CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000128
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Pyridoxal kinase 
Protein Synonyms/Alias
 Pyridoxine kinase 
Gene Name
 PDXK 
Gene Synonyms/Alias
 C21orf124; C21orf97; PKH; PNK; PRED79 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
111LLPVYKEKVVPLADIubiquitination[1]
Reference
 [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661
Functional Description
 Required for synthesis of pyridoxal-5-phosphate from vitamin B6. 
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.
 MOD_RES 164 164 Phosphoserine.
 MOD_RES 213 213 Phosphoserine.
 MOD_RES 285 285 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; ATP-binding; Complete proteome; Cytoplasm; Kinase; Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 312 AA 
Protein Sequence
MEEECRVLSI QSHVIRGYVG NRAATFPLQV LGFEIDAVNS VQFSNHTGYA HWKGQVLNSD 60
ELQELYEGLR LNNMNKYDYV LTVCDPVLGD KWDGEGSMYV PEDLLPVYKE KVVPLADIIT 120
PNQFEAELLS GRKIHSQEEA LRVMDMLHSM GPDTVVITSS DLPSPQGSNY LIVLGSQRRR 180
NPAGSVVMER IRMDIRKVDA VFVGTGDLFA AMLLAWTHKH PNNLKVACEK TVSTLHHVLQ 240
RTIQCAKAQA GEGVRPSPMQ LELRMVQSKR DIEDPEIVVQ ATVL 284 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0005524; F:ATP binding; IDA:UniProtKB.
 GO:0031403; F:lithium ion binding; IDA:UniProtKB.
 GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
 GO:0030955; F:potassium ion binding; IDA:UniProtKB.
 GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
 GO:0008478; F:pyridoxal kinase activity; IDA:UniProtKB.
 GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
 GO:0031402; F:sodium ion binding; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IDA:UniProtKB.
 GO:0008283; P:cell proliferation; IDA:UniProtKB.
 GO:0009443; P:pyridoxal 5'-phosphate salvage; IEA:InterPro.
 GO:0042823; P:pyridoxal phosphate biosynthetic process; IDA:UniProtKB.
 GO:0042816; P:vitamin B6 metabolic process; IC:UniProtKB. 
Interpro
 IPR011611; PfkB_dom.
 IPR004625; PyrdxlP_synth_PyrdxlKinase. 
Pfam
 PF00294; PfkB 
SMART
  
PROSITE
  
PRINTS