CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015940
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 L-xylulose reductase 
Protein Synonyms/Alias
 XR; Carbonyl reductase II; Dicarbonyl/L-xylulose reductase; Kidney dicarbonyl reductase; kiDCR; Sperm surface protein P34H 
Gene Name
 DCXR 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
17VLVTGAGKGIGRGTVubiquitination[1, 2, 3]
153HSVYCSTKGALDMLTubiquitination[3]
161GALDMLTKVMALELGubiquitination[1, 3, 4]
171ALELGPHKIRVNAVNubiquitination[1, 3, 4]
196ATWSDPHKAKTMLNRubiquitination[1]
198WSDPHKAKTMLNRIPubiquitination[3]
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] 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]
 [3] 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]
 [4] 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
 Catalyzes the NADPH-dependent reduction of several pentoses, tetroses, trioses, alpha-dicarbonyl compounds and L- xylulose. Participates in the uronate cycle of glucose metabolism. May play a role in the water absorption and cellular osmoregulation in the proximal renal tubules by producing xylitol, an osmolyte, thereby preventing osmolytic stress from occurring in the renal tubules. 
Sequence Annotation
 NP_BIND 11 40 NADP.
 ACT_SITE 149 149 Proton acceptor.
 BINDING 136 136 Substrate.
 BINDING 153 153 NADP.
 MOD_RES 1 1 N-acetylmethionine.  
Keyword
 3D-structure; Acetylation; Carbohydrate metabolism; Complete proteome; Direct protein sequencing; Glucose metabolism; Membrane; NADP; Oxidoreductase; Reference proteome; Xylose metabolism. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 244 AA 
Protein Sequence
MELFLAGRRV LVTGAGKGIG RGTVQALHAT GARVVAVSRT QADLDSLVRE CPGIEPVCVD 60
LGDWEATERA LGSVGPVDLL VNNAAVALLQ PFLEVTKEAF DRSFEVNLRA VIQVSQIVAR 120
GLIARGVPGA IVNVSSQCSQ RAVTNHSVYC STKGALDMLT KVMALELGPH KIRVNAVNPT 180
VVMTSMGQAT WSDPHKAKTM LNRIPLGKFA EVEHVVNAIL FLLSDRSGMT TGSTLPVEGG 240
FWAC 244 
Gene Ontology
 GO:0005903; C:brush border; IEA:Compara.
 GO:0005881; C:cytoplasmic microtubule; IDA:UniProtKB.
 GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
 GO:0005902; C:microvillus; IEA:Compara.
 GO:0050038; F:L-xylulose reductase (NADP+) activity; IDA:UniProtKB.
 GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IDA:UniProtKB.
 GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-KW.
 GO:0006006; P:glucose metabolic process; IDA:UniProtKB.
 GO:0006739; P:NADP metabolic process; IEA:Compara.
 GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
 GO:0005997; P:xylulose metabolic process; IDA:UniProtKB. 
Interpro
 IPR002198; DH_sc/Rdtase_SDR.
 IPR002347; Glc/ribitol_DH.
 IPR016040; NAD(P)-bd_dom.
 IPR020904; Sc_DH/Rdtase_CS. 
Pfam
  
SMART
  
PROSITE
 PS00061; ADH_SHORT 
PRINTS
 PR00081; GDHRDH.
 PR00080; SDRFAMILY.