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Protein Page:
APRT (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
APRT Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. Defects in APRT are the cause of adenine phosphoribosyltransferase deficiency (APRTD); also known as 2,8-dihydroxyadenine urolithiasis. An enzymatic deficiency that can lead to urolithiasis and renal failure. Patients have 2,8-dihydroxyadenine (DHA) urinary stones. Belongs to the purine/pyrimidine phosphoribosyltransferase family. Note: This description may include information from UniProtKB.
Protein type: EC 2.4.2.7; Transferase; Nucleotide Metabolism - purine
Cellular Component: cytoplasm; nucleolus; cytosol; nucleus
Molecular Function: adenine binding; adenine phosphoribosyltransferase activity; AMP binding
Biological Process: lactation; grooming behavior; cellular response to insulin stimulus; nucleobase, nucleoside and nucleotide metabolic process; adenine salvage; purine ribonucleoside salvage; purine base metabolic process; purine salvage
Reference #:  P07741 (UniProtKB)
Alt. Names/Synonyms: Adenine phosphoribosyltransferase; AMP; AMP diphosphorylase; AMP pyrophosphorylase; APRT; APT; DKFZp686D13177; MGC125856; MGC125857; MGC129961; transphosphoribosidase
Gene Symbols: APRT
Molecular weight: 19,608 Da
Basal Isoelectric point: 5.78  Predict pI for various phosphorylation states
Select Structure to View Below

APRT

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 1 A2 ______MADsELQLV
0 1 S4-p ____MADsELQLVEQ
0 27 S15-p LVEQRIRsFPDFPTP
0 4 S30-p GVVFRDIsPVLkDPA
0 23 K34-ub RDIsPVLkDPAsFRA
0 1 S38-p PVLkDPAsFRAAIGL
0 1 R57 LKATHGGRIDyIAGL
0 6 Y60-p THGGRIDyIAGLDsR
0 4 S66-p DyIAGLDsRGFLFGP
0 1 T96-p RGKLPGPtLWASYSL
0 12 K107 SYSLEYGKAELEIQk
0 2 K114-ac KAELEIQkDALEPGQ
0 7 K114-ub KAELEIQkDALEPGQ
0 1 T135-p DLLATGGtMNAACEL
0 7 K167-ub TSLKGREkLAPVPFF
  mouse

 
S2-p ______MsEPELKLV
P4 ____MsEPELKLVAR
S15-p LVARRIRsFPDFPIP
S30 GVLFRDISPLLkDPD
K34-ub RDISPLLkDPDSFRA
S38 PLLkDPDSFRASIRL
K57-ub LKSTHSGkIDYIAGL
Y60 THSGkIDYIAGLDSR
S66 DYIAGLDSRGFLFGP
T96 QGKLPGPTVSASYSL
K107-ub SYSLEYGkAELEIQk
K114-ac kAELEIQkDALEPGQ
K114 kAELEIQKDALEPGQ
T135 DLLATGGTMFAACDL
R167 TSLKGRERLGPIPFF
  rat

 
S2 ______MSESELQLV
S4 ____MSESELQLVAR
S15-p LVARRIRsFPDFPIP
S30 GVLFRDISPLLKDPD
K34 RDISPLLKDPDSFRA
S38 PLLKDPDSFRASIRL
K57 LKSTHGGKIDyIAGL
Y60-p THGGKIDyIAGLDsR
S66-p DyIAGLDsRGFLFGP
T96 RGKLPGPTVSASYSL
K107 SYSLEYGKAELEIQK
K114 KAELEIQKDALEPGQ
K114 KAELEIQKDALEPGQ
T135 DLLATGGTMCAACEL
K167 TSLKGREKLGPVPFF
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