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Q9Y2T3

- GUAD_HUMAN

UniProt

Q9Y2T3 - GUAD_HUMAN

Protein

Guanine deaminase

Gene

GDA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    Functioni

    Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia.By similarity

    Catalytic activityi

    Guanine + H2O = xanthine + NH3.

    Cofactori

    Binds 1 zinc ion per subunit.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi82 – 821Zinc; via tele nitrogen
    Metal bindingi84 – 841Zinc; via tele nitrogen
    Binding sitei87 – 871Substrate
    Binding sitei213 – 2131Substrate
    Metal bindingi240 – 2401Zinc; via tele nitrogen
    Binding sitei243 – 2431Substrate
    Binding sitei279 – 2791Substrate
    Metal bindingi330 – 3301ZincBy similarity

    GO - Molecular functioni

    1. guanine deaminase activity Source: Reactome
    2. zinc ion binding Source: ProtInc

    GO - Biological processi

    1. guanine catabolic process Source: UniProtKB-UniPathway
    2. nervous system development Source: ProtInc
    3. nucleobase-containing compound metabolic process Source: ProtInc
    4. nucleobase-containing small molecule metabolic process Source: Reactome
    5. purine nucleobase metabolic process Source: Reactome
    6. purine nucleotide catabolic process Source: Reactome
    7. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciMetaCyc:HS04276-MONOMER.
    ReactomeiREACT_2086. Purine catabolism.
    SABIO-RKQ9Y2T3.
    UniPathwayiUPA00603; UER00660.

    Protein family/group databases

    MEROPSiM38.981.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Guanine deaminase (EC:3.5.4.3)
    Short name:
    Guanase
    Short name:
    Guanine aminase
    Alternative name(s):
    Guanine aminohydrolase
    Short name:
    GAH
    p51-nedasin
    Gene namesi
    Name:GDA
    Synonyms:KIAA1258
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:4212. GDA.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt
    3. intracellular Source: ProtInc

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28625.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 454454Guanine deaminasePRO_0000122298Add
    BLAST

    Proteomic databases

    MaxQBiQ9Y2T3.
    PaxDbiQ9Y2T3.
    PRIDEiQ9Y2T3.

    PTM databases

    PhosphoSiteiQ9Y2T3.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9Y2T3.
    BgeeiQ9Y2T3.
    CleanExiHS_GDA.
    GenevestigatoriQ9Y2T3.

    Organism-specific databases

    HPAiHPA019352.
    HPA024099.
    HPA030387.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi114976. 20 interactions.
    MINTiMINT-109340.
    STRINGi9606.ENSP00000351170.

    Structurei

    Secondary structure

    1
    454
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi11 – 199
    Beta strandi27 – 3610
    Beta strandi40 – 478
    Helixi48 – 503
    Helixi51 – 577
    Helixi62 – 643
    Beta strandi65 – 673
    Beta strandi73 – 764
    Beta strandi78 – 847
    Helixi85 – 906
    Helixi99 – 1057
    Helixi107 – 1126
    Helixi113 – 1153
    Helixi117 – 13317
    Beta strandi136 – 1427
    Helixi147 – 16014
    Beta strandi163 – 1675
    Beta strandi175 – 1773
    Helixi184 – 20118
    Beta strandi204 – 2085
    Beta strandi210 – 2123
    Turni215 – 2173
    Helixi220 – 23213
    Beta strandi237 – 2426
    Helixi245 – 25410
    Beta strandi258 – 2603
    Helixi261 – 2666
    Turni267 – 2693
    Beta strandi275 – 2795
    Helixi285 – 29410
    Beta strandi297 – 3004
    Helixi302 – 3076
    Helixi315 – 3206
    Beta strandi324 – 3274
    Turni331 – 3333
    Helixi339 – 35517
    Beta strandi358 – 3614
    Helixi365 – 3728
    Helixi374 – 3796
    Turni383 – 3853
    Beta strandi386 – 3883
    Beta strandi397 – 4004
    Helixi414 – 4174
    Beta strandi418 – 4203
    Helixi423 – 4319
    Helixi434 – 4363
    Beta strandi437 – 4426
    Beta strandi445 – 4484

