Full text data of GMPR
GMPR
(GMPR1)
[Confidence: high (present in two of the MS resources)]
GMP reductase 1; 1.7.1.7 (Guanosine 5'-monophosphate oxidoreductase 1; Guanosine monophosphate reductase 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
GMP reductase 1; 1.7.1.7 (Guanosine 5'-monophosphate oxidoreductase 1; Guanosine monophosphate reductase 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00304803
IPI00304803 GMP reductase Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP, Inosine 5-phosphate + NH3 + NADP+ = guanosine 5-phosphate + NADPH soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00304803 GMP reductase Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP, Inosine 5-phosphate + NH3 + NADP+ = guanosine 5-phosphate + NADPH soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
P36959
ID GMPR1_HUMAN Reviewed; 345 AA.
AC P36959; Q96HQ6;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-1994, sequence version 1.
DT 22-JAN-2014, entry version 138.
DE RecName: Full=GMP reductase 1;
DE EC=1.7.1.7;
DE AltName: Full=Guanosine 5'-monophosphate oxidoreductase 1;
DE Short=Guanosine monophosphate reductase 1;
GN Name=GMPR; Synonyms=GMPR1;
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 [GENOMIC DNA / MRNA].
RX PubMed=2758468; DOI=10.1016/0092-8674(89)90440-6;
RA Kanno H., Huang I.Y., Kan Y.W., Yoshida A.;
RT "Two structural genes on different chromosomes are required for
RT encoding the major subunit of human red cell glucose-6-phosphate
RT dehydrogenase.";
RL Cell 58:595-606(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1661705;
RA Kondoh T., Kanno H., Chang L., Yoshida A.;
RT "Genomic structure and expression of human guanosine monophosphate
RT reductase.";
RL Hum. Genet. 88:219-224(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-256.
RC TISSUE=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 [5]
RP SIMILARITY TO GMP REDUCTASE.
RX PubMed=2570640; DOI=10.1016/0092-8674(89)90498-4;
RA Henikoff S., Smith J.M.;
RT "The human mRNA that provides the N-terminus of chimeric G6PD encodes
RT GMP reductase.";
RL Cell 58:1021-1022(1989).
RN [6]
RP LACK OF ROLE IN G6PD.
RX PubMed=1694726; DOI=10.1016/0092-8674(90)90233-5;
RA Yoshida A., Kan Y.W.;
RT "Origin of 'fused' glucose-6-phosphate dehydrogenase.";
RL Cell 62:11-12(1990).
RN [7]
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).
RN [8]
RP VARIANTS THR-234 AND ILE-256.
RX PubMed=1757097;
RA Kondoh T., Kanno H., Chang L., Yoshida A.;
RT "Identification of common variant alleles of the human guanosine
RT monophosphate reductase gene.";
RL Hum. Genet. 88:225-227(1991).
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 -!- CATALYTIC ACTIVITY: Inosine 5'-phosphate + NH(3) + NADP(+) =
CC guanosine 5'-phosphate + NADPH.
CC -!- SUBUNIT: Homotetramer.
CC -!- POLYMORPHISM: At least two different alleles are known.
CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family.
CC -!- CAUTION: The N-terminus was initially (PubMed:2758468) thought to
CC be fused with glucose-6-phosphate-dehydrogenase (G6PD) protein in
CC vivo. However, PubMed:2570640 showed that it encodes a GMP
CC reductase, and PubMed:1694726 showed that the chimeric protein is
CC an artifact.
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; L35304; AAA52503.1; -; Genomic_DNA.
DR EMBL; M27941; AAA53106.1; -; Genomic_DNA.
DR EMBL; M24470; AAA52498.1; -; mRNA.
DR EMBL; AL009031; CAI21422.1; -; Genomic_DNA.
DR EMBL; AL138883; CAI21422.1; JOINED; Genomic_DNA.
DR EMBL; AL138883; CAI19917.1; -; Genomic_DNA.
DR EMBL; AL009031; CAI19917.1; JOINED; Genomic_DNA.
DR EMBL; BC008281; AAH08281.1; -; mRNA.
DR PIR; B32902; B32902.
DR RefSeq; NP_006868.3; NM_006877.3.
