CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012663
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 UDP-N-acetylhexosamine pyrophosphorylase 
Protein Synonyms/Alias
 Antigen X; AGX; Sperm-associated antigen 2; UDP-N-acetylgalactosamine pyrophosphorylase; AGX-1; UDP-N-acetylglucosamine pyrophosphorylase; AGX-2 
Gene Name
 UAP1 
Gene Synonyms/Alias
 SPAG2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
7*MNINDLKLTLSKAGubiquitination[1, 2]
12DLKLTLSKAGQEHLLubiquitination[1, 2, 3, 4]
63FNQSSHQKNVDARMEubiquitination[1, 2, 3, 4, 5]
122RLGVAYPKGMYDVGLubiquitination[2]
133DVGLPSRKTLFQIQAubiquitination[2]
145IQAERILKLQQVAEKubiquitination[2]
152KLQQVAEKYYGNKCIubiquitination[1]
180STKEFFTKHKYFGLKacetylation[6]
215IILEEKNKVSMAPDGubiquitination[2]
271FIGFCIQKGADCGAKubiquitination[2]
282CGAKVVEKTNPTEPVubiquitination[2, 7]
357QHHVAQKKIPYVDTQubiquitination[2]
390FDIFQFAKKFVVYEVubiquitination[5]
391DIFQFAKKFVVYEVLubiquitination[2]
415NADSQNGKDNPTTARubiquitination[5]
459PRSATNGKSETITADacetylation[8]
Reference
 [1] 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]
 [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] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [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] 
Functional Description
 Converts UDP and GlcNAc-1-P into UDP-GlcNAc, and UDP and GalNAc-1-P into UDP-GalNAc. Isoform AGX1 has 2 to 3 times higher activity towards GalNAc-1-P, while isoform AGX2 has 8 times more activity towards GlcNAc-1-P. 
Sequence Annotation
 MOTIF 108 111 Substrate binding.
 MOTIF 303 304 Substrate binding.
 BINDING 223 223 Substrate.
 BINDING 407 407 Substrate.  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; Nucleotidyltransferase; Polymorphism; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 522 AA 
Protein Sequence
MNINDLKLTL SKAGQEHLLR FWNELEEAQQ VELYAELQAM NFEELNFFFQ KAIEGFNQSS 60
HQKNVDARME PVPREVLGSA TRDQDQLQAW ESEGLFQISQ NKVAVLLLAG GQGTRLGVAY 120
PKGMYDVGLP SRKTLFQIQA ERILKLQQVA EKYYGNKCII PWYIMTSGRT MESTKEFFTK 180
HKYFGLKKEN VIFFQQGMLP AMSFDGKIIL EEKNKVSMAP DGNGGLYRAL AAQNIVEDME 240
QRGIWSIHVY CVDNILVKVA DPRFIGFCIQ KGADCGAKVV EKTNPTEPVG VVCRVDGVYQ 300
VVEYSEISLA TAQKRSSDGR LLFNAGNIAN HFFTVPFLRD VVNVYEPQLQ HHVAQKKIPY 360
VDTQGQLIKP DKPNGIKMEK FVFDIFQFAK KFVVYEVLRE DEFSPLKNAD SQNGKDNPTT 420
ARHALMSLHH CWVLNAGGHF IDENGSRLPA IPRSATNGKS ETITADVNHN LKDANDVPIQ 480
CEISPLISYA GEGLESYVAD KEFHAPLIID ENGVHELVKN GI 522 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0030246; F:carbohydrate binding; IEA:Compara.
 GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; TAS:Reactome.
 GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; TAS:Reactome.
 GO:0043687; P:post-translational protein modification; TAS:Reactome.
 GO:0018279; P:protein N-linked glycosylation via asparagine; TAS:Reactome.
 GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; TAS:Reactome. 
Interpro
 IPR002618; UDPGP_trans. 
Pfam
 PF01704; UDPGP 
SMART
  
PROSITE
  
PRINTS