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Q9UGB7

- MIOX_HUMAN

UniProt

Q9UGB7 - MIOX_HUMAN

Protein

Inositol oxygenase

Gene

MIOX

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    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 – 291SubstrateBy similarity
    Metal bindingi98 – 981Iron 11 Publication
    Metal bindingi123 – 1231Iron 11 Publication
    Metal bindingi124 – 1241Iron 11 Publication
    Metal bindingi124 – 1241Iron 21 Publication
    Binding sitei127 – 1271Substrate
    Metal bindingi194 – 1941Iron 21 Publication
    Metal bindingi220 – 2201Iron 21 Publication
    Metal bindingi253 – 2531Iron 11 Publication

    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

    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

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UGB7.

    Family & Domainsi

    Region

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

    Sequence similaritiesi

    Belongs to the myo-inositol oxygenase family.Curated

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti4 – 41T → D in AAF25204. (PubMed:10944187)Curated
    Sequence conflicti199 – 1991Y → F in AAK00766. 1 PublicationCurated
    Sequence conflicti219 – 2213FHS → VHF in AAK00766. 1 PublicationCurated
    Sequence conflicti282 – 2821I → T in AAF25204. (PubMed:10944187)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei114 – 231118DWFHL…TGRDY → VPNLPCPSPSQTGSTSSGSC TTWGRSWPCSGSPSGLSSAT PSPSDAVRRPPWFSATPPSR TTLTSRILDTAQSSGCISPT VGSTGSSCPGAMMQVRPLHQ VPGPAGRGQAAALLPGAH in isoform 2. 1 PublicationVSP_041667Add
    BLAST
    Alternative sequencei232 – 28554Missing in isoform 2. 1 PublicationVSP_041668Add
    BLAST

    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

    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: October 1, 2014
    This is version 115 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