UniProt Accession

 HPRT_HUMAN; P00492; A6NHF0; B2R8M9 

Genbank Protein ID

 M31642; M26434; AK313435; BT019350; AY780550; AC004383; CH471107; BC000578; M12452; S79313; L29383; L29382; S60300 

Genbank Nucleotide ID

 AAA52690.1; AAA36012.1; BAG36226.1; AAV38157.1; AAV31777.1; EAX11761.1; AAH00578.1; AAA52691.1; AAB21289.1; AAB59391.1; AAB59392.1; AAC60591.2 

Protein Name

 Hypoxanthine-guanine phosphoribosyltransferase 

Protein Synonyms/Alias

 HGPRT; HGPRTase 

Gene Name

 HPRT1 

Gene Synonyms/Alias

 HPRT 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
73	CVLKGGYKFFADLLD	ubiquitination	[1]
83	ADLLDYIKALNRNSD	acetylation	[2]
103	TVDFIRLKSYCNDQS	ubiquitination	[1, 3, 4, 5, 6, 7]
115	DQSTGDIKVIGGDDL	acetylation	[7, 8]
115	DQSTGDIKVIGGDDL	ubiquitination	[1, 4, 6]
128	DLSTLTGKNVLIVED	ubiquitination	[3, 9]
159	QYNPKMVKVASLLVK	ubiquitination	[1, 7, 10]
166	KVASLLVKRTPRSVG	ubiquitination	[1, 4, 11]
175	TPRSVGYKPDFVGFE	ubiquitination	[3, 9, 10, 11, 12, 13, 14]
213	CVISETGKAKYKA**	ubiquitination	[4]
215	ISETGKAKYKA****	ubiquitination	[1]

Reference

 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Monoclonal antibody cocktail as an enrichment tool for acetylome analysis.
 Shaw PG, Chaerkady R, Zhang Z, Davidson NE, Pandey A.
 Anal Chem. 2011 May 15;83(10):3623-6. [PMID: 21466224]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [5] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [6] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [7] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [8] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [9] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [10] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [11] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [12] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [13] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [14] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931] 

Functional Description

 Converts guanine to guanosine monophosphate, and hypoxanthine to inosine monophosphate. Transfers the 5- phosphoribosyl group from 5-phosphoribosylpyrophosphate onto the purine. Plays a central role in the generation of purine nucleotides through the purine salvage pathway. 

Sequence Annotation

 NP_BIND 134 142 GMP.
 NP_BIND 186 188 GMP.
 ACT_SITE 138 138 Proton acceptor (Probable).
 METAL 194 194 Magnesium.
 BINDING 69 69 GMP.
 BINDING 166 166 GMP.
 BINDING 194 194 GMP; via carbonyl oxygen.
 MOD_RES 2 2 N-acetylalanine.  

Keyword

 3D-structure; Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Disease mutation; Glycosyltransferase; Gout; Magnesium; Metal-binding; Nucleotide-binding; Purine salvage; Reference proteome; Transferase. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 218 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; IBA:RefGenome.
 GO:0052657; F:guanine phosphoribosyltransferase activity; IDA:UniProtKB.
 GO:0004422; F:hypoxanthine phosphoribosyltransferase activity; IDA:UniProtKB.
 GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
 GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
 GO:0006168; P:adenine salvage; IBA:RefGenome.
 GO:0007610; P:behavior; IMP:UniProtKB.
 GO:0021954; P:central nervous system neuron development; IEA:Compara.
 GO:0021895; P:cerebral cortex neuron differentiation; IEA:Compara.
 GO:0019835; P:cytolysis; IEA:Compara.
 GO:0048813; P:dendrite morphogenesis; IEA:Compara.
 GO:0042417; P:dopamine metabolic process; IEA:Compara.
 GO:0046038; P:GMP catabolic process; IDA:UniProtKB.
 GO:0032263; P:GMP salvage; IBA:RefGenome.
 GO:0007625; P:grooming behavior; IEA:Compara.
 GO:0006178; P:guanine salvage; IDA:UniProtKB.
 GO:0043103; P:hypoxanthine salvage; IDA:UniProtKB.
 GO:0032264; P:IMP salvage; IBA:RefGenome.
 GO:0046651; P:lymphocyte proliferation; IEA:Compara.
 GO:0045964; P:positive regulation of dopamine metabolic process; IMP:UniProtKB.
 GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
 GO:0006166; P:purine ribonucleoside salvage; IMP:UniProtKB.
 GO:0001975; P:response to amphetamine; IEA:Compara.
 GO:0021756; P:striatum development; IEA:Compara. 

Interpro

 IPR005904; Hxn_phspho_trans.
 IPR000836; PRibTrfase_dom. 

Pfam

 PF00156; Pribosyltran 

SMART

  

PROSITE

 PS00103; PUR_PYR_PR_TRANSFER 

PRINTS