CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017209
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Pyridoxal kinase 
Protein Synonyms/Alias
 Pyridoxine kinase 
Gene Name
 Pdxk 
Gene Synonyms/Alias
 Pkh 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
76LKVNDVNKYDYVLTGubiquitination[1]
139LLPVYRDKVVPVADIubiquitination[1]
258NLKVACEKTVSAMQHacetylation[2]
258NLKVACEKTVSAMQHubiquitination[1]
283AEAGEGQKPSPAQLEubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441
Functional Description
 Required for synthesis of pyridoxal-5-phosphate from vitamin B6 (By similarity). 
Sequence Annotation
 NP_BIND 186 187 ATP (By similarity).
 NP_BIND 223 234 ATP (By similarity).
 BINDING 12 12 Substrate (By similarity).
 BINDING 47 47 Substrate (By similarity).
 BINDING 127 127 Substrate (By similarity).
 BINDING 235 235 Substrate (By similarity).
 MOD_RES 1 1 N-acetylmethionine (By similarity).
 MOD_RES 59 59 Phosphoserine (By similarity).
 MOD_RES 164 164 Phosphoserine (By similarity).
 MOD_RES 213 213 Phosphoserine (By similarity).
 MOD_RES 285 285 Phosphoserine (By similarity).  
Keyword
 Acetylation; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Kinase; Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 312 AA 
Protein Sequence
MEGECRVLSI QSHVVRGYVG NRAAMFPLQV LGFEVDAVNS VQFSNHTGYA HWKGQVLKSQ 60
ELHELYEGLK VNDVNKYDYV LTGYTRDKSF LAMVVDIVRE LKQQNSRLVY VCDPVMGDKW 120
NGEGSMYVPQ DLLPVYRDKV VPVADIITPN QFEAELLSGR KIHSQEEAFE VMDMLHCMGP 180
DTVVITSSDL PSSQGSDYLI ALGSQRMRKP DGSTVTQRIR MEMRKVEAVF VGTGDLFAAM 240
LLAWTHKHPD NLKVACEKTV SAMQHVLQRT IRCAKAEAGE GQKPSPAQLE LRMVQSKRDI 300
EDPEIVVQAT VL 312 
Gene Ontology
 GO:0005829; C:cytosol; IEA:Compara.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0031403; F:lithium ion binding; IEA:Compara.
 GO:0000287; F:magnesium ion binding; IEA:Compara.
 GO:0030955; F:potassium ion binding; IEA:Compara.
 GO:0008478; F:pyridoxal kinase activity; IEA:EC.
 GO:0030170; F:pyridoxal phosphate binding; IEA:Compara.
 GO:0031402; F:sodium ion binding; IEA:Compara.
 GO:0008270; F:zinc ion binding; IEA:Compara.
 GO:0008283; P:cell proliferation; IEA:Compara.
 GO:0009443; P:pyridoxal 5'-phosphate salvage; IEA:InterPro. 
Interpro
 IPR011611; PfkB_dom.
 IPR004625; PyrdxlP_synth_PyrdxlKinase. 
Pfam
 PF00294; PfkB 
SMART
  
PROSITE
  
PRINTS