CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001139
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Xylulose kinase 
Protein Synonyms/Alias
 Xylulokinase 
Gene Name
 XYLB 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
178FTGNQIAKIYQQNPEubiquitination[1, 2, 3, 4]
419IEGQFMAKRIHAEGLubiquitination[3]
435YRVMSKTKILATGGAubiquitination[3]
494VPFSEVVKLAPNPRLubiquitination[3]
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] 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]
 [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] 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
Functional Description
 Phosphorylates D-xylulose to produce D-xylulose 5- phosphate, a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. 
Sequence Annotation
 NP_BIND 441 442 ATP.
 BINDING 99 99 Substrate.
 BINDING 170 170 Substrate.
 BINDING 280 280 Substrate.
 BINDING 281 281 Substrate.
 BINDING 355 355 ATP.
 BINDING 445 445 ATP.  
Keyword
 3D-structure; ATP-binding; Carbohydrate metabolism; Complete proteome; Kinase; Nucleotide-binding; Polymorphism; Reference proteome; Transferase; Xylose metabolism. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 536 AA 
Protein Sequence
MAEHAPRRCC LGWDFSTQQV KVVAVDAELN VFYEESVHFD RDLPEFGTQG GVHVHKDGLT 60
VTSPVLMWVQ ALDIILEKMK ASGFDFSQVL ALSGAGQQHG SIYWKAGAQQ ALTSLSPDLR 120
LHQQLQDCFS ISDCPVWMDS STTAQCRQLE AAVGGAQALS CLTGSRAYER FTGNQIAKIY 180
QQNPEAYSHT ERISLVSSFA ASLFLGSYSP IDYSDGSGMN LLQIQDKVWS QACLGACAPH 240
LEEKLSPPVP SCSVVGAISS YYVQRYGFPP GCKVVAFTGD NPASLAGMRL EEGDIAVSLG 300
TSDTLFLWLQ EPMPALEGHI FCNPVDSQHY MALLCFKNGS LMREKIRNES VSRSWSDFSK 360
ALQSTEMGNG GNLGFYFDVM EITPEIIGRH RFNTENHKVA AFPGDVEVRA LIEGQFMAKR 420
IHAEGLGYRV MSKTKILATG GASHNREILQ VLADVFDAPV YVIDTANSAC VGSAYRAFHG 480
LAGGTDVPFS EVVKLAPNPR LAATPSPGAS QVYEALLPQY AKLEQRILSQ TRGPPE 536 
Gene Ontology
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004856; F:xylulokinase activity; IDA:UniProtKB.
 GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-KW.
 GO:0006091; P:generation of precursor metabolites and energy; TAS:ProtInc.
 GO:0005998; P:xylulose catabolic process; TAS:BHF-UCL. 
Interpro
 IPR018485; Carb_kinase_FGGY_C.
 IPR018484; Carb_kinase_FGGY_N. 
Pfam
 PF02782; FGGY_C
 PF00370; FGGY_N 
SMART
  
PROSITE
  
PRINTS