Full text data of GMPR2
GMPR2
[Confidence: low (only semi-automatic identification from reviews)]
GMP reductase 2; 1.7.1.7 (Guanosine 5'-monophosphate oxidoreductase 2; Guanosine monophosphate reductase 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
GMP reductase 2; 1.7.1.7 (Guanosine 5'-monophosphate oxidoreductase 2; Guanosine monophosphate reductase 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9P2T1
ID GMPR2_HUMAN Reviewed; 348 AA.
AC Q9P2T1; D3DS66; Q567T0; Q6IAJ8;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 117.
DE RecName: Full=GMP reductase 2;
DE EC=1.7.1.7;
DE AltName: Full=Guanosine 5'-monophosphate oxidoreductase 2;
DE Short=Guanosine monophosphate reductase 2;
GN Name=GMPR2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=12009299; DOI=10.1016/S1357-2725(02)00024-9;
RA Deng Y., Wang Z., Ying K., Gu S., Ji C., Huang Y., Gu X., Wang Y.,
RA Xu Y., Li Y., Xie Y., Mao Y.;
RT "NADPH-dependent GMP reductase isoenzyme of human (GMPR2). Expression,
RT purification, and kinetic properties.";
RL Int. J. Biochem. Cell Biol. 34:1035-1050(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=12669231; DOI=10.1007/s00432-002-0413-7;
RA Zhang J., Zhang W., Zou D., Chen G., Wan T., Zhang M., Cao X.;
RT "Cloning and functional characterization of GMPR2, a novel human
RT guanosine monophosphate reductase, which promotes the monocytic
RT differentiation of HL-60 leukemia cells.";
RL J. Cancer Res. Clin. Oncol. 129:76-83(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Okaze H., Hayashi A., Kozuma S., Saito T.;
RT "A novel protein related to guanosine monophosphate reductase.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-291, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Catalyzes the irreversible NADPH-dependent deamination
CC of GMP to IMP. It functions in the conversion of nucleobase,
CC nucleoside and nucleotide derivatives of G to A nucleotides, and
CC in maintaining the intracellular balance of A and G nucleotides.
CC Plays a role in modulating cellular differentiation.
CC -!- CATALYTIC ACTIVITY: Inosine 5'-phosphate + NH(3) + NADP(+) =
CC guanosine 5'-phosphate + NADPH.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9P2T1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P2T1-2; Sequence=VSP_041459;
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle,
CC kidney, brain, liver, prostate, spleen, placenta, testis and
CC ovary. Low expression in colon, thymus and peripheral blood
CC leukocytes.
CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF419346; AAN32701.1; -; mRNA.
DR EMBL; AF135159; AAG09132.1; -; mRNA.
DR EMBL; AB032903; BAA93080.1; -; mRNA.
DR EMBL; BX161436; CAD61908.1; -; mRNA.
DR EMBL; CR457156; CAG33437.1; -; mRNA.
DR EMBL; CH471078; EAW66051.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66053.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66054.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66057.1; -; Genomic_DNA.
DR EMBL; BC008021; AAH08021.2; -; mRNA.
DR EMBL; BC009832; AAH09832.1; -; mRNA.
DR EMBL; BC093039; AAH93039.1; -; mRNA.
DR RefSeq; NP_001002000.1; NM_001002000.2.
DR RefSeq; NP_001002001.1; NM_001002001.2.
DR RefSeq; NP_001002002.1; NM_001002002.2.
DR RefSeq; NP_001269950.1; NM_001283021.1.
DR RefSeq; NP_001269951.1; NM_001283022.1.
DR RefSeq; NP_001269952.1; NM_001283023.1.
DR RefSeq; NP_057660.2; NM_016576.4.
DR UniGene; Hs.368855; -.
DR PDB; 2A7R; X-ray; 3.00 A; A/B/C/D=1-348.
DR PDB; 2BZN; X-ray; 2.15 A; A/B/C/D/E/F/G/H=10-341.
DR PDB; 2C6Q; X-ray; 1.70 A; A/B/C/D/E/F/G/H=10-341.
DR PDBsum; 2A7R; -.
