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Q9UGB7

- MIOX_HUMAN

UniProt

Q9UGB7 - MIOX_HUMAN

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Protein

Inositol oxygenase

Gene
MIOX, ALDRL6, KSP32, RSOR
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

Myo-inositol + O2 = D-glucuronate + H2O.1 Publication

Cofactori

Binds 2 iron ions per subunit.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei29 – 291Substrate By similarity
Metal bindingi98 – 981Iron 1
Metal bindingi123 – 1231Iron 1
Metal bindingi124 – 1241Iron 1
Metal bindingi124 – 1241Iron 2
Binding sitei127 – 1271Substrate
Metal bindingi194 – 1941Iron 2
Metal bindingi220 – 2201Iron 2
Metal bindingi253 – 2531Iron 1

GO - Molecular functioni

  1. aldo-keto reductase (NADP) activity Source: UniProtKB
  2. ferric iron binding Source: UniProtKB
  3. inositol oxygenase activity Source: UniProtKB
  4. NADP binding Source: Ensembl
  5. oxidoreductase activity, acting on NAD(P)H Source: Ensembl
  6. oxidoreductase activity, acting on single donors with incorporation of molecular oxygen Source: UniProtKB

GO - Biological processi

  1. inositol catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BRENDAi1.13.99.1. 2681.
SABIO-RKQ9UGB7.
UniPathwayiUPA00111; UER00527.

Names & Taxonomyi

Protein namesi
Recommended name:
Inositol oxygenase (EC:1.13.99.1)
Alternative name(s):
Aldehyde reductase-like 6
Kidney-specific protein 32
Myo-inositol oxygenase
Short name:
MI oxygenase
Renal-specific oxidoreductase
Gene namesi
Name:MIOX
Synonyms:ALDRL6, KSP32, RSOR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:14522. MIOX.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProt
  3. inclusion body Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi127 – 1271K → S: Strongly reduced enzyme activity. 1 Publication

Organism-specific databases

PharmGKBiPA24716.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 285285Inositol oxygenasePRO_0000079148Add
BLAST

Proteomic databases

PaxDbiQ9UGB7.
PRIDEiQ9UGB7.

PTM databases

PhosphoSiteiQ9UGB7.

Expressioni

Tissue specificityi

Kidney specific.

Gene expression databases

BgeeiQ9UGB7.
CleanExiHS_MIOX.
GenevestigatoriQ9UGB7.

Organism-specific databases

HPAiHPA039451.
HPA039562.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000216075.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi38 – 5013
Helixi53 – 6311
Beta strandi68 – 714
Helixi73 – 797
Helixi80 – 823
Helixi95 – 10915
Helixi114 – 1229
Helixi125 – 1273
Helixi128 – 1314
Helixi136 – 1383
Beta strandi145 – 1484
Helixi157 – 1604
Helixi165 – 1684
Turni170 – 1723
Beta strandi173 – 1764
Helixi185 – 1873
Helixi194 – 20512
Helixi211 – 2199
Helixi223 – 2264
Turni232 – 2343
Helixi237 – 25317
Helixi264 – 27815
Beta strandi283 – 2853

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IBNX-ray1.50A/B38-285[»]
ProteinModelPortaliQ9UGB7.
SMRiQ9UGB7. Positions 37-285.

Miscellaneous databases

EvolutionaryTraceiQ9UGB7.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni85 – 873Substrate binding
Regioni141 – 1422Substrate binding
Regioni220 – 2212Substrate binding

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG135479.
HOGENOMiHOG000163182.
HOVERGENiHBG039556.
InParanoidiQ9UGB7.
KOiK00469.
OMAiNFYREQH.
OrthoDBiEOG7DZ8KD.
PhylomeDBiQ9UGB7.
TreeFamiTF300089.

Family and domain databases

InterProiIPR007828. Inositol_oxygenase.
[Graphical view]
PANTHERiPTHR12588. PTHR12588. 1 hit.
PfamiPF05153. DUF706. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UGB7-1) [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

MKVTVGPDPS LVYRPDVDPE VAKDKASFRN YTSGPLLDRV FTTYKLMHTH    50
QTVDFVRSKH AQFGGFSYKK MTVMEAVDLL DGLVDESDPD VDFPNSFHAF 100
QTAEGIRKAH PDKDWFHLVG LLHDLGKVLA LFGEPQWAVV GDTFPVGCRP 150
QASVVFCDST FQDNPDLQDP RYSTELGMYQ PHCGLDRVLM SWGHDEYMYQ 200
VMKFNKFSLP PEAFYMIRFH SFYPWHTGRD YQQLCSQQDL AMLPWVREFN 250
KFDLYTKCPD LPDVDKLRPY YQGLIDKYCP GILSW 285
Length:285
Mass (Da):33,010
Last modified:May 1, 2000 - v1
Checksum:iED70B197FF267B2B
GO
Isoform 2 (identifier: Q9UGB7-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     114-231: DWFHLVGLLH...FYPWHTGRDY → VPNLPCPSPS...QAAALLPGAH
     232-285: Missing.

Show »
Length:231
Mass (Da):24,516
Checksum:i4C63EF35422491AF
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei114 – 231118DWFHL…TGRDY → VPNLPCPSPSQTGSTSSGSC TTWGRSWPCSGSPSGLSSAT PSPSDAVRRPPWFSATPPSR TTLTSRILDTAQSSGCISPT VGSTGSSCPGAMMQVRPLHQ VPGPAGRGQAAALLPGAH in isoform 2. VSP_041667Add
BLAST
Alternative sequencei232 – 28554Missing in isoform 2. VSP_041668Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41T → D in AAF25204. 1 Publication
Sequence conflicti199 – 1991Y → F in AAK00766. 1 Publication
Sequence conflicti219 – 2213FHS → VHF in AAK00766. 1 Publication
Sequence conflicti282 – 2821I → T in AAF25204. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY064416 mRNA. Translation: AAL47192.1.
AF230095 mRNA. Translation: AAK00766.1.
AF197129 mRNA. Translation: AAF25204.1.
AY738258 mRNA. Translation: AAV65816.1.
AK000576 mRNA. Translation: BAA91266.1.
CR456478 mRNA. Translation: CAG30364.1.
AL096767 Genomic DNA. Translation: CAB63064.1.
AL096767 Genomic DNA. Translation: CAO03465.1.
CH471138 Genomic DNA. Translation: EAW73547.1.
BC012025 mRNA. Translation: AAH12025.1.
BC073848 mRNA. Translation: AAH73848.1.
CCDSiCCDS14092.1. [Q9UGB7-1]
RefSeqiNP_060054.4. NM_017584.5. [Q9UGB7-1]
UniGeneiHs.129227.

Genome annotation databases

EnsembliENST00000216075; ENSP00000216075; ENSG00000100253. [Q9UGB7-1]
ENST00000395733; ENSP00000379082; ENSG00000100253. [Q9UGB7-2]
GeneIDi55586.
KEGGihsa:55586.
UCSCiuc003bll.1. human. [Q9UGB7-1]
uc003bln.1. human. [Q9UGB7-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY064416 mRNA. Translation: AAL47192.1 .
AF230095 mRNA. Translation: AAK00766.1 .
AF197129 mRNA. Translation: AAF25204.1 .
AY738258 mRNA. Translation: AAV65816.1 .
AK000576 mRNA. Translation: BAA91266.1 .
CR456478 mRNA. Translation: CAG30364.1 .
AL096767 Genomic DNA. Translation: CAB63064.1 .
AL096767 Genomic DNA. Translation: CAO03465.1 .
CH471138 Genomic DNA. Translation: EAW73547.1 .
BC012025 mRNA. Translation: AAH12025.1 .
BC073848 mRNA. Translation: AAH73848.1 .
CCDSi CCDS14092.1. [Q9UGB7-1 ]
RefSeqi NP_060054.4. NM_017584.5. [Q9UGB7-1 ]
UniGenei Hs.129227.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2IBN X-ray 1.50 A/B 38-285 [» ]
ProteinModelPortali Q9UGB7.
SMRi Q9UGB7. Positions 37-285.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000216075.

