CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006027
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Bifunctional purine biosynthesis protein PURH 
Protein Synonyms/Alias
 Phosphoribosylaminoimidazolecarboxamide formyltransferase; 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase; AICAR transformylase; IMP cyclohydrolase; ATIC; IMP synthase; Inosinicase 
Gene Name
 ATIC 
Gene Synonyms/Alias
 PURH; OK/SW-cl.86 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
14ALFSVSDKTGLVEFAubiquitination[1, 2, 3, 4, 5]
39VASGGTAKALRDAGLubiquitination[1, 3, 4, 5]
66EMLGGRVKTLHPAVHubiquitination[1, 3, 4, 5, 6, 7]
177TRRQLALKAFTHTAQubiquitination[1, 4, 5]
199YFRKQYSKGVSQMPLacetylation[8]
199YFRKQYSKGVSQMPLubiquitination[1, 4, 5]
254WQLVKELKEALGIPAubiquitination[4]
266IPAAASFKHVSPAGAubiquitination[4]
285PLSEDEAKVCMVYDLubiquitination[4]
294CMVYDLYKTLTPISAubiquitination[4]
331VCDVPTAKIISREVSubiquitination[2, 4, 7, 9]
356EALTILSKKKNGNYCacetylation[8]
356EALTILSKKKNGNYCubiquitination[1, 4, 5, 6, 10]
357ALTILSKKKNGNYCVubiquitination[4]
358LTILSKKKNGNYCVLubiquitination[4]
372LQMDQSYKPDENEVRubiquitination[4]
389FGLHLSQKRNNGVVDubiquitination[1, 4, 5]
397RNNGVVDKSLFSNVVubiquitination[1, 3, 4, 5, 6, 7]
406LFSNVVTKNKDLPESubiquitination[1, 4, 5, 6, 7, 10]
408SNVVTKNKDLPESALubiquitination[4]
437SNSVCYAKNGQVIGIubiquitination[4, 7]
461CTRLAGDKANYWWLRubiquitination[4]
477HPQVLSMKFKTGVKRubiquitination[4]
507GEDEDLIKWKALFEEubiquitination[6]
509DEDLIKWKALFEEVPubiquitination[10, 11]
524ELLTEAEKKEWVEKLubiquitination[6]
525LLTEAEKKEWVEKLTubiquitination[4]
530EKKEWVEKLTEVSISubiquitination[4]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] 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]
 [11] 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] 
Functional Description
 Bifunctional enzyme that catalyzes 2 steps in purine biosynthesis. 
Sequence Annotation
 NP_BIND 12 14 IMP.
 NP_BIND 34 37 IMP.
 NP_BIND 64 67 IMP.
 NP_BIND 101 104 IMP.
 NP_BIND 125 127 IMP.
 REGION 207 208 AICAR binding.
 ACT_SITE 137 137 Proton acceptor (Potential).
 ACT_SITE 267 267 Proton acceptor (Probable).
 BINDING 316 316 AICAR; via carbonyl oxygen.
 BINDING 339 339 AICAR.
 BINDING 431 431 AICAR; shared with dimeric partner.
 BINDING 451 451 AICAR; shared with dimeric partner.
 BINDING 541 541 AICAR; via carbonyl oxygen; shared with
 BINDING 588 588 AICAR; shared with dimeric partner.
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 199 199 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Direct protein sequencing; Disease mutation; Epilepsy; Hydrolase; Multifunctional enzyme; Polymorphism; Purine biosynthesis; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 592 AA 
Protein Sequence
MAPGQLALFS VSDKTGLVEF ARNLTALGLN LVASGGTAKA LRDAGLAVRD VSELTGFPEM 60
LGGRVKTLHP AVHAGILARN IPEDNADMAR LDFNLIRVVA CNLYPFVKTV ASPGVTVEEA 120
VEQIDIGGVT LLRAAAKNHA RVTVVCEPED YVVVSTEMQS SESKDTSLET RRQLALKAFT 180
HTAQYDEAIS DYFRKQYSKG VSQMPLRYGM NPHQTPAQLY TLQPKLPITV LNGAPGFINL 240
CDALNAWQLV KELKEALGIP AAASFKHVSP AGAAVGIPLS EDEAKVCMVY DLYKTLTPIS 300
AAYARARGAD RMSSFGDFVA LSDVCDVPTA KIISREVSDG IIAPGYEEEA LTILSKKKNG 360
NYCVLQMDQS YKPDENEVRT LFGLHLSQKR NNGVVDKSLF SNVVTKNKDL PESALRDLIV 420
ATIAVKYTQS NSVCYAKNGQ VIGIGAGQQS RIHCTRLAGD KANYWWLRHH PQVLSMKFKT 480
GVKRAEISNA IDQYVTGTIG EDEDLIKWKA LFEEVPELLT EAEKKEWVEK LTEVSISSDA 540
FFPFRDNVDR AKRSGVAYIA APSGSAADKV VIEACDELGI ILAHTNLRLF HH 592 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0003937; F:IMP cyclohydrolase activity; TAS:Reactome.
 GO:0004643; F:phosphoribosylaminoimidazolecarboxamide formyltransferase activity; TAS:Reactome.
 GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0003360; P:brainstem development; IEA:Compara.
 GO:0021549; P:cerebellum development; IEA:Compara.
 GO:0021987; P:cerebral cortex development; IEA:Compara.
 GO:0046452; P:dihydrofolate metabolic process; IEA:Compara.
 GO:0009116; P:nucleoside metabolic process; IEA:Compara.
 GO:0031100; P:organ regeneration; IEA:Compara.
 GO:0006144; P:purine nucleobase metabolic process; TAS:Reactome.
 GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; TAS:Reactome.
 GO:0010035; P:response to inorganic substance; IEA:Compara.
 GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:Compara. 
Interpro
 IPR024051; AICAR_Tfase_dom.
 IPR024050; AICAR_Tfase_insert_dom.
 IPR002695; AICARFT_IMPCHas.
 IPR016193; Cytidine_deaminase-like.
 IPR011607; MGS-like_dom. 
Pfam
 PF01808; AICARFT_IMPCHas
 PF02142; MGS 
SMART
 SM00798; AICARFT_IMPCHas
 SM00851; MGS 
PROSITE
  
PRINTS