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Reviewed, UniProtKB/Swiss-Prot Q9P2T1 (GMPR2_HUMAN)

Last modified June 16, 2009. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    GMP reductase 2
    EC=1.7.1.7
Alternative name(s):
    Guanosine 5'-monophosphate oxidoreductase 2
      Short name=Guanosine monophosphate reductase 2
Gene names
Name: GMPR2
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length348 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides. Plays a role in modulating cellular differentiation. Ref.1 Ref.2

Catalytic activity

Inosine 5'-phosphate + NH3 + NADP+ = guanosine 5'-phosphate + NADPH.

Tissue specificity

Highly expressed in heart, skeletal muscle, kidney, brain, liver, prostate, spleen, placenta, testis and ovary. Low expression in colon, thymus and peripheral blood leukocytes. Ref.1 Ref.2

Sequence similarities

Belongs to the IMPDH/GMPR family.

Ontologies

Keywords
   Coding sequence diversityPolymorphism
   LigandMetal-binding
NADP
Potassium
   Molecular functionOxidoreductase
   Technical term3D-structure
Gene Ontology (GO)
   Biological processnucleotide metabolic process

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionGMP reductase activity

Inferred from electronic annotation. Source: EC

potassium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 348348GMP reductase 2
PRO_0000093726

Regions

Nucleotide binding108 – 13124NADP By similarity

Sites

Active site1861Thioimidate intermediate By similarity
Metal binding1811Potassium; via carbonyl oxygen By similarity
Metal binding1831Potassium; via carbonyl oxygen By similarity
Binding site2191NADP By similarity

Natural variations

Natural variant2421G → D: dbSNP rs34354104.
VAR_049602

Experimental info

Sequence conflict911Q → R in CAG33437. Ref.5
Sequence conflict2001S → G in CAG33437. Ref.5
Sequence conflict2231S → N in CAG33437. Ref.5

Secondary structure

................................................................. 348
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9P2T1-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: E7812A754C433E51

FASTA34837,874
        10         20         30         40         50         60 
MPHIDNDVKL DFKDVLLRPK RSTLKSRSEV DLTRSFSFRN SKQTYSGVPI IAANMDTVGT 

        70         80         90        100        110        120 
FEMAKVLCKF SLFTAVHKHY SLVQWQEFAG QNPDCLEHLA ASSGTGSSDF EQLEQILEAI 

       130        140        150        160        170        180 
PQVKYICLDV ANGYSEHFVE FVKDVRKRFP QHTIMAGNVV TGEMVEELIL SGADIIKVGI 

       190        200        210        220        230        240 
GPGSVCTTRK KTGVGYPQLS AVMECADAAH GLKGHIISDG GCSCPGDVAK AFGAGADFVM 

       250        260        270        280        290        300 
LGGMLAGHSE SGGELIERDG KKYKLFYGMS SEMAMKKYAG GVAEYRASEG KTVEVPFKGD 

       310        320        330        340 
VEHTIRDILG GIRSTCTYVG AAKLKELSRR TTFIRVTQQV NPIFSEAC 

« Hide

References

« Hide 'large scale' references
[1]"NADPH-dependent GMP reductase isoenzyme of human (GMPR2). Expression, purification, and kinetic properties."
Deng Y., Wang Z., Ying K., Gu S., Ji C., Huang Y., Gu X., Wang Y., Xu Y., Li Y., Xie Y., Mao Y.
Int. J. Biochem. Cell Biol. 34:1035-1050(2002) [PubMed: 12009299] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
[2]"Cloning and functional characterization of GMPR2, a novel human guanosine monophosphate reductase, which promotes the monocytic differentiation of HL-60 leukemia cells."
Zhang J., Zhang W., Zou D., Chen G., Wan T., Zhang M., Cao X.
J. Cancer Res. Clin. Oncol. 129:76-83(2003) [PubMed: 12669231] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
[3]"A novel protein related to guanosine monophosphate reductase."
Okaze H., Hayashi A., Kozuma S., Saito T.
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Full-length cDNA libraries and normalization."
Li W.B., Gruber C., Jessee J., Polayes D.
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta.
[5]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung and Placenta.
[7]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF419346 mRNA. Translation: AAN32701.1.
AF135159 mRNA. Translation: AAG09132.1.
AB032903 mRNA. Translation: BAA93080.1.
BX161436 mRNA. Translation: CAD61908.1.
CR457156 mRNA. Translation: CAG33437.1.
BC008021 mRNA. Translation: AAH08021.2. Different initiation.
BC009832 mRNA. Translation: AAH09832.1.
BC093039 mRNA. Translation: AAH93039.1.
IPIIPI00009844.
RefSeqNP_001002000.1.
NP_001002001.1.
NP_001002002.1.
NP_057660.2.
UniGeneHs.368855

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2A7RX-ray3.00A/B/C/D1-348[»]
2BZNX-ray2.15A/B/C/D/E/F/G/H10-341[»]
2C6QX-ray1.70A/B/C/D/E/F/G/H10-341[»]
ModBaseSearch...

Proteomic databases

PRIDEQ9P2T1.

Genome annotation databases

EnsemblENSG00000100938. Homo sapiens. [Contig view]
GeneID51292.
KEGGhsa:51292.
NMPDRfig|9606.3.peg.9389.

Organism-specific databases

GeneCardsGC14P023771.
H-InvDBHIX0011563.
HGNCHGNC:4377. GMPR2.
HPAHPA000904.
MIM610781. gene.
PharmGKBPA28762.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ9P2T1.
OMAQ9P2T1. QNPDCLE.

Enzyme and pathway databases

BRENDA1.7.1.7. 247.

Gene expression databases

BgeeQ9P2T1.
CleanExHS_GMPR2.

Family and domain databases

InterProIPR013785. Aldolase_TIM.
IPR005993. GMP_reduct1.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PfamPF00478. IMPDH. 1 hit.
[Graphical view]
PIRSFPIRSF000235. GMP_reductase. 1 hit.
TIGRFAMsTIGR01305. GMP_reduct_1. 1 hit.
PROSITEPS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio54555.
SOURCESearch...

Entry information

Entry nameGMPR2_HUMAN
AccessionPrimary (citable) accession number: Q9P2T1
Secondary accession number(s): Q567T0, Q6IAJ8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: October 1, 2000
Last modified: June 16, 2009
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents