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APRT (human)

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: Transferase; Nucleotide Metabolism - purine; EC 2.4.2.7 Cellular Component: cytoplasm; nucleolus; cytosol; nucleus Molecular Function: adenine binding; adenine phosphoribosyltransferase activity; AMP binding Biological Process: lactation; grooming behavior; nucleobase, nucleoside and nucleotide metabolic process; adenine salvage; purine ribonucleoside salvage; purine salvage; purine base metabolic process 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 1OPU - A=1-180 (human) 1ORE - A=1-180 (human) 1ZN7 - A/B=1-180 (human) 1ZN8 - A/B=1-180 (human) 1ZN9 - A/B=1-180 (human)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 1OPU 1ORE 1ZN7 1ZN8 1ZN9  |  ENZYME  |  Phospho3D  |  DISEASE  |  Source  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene

	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

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	24		S15-p	LVEQRIRsFPDFPTP
0	1		S30-p	GVVFRDIsPVLkDPA
0	23		K34-u	RDIsPVLkDPAsFRA
0	1		S38-p	PVLkDPAsFRAAIGL
0	1		R57	LKATHGGRIDyIAGL
0	6		Y60-p	THGGRIDyIAGLDsR
0	2		S66-p	DyIAGLDsRGFLFGP
0	12		K107	SYSLEYGKAELEIQk
0	1		K114-a	KAELEIQkDALEPGQ
0	7		K114-u	KAELEIQkDALEPGQ
0	1		T135-p	DLLATGGtMNAACEL
0	7		K167-u	TSLKGREkLAPVPFF

	mouse ► Hide Isoforms
S2-p	______MsEPELKLV
P4	____MsEPELKLVAR
V15	LVARRIRVFPDFPIP
S30	GVLFRDISPLLkDPD
K34-u	RDISPLLkDPDSFRA
S38	PLLkDPDSFRASIRL
K57-u	LKSTHSGkIDYIAGL
Y60	THSGkIDYIAGLDSR
S66	DYIAGLDSRGFLFGP
K107-u	SYSLEYGkAELEIQK
K114	kAELEIQKDALEPGQ
K114	kAELEIQKDALEPGQ
T135	DLLATGGTMFAACDL
R167	TSLKGRERLGPIPFF

	APRT iso3
S2	______MSEPELKLV
P4	____MSEPELKLVAR
S15-p	LVARRIRsFPDFPIP
S30	GVLFRDISPLLKDPD
K34	RDISPLLKDPDSFRA
S38	PLLKDPDSFRASIRL
K57	LKSTHSGKIDYIAGL
Y60	THSGKIDYIAGLDSR
S66	DYIAGLDSRGFLFGP
K107	SYSLEYGKAELEIQK
K114	KAELEIQKDALEPGQ
K114	KAELEIQKDALEPGQ
I135	DLLATGGIMFAACDL
R167	TSLKGRERLGPIPFF

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

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