DR PDBsum; 2BZN; -.
DR PDBsum; 2C6Q; -.
DR ProteinModelPortal; Q9P2T1; -.
DR SMR; Q9P2T1; 10-337.
DR IntAct; Q9P2T1; 1.
DR STRING; 9606.ENSP00000392859; -.
DR PhosphoSite; Q9P2T1; -.
DR DMDM; 25008511; -.
DR PaxDb; Q9P2T1; -.
DR PRIDE; Q9P2T1; -.
DR DNASU; 51292; -.
DR Ensembl; ENST00000355299; ENSP00000347449; ENSG00000100938.
DR Ensembl; ENST00000399440; ENSP00000382369; ENSG00000100938.
DR Ensembl; ENST00000420554; ENSP00000392859; ENSG00000100938.
DR Ensembl; ENST00000559836; ENSP00000453299; ENSG00000100938.
DR GeneID; 51292; -.
DR KEGG; hsa:51292; -.
DR UCSC; uc001wnr.3; human.
DR CTD; 51292; -.
DR GeneCards; GC14P024701; -.
DR HGNC; HGNC:4377; GMPR2.
DR HPA; HPA000904; -.
DR MIM; 610781; gene.
DR neXtProt; NX_Q9P2T1; -.
DR PharmGKB; PA28762; -.
DR eggNOG; COG0516; -.
DR HOGENOM; HOG000165756; -.
DR HOVERGEN; HBG051744; -.
DR InParanoid; Q9P2T1; -.
DR KO; K00364; -.
DR OrthoDB; EOG73804S; -.
DR PhylomeDB; Q9P2T1; -.
DR BRENDA; 1.7.1.7; 2681.
DR Reactome; REACT_111217; Metabolism.
DR ChiTaRS; GMPR2; human.
DR EvolutionaryTrace; Q9P2T1; -.
DR GenomeRNAi; 51292; -.
DR NextBio; 54555; -.
DR PRO; PR:Q9P2T1; -.
DR ArrayExpress; Q9P2T1; -.
DR Bgee; Q9P2T1; -.
DR CleanEx; HS_GMPR2; -.
DR Genevestigator; Q9P2T1; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0003920; F:GMP reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:InterPro.
DR GO; GO:0006144; P:purine nucleobase metabolic process; TAS:Reactome.
DR GO; GO:0043101; P:purine-containing compound salvage; TAS:Reactome.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR005993; GMP_reduct1.
DR InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS.
DR InterPro; IPR001093; IMP_DH_GMPRt.
DR Pfam; PF00478; IMPDH; 1.
DR PIRSF; PIRSF000235; GMP_reductase; 1.
DR TIGRFAMs; TIGR01305; GMP_reduct_1; 1.
DR PROSITE; PS00487; IMP_DH_GMP_RED; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Metal-binding; NADP; Oxidoreductase; Polymorphism; Potassium;
KW Reference proteome.
FT CHAIN 1 348 GMP reductase 2.
FT /FTId=PRO_0000093726.
FT NP_BIND 108 131 NADP (By similarity).
FT ACT_SITE 186 186 Thioimidate intermediate (By similarity).
FT METAL 181 181 Potassium; via carbonyl oxygen (By
FT similarity).
FT METAL 183 183 Potassium; via carbonyl oxygen (By
FT similarity).
FT BINDING 219 219 NADP (By similarity).
FT MOD_RES 291 291 N6-acetyllysine.
FT VAR_SEQ 1 1 M -> MTSCLPALRFIATPRLSAM (in isoform 2).
FT /FTId=VSP_041459.
FT VARIANT 242 242 G -> D (in dbSNP:rs34354104).
FT /FTId=VAR_049602.
FT CONFLICT 91 91 Q -> R (in Ref. 5; CAG33437).
FT CONFLICT 200 200 S -> G (in Ref. 5; CAG33437).
FT CONFLICT 223 223 S -> N (in Ref. 5; CAG33437).
