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Q9Y2T3 (GUAD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Guanine deaminase

Short name=Guanase
Short name=Guanine aminase
EC=3.5.4.3
Alternative name(s):
Guanine aminohydrolase
Short name=GAH
p51-nedasin
Gene names
Name:GDA
Synonyms:KIAA1258
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length454 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

Guanine + H2O = xanthine + NH3.

Cofactor

Binds 1 zinc ion per subunit.

Pathway

Purine metabolism; guanine degradation; xanthine from guanine: step 1/1.

Subunit structure

Homodimer.

Sequence similarities

Belongs to the ATZ/TRZ family.

Sequence caution

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

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y2T3-1)

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.
Isoform 2 (identifier: Q9Y2T3-2)

Also known as: c;

The sequence of this isoform differs from the canonical sequence as follows:
     1-74: Missing.
Isoform 3 (identifier: Q9Y2T3-3)

Also known as: a;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 454454Guanine deaminase
PRO_0000122298

Sites

Metal binding821Zinc; via tele nitrogen
Metal binding841Zinc; via tele nitrogen
Metal binding2401Zinc; via tele nitrogen
Metal binding3301Zinc By similarity
Binding site871Substrate
Binding site2131Substrate
Binding site2431Substrate
Binding site2791Substrate

Natural variations

Alternative sequence1 – 7474Missing in isoform 2.
VSP_042075
Alternative sequence4541V → VKETIHLPASSPHPPPFP in isoform 3.
VSP_042076

Experimental info

Sequence conflict316 – 3183LEV → ARI in AAG40469. Ref.3

Secondary structure

....................................................................................... 454
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: A45C868E6EEA7380

FASTA45451,003
        10         20         30         40         50         60 
MCAAQMPPLA HIFRGTFVHS TWTCPMEVLR DHLLGVSDSG KIVFLEEASQ QEKLAKEWCF 

        70         80         90        100        110        120 
KPCEIRELSH HEFFMPGLVD THIHASQYSF AGSSIDLPLL EWLTKYTFPA EHRFQNIDFA 

       130        140        150        160        170        180 
EEVYTRVVRR TLKNGTTTAC YFATIHTDSS LLLADITDKF GQRAFVGKVC MDLNDTFPEY 

       190        200        210        220        230        240 
KETTEESIKE TERFVSEMLQ KNYSRVKPIV TPRFSLSCSE TLMGELGNIA KTRDLHIQSH 

       250        260        270        280        290        300 
ISENRDEVEA VKNLYPSYKN YTSVYDKNNL LTNKTVMAHG CYLSAEELNV FHERGASIAH 

       310        320        330        340        350        360 
CPNSNLSLSS GFLNVLEVLK HEVKIGLGTD VAGGYSYSML DAIRRAVMVS NILLINKVNE 

       370        380        390        400        410        420 
KSLTLKEVFR LATLGGSQAL GLDGEIGNFE VGKEFDAILI NPKASDSPID LFYGDFFGDI 

       430        440        450 
SEAVIQKFLY LGDDRNIEEV YVGGKQVVPF SSSV 

« Hide

Isoform 2 (c) [UniParc].

Checksum: 6AD0F99117A467CE
Show »

FASTA38042,445
Isoform 3 (a) [UniParc].

Checksum: 5B9BF9B0E1111F88
Show »

FASTA47152,837

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS56576.1. [Q9Y2T3-3]
CCDS56577.1. [Q9Y2T3-2]
CCDS6641.1. [Q9Y2T3-1]
RefSeqNP_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]
UniGeneHs.494163.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2UZ9X-ray2.30A1-454[»]
3E0LX-ray2.37A/B1-454[»]
4AQLX-ray1.99A1-454[»]
ProteinModelPortalQ9Y2T3.
SMRQ9Y2T3. Positions 8-451.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114976. 20 interactions.
MINTMINT-109340.
STRING9606.ENSP00000351170.

Chemistry

BindingDBQ9Y2T3.
ChEMBLCHEMBL3129.

Protein family/group databases

MEROPSM38.981.

PTM databases

PhosphoSiteQ9Y2T3.

Polymorphism databases

DMDM9910736.

Proteomic databases

MaxQBQ9Y2T3.
PaxDbQ9Y2T3.
PRIDEQ9Y2T3.

Protocols and materials databases

DNASU9615.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000238018; ENSP00000238018; ENSG00000119125. [Q9Y2T3-3]
ENST00000358399; ENSP00000351170; ENSG00000119125. [Q9Y2T3-1]
ENST00000475764; ENSP00000436619; ENSG00000119125. [Q9Y2T3-1]
ENST00000545168; ENSP00000437972; ENSG00000119125. [Q9Y2T3-2]
GeneID9615.
KEGGhsa:9615.
UCSCuc004aiq.3. human. [Q9Y2T3-1]
uc004air.3. human. [Q9Y2T3-3]

Organism-specific databases

CTD9615.
GeneCardsGC09P074729.
HGNCHGNC:4212. GDA.
HPAHPA019352.
HPA024099.
HPA030387.
MIM139260. gene.
neXtProtNX_Q9Y2T3.
PharmGKBPA28625.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0402.
HOGENOMHOG000257692.
HOVERGENHBG005930.
InParanoidQ9Y2T3.
KOK01487.
OMAMSYDETR.
PhylomeDBQ9Y2T3.
TreeFamTF324539.

Enzyme and pathway databases

BioCycMetaCyc:HS04276-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKQ9Y2T3.
UniPathwayUPA00603; UER00660.

Gene expression databases

ArrayExpressQ9Y2T3.
BgeeQ9Y2T3.
CleanExHS_GDA.
GenevestigatorQ9Y2T3.

Family and domain databases

InterProIPR006680. Amidohydro_1.
IPR014311. Guanine_deaminase.
[Graphical view]
PANTHERPTHR11271:SF6. PTHR11271:SF6. 1 hit.
PfamPF01979. Amidohydro_1. 1 hit.
[Graphical view]
TIGRFAMsTIGR02967. guan_deamin. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9Y2T3.
GenomeRNAi9615.
NextBio36069.
PROQ9Y2T3.
SOURCESearch...

Entry information

Entry nameGUAD_HUMAN
AccessionPrimary (citable) accession number: Q9Y2T3
Secondary accession number(s): B4DTY5 expand/collapse secondary AC list , Q5SZC7, Q9H335, Q9ULG2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM