UniProt Accession

 PDXK_HUMAN; O00764; Q7Z2Y0; Q9BS02 

Genbank Protein ID

 U89606; AY303972; AP001752; BC000123; BC005825 

Genbank Nucleotide ID

 AAC51233.1; AAP73047.1; BAA95540.1; AAH00123.1; AAH05825.1 

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
76	LRLNNMNKYDYVLTG	ubiquitination	[1, 2, 3, 4, 5]
137	EDLLPVYKEKVVPLA	ubiquitination	[2]
139	LLPVYKEKVVPLADI	ubiquitination	[2, 4]
161	AELLSGRKIHSQEEA	ubiquitination	[2, 4]
258	NLKVACEKTVSTLHH	ubiquitination	[4]
275	QRTIQCAKAQAGEGV	ubiquitination	[4]

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] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [4] 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]
 [5] 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

 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

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