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Protein

GMP reductase 2

Gene

GMPR2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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 (PubMed:12009299, PubMed:12669231, PubMed:16359702, PubMed:22037469). Plays a role in modulating cellular differentiation (PubMed:12669231).UniRule annotation4 Publications

Catalytic activityi

Inosine 5'-phosphate + NH3 + NADP+ = guanosine 5'-phosphate + NADPH.UniRule annotation3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei78 – 781NADPUniRule annotation1 Publication
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 annotation1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi26 – 272NADP; shared with neighboring subunitUniRule annotation1 Publication
Nucleotide bindingi129 – 1313NADPUniRule annotation1 Publication
Nucleotide bindingi180 – 1812NADPUniRule annotation1 Publication
Nucleotide bindingi285 – 2862NADPUniRule annotation1 Publication
Nucleotide bindingi314 – 3174NADP; shared with neighboring subunitUniRule annotation1 Publication

GO - Molecular functioni

  • GMP reductase activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW

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

BRENDAi1.7.1.7. 2681.
ReactomeiR-HSA-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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:4377. GMPR2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi186 – 1861C → A: Loss of enzyme activity. 2 Publications
Mutagenesisi188 – 1881T → A: Loss of enzyme activity. 1 Publication
Mutagenesisi289 – 2891E → Q: Loss of enzyme activity. 1 Publication

Organism-specific databases

PharmGKBiPA28762.

Polymorphism and mutation databases

BioMutaiGMPR2.
DMDMi25008511.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 348348GMP reductase 2PRO_0000093726Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei291 – 2911N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9P2T1.
MaxQBiQ9P2T1.
PaxDbiQ9P2T1.
PRIDEiQ9P2T1.

PTM databases

iPTMnetiQ9P2T1.
PhosphoSiteiQ9P2T1.

Expressioni

Tissue specificityi

Highly expressed in heart, skeletal muscle, kidney, brain, liver, prostate, spleen, placenta, testis and ovary. Low expression in colon, thymus and peripheral blood leukocytes.2 Publications

Gene expression databases

BgeeiQ9P2T1.
CleanExiHS_GMPR2.
ExpressionAtlasiQ9P2T1. baseline and differential.
GenevisibleiQ9P2T1. HS.

Organism-specific databases

HPAiHPA000904.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation2 Publications

Protein-protein interaction databases

BioGridi119443. 7 interactions.
IntActiQ9P2T1. 2 interactions.
STRINGi9606.ENSP00000392859.

Structurei

Secondary structure

1
348
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 97Combined sources
Helixi12 – 143Combined sources
Beta strandi15 – 173Combined sources
Helixi27 – 293Combined sources
Beta strandi34 – 374Combined sources
Turni39 – 413Combined sources
Beta strandi44 – 474Combined sources
Beta strandi50 – 523Combined sources
Turni56 – 583Combined sources
Helixi61 – 699Combined sources
Beta strandi73 – 753Combined sources
Helixi82 – 9110Combined sources
Helixi93 – 953Combined sources
Beta strandi99 – 1035Combined sources
Helixi107 – 11913Combined sources
Beta strandi125 – 1295Combined sources
Helixi136 – 14813Combined sources
Beta strandi152 – 1598Combined sources
Helixi162 – 1709Combined sources
Beta strandi174 – 1785Combined sources
Helixi188 – 1925Combined sources
Helixi198 – 21114Combined sources
Beta strandi215 – 2206Combined sources
Helixi225 – 2339Combined sources
Beta strandi237 – 2426Combined sources
Turni243 – 2475Combined sources
Beta strandi248 – 2514Combined sources
Beta strandi255 – 2584Combined sources
Beta strandi261 – 2677Combined sources
Beta strandi269 – 2713Combined sources
Helixi272 – 2787Combined sources
Beta strandi279 – 2813Combined sources
Turni283 – 2853Combined sources
Beta strandi286 – 2883Combined sources
Beta strandi292 – 2965Combined sources
Helixi301 – 31919Combined sources
Helixi324 – 3263Combined sources
Helixi327 – 3304Combined sources
Beta strandi333 – 3353Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A7RX-ray3.00A/B/C/D1-348[»]
2BZNX-ray2.15A/B/C/D/E/F/G/H10-341[»]
2C6QX-ray1.70A/B/C/D/E/F/G/H10-341[»]
ProteinModelPortaliQ9P2T1.
SMRiQ9P2T1. Positions 10-337.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9P2T1.

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.
InParanoidiQ9P2T1.
KOiK00364.
OrthoDBiEOG73804S.
PhylomeDBiQ9P2T1.
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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9P2T1-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPHIDNDVKL DFKDVLLRPK RSTLKSRSEV DLTRSFSFRN SKQTYSGVPI
60 70 80 90 100
IAANMDTVGT FEMAKVLCKF SLFTAVHKHY SLVQWQEFAG QNPDCLEHLA
110 120 130 140 150
ASSGTGSSDF 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 SEMAMKKYAG GVAEYRASEG KTVEVPFKGD
310 320 330 340
VEHTIRDILG GIRSTCTYVG AAKLKELSRR TTFIRVTQQV NPIFSEAC
Length:348
Mass (Da):37,874
Last modified:October 1, 2000 - v1
Checksum:iE7812A754C433E51
GO
Isoform 2 (identifier: Q9P2T1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MTSCLPALRFIATPRLSAM

Show »
Length:366
Mass (Da):39,805
Checksum:i009CF162967F2112
GO
Isoform 3 (identifier: Q9P2T1-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     70-97: Missing.

Note: No experimental confirmation available.
Show »
Length:320
Mass (Da):34,597
Checksum:iA54872F5C9635EAC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti91 – 911Q → R in CAG33437 (Ref. 5) Curated
Sequence conflicti200 – 2001S → G in CAG33437 (Ref. 5) Curated
Sequence conflicti223 – 2231S → N in CAG33437 (Ref. 5) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti242 – 2421G → D.
Corresponds to variant rs34354104 [ dbSNP | Ensembl ].
VAR_049602

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MTSCLPALRFIATPRLSAM in isoform 2. 1 PublicationVSP_041459
Alternative sequencei70 – 9728Missing in isoform 3. 1 PublicationVSP_054585Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF419346 mRNA. Translation: AAN32701.1.
AF135159 mRNA. Translation: AAG09132.1.
AB032903 mRNA. Translation: BAA93080.1.
BX161436 mRNA. Translation: CAD61908.1.
BX247993 mRNA. Translation: CAD62327.1.
CR457156 mRNA. Translation: CAG33437.1.
AL096870 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW66051.1.
CH471078 Genomic DNA. Translation: EAW66053.1.
CH471078 Genomic DNA. Translation: EAW66054.1.
CH471078 Genomic DNA. Translation: EAW66056.1.
CH471078 Genomic DNA. Translation: EAW66057.1.
BC008021 mRNA. Translation: AAH08021.2.
BC009832 mRNA. Translation: AAH09832.1.
BC093039 mRNA. Translation: AAH93039.1.
CCDSiCCDS41935.1. [Q9P2T1-1]
CCDS45087.1. [Q9P2T1-2]
CCDS61419.1. [Q9P2T1-3]
RefSeqiNP_001002000.1. NM_001002000.2. [Q9P2T1-1]
NP_001002001.1. NM_001002001.2. [Q9P2T1-1]
NP_001002002.1. NM_001002002.2. [Q9P2T1-1]
NP_001269950.1. NM_001283021.1.
NP_001269951.1. NM_001283022.1.
NP_001269952.1. NM_001283023.1. [Q9P2T1-3]
NP_057660.2. NM_016576.4. [Q9P2T1-2]
UniGeneiHs.368855.

Genome annotation databases

EnsembliENST00000355299; ENSP00000347449; ENSG00000100938. [Q9P2T1-1]
ENST00000399440; ENSP00000382369; ENSG00000100938. [Q9P2T1-1]
ENST00000420554; ENSP00000392859; ENSG00000100938. [Q9P2T1-2]
ENST00000456667; ENSP00000405743; ENSG00000100938. [Q9P2T1-3]
ENST00000559836; ENSP00000453299; ENSG00000100938. [Q9P2T1-1]
GeneIDi51292.
KEGGihsa:51292.
UCSCiuc001wnr.5. human. [Q9P2T1-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF419346 mRNA. Translation: AAN32701.1.
AF135159 mRNA. Translation: AAG09132.1.
AB032903 mRNA. Translation: BAA93080.1.
BX161436 mRNA. Translation: CAD61908.1.
BX247993 mRNA. Translation: CAD62327.1.
CR457156 mRNA. Translation: CAG33437.1.
AL096870 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW66051.1.
CH471078 Genomic DNA. Translation: EAW66053.1.
CH471078 Genomic DNA. Translation: EAW66054.1.
CH471078 Genomic DNA. Translation: EAW66056.1.
CH471078 Genomic DNA. Translation: EAW66057.1.
BC008021 mRNA. Translation: AAH08021.2.
BC009832 mRNA. Translation: AAH09832.1.
BC093039 mRNA. Translation: AAH93039.1.
CCDSiCCDS41935.1. [Q9P2T1-1]
CCDS45087.1. [Q9P2T1-2]
CCDS61419.1. [Q9P2T1-3]
RefSeqiNP_001002000.1. NM_001002000.2. [Q9P2T1-1]
NP_001002001.1. NM_001002001.2. [Q9P2T1-1]
NP_001002002.1. NM_001002002.2. [Q9P2T1-1]
NP_001269950.1. NM_001283021.1.
NP_001269951.1. NM_001283022.1.
NP_001269952.1. NM_001283023.1. [Q9P2T1-3]
NP_057660.2. NM_016576.4. [Q9P2T1-2]
UniGeneiHs.368855.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A7RX-ray3.00A/B/C/D1-348[»]
2BZNX-ray2.15A/B/C/D/E/F/G/H10-341[»]
2C6QX-ray1.70A/B/C/D/E/F/G/H10-341[»]
ProteinModelPortaliQ9P2T1.
SMRiQ9P2T1. Positions 10-337.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119443. 7 interactions.
IntActiQ9P2T1. 2 interactions.
STRINGi9606.ENSP00000392859.

PTM databases

iPTMnetiQ9P2T1.
PhosphoSiteiQ9P2T1.

Polymorphism and mutation databases

BioMutaiGMPR2.
DMDMi25008511.

Proteomic databases

EPDiQ9P2T1.
MaxQBiQ9P2T1.
PaxDbiQ9P2T1.
PRIDEiQ9P2T1.

Protocols and materials databases

DNASUi51292.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000355299; ENSP00000347449; ENSG00000100938. [Q9P2T1-1]
ENST00000399440; ENSP00000382369; ENSG00000100938. [Q9P2T1-1]
ENST00000420554; ENSP00000392859; ENSG00000100938. [Q9P2T1-2]
ENST00000456667; ENSP00000405743; ENSG00000100938. [Q9P2T1-3]
ENST00000559836; ENSP00000453299; ENSG00000100938. [Q9P2T1-1]
GeneIDi51292.
KEGGihsa:51292.
UCSCiuc001wnr.5. human. [Q9P2T1-1]

Organism-specific databases

CTDi51292.
GeneCardsiGMPR2.
HGNCiHGNC:4377. GMPR2.
HPAiHPA000904.
MIMi610781. gene.
neXtProtiNX_Q9P2T1.
PharmGKBiPA28762.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2550. Eukaryota.
COG0516. LUCA.
GeneTreeiENSGT00530000062923.
HOGENOMiHOG000165756.
HOVERGENiHBG051744.
InParanoidiQ9P2T1.
KOiK00364.
OrthoDBiEOG73804S.
PhylomeDBiQ9P2T1.
TreeFamiTF300378.

Enzyme and pathway databases

BRENDAi1.7.1.7. 2681.
ReactomeiR-HSA-74217. Purine salvage.

Miscellaneous databases

ChiTaRSiGMPR2. human.
EvolutionaryTraceiQ9P2T1.
GenomeRNAii51292.
NextBioi54555.
PROiQ9P2T1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9P2T1.
CleanExiHS_GMPR2.
ExpressionAtlasiQ9P2T1. baseline and differential.
GenevisibleiQ9P2T1. HS.

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

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
    Tissue: Fetal brain.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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] (ISOFORM 1).
  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] (ISOFORMS 1 AND 3).
    Tissue: Placenta and T-cell.
  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] (ISOFORM 1).
  6. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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] (ISOFORMS 1 AND 2).
    Tissue: Lung and Placenta.
  9. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-291, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. "Crystal structure of human guanosine monophosphate reductase 2 (GMPR2) in complex with GMP."
    Li J., Wei Z., Zheng M., Gu X., Deng Y., Qiu R., Chen F., Ji C., Gong W., Xie Y., Mao Y.
    J. Mol. Biol. 355:980-988(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH GMP, CATALYTIC ACTIVITY, FUNCTION, ACTIVE SITE, SUBUNIT, MUTAGENESIS OF CYS-186.
  13. "Cofactor mobility determines reaction outcome in the IMPDH and GMPR (beta-alpha)8 barrel enzymes."
    Patton G.C., Stenmark P., Gollapalli D.R., Sevastik R., Kursula P., Flodin S., Schuler H., Swales C.T., Eklund H., Himo F., Nordlund P., Hedstrom L.
    Nat. Chem. Biol. 7:950-958(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 10-341 IN COMPLEX WITH IMP AND NADP, CATALYTIC ACTIVITY, FUNCTION, ACTIVE SITE, SUBUNIT, MUTAGENESIS OF CYS-186; THR-188 AND GLU-289.

Entry informationi

Entry nameiGMPR2_HUMAN
AccessioniPrimary (citable) accession number: Q9P2T1
Secondary accession number(s): D3DS66
, Q567T0, Q6IAJ8, Q86T14
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: October 1, 2000
Last modified: March 16, 2016
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.