PDXK_HUMAN - dbPTM
PDXK_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PDXK_HUMAN
UniProt AC O00764
Protein Name Pyridoxal kinase
Gene Name PDXK
Organism Homo sapiens (Human).
Sequence Length 312
Subcellular Localization Cytoplasm.
Protein Description Required for synthesis of pyridoxal-5-phosphate from vitamin B6..
Protein Sequence MEEECRVLSIQSHVIRGYVGNRAATFPLQVLGFEIDAVNSVQFSNHTGYAHWKGQVLNSDELQELYEGLRLNNMNKYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDKWDGEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGPDTVVITSSDLPSPQGSNYLIVLGSQRRRNPAGSVVMERIRMDIRKVDAVFVGTGDLFAAMLLAWTHKHPNNLKVACEKTVSTLHHVLQRTIQCAKAQAGEGVRPSPMQLELRMVQSKRDIEDPEIVVQATVL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
1Acetylation-------MEEECRVL
-------CHHHHEEE		15.33-
9PhosphorylationEEECRVLSIQSHVIR
HHHHEEEEEECHHHH		18.7428857561
36 (in isoform 3)Ubiquitination-36.9521890473
59PhosphorylationWKGQVLNSDELQELY
EECEECCHHHHHHHH		28.4422817900
66PhosphorylationSDELQELYEGLRLNN
HHHHHHHHHHHCCCC		13.7527642862
70MethylationQELYEGLRLNNMNKY
HHHHHHHCCCCCCCC		46.34115486963
76UbiquitinationLRLNNMNKYDYVLTG
HCCCCCCCCCEEEEE		28.8221890473
76 (in isoform 1)Ubiquitination-28.8221890473
84PhosphorylationYDYVLTGYTRDKSFL
CCEEEEEECCCHHHH		8.0522817900
93SulfoxidationRDKSFLAMVVDIVQE
CCHHHHHHHHHHHHH		3.0830846556
97 (in isoform 3)Ubiquitination-2.0221890473
99 (in isoform 3)Ubiquitination-51.1121890473
109 (in isoform 2)Ubiquitination-3.3921906983
111 (in isoform 2)Ubiquitination-2.0221906983
119UbiquitinationCDPVLGDKWDGEGSM
ECCCCCCCCCCCCCE		45.44-
121 (in isoform 3)Ubiquitination-51.5121890473
125PhosphorylationDKWDGEGSMYVPEDL
CCCCCCCCEECCHHH		11.5725002506
126SulfoxidationKWDGEGSMYVPEDLL
CCCCCCCEECCHHHH		6.0130846556
127PhosphorylationWDGEGSMYVPEDLLP
CCCCCCEECCHHHHH		17.9825002506
133 (in isoform 2)Ubiquitination-4.1121906983
137UbiquitinationEDLLPVYKEKVVPLA
HHHHHHHHCCEEEHH		51.8221906983
137 (in isoform 1)Ubiquitination-51.8221890473
139UbiquitinationLLPVYKEKVVPLADI
HHHHHHCCEEEHHHC		44.3621906983
139 (in isoform 1)Ubiquitination-44.3621890473
148PhosphorylationVPLADIITPNQFEAE
EEHHHCCCCCHHHHH		19.27-
161UbiquitinationAELLSGRKIHSQEEA
HHHHHCCCCCCHHHH		48.582190698
161 (in isoform 1)Ubiquitination-48.5821890473
1612-HydroxyisobutyrylationAELLSGRKIHSQEEA
HHHHHCCCCCCHHHH		48.58-
164PhosphorylationLSGRKIHSQEEALRV
HHCCCCCCHHHHHHH		42.6420068231
196PhosphorylationDLPSPQGSNYLIVLG
CCCCCCCCCEEEEEC		19.6319369195
204PhosphorylationNYLIVLGSQRRRNPA
CEEEEECCCCCCCCC		19.1619369195
213PhosphorylationRRRNPAGSVVMERIR
CCCCCCCCHHHHHHH		17.4021082442
216SulfoxidationNPAGSVVMERIRMDI
CCCCCHHHHHHHHHH		2.4121406390
253UbiquitinationHKHPNNLKVACEKTV
CCCCCCHHHHEEHHH		29.88-
2582-HydroxyisobutyrylationNLKVACEKTVSTLHH
CHHHHEEHHHHHHHH		54.86-
258AcetylationNLKVACEKTVSTLHH
CHHHHEEHHHHHHHH		54.8626051181
258UbiquitinationNLKVACEKTVSTLHH
CHHHHEEHHHHHHHH		54.86-
259PhosphorylationLKVACEKTVSTLHHV
HHHHEEHHHHHHHHH		9.4419060867
261PhosphorylationVACEKTVSTLHHVLQ
HHEEHHHHHHHHHHH		30.4028857561
262PhosphorylationACEKTVSTLHHVLQR
HEEHHHHHHHHHHHH		26.2728857561
270PhosphorylationLHHVLQRTIQCAKAQ
HHHHHHHHHHHHHHH		11.48-
275UbiquitinationQRTIQCAKAQAGEGV
HHHHHHHHHHCCCCC		48.97-
285PhosphorylationAGEGVRPSPMQLELR
CCCCCCCCCCCEEEE		23.5715154080
287SulfoxidationEGVRPSPMQLELRMV
CCCCCCCCCEEEEEH		9.2421406390
292MethylationSPMQLELRMVQSKRD
CCCCEEEEEHHCCCC		17.53115486955
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of PDXK_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PDXK_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PDXK_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GABT_HUMANABATphysical
26344197
OGT1_HUMANOGTphysical
26344197
MSS4_HUMANRABIFphysical
26344197
TPIS_HUMANTPI1physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00147Pyridoxal
DB00165Pyridoxine
Regulatory Network of PDXK_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.
"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.

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