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Protein

Guanine deaminase

Gene

GDA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

Zn2+Note: 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
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: UniProtKB
  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 deaminasePRO_0000122298Add
BLAST

Proteomic databases

MaxQBiQ9Y2T3.
PaxDbiQ9Y2T3.
PRIDEiQ9Y2T3.

PTM databases

PhosphoSiteiQ9Y2T3.

Expressioni

Gene expression databases

BgeeiQ9Y2T3.
CleanExiHS_GDA.
ExpressionAtlasiQ9Y2T3. baseline and differential.
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 – 199Combined sources
Beta strandi27 – 3610Combined sources
Beta strandi40 – 478Combined sources
Helixi48 – 503Combined sources
Helixi51 – 577Combined sources
Helixi62 – 643Combined sources
Beta strandi65 – 673Combined sources
Beta strandi73 – 764Combined sources
Beta strandi78 – 847Combined sources
Helixi85 – 906Combined sources
Helixi99 – 1057Combined sources
Helixi107 – 1126Combined sources
Helixi113 – 1153Combined sources
Helixi117 – 13317Combined sources
Beta strandi136 – 1427Combined sources
Helixi147 – 16014Combined sources
Beta strandi163 – 1675Combined sources
Beta strandi175 – 1773Combined sources
Helixi184 – 20118Combined sources
Beta strandi204 – 2085Combined sources
Beta strandi210 – 2123Combined sources
Turni215 – 2173Combined sources
Helixi220 – 23213Combined sources
Beta strandi237 – 2426Combined sources
Helixi245 – 25410Combined sources
Beta strandi258 – 2603Combined sources
Helixi261 – 2666Combined sources
Turni267 – 2693Combined sources
Beta strandi275 – 2795Combined sources
Helixi285 – 29410Combined sources
Beta strandi297 – 3004Combined sources
Helixi302 – 3076Combined sources
Helixi315 – 3206Combined sources
Beta strandi324 – 3274Combined sources
Turni331 – 3333Combined sources
Helixi339 – 35517Combined sources
Beta strandi358 – 3614Combined sources
Helixi365 – 3728Combined sources
Helixi374 – 3796Combined sources
Turni383 – 3853Combined sources
Beta strandi386 – 3883Combined sources
Beta strandi397 – 4004Combined sources
Helixi414 – 4174Combined sources
Beta strandi418 – 4203Combined sources
Helixi423 – 4319Combined sources
Helixi434 – 4363Combined sources
Beta strandi437 – 4426Combined sources
Beta strandi445 – 4484Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000017130.
HOGENOMiHOG000257692.
HOVERGENiHBG005930.
InParanoidiQ9Y2T3.
KOiK01487.
OMAiCEAFYHA.
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

        10         20         30         40         50
MCAAQMPPLA HIFRGTFVHS TWTCPMEVLR DHLLGVSDSG KIVFLEEASQ
60 70 80 90 100
QEKLAKEWCF KPCEIRELSH HEFFMPGLVD THIHASQYSF AGSSIDLPLL
110 120 130 140 150
EWLTKYTFPA EHRFQNIDFA EEVYTRVVRR TLKNGTTTAC YFATIHTDSS
160 170 180 190 200
LLLADITDKF GQRAFVGKVC MDLNDTFPEY KETTEESIKE TERFVSEMLQ
210 220 230 240 250
KNYSRVKPIV TPRFSLSCSE TLMGELGNIA KTRDLHIQSH ISENRDEVEA
260 270 280 290 300
VKNLYPSYKN YTSVYDKNNL LTNKTVMAHG CYLSAEELNV FHERGASIAH
310 320 330 340 350
CPNSNLSLSS GFLNVLEVLK HEVKIGLGTD VAGGYSYSML DAIRRAVMVS
360 370 380 390 400
NILLINKVNE KSLTLKEVFR LATLGGSQAL GLDGEIGNFE VGKEFDAILI
410 420 430 440 450
NPKASDSPID LFYGDFFGDI SEAVIQKFLY LGDDRNIEEV YVGGKQVVPF

SSSV
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.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

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

Chemistry

BindingDBiQ9Y2T3.
ChEMBLiCHEMBL3129.

Protein family/group databases

MEROPSiM38.981.

PTM databases

PhosphoSiteiQ9Y2T3.

Polymorphism databases

DMDMi9910736.

Proteomic databases

MaxQBiQ9Y2T3.
PaxDbiQ9Y2T3.
PRIDEiQ9Y2T3.

Protocols and materials databases

DNASUi9615.
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi9615.
GeneCardsiGC09P074729.
HGNCiHGNC:4212. GDA.
HPAiHPA019352.
HPA024099.
HPA030387.
MIMi139260. gene.
neXtProtiNX_Q9Y2T3.
PharmGKBiPA28625.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0402.
GeneTreeiENSGT00390000017130.
HOGENOMiHOG000257692.
HOVERGENiHBG005930.
InParanoidiQ9Y2T3.
KOiK01487.
OMAiCEAFYHA.
PhylomeDBiQ9Y2T3.
TreeFamiTF324539.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiGDA. human.
EvolutionaryTraceiQ9Y2T3.
GenomeRNAii9615.
NextBioi36069.
PROiQ9Y2T3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y2T3.
CleanExiHS_GDA.
ExpressionAtlasiQ9Y2T3. baseline and differential.
GenevestigatoriQ9Y2T3.

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.
ProtoNetiSearch...

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: January 7, 2015
This is version 129 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.