PNPO_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PNPO_HUMAN
• UniProt AC: Q9NVS9
• Protein Name: Pyridoxine-5'-phosphate oxidase
• Gene Name: PNPO
• Organism: Homo sapiens (Human).
• Sequence Length: 261
• Protein Description: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP)..
• Protein Sequence: MTCWLRGVTATFGRPAEWPGYLSHLCGRSAAMDLGPMRKSYRGDREAFEETHLTSLDPVKQFAAWFEEAVQCPDIGEANAMCLATCTRDGKPSARMLLLKGFGKDGFRFFTNFESRKGKELDSNPFASLVFYWEPLNRQVRVEGPVKKLPEEEAECYFHSRPKSSQIGAVVSHQSSVIPDREYLRKKNEELEQLYQDQEVPKPKSWGGYVLYPQVMEFWQGQTNRLHDRIVFRRGLPTGDSPLGPMTHRGEEDWLYERLAP

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
29	Phosphorylation	LSHLCGRSAAMDLGP HHHHHCCHHCHHHHH	12.98	20068231
40	Phosphorylation	DLGPMRKSYRGDREA HHHHCCHHHCCCHHH	15.08	17287340
41	Phosphorylation	LGPMRKSYRGDREAF HHHCCHHHCCCHHHH	22.96	20068231
51	Phosphorylation	DREAFEETHLTSLDP CHHHHHHHCCCCCCH	18.26	23186163
54	Phosphorylation	AFEETHLTSLDPVKQ HHHHHCCCCCCHHHH	21.46	28122231
55	Phosphorylation	FEETHLTSLDPVKQF HHHHCCCCCCHHHHH	36.82	28122231
157	Phosphorylation	PEEEAECYFHSRPKS CHHHHHHEEECCCCC	8.88	26356563
160	Phosphorylation	EAECYFHSRPKSSQI HHHHEEECCCCCCCC	40.14	26356563
164	Phosphorylation	YFHSRPKSSQIGAVV EEECCCCCCCCCCCC	30.11	23898821
165	Phosphorylation	FHSRPKSSQIGAVVS EECCCCCCCCCCCCC	31.76	21082442
172	Phosphorylation	SQIGAVVSHQSSVIP CCCCCCCCCCCCCCC	14.81	28857561
175	Phosphorylation	GAVVSHQSSVIPDRE CCCCCCCCCCCCCHH	22.58	28857561
176	Phosphorylation	AVVSHQSSVIPDREY CCCCCCCCCCCCHHH	19.93	28857561
181	Methylation	QSSVIPDREYLRKKN CCCCCCCHHHHHHHH	29.16	115488007
183	Phosphorylation	SVIPDREYLRKKNEE CCCCCHHHHHHHHHH	16.83	-
187	Ubiquitination	DREYLRKKNEELEQL CHHHHHHHHHHHHHH	64.26	-
212	Phosphorylation	SWGGYVLYPQVMEFW CCCCEEEHHHHHHHH	4.99	-
238	Phosphorylation	VFRRGLPTGDSPLGP EEECCCCCCCCCCCC	59.68	30266825
241	Phosphorylation	RGLPTGDSPLGPMTH CCCCCCCCCCCCCCC	24.30	30266825
246	Sulfoxidation	GDSPLGPMTHRGEED CCCCCCCCCCCCCCC	4.71	30846556
247	Phosphorylation	DSPLGPMTHRGEEDW CCCCCCCCCCCCCCC	16.14	29255136
256	Phosphorylation	RGEEDWLYERLAP-- CCCCCCHHHHCCC--	8.51	27642862

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of PNPO_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PNPO_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of PNPO_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
FUMH_HUMAN	FH	physical	26344197
GMPPB_HUMAN	GMPPB	physical	26344197
CH10_HUMAN	HSPE1	physical	26344197
PCP_HUMAN	PRCP	physical	26344197
MSS4_HUMAN	RABIF	physical	26344197
SGT1_HUMAN	SUGT1	physical	26344197
TALDO_HUMAN	TALDO1	physical	26344197
TRXR1_HUMAN	TXNRD1	physical	26344197

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 610090: Pyridoxine-5'-phosphate oxidase deficiency (PNPO deficiency)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40, AND MASSSPECTROMETRY.
PubMed: 17287340