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UniProtKB/Swiss-Prot entry Q9P2T1


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GMPR2_HUMAN
Primary accession number Q9P2T1
Secondary accession numbers Q567T0 Q6IAJ8
Integrated into Swiss-Prot on November 8, 2002
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 64)
Name and origin of the protein
Protein name GMP reductase 2
Synonyms EC 1.7.1.7
Guanosine 5'-monophosphate oxidoreductase 2
Guanosine monophosphate reductase 2
Gene name
Name: GMPR2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
DOI=10.1016/S1357-2725(02)00024-9; PubMed=12009299 [NCBI, ExPASy, EBI, Israel, Japan]
Deng Y., Wang Z., Ying K., Gu S., Ji C., Huang Y., Gu X., Wang Y., Xu Y., Li Y., Xie Y., Mao Y.;
"NADPH-dependent GMP reductase isoenzyme of human (GMPR2). Expression, purification, and kinetic properties.";
Int. J. Biochem. Cell Biol. 34:1035-1050(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
DOI=10.1007/s00432-002-0413-7; PubMed=12669231 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang J., Zhang W., Zou D., Chen G., Wan T., Zhang M., Cao X.;
"Cloning and functional characterization of GMPR2, a novel human guanosine monophosphate reductase, which promotes the monocytic differentiation of HL-60 leukemia cells.";
J. Cancer Res. Clin. Oncol. 129:76-83(2003).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Okaze H., Hayashi A., Kozuma S., Saito T.;
"A novel protein related to guanosine monophosphate reductase.";
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
Li W.B., Gruber C., Jessee J., Polayes D.;
"Full-length cDNA libraries and normalization.";
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung, and Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
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.
  • 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.
  • SIMILARITY: Belongs to the IMPDH/GMPR family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF419346; AAN32701.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF135159; AAG09132.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB032903; BAA93080.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BX161436; CAD61908.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR457156; CAG33437.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC008021; AAH08021.2; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC009832; AAH09832.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC093039; AAH93039.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_001002000.1; -.
NP_001002001.1; -.
NP_001002002.1; -.
NP_057660.2; -.
UniGene Hs.368855
3D structure databases
PDB
2A7R; X-ray; 3.00 A; A/B/C/D=1-348.[ExPASy / RCSB / EBI]
2BZN; X-ray; 2.15 A; A/B/C/D/E/F/G/H=10-341.[ExPASy / RCSB / EBI]
2C6Q; X-ray; 1.70 A; A/B/C/D/E/F/G/H=10-341.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2A7R; -.
2BZN; -.
2C6Q; -.
ModBase Q9P2T1.
Organism-specific databases
H-InvDB HIX0011563; -.
HGNC HGNC:4377; GMPR2.
GenAtlas GMPR2.
HPA HPA000904; -.
MIM 610781; gene. [NCBI / EBI]
PharmGKB PA28762; -.
GeneCards Q9P2T1.
Gene expression databases
CleanEx HS_GMPR2; -.
Family and domain databases
InterPro IPR013785; Aldolase_TIM.
IPR005993; GMP_reduct1.
IPR015875; IMP_DH/GMP_Rdtase_CS.
IPR001093; IMP_DHase_GMPRtase.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.70; Aldolase_TIM; 1.
Pfam PF00478; IMPDH; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000235; GMP_reductase; 1.
TIGRFAMs TIGR01305; GMP_reduct_1; 1.
PROSITE PS00487; IMP_DH_GMP_RED; 1.
BLOCKS Q9P2T1.
Genome annotation databases
Ensembl ENSG00000100938; Homo sapiens. [Contig view]
GeneID 51292; -.
KEGG hsa:51292; -.
NMPDR fig|9606.3.peg.9389; -.
Phylogenomic databases
HOVERGEN Q9P2T1; -.
Other
LinkHub Q9P2T1; -.
SOURCE GMPR2; Homo sapiens.
ProtoNet Q9P2T1.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Metal-binding; NADP; Oxidoreductase; Potassium.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   348  348     GMP reductase 2. PRO_0000093726
NP_BIND   108   131  24     NADP (By similarity). 
ACT_SITE   186   186        Thioimidate intermediate (By similarity). 
METAL   181   181        Potassium; via carbonyl oxygen (By similarity). 
METAL   183   183        Potassium; via carbonyl oxygen (By similarity). 
BINDING   219   219        NADP (By similarity). 
CONFLICT   91    91        Q -> R (in Ref. 5; CAG33437). 
CONFLICT   200   200        S -> G (in Ref. 5; CAG33437). 
CONFLICT   223   223        S -> N (in Ref. 5; CAG33437). 
STRAND   3     9  7      
HELIX   12    14  3      
STRAND   15    17  3      
STRAND   34    37  4      
TURN   39    41  3      
STRAND   44    47  4      
STRAND   50    52  3      
TURN   56    58  3      
HELIX   61    69  9      
STRAND   73    75  3      
HELIX   82    91  10      
HELIX   93    95  3      
STRAND   99   103  5      
HELIX   107   119  13      
STRAND   125   129  5      
HELIX   136   148  13      
STRAND   152   159  8      
HELIX   162   170  9      
STRAND   174   178  5      
HELIX   188   192  5      
HELIX   198   210  13      
TURN   211   213  3      
STRAND   215   220  6      
HELIX   225   233  9      
STRAND   237   242  6      
TURN   243   247  5      
STRAND   255   258  4      
STRAND   261   267  7      
HELIX   272   277  6      
STRAND   292   296  5      
HELIX   301   319  19      
HELIX   324   326  3      
TURN   327   330  4      
STRAND   333   335  3      
Sequence information
Length: 348 AA [This is the length of the unprocessed precursor] Molecular weight: 37874 Da [This is the MW of the unprocessed precursor] CRC64: E7812A754C433E51 [This is a checksum on the sequence]
        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 

Q9P2T1 in FASTA format

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