DR UniGene; Hs.484741; -.
DR PDB; 2BLE; X-ray; 1.90 A; A=1-345.
DR PDB; 2BWG; X-ray; 2.40 A; A/B/C/D=1-345.
DR PDBsum; 2BLE; -.
DR PDBsum; 2BWG; -.
DR ProteinModelPortal; P36959; -.
DR SMR; P36959; 2-338.
DR STRING; 9606.ENSP00000259727; -.
DR PhosphoSite; P36959; -.
DR DMDM; 544455; -.
DR PaxDb; P36959; -.
DR PeptideAtlas; P36959; -.
DR PRIDE; P36959; -.
DR DNASU; 2766; -.
DR Ensembl; ENST00000259727; ENSP00000259727; ENSG00000137198.
DR GeneID; 2766; -.
DR KEGG; hsa:2766; -.
DR UCSC; uc003nbs.3; human.
DR CTD; 2766; -.
DR GeneCards; GC06P016238; -.
DR HGNC; HGNC:4376; GMPR.
DR HPA; HPA000904; -.
DR HPA; HPA021476; -.
DR MIM; 139265; gene.
DR neXtProt; NX_P36959; -.
DR PharmGKB; PA28761; -.
DR eggNOG; COG0516; -.
DR HOGENOM; HOG000165756; -.
DR HOVERGEN; HBG051744; -.
DR InParanoid; P36959; -.
DR KO; K00364; -.
DR OMA; SKFPEHT; -.
DR OrthoDB; EOG73804S; -.
DR PhylomeDB; P36959; -.
DR Reactome; REACT_111217; Metabolism.
DR ChiTaRS; GMPR; human.
DR EvolutionaryTrace; P36959; -.
DR GenomeRNAi; 2766; -.
DR NextBio; 10880; -.
DR PRO; PR:P36959; -.
DR Bgee; P36959; -.
DR CleanEx; HS_GMPR; -.
DR Genevestigator; P36959; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0003920; F:GMP reductase activity; TAS:ProtInc.
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 GO; GO:0009409; P:response to cold; TAS:ProtInc.
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; Complete proteome; Metal-binding; NADP; Oxidoreductase;
KW Polymorphism; Potassium; Reference proteome.
FT CHAIN 1 345 GMP reductase 1.
FT /FTId=PRO_0000093723.
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 VARIANT 234 234 A -> T.
FT /FTId=VAR_003969.
FT VARIANT 256 256 F -> I (in dbSNP:rs1042391).
FT /FTId=VAR_003970.
FT STRAND 3 8
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 67
FT HELIX 68 70
FT STRAND 73 75
FT HELIX 82 91
FT HELIX 93 98
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 188 191
FT HELIX 198 210
FT TURN 211 213
FT STRAND 215 220
FT HELIX 225 234
FT STRAND 237 242
FT HELIX 243 245
FT STRAND 251 253
FT STRAND 263 267
FT HELIX 272 277
FT STRAND 285 288
FT STRAND 292 296
FT HELIX 301 319
FT HELIX 324 326
FT HELIX 327 330
FT STRAND 333 335
SQ SEQUENCE 345 AA; 37419 MW; 217E1A5A599CA510 CRC64;
MPRIDADLKL DFKDVLLRPK RSSLKSRAEV DLERTFTFRN SKQTYSGIPI IVANMDTVGT
FEMAAVMSQH SMFTAIHKHY SLDDWKLFAT NHPECLQNVA VSSGSGQNDL EKMTSILEAV
PQVKFICLDV ANGYSEHFVE FVKLVRAKFP EHTIMAGNVV TGEMVEELIL SGADIIKVGV
GPGSVCTTRT KTGVGYPQLS AVIECADSAH GLKGHIISDG GCTCPGDVAK AFGAGADFVM
LGGMFSGHTE CAGEVFERNG RKLKLFYGMS SDTAMNKHAG GVAEYRASEG KTVEVPYKGD
VENTILDILG GLRSTCTYVG AAKLKELSRR ATFIRVTQQH NTVFS
//
ID GMPR1_HUMAN Reviewed; 345 AA.
AC P36959; Q96HQ6;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-1994, sequence version 1.
DT 22-JAN-2014, entry version 138.
DE RecName: Full=GMP reductase 1;
DE EC=1.7.1.7;
DE AltName: Full=Guanosine 5'-monophosphate oxidoreductase 1;
DE Short=Guanosine monophosphate reductase 1;
GN Name=GMPR; Synonyms=GMPR1;
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 [GENOMIC DNA / MRNA].
RX PubMed=2758468; DOI=10.1016/0092-8674(89)90440-6;
RA Kanno H., Huang I.Y., Kan Y.W., Yoshida A.;
RT "Two structural genes on different chromosomes are required for
RT encoding the major subunit of human red cell glucose-6-phosphate
RT dehydrogenase.";
RL Cell 58:595-606(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1661705;
RA Kondoh T., Kanno H., Chang L., Yoshida A.;
RT "Genomic structure and expression of human guanosine monophosphate
RT reductase.";
RL Hum. Genet. 88:219-224(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-256.
RC TISSUE=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 [5]
RP SIMILARITY TO GMP REDUCTASE.
RX PubMed=2570640; DOI=10.1016/0092-8674(89)90498-4;
RA Henikoff S., Smith J.M.;
RT "The human mRNA that provides the N-terminus of chimeric G6PD encodes
RT GMP reductase.";
RL Cell 58:1021-1022(1989).
RN [6]
RP LACK OF ROLE IN G6PD.
RX PubMed=1694726; DOI=10.1016/0092-8674(90)90233-5;
RA Yoshida A., Kan Y.W.;
RT "Origin of 'fused' glucose-6-phosphate dehydrogenase.";
RL Cell 62:11-12(1990).
RN [7]
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).
RN [8]
RP VARIANTS THR-234 AND ILE-256.
RX PubMed=1757097;
RA Kondoh T., Kanno H., Chang L., Yoshida A.;
RT "Identification of common variant alleles of the human guanosine
RT monophosphate reductase gene.";
RL Hum. Genet. 88:225-227(1991).
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 -!- CATALYTIC ACTIVITY: Inosine 5'-phosphate + NH(3) + NADP(+) =
CC guanosine 5'-phosphate + NADPH.
CC -!- SUBUNIT: Homotetramer.
CC -!- POLYMORPHISM: At least two different alleles are known.
CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family.
CC -!- CAUTION: The N-terminus was initially (PubMed:2758468) thought to
CC be fused with glucose-6-phosphate-dehydrogenase (G6PD) protein in
CC vivo. However, PubMed:2570640 showed that it encodes a GMP
CC reductase, and PubMed:1694726 showed that the chimeric protein is
CC an artifact.
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; L35304; AAA52503.1; -; Genomic_DNA.
DR EMBL; M27941; AAA53106.1; -; Genomic_DNA.
DR EMBL; M24470; AAA52498.1; -; mRNA.
DR EMBL; AL009031; CAI21422.1; -; Genomic_DNA.
DR EMBL; AL138883; CAI21422.1; JOINED; Genomic_DNA.
DR EMBL; AL138883; CAI19917.1; -; Genomic_DNA.
DR EMBL; AL009031; CAI19917.1; JOINED; Genomic_DNA.
DR EMBL; BC008281; AAH08281.1; -; mRNA.
DR PIR; B32902; B32902.
DR RefSeq; NP_006868.3; NM_006877.3.
DR UniGene; Hs.484741; -.
DR PDB; 2BLE; X-ray; 1.90 A; A=1-345.
DR PDB; 2BWG; X-ray; 2.40 A; A/B/C/D=1-345.
DR PDBsum; 2BLE; -.
DR PDBsum; 2BWG; -.
DR ProteinModelPortal; P36959; -.
DR SMR; P36959; 2-338.
DR STRING; 9606.ENSP00000259727; -.
DR PhosphoSite; P36959; -.
DR DMDM; 544455; -.
DR PaxDb; P36959; -.
DR PeptideAtlas; P36959; -.
DR PRIDE; P36959; -.
DR DNASU; 2766; -.
DR Ensembl; ENST00000259727; ENSP00000259727; ENSG00000137198.
DR GeneID; 2766; -.
DR KEGG; hsa:2766; -.
DR UCSC; uc003nbs.3; human.
DR CTD; 2766; -.
DR GeneCards; GC06P016238; -.
DR HGNC; HGNC:4376; GMPR.
DR HPA; HPA000904; -.
DR HPA; HPA021476; -.
DR MIM; 139265; gene.
DR neXtProt; NX_P36959; -.
DR PharmGKB; PA28761; -.
DR eggNOG; COG0516; -.
DR HOGENOM; HOG000165756; -.
DR HOVERGEN; HBG051744; -.
DR InParanoid; P36959; -.
DR KO; K00364; -.
DR OMA; SKFPEHT; -.
DR OrthoDB; EOG73804S; -.
DR PhylomeDB; P36959; -.
DR Reactome; REACT_111217; Metabolism.
DR ChiTaRS; GMPR; human.
DR EvolutionaryTrace; P36959; -.
DR GenomeRNAi; 2766; -.
DR NextBio; 10880; -.
DR PRO; PR:P36959; -.
DR Bgee; P36959; -.
DR CleanEx; HS_GMPR; -.
DR Genevestigator; P36959; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0003920; F:GMP reductase activity; TAS:ProtInc.
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 GO; GO:0009409; P:response to cold; TAS:ProtInc.
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; Complete proteome; Metal-binding; NADP; Oxidoreductase;
KW Polymorphism; Potassium; Reference proteome.
FT CHAIN 1 345 GMP reductase 1.
FT /FTId=PRO_0000093723.
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 VARIANT 234 234 A -> T.
FT /FTId=VAR_003969.
FT VARIANT 256 256 F -> I (in dbSNP:rs1042391).
FT /FTId=VAR_003970.
FT STRAND 3 8
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 67
FT HELIX 68 70
FT STRAND 73 75
FT HELIX 82 91
FT HELIX 93 98
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 188 191
FT HELIX 198 210
FT TURN 211 213
FT STRAND 215 220
FT HELIX 225 234
FT STRAND 237 242
FT HELIX 243 245
FT STRAND 251 253
FT STRAND 263 267
FT HELIX 272 277
FT STRAND 285 288
FT STRAND 292 296
FT HELIX 301 319
FT HELIX 324 326
FT HELIX 327 330
FT STRAND 333 335
SQ SEQUENCE 345 AA; 37419 MW; 217E1A5A599CA510 CRC64;
MPRIDADLKL DFKDVLLRPK RSSLKSRAEV DLERTFTFRN SKQTYSGIPI IVANMDTVGT
FEMAAVMSQH SMFTAIHKHY SLDDWKLFAT NHPECLQNVA VSSGSGQNDL EKMTSILEAV
PQVKFICLDV ANGYSEHFVE FVKLVRAKFP EHTIMAGNVV TGEMVEELIL SGADIIKVGV
GPGSVCTTRT KTGVGYPQLS AVIECADSAH GLKGHIISDG GCTCPGDVAK AFGAGADFVM
LGGMFSGHTE CAGEVFERNG RKLKLFYGMS SDTAMNKHAG GVAEYRASEG KTVEVPYKGD
VENTILDILG GLRSTCTYVG AAKLKELSRR ATFIRVTQQH NTVFS
//
MIM
139265
*RECORD*
*FIELD* NO
139265
*FIELD* TI
*139265 GUANOSINE MONOPHOSPHATE REDUCTASE; GMPR
;;GUANOSINE MONOPHOSPHATE REDUCTASE 1; GMPR1;;
read moreGMP REDUCTASE
*FIELD* TX
DESCRIPTION
Guanosine monophosphate reductase (EC 1.7.1.7) catalyzes the
irreversible NADPH-dependent reductive deamination of guanosine
monophosphate (GMP) to inosine monophosphate (IMP). GMPR is able to
convert guanosine nucleotides to the pivotal precursor of both guanine
(G) and adenine (A) nucleotides. It plays an important role in
maintaining the intracellular balance of A and G nucleotides.
CLONING
Beutler et al. (1990) and Mason et al. (1990) presented evidence that a
gene mapped to chromosome 6 by Kanno et al. (1989) was GMP reductase.
Henikoff and Smith (1989) had pointed out similarities between the
sequence described by Kanno et al. (1989) for the chromosome 6-encoded
gene and the sequence of E. coli GMP reductase. Kondoh et al. (1991)
found that the GMPR gene encodes a deduced 345-amino acid protein.
By Northern blot analysis, Deng et al. (2002) detected relatively high
levels of both GMPR1 and GMPR2 (610781) 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.
GENE STRUCTURE
Kondoh et al. (1991) determined that the GMPR gene spans about 50 kb and
contains 9 exons. The gene contains 2 potential Sp1 binding sites within
exon 1, and a functional, atypical polyadenylation signal in exon 9.
MAPPING
By fluorescence in situ hybridization, Murano et al. (1994) mapped the
GMPR gene to 6p23.
HISTORY
Kanno et al. (1989) suggested that red cell G6PD (305900) is a fusion
protein consisting of an NH2-terminus encoded by chromosome 6 and a
COOH-portion coded by an X chromosome. This was subsequently disproved
by Beutler et al. (1990) and by Mason et al. (1990).
*FIELD* AV
.0001
GMP REDUCTASE POLYMORPHISM
GMPR, PHE256ILE
Kondoh et al. (1991) identified a T-to-A substitution at nucleotide 766
of the GMPR gene resulting in substitution of isoleucine for
phenylalanine at amino acid residue 256 in the variant protein. The
frequency of the ile256 variant was thought to be about 30%. A silent
C-to-T change at codon 630 was also found, with a frequency of about
10%; the silent change created an additional restriction cleavage site.
*FIELD* SA
Yoshida and Kan (1990)
*FIELD* RF
1. Beutler, E.; Gelbart, T.; Kuhl, W.: Human red cell glucose-6-phosphate
dehydrogenase: all active enzyme has sequence predicted by the X chromosome-encoded
cDNA. Cell 62: 7-9, 1990.
2. 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.
3. Henikoff, S.; Smith, J. M.: The human mRNA that provides the N-terminus
of chimeric G6PD encodes GMP reductase. Cell 58: 1021-1022, 1989.
4. Kanno, H.; Huang, I.-Y.; Kan, Y. W.; Yoshida, A.: Two structural
genes on different chromosomes are required for encoding the major
subunit of human red cell glucose-6-phosphate dehydrogenase. Cell 58:
595-606, 1989.
5. Kondoh, T.; Kanno, H.; Chang, L.; Yoshida, A.: Identification
of common variant alleles of the human guanosine monophosphate reductase
gene. Hum. Genet. 88: 225-227, 1991.
6. Kondoh, T.; Kanno, H.; Chang, L.; Yoshida, A.: Genomic structure
and expression of human guanosine monophosphate reductase. Hum. Genet. 88:
219-224, 1991.
7. Mason, P. J.; Bautista, J. M.; Vulliamy, T. J.; Turner, N.; Luzzatto,
L.: Human red cell glucose-6-phosphate dehydrogenase is encoded only
on the X chromosome. Cell 62: 9-10, 1990.
8. Murano, I.; Tsukahara, M.; Kajii, T.; Yoshida, A.: Mapping of
the human guanosine monophosphate reductase gene (GMPR) to chromosome
6p23 by fluorescence in situ hybridization. Genomics 19: 179-180,
1994.
9. Yoshida, A.; Kan, Y. W.: Origin of 'fused' glucose-6-phosphate
dehydrogenase. Cell 62: 11-12, 1990.
*FIELD* CD
Victor A. McKusick: 2/13/1991
*FIELD* ED
carol: 02/21/2007
carol: 2/21/2007
carol: 2/8/1994
supermim: 3/16/1992
carol: 1/23/1992
carol: 2/13/1991
*RECORD*
*FIELD* NO
139265
*FIELD* TI
*139265 GUANOSINE MONOPHOSPHATE REDUCTASE; GMPR
;;GUANOSINE MONOPHOSPHATE REDUCTASE 1; GMPR1;;
read moreGMP REDUCTASE
*FIELD* TX
DESCRIPTION
Guanosine monophosphate reductase (EC 1.7.1.7) catalyzes the
irreversible NADPH-dependent reductive deamination of guanosine
monophosphate (GMP) to inosine monophosphate (IMP). GMPR is able to
convert guanosine nucleotides to the pivotal precursor of both guanine
(G) and adenine (A) nucleotides. It plays an important role in
maintaining the intracellular balance of A and G nucleotides.
CLONING
Beutler et al. (1990) and Mason et al. (1990) presented evidence that a
gene mapped to chromosome 6 by Kanno et al. (1989) was GMP reductase.
Henikoff and Smith (1989) had pointed out similarities between the
sequence described by Kanno et al. (1989) for the chromosome 6-encoded
gene and the sequence of E. coli GMP reductase. Kondoh et al. (1991)
found that the GMPR gene encodes a deduced 345-amino acid protein.
By Northern blot analysis, Deng et al. (2002) detected relatively high
levels of both GMPR1 and GMPR2 (610781) 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.
GENE STRUCTURE
Kondoh et al. (1991) determined that the GMPR gene spans about 50 kb and
contains 9 exons. The gene contains 2 potential Sp1 binding sites within
exon 1, and a functional, atypical polyadenylation signal in exon 9.
MAPPING
By fluorescence in situ hybridization, Murano et al. (1994) mapped the
GMPR gene to 6p23.
HISTORY
Kanno et al. (1989) suggested that red cell G6PD (305900) is a fusion
protein consisting of an NH2-terminus encoded by chromosome 6 and a
COOH-portion coded by an X chromosome. This was subsequently disproved
by Beutler et al. (1990) and by Mason et al. (1990).
*FIELD* AV
.0001
GMP REDUCTASE POLYMORPHISM
GMPR, PHE256ILE
Kondoh et al. (1991) identified a T-to-A substitution at nucleotide 766
of the GMPR gene resulting in substitution of isoleucine for
phenylalanine at amino acid residue 256 in the variant protein. The
frequency of the ile256 variant was thought to be about 30%. A silent
C-to-T change at codon 630 was also found, with a frequency of about
10%; the silent change created an additional restriction cleavage site.
*FIELD* SA
Yoshida and Kan (1990)
*FIELD* RF
1. Beutler, E.; Gelbart, T.; Kuhl, W.: Human red cell glucose-6-phosphate
dehydrogenase: all active enzyme has sequence predicted by the X chromosome-encoded
cDNA. Cell 62: 7-9, 1990.
2. 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.
3. Henikoff, S.; Smith, J. M.: The human mRNA that provides the N-terminus
of chimeric G6PD encodes GMP reductase. Cell 58: 1021-1022, 1989.
4. Kanno, H.; Huang, I.-Y.; Kan, Y. W.; Yoshida, A.: Two structural
genes on different chromosomes are required for encoding the major
subunit of human red cell glucose-6-phosphate dehydrogenase. Cell 58:
595-606, 1989.
5. Kondoh, T.; Kanno, H.; Chang, L.; Yoshida, A.: Identification
of common variant alleles of the human guanosine monophosphate reductase
gene. Hum. Genet. 88: 225-227, 1991.
6. Kondoh, T.; Kanno, H.; Chang, L.; Yoshida, A.: Genomic structure
and expression of human guanosine monophosphate reductase. Hum. Genet. 88:
219-224, 1991.
7. Mason, P. J.; Bautista, J. M.; Vulliamy, T. J.; Turner, N.; Luzzatto,
L.: Human red cell glucose-6-phosphate dehydrogenase is encoded only
on the X chromosome. Cell 62: 9-10, 1990.
8. Murano, I.; Tsukahara, M.; Kajii, T.; Yoshida, A.: Mapping of
the human guanosine monophosphate reductase gene (GMPR) to chromosome
6p23 by fluorescence in situ hybridization. Genomics 19: 179-180,
1994.
9. Yoshida, A.; Kan, Y. W.: Origin of 'fused' glucose-6-phosphate
dehydrogenase. Cell 62: 11-12, 1990.
*FIELD* CD
Victor A. McKusick: 2/13/1991
*FIELD* ED
carol: 02/21/2007
carol: 2/21/2007
carol: 2/8/1994
supermim: 3/16/1992
carol: 1/23/1992
carol: 2/13/1991