CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019051
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ribulose-phosphate 3-epimerase 
Protein Synonyms/Alias
 Ribulose-5-phosphate-3-epimerase 
Gene Name
 RPE 
Gene Synonyms/Alias
 HUSSY-17 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
223VCSEAAQKRSLDR**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
Functional Description
 Catalyzes the reversible epimerization of D-ribulose 5- phosphate to D-xylulose 5-phosphate. 
Sequence Annotation
 REGION 146 149 Substrate binding.
 REGION 197 198 Substrate binding.
 ACT_SITE 37 37 Proton acceptor (Probable).
 ACT_SITE 175 175 Proton donor (Probable).
 METAL 35 35 Divalent metal cation.
 METAL 37 37 Divalent metal cation.
 METAL 70 70 Divalent metal cation.
 METAL 175 175 Divalent metal cation.
 BINDING 10 10 Substrate.
 BINDING 70 70 Substrate.
 BINDING 177 177 Substrate; via amide nitrogen.  
Keyword
 3D-structure; Alternative splicing; Carbohydrate metabolism; Cobalt; Complete proteome; Iron; Isomerase; Manganese; Metal-binding; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 228 AA 
Protein Sequence
MASGCKIGPS ILNSDLANLG AECLRMLDSG ADYLHLDVMD GHFVPNITFG HPVVESLRKQ 60
LGQDPFFDMH MMVSKPEQWV KPMAVAGANQ YTFHLEATEN PGALIKDIRE NGMKVGLAIK 120
PGTSVEYLAP WANQIDMALV MTVEPGFGGQ KFMEDMMPKV HWLRTQFPSL DIEVDGGVGP 180
DTVHKCAEAG ANMIVSGSAI MRSEDPRSVI NLLRNVCSEA AQKRSLDR 228 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0043231; C:intracellular membrane-bounded organelle; IEA:Compara.
 GO:0046872; F:metal ion binding; IDA:UniProtKB.
 GO:0048029; F:monosaccharide binding; IEA:Compara.
 GO:0004750; F:ribulose-phosphate 3-epimerase activity; IDA:UniProtKB.
 GO:0006098; P:pentose-phosphate shunt; IDA:UniProtKB.
 GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IEA:Compara. 
Interpro
 IPR013785; Aldolase_TIM.
 IPR026019; Ribul_P_3_epim.
 IPR000056; Ribul_P_3_epim-like.
 IPR011060; RibuloseP-bd_barrel. 
Pfam
 PF00834; Ribul_P_3_epim 
SMART
  
PROSITE
 PS01085; RIBUL_P_3_EPIMER_1
 PS01086; RIBUL_P_3_EPIMER_2 
PRINTS