FT STRAND 3 9
FT HELIX 12 14
FT STRAND 15 17
FT HELIX 27 29
FT STRAND 34 37
FT TURN 39 41
FT STRAND 44 47
FT STRAND 50 52
FT TURN 56 58
FT HELIX 61 69
FT STRAND 73 75
FT HELIX 82 91
FT HELIX 93 95
FT STRAND 99 103
FT HELIX 107 119
FT STRAND 125 129
FT HELIX 136 148
FT STRAND 152 159
FT HELIX 162 170
FT STRAND 174 178
FT HELIX 188 192
FT HELIX 198 211
FT STRAND 215 220
FT HELIX 225 233
FT STRAND 237 242
FT TURN 243 247
FT STRAND 248 251
FT STRAND 255 258
FT STRAND 261 267
FT STRAND 269 271
FT HELIX 272 278
FT STRAND 279 281
FT TURN 283 285
FT STRAND 286 288
FT STRAND 292 296
FT HELIX 301 319
FT HELIX 324 326
FT HELIX 327 330
FT STRAND 333 335
SQ SEQUENCE 348 AA; 37874 MW; E7812A754C433E51 CRC64;
MPHIDNDVKL DFKDVLLRPK RSTLKSRSEV DLTRSFSFRN SKQTYSGVPI IAANMDTVGT
FEMAKVLCKF SLFTAVHKHY SLVQWQEFAG QNPDCLEHLA ASSGTGSSDF EQLEQILEAI
PQVKYICLDV ANGYSEHFVE FVKDVRKRFP QHTIMAGNVV TGEMVEELIL SGADIIKVGI
GPGSVCTTRK KTGVGYPQLS AVMECADAAH GLKGHIISDG GCSCPGDVAK AFGAGADFVM
LGGMLAGHSE SGGELIERDG KKYKLFYGMS SEMAMKKYAG GVAEYRASEG KTVEVPFKGD
VEHTIRDILG GIRSTCTYVG AAKLKELSRR TTFIRVTQQV NPIFSEAC
//
ID GMPR2_HUMAN Reviewed; 348 AA.
AC Q9P2T1; D3DS66; Q567T0; Q6IAJ8;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 117.
DE RecName: Full=GMP reductase 2;
DE EC=1.7.1.7;
DE AltName: Full=Guanosine 5'-monophosphate oxidoreductase 2;
DE Short=Guanosine monophosphate reductase 2;
GN Name=GMPR2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=12009299; DOI=10.1016/S1357-2725(02)00024-9;
RA Deng Y., Wang Z., Ying K., Gu S., Ji C., Huang Y., Gu X., Wang Y.,
RA Xu Y., Li Y., Xie Y., Mao Y.;
RT "NADPH-dependent GMP reductase isoenzyme of human (GMPR2). Expression,
RT purification, and kinetic properties.";
RL Int. J. Biochem. Cell Biol. 34:1035-1050(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=12669231; DOI=10.1007/s00432-002-0413-7;
RA Zhang J., Zhang W., Zou D., Chen G., Wan T., Zhang M., Cao X.;
RT "Cloning and functional characterization of GMPR2, a novel human
RT guanosine monophosphate reductase, which promotes the monocytic
RT differentiation of HL-60 leukemia cells.";
RL J. Cancer Res. Clin. Oncol. 129:76-83(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Okaze H., Hayashi A., Kozuma S., Saito T.;
RT "A novel protein related to guanosine monophosphate reductase.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-291, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Catalyzes the irreversible NADPH-dependent deamination
CC of GMP to IMP. It functions in the conversion of nucleobase,
CC nucleoside and nucleotide derivatives of G to A nucleotides, and
CC in maintaining the intracellular balance of A and G nucleotides.
CC Plays a role in modulating cellular differentiation.
CC -!- CATALYTIC ACTIVITY: Inosine 5'-phosphate + NH(3) + NADP(+) =
CC guanosine 5'-phosphate + NADPH.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9P2T1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P2T1-2; Sequence=VSP_041459;
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle,
CC kidney, brain, liver, prostate, spleen, placenta, testis and
CC ovary. Low expression in colon, thymus and peripheral blood
CC leukocytes.
CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF419346; AAN32701.1; -; mRNA.
DR EMBL; AF135159; AAG09132.1; -; mRNA.
DR EMBL; AB032903; BAA93080.1; -; mRNA.
DR EMBL; BX161436; CAD61908.1; -; mRNA.
DR EMBL; CR457156; CAG33437.1; -; mRNA.
DR EMBL; CH471078; EAW66051.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66053.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66054.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66057.1; -; Genomic_DNA.
DR EMBL; BC008021; AAH08021.2; -; mRNA.
DR EMBL; BC009832; AAH09832.1; -; mRNA.
DR EMBL; BC093039; AAH93039.1; -; mRNA.
DR RefSeq; NP_001002000.1; NM_001002000.2.
DR RefSeq; NP_001002001.1; NM_001002001.2.
DR RefSeq; NP_001002002.1; NM_001002002.2.
DR RefSeq; NP_001269950.1; NM_001283021.1.
DR RefSeq; NP_001269951.1; NM_001283022.1.
DR RefSeq; NP_001269952.1; NM_001283023.1.
DR RefSeq; NP_057660.2; NM_016576.4.
DR UniGene; Hs.368855; -.
DR PDB; 2A7R; X-ray; 3.00 A; A/B/C/D=1-348.
DR PDB; 2BZN; X-ray; 2.15 A; A/B/C/D/E/F/G/H=10-341.
DR PDB; 2C6Q; X-ray; 1.70 A; A/B/C/D/E/F/G/H=10-341.
DR PDBsum; 2A7R; -.
DR PDBsum; 2BZN; -.
DR PDBsum; 2C6Q; -.
DR ProteinModelPortal; Q9P2T1; -.
DR SMR; Q9P2T1; 10-337.
DR IntAct; Q9P2T1; 1.
DR STRING; 9606.ENSP00000392859; -.
DR PhosphoSite; Q9P2T1; -.
DR DMDM; 25008511; -.
DR PaxDb; Q9P2T1; -.
DR PRIDE; Q9P2T1; -.
DR DNASU; 51292; -.
DR Ensembl; ENST00000355299; ENSP00000347449; ENSG00000100938.
DR Ensembl; ENST00000399440; ENSP00000382369; ENSG00000100938.
DR Ensembl; ENST00000420554; ENSP00000392859; ENSG00000100938.
DR Ensembl; ENST00000559836; ENSP00000453299; ENSG00000100938.
DR GeneID; 51292; -.
DR KEGG; hsa:51292; -.
DR UCSC; uc001wnr.3; human.
DR CTD; 51292; -.
DR GeneCards; GC14P024701; -.
DR HGNC; HGNC:4377; GMPR2.
DR HPA; HPA000904; -.
DR MIM; 610781; gene.
DR neXtProt; NX_Q9P2T1; -.
DR PharmGKB; PA28762; -.
DR eggNOG; COG0516; -.
DR HOGENOM; HOG000165756; -.
DR HOVERGEN; HBG051744; -.
DR InParanoid; Q9P2T1; -.
DR KO; K00364; -.
DR OrthoDB; EOG73804S; -.
DR PhylomeDB; Q9P2T1; -.
DR BRENDA; 1.7.1.7; 2681.
DR Reactome; REACT_111217; Metabolism.
DR ChiTaRS; GMPR2; human.
DR EvolutionaryTrace; Q9P2T1; -.
DR GenomeRNAi; 51292; -.
DR NextBio; 54555; -.
DR PRO; PR:Q9P2T1; -.
DR ArrayExpress; Q9P2T1; -.
DR Bgee; Q9P2T1; -.
DR CleanEx; HS_GMPR2; -.
DR Genevestigator; Q9P2T1; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0003920; F:GMP reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:InterPro.
DR GO; GO:0006144; P:purine nucleobase metabolic process; TAS:Reactome.
DR GO; GO:0043101; P:purine-containing compound salvage; TAS:Reactome.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR005993; GMP_reduct1.
DR InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS.
DR InterPro; IPR001093; IMP_DH_GMPRt.
DR Pfam; PF00478; IMPDH; 1.
