CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011373
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Amidophosphoribosyltransferase 
Protein Synonyms/Alias
 ATase; Glutamine phosphoribosylpyrophosphate amidotransferase; GPAT 
Gene Name
 PPAT 
Gene Synonyms/Alias
 GPAT 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
62GSSVPTFKSHKGMGLubiquitination[1, 2, 3]
65VPTFKSHKGMGLVNHubiquitination[2]
80VFTEDNLKKLYVSNLubiquitination[1, 2, 3]
81FTEDNLKKLYVSNLGacetylation[4]
81FTEDNLKKLYVSNLGubiquitination[2]
99TRYATTGKCELENCQubiquitination[2, 5]
178ARIKNLMKEAPTAYSubiquitination[2]
220PVSDINDKEKKTSETubiquitination[2]
223DINDKEKKTSETEGWubiquitination[2]
349PYVEVLCKNRYVGRTubiquitination[2, 5, 6]
372RQLGVAKKFGVLSDNacetylation[6]
372RQLGVAKKFGVLSDNubiquitination[2, 5, 7]
381GVLSDNFKGKRIVLVubiquitination[1, 2, 6]
403NTISPIIKLLKESGAubiquitination[1, 2, 3, 6]
406SPIIKLLKESGAKEVubiquitination[2]
411LLKESGAKEVHIRVAubiquitination[1, 6]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [5] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [6] 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]
 [7] 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
Functional Description
  
Sequence Annotation
 DOMAIN 12 261 Glutamine amidotransferase type-2.
 ACT_SITE 12 12 For GATase activity (By similarity).
 METAL 280 280 Iron-sulfur (4Fe-4S) (By similarity).
 METAL 327 327 Magnesium (By similarity).
 METAL 389 389 Magnesium (By similarity).
 METAL 390 390 Magnesium (By similarity).
 METAL 426 426 Iron-sulfur (4Fe-4S) (By similarity).
 METAL 503 503 Iron-sulfur (4Fe-4S) (By similarity).
 METAL 506 506 Iron-sulfur (4Fe-4S) (By similarity).  
Keyword
 4Fe-4S; Allosteric enzyme; Complete proteome; Glutamine amidotransferase; Glycosyltransferase; Iron; Iron-sulfur; Magnesium; Metal-binding; Purine biosynthesis; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 517 AA 
Protein Sequence
MELEELGIRE ECGVFGCIAS GEWPTQLDVP HVITLGLVGL QHRGQESAGI VTSDGSSVPT 60
FKSHKGMGLV NHVFTEDNLK KLYVSNLGIG HTRYATTGKC ELENCQPFVV ETLHGKIAVA 120
HNGELVNAAR LRKKLLRHGI GLSTSSDSEM ITQLLAYTPP QEQDDTPDWV ARIKNLMKEA 180
PTAYSLLIMH RDVIYAVRDP YGNRPLCIGR LIPVSDINDK EKKTSETEGW VVSSESCSFL 240
SIGARYYREV LPGEIVEISR HNVQTLDIIS RSEGNPVAFC IFEYVYFARP DSMFEDQMVY 300
TVRYRCGQQL AIEAPVDADL VSTVPESATP AALAYAGKCG LPYVEVLCKN RYVGRTFIQP 360
NMRLRQLGVA KKFGVLSDNF KGKRIVLVDD SIVRGNTISP IIKLLKESGA KEVHIRVASP 420
PIKYPCFMGI NIPTKEELIA NKPEFDHLAE YLGANSVVYL SVEGLVSSVQ EGIKFKKQKE 480
KKHDIMIQEN GNGLECFEKS GHCTACLTGK YPVELEW 517 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
 GO:0004044; F:amidophosphoribosyltransferase activity; TAS:ProtInc.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0035690; P:cellular response to drug; IEA:Compara.
 GO:0032869; P:cellular response to insulin stimulus; IEA:Compara.
 GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Compara.
 GO:0006543; P:glutamine catabolic process; IEA:Compara.
 GO:0001822; P:kidney development; IEA:Compara.
 GO:0007595; P:lactation; IEA:Compara.
 GO:0060135; P:maternal process involved in female pregnancy; IEA:Compara.
 GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
 GO:0031100; P:organ regeneration; IEA:Compara.
 GO:0051289; P:protein homotetramerization; IEA:Compara.
 GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
 GO:0006144; P:purine nucleobase metabolic process; TAS:Reactome.
 GO:0006164; P:purine nucleotide biosynthetic process; TAS:ProtInc.
 GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; TAS:Reactome. 
Interpro
 IPR005854; Amd_phspho_trans.
 IPR017932; GATase_2_dom.
 IPR000583; GATase_dom.
 IPR000836; PRibTrfase_dom. 
Pfam
 PF00310; GATase_2
 PF00156; Pribosyltran 
SMART
  
PROSITE
 PS51278; GATASE_TYPE_2
 PS00103; PUR_PYR_PR_TRANSFER 
PRINTS