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2UZ9X-ray2.30A1-454[»]
    3E0LX-ray2.37A/B1-454[»]
    4AQLX-ray1.99A1-454[»]
    ProteinModelPortaliQ9Y2T3.
    SMRiQ9Y2T3. Positions 8-451.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y2T3.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ATZ/TRZ family.Curated

    Phylogenomic databases

    eggNOGiCOG0402.
    HOGENOMiHOG000257692.
    HOVERGENiHBG005930.
    InParanoidiQ9Y2T3.
    KOiK01487.
    OMAiMSYDETR.
    PhylomeDBiQ9Y2T3.
    TreeFamiTF324539.

    Family and domain databases

    InterProiIPR006680. Amidohydro_1.
    IPR014311. Guanine_deaminase.
    [Graphical view]
    PANTHERiPTHR11271:SF6. PTHR11271:SF6. 1 hit.
    PfamiPF01979. Amidohydro_1. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR02967. guan_deamin. 1 hit.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Y2T3-1) [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

    MCAAQMPPLA HIFRGTFVHS TWTCPMEVLR DHLLGVSDSG KIVFLEEASQ    50
    QEKLAKEWCF KPCEIRELSH HEFFMPGLVD THIHASQYSF AGSSIDLPLL 100
    EWLTKYTFPA EHRFQNIDFA EEVYTRVVRR TLKNGTTTAC YFATIHTDSS 150
    LLLADITDKF GQRAFVGKVC MDLNDTFPEY KETTEESIKE TERFVSEMLQ 200
    KNYSRVKPIV TPRFSLSCSE TLMGELGNIA KTRDLHIQSH ISENRDEVEA 250
    VKNLYPSYKN YTSVYDKNNL LTNKTVMAHG CYLSAEELNV FHERGASIAH 300
    CPNSNLSLSS GFLNVLEVLK HEVKIGLGTD VAGGYSYSML DAIRRAVMVS 350
    NILLINKVNE KSLTLKEVFR LATLGGSQAL GLDGEIGNFE VGKEFDAILI 400
    NPKASDSPID LFYGDFFGDI SEAVIQKFLY LGDDRNIEEV YVGGKQVVPF 450
    SSSV 454
    Length:454
    Mass (Da):51,003
    Last modified:November 1, 1999 - v1
    Checksum:iA45C868E6EEA7380
    GO
    Isoform 2 (identifier: Q9Y2T3-2) [UniParc]FASTAAdd to Basket

    Also known as: c

    The sequence of this isoform differs from the canonical sequence as follows:
         1-74: Missing.

    Show »
    Length:380
    Mass (Da):42,445
    Checksum:i6AD0F99117A467CE
    GO
    Isoform 3 (identifier: Q9Y2T3-3) [UniParc]FASTAAdd to Basket

    Also known as: a

    The sequence of this isoform differs from the canonical sequence as follows:
         454-454: V → VKETIHLPASSPHPPPFP

    Show »
    Length:471
    Mass (Da):52,837
    Checksum:i5B9BF9B0E1111F88
    GO

    Sequence cautioni

    The sequence BAA86572.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti316 – 3183LEV → ARI in AAG40469. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7474Missing in isoform 2. 2 PublicationsVSP_042075Add
    BLAST
    Alternative sequencei454 – 4541V → VKETIHLPASSPHPPPFP in isoform 3. 1 PublicationVSP_042076

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF095286 mRNA. Translation: AAD25978.1.
    AF019638 mRNA. Translation: AAF13301.1.
    AF144745 mRNA. Translation: AAG40469.1.
    AB033084 mRNA. Translation: BAA86572.1. Different initiation.
    AK300418 mRNA. Translation: BAG62147.1.
    AK315988 mRNA. Translation: BAH14359.1.
    AL583829 Genomic DNA. No translation available.
    AL590311, AL135924 Genomic DNA. Translation: CAI12631.1.
    AL135924, AL590311 Genomic DNA. Translation: CAI16261.1.
    CH471089 Genomic DNA. Translation: EAW62529.1.
    BC053584 mRNA. Translation: AAH53584.1.
    CCDSiCCDS56576.1. [Q9Y2T3-3]
    CCDS56577.1. [Q9Y2T3-2]
    CCDS6641.1. [Q9Y2T3-1]
    RefSeqiNP_001229434.1. NM_001242505.2. [Q9Y2T3-3]
    NP_001229435.1. NM_001242506.2. [Q9Y2T3-2]
    NP_001229436.1. NM_001242507.2. [Q9Y2T3-2]
    NP_004284.1. NM_004293.4. [Q9Y2T3-1]
    XP_005252374.1. XM_005252317.1. [Q9Y2T3-3]
    XP_006717389.1. XM_006717326.1. [Q9Y2T3-3]
    UniGeneiHs.494163.

    Genome annotation databases

    EnsembliENST00000238018; ENSP00000238018; ENSG00000119125. [Q9Y2T3-3]
    ENST00000358399; ENSP00000351170; ENSG00000119125. [Q9Y2T3-1]
    ENST00000475764; ENSP00000436619; ENSG00000119125. [Q9Y2T3-1]
    ENST00000545168; ENSP00000437972; ENSG00000119125. [Q9Y2T3-2]
    GeneIDi9615.
    KEGGihsa:9615.
    UCSCiuc004aiq.3. human. [Q9Y2T3-1]
    uc004air.3. human. [Q9Y2T3-3]

    Polymorphism databases

    DMDMi9910736.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF095286 mRNA. Translation: AAD25978.1 .
    AF019638 mRNA. Translation: AAF13301.1 .
    AF144745 mRNA. Translation: AAG40469.1 .
    AB033084 mRNA. Translation: BAA86572.1 . Different initiation.
    AK300418 mRNA. Translation: BAG62147.1 .
    AK315988 mRNA. Translation: BAH14359.1 .
    AL583829 Genomic DNA. No translation available.
    AL590311 , AL135924 Genomic DNA. Translation: CAI12631.1 .
    AL135924 , AL590311 Genomic DNA. Translation: CAI16261.1 .
    CH471089 Genomic DNA. Translation: EAW62529.1 .
    BC053584 mRNA. Translation: AAH53584.1 .
    CCDSi CCDS56576.1. [Q9Y2T3-3 ]
    CCDS56577.1. [Q9Y2T3-2 ]
    CCDS6641.1. [Q9Y2T3-1 ]
    RefSeqi NP_001229434.1. NM_001242505.2. [Q9Y2T3-3 ]
    NP_001229435.1. NM_001242506.2. [Q9Y2T3-2 ]
    NP_001229436.1. NM_001242507.2. [Q9Y2T3-2 ]
    NP_004284.1. NM_004293.4. [Q9Y2T3-1 ]
    XP_005252374.1. XM_005252317.1. [Q9Y2T3-3 ]
    XP_006717389.1. XM_006717326.1. [Q9Y2T3-3 ]
    UniGenei Hs.494163.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2UZ9 X-ray 2.30 A 1-454 [» ]
    3E0L X-ray 2.37 A/B 1-454 [» ]
    4AQL X-ray 1.99 A 1-454 [» ]
    ProteinModelPortali Q9Y2T3.
    SMRi Q9Y2T3. Positions 8-451.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114976. 20 interactions.
    MINTi MINT-109340.
    STRINGi 9606.ENSP00000351170.

    Chemistry

    BindingDBi Q9Y2T3.
    ChEMBLi CHEMBL3129.

