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Q9UBQ7

- GRHPR_HUMAN

UniProt

Q9UBQ7 - GRHPR_HUMAN

Protein

Glyoxylate reductase/hydroxypyruvate reductase

Gene

GRHPR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Enzyme with hydroxy-pyruvate reductase, glyoxylate reductase and D-glycerate dehydrogenase enzymatic activities. Reduces hydroxypyruvate to D-glycerate, glyoxylate to glycolate oxidizes D-glycerate to hydroxypyruvate.

    Catalytic activityi

    Glycolate + NADP+ = glyoxylate + NADPH.
    D-glycerate + NAD(P)+ = hydroxypyruvate + NAD(P)H.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei217 – 2171NADP1 Publication
    Binding sitei243 – 2431NADP; via carbonyl oxygen1 Publication
    Binding sitei245 – 2451Substrate1 Publication
    Binding sitei269 – 2691Substrate1 Publication
    Sitei274 – 2741Raises pKa of active site His
    Active sitei293 – 2931Proton donor
    Binding sitei295 – 2951NADP; via amide nitrogen1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi162 – 1643NADP1 Publication
    Nucleotide bindingi185 – 1884NADP1 Publication

    GO - Molecular functioni

    1. carboxylic acid binding Source: Ensembl
    2. glycerate dehydrogenase activity Source: UniProtKB
    3. glyoxylate reductase (NADP) activity Source: UniProtKB
    4. hydroxypyruvate reductase activity Source: UniProtKB
    5. NAD binding Source: UniProtKB
    6. NADPH binding Source: UniProtKB
    7. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. cellular nitrogen compound metabolic process Source: Reactome
    2. dicarboxylic acid metabolic process Source: Ensembl
    3. excretion Source: UniProtKB
    4. glyoxylate metabolic process Source: Reactome
    5. metabolic process Source: UniProtKB
    6. oxidation-reduction process Source: UniProtKB
    7. protein oligomerization Source: UniProtKB
    8. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    ReactomeiREACT_16925. Glyoxylate metabolism.
    SABIO-RKQ9UBQ7.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glyoxylate reductase/hydroxypyruvate reductase (EC:1.1.1.79, EC:1.1.1.81)
    Gene namesi
    Name:GRHPR
    Synonyms:GLXR
    ORF Names:MSTP035
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:4570. GRHPR.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: LIFEdb
    2. cytosol Source: Ensembl
    3. extracellular vesicular exosome Source: UniProt
    4. peroxisomal matrix Source: Reactome

    Pathology & Biotechi

    Involvement in diseasei

    Hyperoxaluria primary 2 (HP2) [MIM:260000]: A disorder characterized by elevated urinary excretion of oxalate and L-glycerate, progressive tissue accumulation of insoluble calcium oxalate, nephrolithiasis, nephrocalcinosis, and end-stage renal disease.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Organism-specific databases

    MIMi260000. phenotype.
    Orphaneti93599. Primary hyperoxaluria type 2.
    PharmGKBiPA28965.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 328328Glyoxylate reductase/hydroxypyruvate reductasePRO_0000075944Add
    BLAST

    Proteomic databases

    MaxQBiQ9UBQ7.
    PaxDbiQ9UBQ7.
    PRIDEiQ9UBQ7.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00037448.
    UCD-2DPAGEQ9UBQ7.

    PTM databases

    PhosphoSiteiQ9UBQ7.

    Expressioni

    Tissue specificityi

    Ubiquitous. Most abundantly expressed in the liver.1 Publication

    Gene expression databases

    ArrayExpressiQ9UBQ7.
    BgeeiQ9UBQ7.
    CleanExiHS_GRHPR.
    GenevestigatoriQ9UBQ7.

    Organism-specific databases

    HPAiHPA022971.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    BioGridi114781. 14 interactions.
    IntActiQ9UBQ7. 5 interactions.
    MINTiMINT-5005010.
    STRINGi9606.ENSP00000313432.