DR PIRSF; PIRSF000235; GMP_reductase; 1.
DR TIGRFAMs; TIGR01305; GMP_reduct_1; 1.
DR PROSITE; PS00487; IMP_DH_GMP_RED; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Metal-binding; NADP; Oxidoreductase; Polymorphism; Potassium;
KW Reference proteome.
FT CHAIN 1 348 GMP reductase 2.
FT /FTId=PRO_0000093726.
FT NP_BIND 108 131 NADP (By similarity).
FT ACT_SITE 186 186 Thioimidate intermediate (By similarity).
FT METAL 181 181 Potassium; via carbonyl oxygen (By
FT similarity).
FT METAL 183 183 Potassium; via carbonyl oxygen (By
FT similarity).
FT BINDING 219 219 NADP (By similarity).
FT MOD_RES 291 291 N6-acetyllysine.
FT VAR_SEQ 1 1 M -> MTSCLPALRFIATPRLSAM (in isoform 2).
FT /FTId=VSP_041459.
FT VARIANT 242 242 G -> D (in dbSNP:rs34354104).
FT /FTId=VAR_049602.
FT CONFLICT 91 91 Q -> R (in Ref. 5; CAG33437).
FT CONFLICT 200 200 S -> G (in Ref. 5; CAG33437).
FT CONFLICT 223 223 S -> N (in Ref. 5; CAG33437).
FT STRAND 3 9
FT HELIX 12 14
FT STRAND 15 17
FT HELIX 27 29
FT STRAND 34 37
FT TURN 39 41
FT STRAND 44 47
FT STRAND 50 52
FT TURN 56 58
FT HELIX 61 69
FT STRAND 73 75
FT HELIX 82 91
FT HELIX 93 95
FT STRAND 99 103
FT HELIX 107 119
FT STRAND 125 129
FT HELIX 136 148
FT STRAND 152 159
FT HELIX 162 170
FT STRAND 174 178
FT HELIX 188 192
FT HELIX 198 211
FT STRAND 215 220
FT HELIX 225 233
FT STRAND 237 242
FT TURN 243 247
FT STRAND 248 251
FT STRAND 255 258
FT STRAND 261 267
FT STRAND 269 271
FT HELIX 272 278
FT STRAND 279 281
FT TURN 283 285
FT STRAND 286 288
FT STRAND 292 296
FT HELIX 301 319
FT HELIX 324 326
FT HELIX 327 330
FT STRAND 333 335
SQ SEQUENCE 348 AA; 37874 MW; E7812A754C433E51 CRC64;
MPHIDNDVKL DFKDVLLRPK RSTLKSRSEV DLTRSFSFRN SKQTYSGVPI IAANMDTVGT
FEMAKVLCKF SLFTAVHKHY SLVQWQEFAG QNPDCLEHLA ASSGTGSSDF EQLEQILEAI
PQVKYICLDV ANGYSEHFVE FVKDVRKRFP QHTIMAGNVV TGEMVEELIL SGADIIKVGI
GPGSVCTTRK KTGVGYPQLS AVMECADAAH GLKGHIISDG GCSCPGDVAK AFGAGADFVM
LGGMLAGHSE SGGELIERDG KKYKLFYGMS SEMAMKKYAG GVAEYRASEG KTVEVPFKGD
VEHTIRDILG GIRSTCTYVG AAKLKELSRR TTFIRVTQQV NPIFSEAC
//
MIM
610781
*RECORD*
*FIELD* NO
610781
*FIELD* TI
*610781 GUANOSINE MONOPHOSPHATE REDUCTASE 2; GMPR2
;;GMP REDUCTASE 2
*FIELD* TX
CLONING
read more
By database searching with the sequence of GMPR1 (GMPR; 139265) as
query, Deng et al. (2002) identified and subsequently cloned GMPR2 from
a human fetal brain cDNA library. The deduced 348-amino acid protein has
a calculated molecular mass of 37.9 kD and shares 90% sequence identity
with GMPR1 and 69% identity with E. coli GMPR. Northern blot analysis
detected relatively high levels of both GMPR1 and GMPR2 in heart,
skeletal muscle, and kidney, and relatively low levels of both in colon,
thymus, and peripheral blood leukocyte. Strong signals of GMPR2 were
detected in brain, liver, and placenta, whereas weak signals of GMPR1
were observed in these tissues. The apparent Km of GMPR2 for NADPH and
GMP are 26.6 and 17.4 microM, respectively.
Zhang et al. (2003) cloned GMPR2 from a human dendritic cell cDNA
library. Northern blot analysis detected ubiquitous expression of an
approximately 2.2-kb transcript, with high expression in testis, ovary,
prostate, heart, liver, spleen, skeletal muscle, and kidney. An
additional transcript of about 1.3 kb was detected in placenta.
Expression was also detected in most cancer cell lines studied.
GENE FUNCTION
Zhang et al. (2003) showed that recombinant GMPR2 protein was able to
reduce GMP. Transfection experiments demonstrated that overexpression of
GMPR2 promoted the monocytic differentiation of HL-60 leukemia cells.
EVOLUTION
Deng et al. (2002) presented evidence that the 2 types of GMP reductase
are derived from duplication of an ancient gene.
GENE STRUCTURE
Deng et al. (2002) determined that the GMPR2 gene contains 10 exons and
spans more than 6.6 kb.
MAPPING
By genomic sequence analysis, Deng et al. (2002) mapped the GMPR2 gene
to chromosome 14p11.2-p11.1. By the same method, Zhang et al. (2003)
mapped the gene to chromosome 14q11-q21.
*FIELD* RF
1. 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. 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.
*FIELD* CD
Carol A. Bocchini: 2/21/2007
*FIELD* ED
carol: 02/21/2007
carol: 2/21/2007
*RECORD*
*FIELD* NO
610781
*FIELD* TI
*610781 GUANOSINE MONOPHOSPHATE REDUCTASE 2; GMPR2
;;GMP REDUCTASE 2
*FIELD* TX
CLONING
read more
By database searching with the sequence of GMPR1 (GMPR; 139265) as
query, Deng et al. (2002) identified and subsequently cloned GMPR2 from
a human fetal brain cDNA library. The deduced 348-amino acid protein has
a calculated molecular mass of 37.9 kD and shares 90% sequence identity
with GMPR1 and 69% identity with E. coli GMPR. Northern blot analysis
detected relatively high levels of both GMPR1 and GMPR2 in heart,
skeletal muscle, and kidney, and relatively low levels of both in colon,
thymus, and peripheral blood leukocyte. Strong signals of GMPR2 were
detected in brain, liver, and placenta, whereas weak signals of GMPR1
were observed in these tissues. The apparent Km of GMPR2 for NADPH and
GMP are 26.6 and 17.4 microM, respectively.
Zhang et al. (2003) cloned GMPR2 from a human dendritic cell cDNA
library. Northern blot analysis detected ubiquitous expression of an
approximately 2.2-kb transcript, with high expression in testis, ovary,
prostate, heart, liver, spleen, skeletal muscle, and kidney. An
additional transcript of about 1.3 kb was detected in placenta.
Expression was also detected in most cancer cell lines studied.
GENE FUNCTION
Zhang et al. (2003) showed that recombinant GMPR2 protein was able to
reduce GMP. Transfection experiments demonstrated that overexpression of
GMPR2 promoted the monocytic differentiation of HL-60 leukemia cells.
EVOLUTION
Deng et al. (2002) presented evidence that the 2 types of GMP reductase
are derived from duplication of an ancient gene.
GENE STRUCTURE
Deng et al. (2002) determined that the GMPR2 gene contains 10 exons and
spans more than 6.6 kb.
MAPPING
By genomic sequence analysis, Deng et al. (2002) mapped the GMPR2 gene
to chromosome 14p11.2-p11.1. By the same method, Zhang et al. (2003)
mapped the gene to chromosome 14q11-q21.
*FIELD* RF
1. 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. 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.
*FIELD* CD
Carol A. Bocchini: 2/21/2007
*FIELD* ED
carol: 02/21/2007
carol: 2/21/2007