    Protein family/group databases

    MEROPSi M38.981.

    PTM databases

    PhosphoSitei Q9Y2T3.

    Polymorphism databases

    DMDMi 9910736.

    Proteomic databases

    MaxQBi Q9Y2T3.
    PaxDbi Q9Y2T3.
    PRIDEi Q9Y2T3.

    Protocols and materials databases

    DNASUi 9615.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000238018 ; ENSP00000238018 ; ENSG00000119125 . [Q9Y2T3-3 ]
    ENST00000358399 ; ENSP00000351170 ; ENSG00000119125 . [Q9Y2T3-1 ]
    ENST00000475764 ; ENSP00000436619 ; ENSG00000119125 . [Q9Y2T3-1 ]
    ENST00000545168 ; ENSP00000437972 ; ENSG00000119125 . [Q9Y2T3-2 ]
    GeneIDi 9615.
    KEGGi hsa:9615.
    UCSCi uc004aiq.3. human. [Q9Y2T3-1 ]
    uc004air.3. human. [Q9Y2T3-3 ]

    Organism-specific databases

    CTDi 9615.
    GeneCardsi GC09P074729.
    HGNCi HGNC:4212. GDA.
    HPAi HPA019352.
    HPA024099.
    HPA030387.
    MIMi 139260. gene.
    neXtProti NX_Q9Y2T3.
    PharmGKBi PA28625.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0402.
    HOGENOMi HOG000257692.
    HOVERGENi HBG005930.
    InParanoidi Q9Y2T3.
    KOi K01487.
    OMAi MSYDETR.
    PhylomeDBi Q9Y2T3.
    TreeFami TF324539.

    Enzyme and pathway databases

    UniPathwayi UPA00603 ; UER00660 .
    BioCyci MetaCyc:HS04276-MONOMER.
    Reactomei REACT_2086. Purine catabolism.
    SABIO-RK Q9Y2T3.

    Miscellaneous databases

    EvolutionaryTracei Q9Y2T3.
    GenomeRNAii 9615.
    NextBioi 36069.
    PROi Q9Y2T3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y2T3.
    Bgeei Q9Y2T3.
    CleanExi HS_GDA.
    Genevestigatori Q9Y2T3.

    Family and domain databases

    InterProi IPR006680. Amidohydro_1.
    IPR014311. Guanine_deaminase.
    [Graphical view ]
    PANTHERi PTHR11271:SF6. PTHR11271:SF6. 1 hit.
    Pfami PF01979. Amidohydro_1. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR02967. guan_deamin. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of human guanine deaminase. Purification and partial amino acid sequence of the mouse protein."
      Yuan G., Bin J.C., McKay D.J., Snyder F.F.
      J. Biol. Chem. 274:8175-8180(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION.
      Tissue: Brain.
    2. "A novel NE-dlg/SAP102-associated protein, p51-nedasin, related to the amidohydrolase superfamily, interferes with the association between NE-dlg/SAP102 and N-methyl-D-aspartate receptor."
      Kuwahara H., Araki N., Makino K., Masuko N., Honda S., Kaibuchi K., Fukunaga K., Miyamoto E., Ogawa M., Saya H.
      J. Biol. Chem. 274:32204-32214(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Brain.
    3. "Molecular cloning of human guanine aminohydrolase."
      Park K.H., Seong Y.S., Park J.B.
      Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    4. "Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.
      DNA Res. 6:337-345(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    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).
    6. "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].
    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).
      Tissue: Colon.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Human guanine deaminase (GUAD) in complex with zinc and its product xanthine."
      Structural genomics consortium (SGC)
      Submitted (JAN-2008) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND XANTHINE.

    Entry informationi

    Entry nameiGUAD_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y2T3
    Secondary accession number(s): B4DTY5
    , Q5SZC7, Q9H335, Q9ULG2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 126 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. 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