    Structurei

    Secondary structure

    1
    328
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 137
    Helixi17 – 259
    Beta strandi29 – 335
    Beta strandi36 – 383
    Helixi42 – 498
    Beta strandi53 – 575
    Helixi65 – 717
    Beta strandi77 – 837
    Helixi90 – 956
    Beta strandi99 – 1013
    Helixi108 – 12316
    Helixi126 – 1349
    Beta strandi143 – 1464
    Beta strandi155 – 1595
    Helixi163 – 17210
    Helixi173 – 1753
    Beta strandi179 – 1868
    Helixi189 – 1935
    Turni194 – 1963
    Beta strandi197 – 1993
    Helixi202 – 2087
    Beta strandi210 – 2145
    Turni220 – 2245
    Helixi228 – 2336
    Beta strandi239 – 2424
    Helixi246 – 2483
    Helixi251 – 2599
    Beta strandi262 – 2698
    Beta strandi272 – 2754
    Helixi281 – 2844
    Beta strandi288 – 2903
    Helixi299 – 31820

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2GCGX-ray2.20A/B/C/D1-328[»]
    2H1SX-ray2.45A/B/C/D2-328[»]
    2Q50X-ray2.45A/B/C/D2-328[»]
    2WWRX-ray2.82A/B/C/D1-328[»]
    ProteinModelPortaliQ9UBQ7.
    SMRiQ9UBQ7. Positions 5-328.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UBQ7.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni83 – 842Substrate binding
    Regioni293 – 2964Substrate binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1052.
    HOVERGENiHBG051838.
    KOiK00049.
    OMAiHRTRNTM.
    PhylomeDBiQ9UBQ7.
    TreeFamiTF324791.

    Family and domain databases

    Gene3Di3.40.50.720. 2 hits.
    InterProiIPR006139. D-isomer_2_OHA_DH_cat_dom.
    IPR006140. D-isomer_DH_NAD-bd.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF00389. 2-Hacid_dh. 1 hit.
    PF02826. 2-Hacid_dh_C. 1 hit.
    [Graphical view]
    PROSITEiPS00671. D_2_HYDROXYACID_DH_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9UBQ7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRPVRLMKVF VTRRIPAEGR VALARAADCE VEQWDSDEPI PAKELERGVA    50
    GAHGLLCLLS DHVDKRILDA AGANLKVIST MSVGIDHLAL DEIKKRGIRV 100
    GYTPDVLTDT TAELAVSLLL TTCRRLPEAI EEVKNGGWTS WKPLWLCGYG 150
    LTQSTVGIIG LGRIGQAIAR RLKPFGVQRF LYTGRQPRPE EAAEFQAEFV 200
    STPELAAQSD FIVVACSLTP ATEGLCNKDF FQKMKETAVF INISRGDVVN 250
    QDDLYQALAS GKIAAAGLDV TSPEPLPTNH PLLTLKNCVI LPHIGSATHR 300
    TRNTMSLLAA NNLLAGLRGE PMPSELKL 328
    Length:328
    Mass (Da):35,668
    Last modified:May 1, 2000 - v1
    Checksum:i68A0E311AA4E5650
    GO

    Sequence cautioni

    The sequence AAD54066.1 differs from that shown. Reason: Frameshift at positions 109 and 137.
    The sequence AAG39286.1 differs from that shown. Reason: Frameshift at position 237.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti170 – 1701R → Q.
    Corresponds to variant rs12002324 [ dbSNP | Ensembl ].
    VAR_032762

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF134895 mRNA. Translation: AAF00111.1.
    AF146018 mRNA. Translation: AAD45886.1.
    AF146689 Genomic DNA. Translation: AAD46517.1.
    AF113215 mRNA. Translation: AAG39286.1. Frameshift.
    AK315690 mRNA. Translation: BAG38053.1.
    AL158155 Genomic DNA. Translation: CAI13848.1.
    CH471071 Genomic DNA. Translation: EAW58284.1.
    BC000605 mRNA. Translation: AAH00605.1.
    AF113251 mRNA. Translation: AAD54066.1. Frameshift.
    CCDSiCCDS6609.1.
    PIRiJC7190.
    RefSeqiNP_036335.1. NM_012203.1.
    UniGeneiHs.155742.

    Genome annotation databases

    EnsembliENST00000318158; ENSP00000313432; ENSG00000137106.
    GeneIDi9380.
    KEGGihsa:9380.
    UCSCiuc003zzt.1. human.

