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Protein

GMP reductase 2

Gene

Gmpr2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 (Probable). Plays a role in modulating cellular differentiation (By similarity).UniRule annotationBy similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei78 – 781NADPUniRule annotation
Metal bindingi181 – 1811Potassium; via carbonyl oxygenUniRule annotation
Metal bindingi183 – 1831Potassium; via carbonyl oxygenUniRule annotation
Active sitei186 – 1861Thioimidate intermediateUniRule annotation
Metal bindingi186 – 1861Potassium; via carbonyl oxygenUniRule annotation
Active sitei188 – 1881Proton donor/acceptorUniRule annotation
Metal bindingi189 – 1891PotassiumUniRule annotation
Binding sitei269 – 2691NADP; via carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi26 – 272NADP; shared with neighboring subunitUniRule annotation
Nucleotide bindingi129 – 1313NADPUniRule annotation
Nucleotide bindingi180 – 1812NADPUniRule annotation
Nucleotide bindingi285 – 2862NADPUniRule annotation
Nucleotide bindingi314 – 3174NADP; shared with neighboring subunitUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Purine metabolism

Keywords - Ligandi

Metal-binding, NADP, Potassium

Enzyme and pathway databases

ReactomeiR-MMU-74217. Purine salvage.

Names & Taxonomyi

Protein namesi
Recommended name:
GMP reductase 2UniRule annotation (EC:1.7.1.7UniRule annotation)
Short name:
GMPR 2UniRule annotation
Alternative name(s):
Guanosine 5'-monophosphate oxidoreductase 2UniRule annotation
Short name:
Guanosine monophosphate reductase 2UniRule annotation
Gene namesi
Name:Gmpr2UniRule annotation
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1917903. Gmpr2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 348348GMP reductase 2PRO_0000093727Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei291 – 2911N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ99L27.
MaxQBiQ99L27.
PaxDbiQ99L27.
PRIDEiQ99L27.

PTM databases

iPTMnetiQ99L27.
PhosphoSiteiQ99L27.

Expressioni

Gene expression databases

BgeeiQ99L27.
CleanExiMM_GMPR2.
GenevisibleiQ99L27. MM.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000002397.

Structurei

3D structure databases

ProteinModelPortaliQ99L27.
SMRiQ99L27. Positions 10-337.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni219 – 2213GMP bindingUniRule annotation
Regioni242 – 2432GMP bindingUniRule annotation
Regioni268 – 2703GMP bindingUniRule annotation
Regioni286 – 2905GMP bindingUniRule annotation

Sequence similaritiesi

Belongs to the IMPDH/GMPR family. GuaC type 1 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiKOG2550. Eukaryota.
COG0516. LUCA.
GeneTreeiENSGT00530000062923.
HOGENOMiHOG000165756.
HOVERGENiHBG051744.
InParanoidiQ99L27.
KOiK00364.
OMAiCSCAGDV.
OrthoDBiEOG73804S.
TreeFamiTF300378.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00596. GMP_reduct_type1.
InterProiIPR013785. Aldolase_TIM.
IPR005993. GMPR.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
PfamiPF00478. IMPDH. 1 hit.
[Graphical view]
PIRSFiPIRSF000235. GMP_reductase. 1 hit.
TIGRFAMsiTIGR01305. GMP_reduct_1. 1 hit.
PROSITEiPS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q99L27-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPHIDNDVKL DFKDVLLRPK RSTLKSRSEV ELTRSFSFRN SKQMYSGIPV
60 70 80 90 100
IAANMDTVGT FEMARVLCKF SLFTAIHKHY SIHQWQEFAS QNPDCLECLA
110 120 130 140 150
ASSGSGSADF EQLEQILEAI PQVKYICLDV ANGYSEHFVE FVKDVRKRFP
160 170 180 190 200
QHTIMAGNVV TGEMVEELIL SGADIIKVGI GPGSVCTTRK KTGVGYPQLS
210 220 230 240 250
AVMECADAAH GLKGHIISDG GCSCPGDVAK AFGAGADFVM LGGMLAGHSE
260 270 280 290 300
SGGELIERDG KKYKLFYGMS SEMAMKKYSG GVAEYRASEG KIVEVPFKGD
310 320 330 340
VEHTIRDILG GIRSTCTYVG AAKLKELSRR TTFIRVTQQV NPIFSNSQ
Length:348
Mass (Da):38,019
Last modified:July 27, 2011 - v2
Checksum:i83E6998193D22FC0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti105 – 1051S → T in AAH03886 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK031004 mRNA. Translation: BAC27211.1.
AK075772 mRNA. Translation: BAC35946.1.
CH466535 Genomic DNA. Translation: EDL36258.1.
BC003886 mRNA. Translation: AAH03886.1.
BC024109 mRNA. Translation: AAH24109.1.
CCDSiCCDS27124.1.
RefSeqiNP_818773.1. NM_177992.2.
XP_006518429.1. XM_006518366.1.
UniGeneiMm.390685.
Mm.486705.

Genome annotation databases

EnsembliENSMUST00000002397; ENSMUSP00000002397; ENSMUSG00000002326.
GeneIDi105446.
KEGGimmu:105446.
UCSCiuc007uae.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK031004 mRNA. Translation: BAC27211.1.
AK075772 mRNA. Translation: BAC35946.1.
CH466535 Genomic DNA. Translation: EDL36258.1.
BC003886 mRNA. Translation: AAH03886.1.
BC024109 mRNA. Translation: AAH24109.1.
CCDSiCCDS27124.1.
RefSeqiNP_818773.1. NM_177992.2.
XP_006518429.1. XM_006518366.1.
UniGeneiMm.390685.
Mm.486705.

3D structure databases

ProteinModelPortaliQ99L27.
SMRiQ99L27. Positions 10-337.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000002397.

PTM databases

iPTMnetiQ99L27.
PhosphoSiteiQ99L27.

Proteomic databases

EPDiQ99L27.
MaxQBiQ99L27.
PaxDbiQ99L27.
PRIDEiQ99L27.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000002397; ENSMUSP00000002397; ENSMUSG00000002326.
GeneIDi105446.
KEGGimmu:105446.
UCSCiuc007uae.1. mouse.

Organism-specific databases

CTDi51292.
MGIiMGI:1917903. Gmpr2.

Phylogenomic databases

eggNOGiKOG2550. Eukaryota.
COG0516. LUCA.
GeneTreeiENSGT00530000062923.
HOGENOMiHOG000165756.
HOVERGENiHBG051744.
InParanoidiQ99L27.
KOiK00364.
OMAiCSCAGDV.
OrthoDBiEOG73804S.
TreeFamiTF300378.

Enzyme and pathway databases

ReactomeiR-MMU-74217. Purine salvage.

Miscellaneous databases

PROiQ99L27.
SOURCEiSearch...

Gene expression databases

BgeeiQ99L27.
CleanExiMM_GMPR2.
GenevisibleiQ99L27. MM.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00596. GMP_reduct_type1.
InterProiIPR013785. Aldolase_TIM.
IPR005993. GMPR.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
PfamiPF00478. IMPDH. 1 hit.
[Graphical view]
PIRSFiPIRSF000235. GMP_reductase. 1 hit.
TIGRFAMsiTIGR01305. GMP_reduct_1. 1 hit.
PROSITEiPS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Pancreas and Thymus.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Kidney, Lung, Spleen and Testis.

Entry informationi

Entry nameiGMPR2_MOUSE
AccessioniPrimary (citable) accession number: Q99L27
Secondary accession number(s): Q542X2, Q8R1T5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.