Reviewed, UniProtKB/Swiss-Prot Q9P2T1 (GMPR2_HUMAN)

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	348 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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 diversity	Polymorphism
Ligand	Metal-binding NADP Potassium
Molecular function	Oxidoreductase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	nucleotide metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	GMP 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 348

348

GMP reductase 2

PRO_0000093726

Regions

Nucleotide binding

108 – 131

24

NADP By similarity

Sites

Active site

186

1

Thioimidate intermediate By similarity

Metal binding

181

1

Potassium; via carbonyl oxygen By similarity

Metal binding

183

1

Potassium; via carbonyl oxygen By similarity

Binding site

219

1

NADP By similarity

Natural variations

Natural variant

242

1

G → D: dbSNP rs34354104.

VAR_049602

Experimental info

Sequence conflict

91

1

Q → R in CAG33437. Ref.5

Sequence conflict

200

1

S → G in CAG33437. Ref.5

Sequence conflict

223

1

S → N in CAG33437. Ref.5

Secondary structure

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348

Helix Strand Turn

Details...

Beta strand

3 – 9

7

Helix

12 – 14

3

Beta strand

15 – 17

3

Beta strand

34 – 37

4

Turn

39 – 41

3

Beta strand

44 – 47

4

Beta strand

50 – 52

3

Turn

56 – 58

3

Helix

61 – 69

9

Beta strand

73 – 75

3

Helix

82 – 91

10

Helix

93 – 95

3

Beta strand

99 – 103

5

Helix

107 – 119

13

Beta strand

125 – 129

5

Helix

136 – 148

13

Beta strand

152 – 159

8

Helix

162 – 170

9

Beta strand

174 – 178

5

Helix

188 – 192

5

Helix

198 – 210

13

Turn

211 – 213

3

Beta strand

215 – 220

6

Helix

225 – 233

9

Beta strand

237 – 242

6

Turn

243 – 247

5

Beta strand

255 – 258

4

Beta strand

261 – 267

7

Helix

272 – 277

6

Beta strand

292 – 296

5

Helix

301 – 319

19

Helix

324 – 326

3

Turn

327 – 330

4

Beta strand

333 – 335

3

Sequences

	Sequence		Length	Mass (Da)
	Q9P2T1-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: E7812A754C433E51	FASTA	348	37,874
	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

References

	« Hide 'large scale' referencesShow '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

EMBLGenBankDDBJ

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.

IPI

IPI00009844.

RefSeq

NP_001002000.1.
NP_001002001.1.
NP_001002002.1.
NP_057660.2.

UniGene

Hs.368855

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2A7R	X-ray	3.00	A/B/C/D	1-348	[»]
2BZN	X-ray	2.15	A/B/C/D/E/F/G/H	10-341	[»]
2C6Q	X-ray	1.70	A/B/C/D/E/F/G/H	10-341	[»]

ModBase

Search...

Proteomic databases

PRIDE

Q9P2T1.

Genome annotation databases

Ensembl

ENSG00000100938. Homo sapiens. [Contig view]

GeneID

51292.

KEGG

hsa:51292.

NMPDR

fig|9606.3.peg.9389.

Organism-specific databases

GeneCards

GC14P023771.

H-InvDB

HIX0011563.

HGNC

HGNC:4377. GMPR2.

HPA

HPA000904.

MIM

610781. gene.

PharmGKB

PA28762.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q9P2T1.

OMA

Q9P2T1. QNPDCLE.

Enzyme and pathway databases

BRENDA

1.7.1.7. 247.

Gene expression databases

Bgee

Q9P2T1.

CleanEx

HS_GMPR2.

Family and domain databases

InterPro

IPR013785. Aldolase_TIM.
IPR005993. GMP_reduct1.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]

Gene3D

G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.

Pfam

PF00478. IMPDH. 1 hit.
[Graphical view]

PIRSF

PIRSF000235. GMP_reductase. 1 hit.

TIGRFAMs

TIGR01305. GMP_reduct_1. 1 hit.

PROSITE

PS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

54555.

SOURCE

Search...

Entry information

Entry name

GMPR2_HUMAN

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)