Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Pyridoxal kinase  

UniProtKB / Swiss-Prot ID :  PDXK_HUMAN

Gene Name (Synonyms) : 
PDXK, C21orf124, C21orf97, PKH, PNK PRED79  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. 

Protein Function :  Required for synthesis of pyridoxal-5-phosphate from vitamin B6. 

Protein Sequence MEEECRVLSIQSHVIRGYVGNRAATFPLQVLGFEIDAVNSVQFSNHTGYAHWKGQVLNSDELQELYEGLR...
Predicted Secondary Structure CCCCCCEEEEECEEEECCCCCHHHHHHHHHCCCEEEEECEEEECCCCCCCCCCCCCCCHHHHHHHHHHHH...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
59PhosphoserineQVLNSDELQ
CCCCHHHHH
28.44Phosphositeplus
Link
59Phosphoserine.QVLNSDELQ
CCCCHHHHH
28.44UniProtKB
Link
76Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NNMNKYDYV
CCCCCCCEE
28.82Phosphositeplus
Link
84PhosphotyrosineVLTGYTRDK
EEEECCCCH
8.05Phosphositeplus
Link
84Phosphotyrosine.VLTGYTRDK
EEEECCCCH
8.05UniProtKB
Link
137Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LPVYKEKVV
HHHHHHHHH
51.82Phosphositeplus
Link
139Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VYKEKVVPL
HHHHHHHCH
44.36Phosphositeplus
Link
161Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LSGRKIHSQ
HCCCCCCCH
48.58Phosphositeplus
Link
164PhosphoserineRKIHSQEEA
CCCCCHHHH
42.64Phosphositeplus
Link
164Phosphoserine.RKIHSQEEA
CCCCCHHHH
42.64UniProtKB
Link
196Phosphoserine.SPQGSNYLI
CCCCCCEEE
19.63UniProtKB
Link
204Phosphoserine.IVLGSQRRR
EEECCHHEE
19.16UniProtKB
Link
213PhosphoserineNPAGSVVME
CCCCEEEEE
17.40HPRD
Link
213PhosphoserineNPAGSVVME
CCCCEEEEE
17.40Phosphositeplus
Link
213Phosphoserine.NPAGSVVME
CCCCEEEEE
17.40UniProtKB
Link
259Phosphothreonine.ACEKTVSTL
HHHHHHHHH
9.44UniProtKB
Link
285PhosphoserineGVRPSPMQL
CCCCCHHHH
23.57HPRD
Link
285PhosphoserineGVRPSPMQL
CCCCCHHHH
23.57Phosphositeplus
Link
285Phosphoserine.GVRPSPMQL
CCCCCHHHH
23.57UniProtKB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
1433Z_HUMANphysical interactionMINT-3304733MINT15161933
PNPO_HUMANENSP00000291565STRING
ADO_HUMANENSP00000291565STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
DrugBank
DB00147Pyridoxal
DB00165Pyridoxine
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213 AND SER-285, ANDMASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59; TYR-84; SER-164;SER-196; SER-204; SER-213; THR-259 AND SER-285, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures