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Protein Page:
GRHPR (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
GRHPR Enzyme with hydroxy-pyruvate reductase, glyoxylate reductase and D-glycerate dehydrogenase enzymatic activities. Reduces hydroxypyruvate to D-glycerate, glyoxylate to glycolate oxidizes D-glycerate to hydroxypyruvate. Defects in GRHPR are the cause of hyperoxaluria primary type 2 (HP2); also known as primary hyperoxaluria type II (PH2). HP2 is a disorder where the main clinical manifestation is calcium oxalate nephrolithiasis though chronic as well as terminal renal insufficiency has been described. It is characterized by an elevated urinary excretion of oxalate and L- glycerate. Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. Note: This description may include information from UniProtKB.
Protein type: EC 1.1.1.81; Oxidoreductase; Carbohydrate Metabolism - glyoxylate and dicarboxylate; Carbohydrate Metabolism - pyruvate; EC 1.1.1.79
Cellular Component: peroxisomal matrix; cytoplasm; cytosol
Molecular Function: glyoxylate reductase (NADP) activity; protein homodimerization activity; carboxylic acid binding; hydroxypyruvate reductase activity; NAD binding; glycerate dehydrogenase activity
Biological Process: dicarboxylic acid metabolic process; glyoxylate metabolic process; metabolic process; excretion; protein oligomerization
Reference #:  Q9UBQ7 (UniProtKB)
Alt. Names/Synonyms: GLXR; glycerate-2-dehydrogenase; GLYD; Glyoxylate reductase/hydroxypyruvate reductase; GRHPR; PH2
Gene Symbols: GRHPR
Molecular weight: 35,668 Da
Basal Isoelectric point: 7.01  Predict pI for various phosphorylation states
Select Structure to View Below

GRHPR

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 2 S36-p CEVEQWDsDEPIPAK
0 43 K65-ac LLSDHVDkRILDAAG
0 1 R66 LSDHVDkRILDAAGA
0 1 T80-p ANLKVIStMSVGIDH
0 2 K94-ac HLALDEIkKRGIRVG
0 1 K94 HLALDEIKKRGIRVG
0 1 K94 HLALDEIKKRGIRVG
0 1 K173 QAIARRLKPFGVQRF
0 19 Y255-p VVNQDDLyQALASGk
0 1 K262-ub yQALASGkIAAAGLD
0 1 T271-p AAAGLDVtsPEPLPT
0 1 S272-p AAGLDVtsPEPLPTN
0 1 T298-p LPHIGSAtHRTRNtM
0 1 R300 HIGSAtHRTRNtMsL
0 1 T304-p AtHRTRNtMsLLAAN
0 1 S306-p HRTRNtMsLLAANNL
0 2 K327-ac EPMPSELkL______
  mouse

 
S36 CEVEQWNSDDPIPRK
K65 RLSDRVDKkLLDAAG
K66-ac LSDRVDKkLLDAAGA
T80 ANLRVISTLSVGVDH
K94-ac HLALDEIkKRGIRVG
K94-ub HLALDEIkKRGIRVG
K94-sc HLALDEIkKRGIRVG
K173-ub QAIARRLkPFGVQRF
Y255 VVNQEDLYQALASGQ
Q262 YQALASGQIAAAGLD
T271 AAAGLDVTTPEPLPP
T272 AAGLDVTTPEPLPPS
T298 LPHIGSATYkTRNTM
K300-ub HIGSATYkTRNTMSL
T304 ATYkTRNTMSLLAAN
S306 YkTRNTMSLLAANNL
K327 EAMPSELKL______
  rat

 
S43 CEVEQWNSDDPIPSK
K72-ac RLSDRVDkkLLDAAG
K73-ac LSDRVDkkLLDAAGA
T87 ANLRVISTLSVGVDH
K101-ac HLALDEIkKRGIRVG
K101 HLALDEIKKRGIRVG
K101 HLALDEIKKRGIRVG
K180 QAIARRLKPFGVQRF
Y262 VVNQEDLYQALASGQ
Q269 YQALASGQIAAAGLD
T278 AAAGLDVTTPEPLPP
T279 AAGLDVTTPEPLPPS
T305-p LPHIGSAtYKTRNTM
K307 HIGSAtYKTRNTMSL
T311 AtYKTRNTMSLLAAN
S313 YKTRNTMSLLAANNL
K334 EPMPSELKL______
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