Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  GMP reductase 2  

UniProtKB / Swiss-Prot ID :  GMPR2_HUMAN

Gene Name (Synonyms) : 
GMPR2  

Species :  Homo sapiens (Human). 

Subcellular Localization :   

Protein 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. 

Protein Sequence MPHIDNDVKLDFKDVLLRPKRSTLKSRSEVDLTRSFSFRNSKQTYSGVPIIAANMDTVGTFEMAKVLCKF...
Predicted Secondary Structure CCCCCCCCCCCCCCEEECCCCCEECCCCCCEEEEEECCEEECEEECCCCEEECCCCCCCCHHHHHHHHHC...
Protein Variant
LocationDescription
242G -> D (in dbSNP:rs34354104). VAR_049602
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
13N6-acetyllysineKLDFKDVLL
CCCCCCEEE
46.74HPRD
Link
13N6-acetyllysineKLDFKDVLL
CCCCCCEEE
46.74Phosphositeplus
Link
13N6-acetyllysine.KLDFKDVLL
CCCCCCEEE
46.74UniProtKB
Link
291N6-acetyllysineASEGKTVEV
CCCCEEEEE
45.40HPRD
Link
291N6-acetyllysineASEGKTVEV
CCCCEEEEE
45.40Phosphositeplus
Link
291N6-acetyllysine.ASEGKTVEV
CCCCEEEEE
45.40UniProtKB
Link
318PhosphotyrosineSTCTYVGAA
HHHHHCCCC
10.07Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
PUR9_HUMANENSP00000347449STRING
AMPD3_HUMANENSP00000347449STRING
AMPD2_HUMANENSP00000347449STRING
GUAA_HUMANENSP00000347449STRING
ENTP3_HUMANENSP00000347449STRING
CANT1_HUMANENSP00000347449STRING
KGUA_HUMANENSP00000347449STRING
IMDH2_HUMANENSP00000347449STRING
ENTP5_HUMANENSP00000347449STRING
ENTP8_HUMANENSP00000347449STRING
ENTP8_HUMANENSP00000347449STRING
IMDH1_HUMANENSP00000347449STRING
ENTP4_HUMANENSP00000347449STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-13 AND LYS-291, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures