFORM 2).
    Tissue: Kidney.
  6. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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] (ISOFORM 1), PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Bone marrow, Skin and Urinary bladder.
  9. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 40-227 (ISOFORM 2).
    Tissue: Liver.
  10. "Human isopentenyl diphosphate: dimethylallyl diphosphate isomerase: overproduction, purification, and characterization."
    Hahn F.M., Xuan J.W., Chambers A.F., Poulter C.D.
    Arch. Biochem. Biophys. 332:30-34(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, COFACTOR.
  11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "The crystal structure of human isopentenyl diphosphate isomerase at 1.7 A resolution reveals its catalytic mechanism in isoprenoid biosynthesis."
    Zheng W., Sun F., Bartlam M., Li X., Li R., Rao Z.
    J. Mol. Biol. 366:1447-1458(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND METAL IONS, SUBUNIT.

Entry informationi

Entry nameiIDI1_HUMAN
AccessioniPrimary (citable) accession number: Q13907
Secondary accession number(s): B4E155
, Q32Q13, Q53GQ6, Q86U81, Q8WUX8, Q96IZ4, Q9BQ74
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: November 26, 2014
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3