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Q9Y2T3

- GUAD_HUMAN

UniProt

Q9Y2T3 - GUAD_HUMAN

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Protein
Guanine deaminase
Gene
GDA, KIAA1258
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 3301Zinc By similarity

GO - Molecular functioni

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

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
Complete GO annotation...

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
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28625.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 454454Guanine deaminase
PRO_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.

Protein-protein interaction databases

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

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiQ9Y2T3.

Family & Domainsi

Sequence similaritiesi

Belongs to the ATZ/TRZ family.

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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7474Missing in isoform 2.
VSP_042075Add
BLAST
Alternative sequencei454 – 4541V → VKETIHLPASSPHPPPFP in isoform 3.
VSP_042076

Sequence conflict

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

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...

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 125 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

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