    Polymorphism databases

    DMDMi47116943.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF134895 mRNA. Translation: AAF00111.1 .
    AF146018 mRNA. Translation: AAD45886.1 .
    AF146689 Genomic DNA. Translation: AAD46517.1 .
    AF113215 mRNA. Translation: AAG39286.1 . Frameshift.
    AK315690 mRNA. Translation: BAG38053.1 .
    AL158155 Genomic DNA. Translation: CAI13848.1 .
    CH471071 Genomic DNA. Translation: EAW58284.1 .
    BC000605 mRNA. Translation: AAH00605.1 .
    AF113251 mRNA. Translation: AAD54066.1 . Frameshift.
    CCDSi CCDS6609.1.
    PIRi JC7190.
    RefSeqi NP_036335.1. NM_012203.1.
    UniGenei Hs.155742.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2GCG X-ray 2.20 A/B/C/D 1-328 [» ]
    2H1S X-ray 2.45 A/B/C/D 2-328 [» ]
    2Q50 X-ray 2.45 A/B/C/D 2-328 [» ]
    2WWR X-ray 2.82 A/B/C/D 1-328 [» ]
    ProteinModelPortali Q9UBQ7.
    SMRi Q9UBQ7. Positions 5-328.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114781. 14 interactions.
    IntActi Q9UBQ7. 5 interactions.
    MINTi MINT-5005010.
    STRINGi 9606.ENSP00000313432.

    PTM databases

    PhosphoSitei Q9UBQ7.

    Polymorphism databases

    DMDMi 47116943.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00037448.
    UCD-2DPAGE Q9UBQ7.

    Proteomic databases

    MaxQBi Q9UBQ7.
    PaxDbi Q9UBQ7.
    PRIDEi Q9UBQ7.

    Protocols and materials databases

    DNASUi 9380.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000318158 ; ENSP00000313432 ; ENSG00000137106 .
    GeneIDi 9380.
    KEGGi hsa:9380.
    UCSCi uc003zzt.1. human.

    Organism-specific databases

    CTDi 9380.
    GeneCardsi GC09P037412.
    GeneReviewsi GRHPR.
    HGNCi HGNC:4570. GRHPR.
    HPAi HPA022971.
    MIMi 260000. phenotype.
    604296. gene.
    neXtProti NX_Q9UBQ7.
    Orphaneti 93599. Primary hyperoxaluria type 2.
    PharmGKBi PA28965.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1052.
    HOVERGENi HBG051838.
    KOi K00049.
    OMAi HRTRNTM.
    PhylomeDBi Q9UBQ7.
    TreeFami TF324791.

    Enzyme and pathway databases

    Reactomei REACT_16925. Glyoxylate metabolism.
    SABIO-RK Q9UBQ7.

    Miscellaneous databases

    ChiTaRSi GRHPR. human.
    EvolutionaryTracei Q9UBQ7.
    GeneWikii GRHPR.
    GenomeRNAii 9380.
    NextBioi 35148.
    PROi Q9UBQ7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UBQ7.
    Bgeei Q9UBQ7.
    CleanExi HS_GRHPR.
    Genevestigatori Q9UBQ7.

    Family and domain databases

    Gene3Di 3.40.50.720. 2 hits.
    InterProi IPR006139. D-isomer_2_OHA_DH_cat_dom.
    IPR006140. D-isomer_DH_NAD-bd.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    Pfami PF00389. 2-Hacid_dh. 1 hit.
    PF02826. 2-Hacid_dh_C. 1 hit.
    [Graphical view ]
    PROSITEi PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification and expression of a cDNA for human hydroxypyruvate/glyoxylate reductase."
      Rumsby G., Cregeen D.P.
      Biochim. Biophys. Acta 1446:383-388(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT.
      Tissue: Liver.
    2. "The gene encoding hydroxypyruvate reductase (GRHPR) is mutated in patients with primary hyperoxaluria type II."
      Cramer S.D., Ferree P.M., Lin K., Milliner D.S., Holmes R.P.
      Hum. Mol. Genet. 8:2063-2069(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], INVOLVEMENT IN HP2.
      Tissue: Liver.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Aorta.
    4. "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].
      Tissue: Testis.
    5. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Kidney.
    8. "Cloning and characterization of a putative human D-2-hydroxyacid dehydrogenase in chromosome 9q."
      Huang T., Yang W., Pereira A.C., Craigen W.J., Shih V.E.
      Biochem. Biophys. Res. Commun. 268:298-301(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 45-328, TISSUE SPECIFICITY.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Structural basis of substrate specificity in human glyoxylate reductase/hydroxypyruvate reductase."
      Booth M.P.S., Conners R., Rumsby G., Brady R.L.
      J. Mol. Biol. 360:178-189(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH NADP AND SUBSTRATE, SUBUNIT.
    11. "Crystal structure of a glyoxylate/hydroxypyruvate reductase from Homo sapiens."
      Center for eukaryotic structural genomics (CESG)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 2-328.

    Entry informationi

    Entry nameiGRHPR_HUMAN
    AccessioniPrimary (citable) accession number: Q9UBQ7
    Secondary accession number(s): Q5T945, Q9H3E9, Q9UKX1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 10, 2004
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 133 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 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3