PTM databases

PhosphoSitei Q9UGB7.

Proteomic databases

PaxDbi Q9UGB7.
PRIDEi Q9UGB7.

Protocols and materials databases

DNASUi 55586.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000216075 ; ENSP00000216075 ; ENSG00000100253 . [Q9UGB7-1 ]
ENST00000395733 ; ENSP00000379082 ; ENSG00000100253 . [Q9UGB7-2 ]
GeneIDi 55586.
KEGGi hsa:55586.
UCSCi uc003bll.1. human. [Q9UGB7-1 ]
uc003bln.1. human. [Q9UGB7-2 ]

Organism-specific databases

CTDi 55586.
GeneCardsi GC22P050925.
HGNCi HGNC:14522. MIOX.
HPAi HPA039451.
HPA039562.
MIMi 606774. gene.
neXtProti NX_Q9UGB7.
PharmGKBi PA24716.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG135479.
HOGENOMi HOG000163182.
HOVERGENi HBG039556.
InParanoidi Q9UGB7.
KOi K00469.
OMAi NFYREQH.
OrthoDBi EOG7DZ8KD.
PhylomeDBi Q9UGB7.
TreeFami TF300089.

Enzyme and pathway databases

UniPathwayi UPA00111 ; UER00527 .
BRENDAi 1.13.99.1. 2681.
SABIO-RK Q9UGB7.

Miscellaneous databases

ChiTaRSi MIOX. human.
EvolutionaryTracei Q9UGB7.
GenomeRNAii 55586.
NextBioi 60104.
PROi Q9UGB7.
SOURCEi Search...

Gene expression databases

Bgeei Q9UGB7.
CleanExi HS_MIOX.
Genevestigatori Q9UGB7.

Family and domain databases

InterProi IPR007828. Inositol_oxygenase.
[Graphical view ]
PANTHERi PTHR12588. PTHR12588. 1 hit.
Pfami PF05153. DUF706. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of human myo-inositol oxygenase (MIOX)."
    Parthasarathy L., Seelan R., Parthasarathy R.
    Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Identification of a novel kidney specific gene, KSP32, that is down regulated in acute ischemic renal failure."
    Hu E., Chen Z., Fredrickson T., Gellai M., Jugus M., Contino L., Spurr N., Sims M., Halsey W., Van Horn S., Mao J., Sathe G., Brooks D.
    Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Kidney.
  3. "Identification of a renal-specific oxido-reductase in newborn diabetic mice."
    Yang Q., Dixit B., Wada J., Tian Y., Wallner E.I., Srivastva S.K., Kanwar Y.S.
    Proc. Natl. Acad. Sci. U.S.A. 97:9896-9901(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Kidney.
  4. "Molecular cloning, expression, and characterization of myo-inositol oxygenase from mouse, rat, and human kidney."
    Arner R.J., Prabhu K.S., Reddy C.C.
    Biochem. Biophys. Res. Commun. 324:1386-1392(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Kidney.
  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 1).
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  7. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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] (ISOFORMS 1 AND 2).
    Tissue: Colon and Kidney.
  10. Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 38-285 IN COMPLEX WITH IRON AND MYO-INOSOSE-1, CATALYTIC ACTIVITY, COFACTOR, MUTAGENESIS OF LYS-127.

Entry informationi

Entry nameiMIOX_HUMAN
AccessioniPrimary (citable) accession number: Q9UGB7
Secondary accession number(s): Q05DJ6
, Q5S8C9, Q9BZZ1, Q9UHB8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 12, 2003
Last sequence update: May 1, 2000
Last modified: September 3, 2014
This is version 114 of the entry and version 1 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 22
    Human chromosome 22: 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

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