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Q13907

- IDI1_HUMAN

UniProt

Q13907 - IDI1_HUMAN

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
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 2 (30 May 2000)
      Previous versions | rss
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    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

    Binds 1 magnesium 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

    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

    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

    ArrayExpressiQ13907.
    BgeeiQ13907.
    CleanExiHS_IDI1.
    GenevestigatoriQ13907.

    Organism-specific databases

    HPAiHPA039169.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    BioGridi109648. 3 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 – 83
    Helixi11 – 166
    Beta strandi20 – 245
    Beta strandi30 – 356
    Helixi36 – 394
    Helixi42 – 454
    Turni46 – 483
    Beta strandi51 – 599
    Beta strandi65 – 706
    Beta strandi75 – 773
    Beta strandi81 – 877
    Beta strandi90 – 923
    Helixi93 – 964
    Helixi99 – 1013
    Helixi102 – 11615
    Helixi120 – 1223
    Helixi125 – 1273
    Beta strandi128 – 13912
    Beta strandi141 – 15616
    Turni165 – 1673
    Beta strandi168 – 1747
    Helixi176 – 18712
    Helixi195 – 2039
    Helixi205 – 2095
    Turni210 – 2134
    Helixi216 – 2183
    Beta strandi224 – 2263

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MPEINTNHLD KQQVQLLAEM CILIDENDNK IGAETKKNCH LNENIEKGLL    50
    HRAFSVFLFN TENKLLLQQR SDAKITFPGC FTNTCCSHPL SNPAELEESD 100
    ALGVRRAAQR RLKAELGIPL EEVPPEEINY LTRIHYKAQS DGIWGEHEID 150
    YILLVRKNVT LNPDPNEIKS YCYVSKEELK ELLKKAASGE IKITPWFKII 200
    AATFLFKWWD NLNHLNQFVD HEKIYRM 227
    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.
    The sequence AAK29357.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAK49434.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAK49435.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAP35407.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAA34890.1 differs from that shown. Reason: Erroneous initiation.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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. 3 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.
    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

    EvolutionaryTracei Q13907.
    GenomeRNAii 3422.
    NextBioi 13496.
    PROi Q13907.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13907.
    Bgeei Q13907.
    CleanExi HS_IDI1.
    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

    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: October 1, 2014
    This is version 143 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