PDX1_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PDX1_SCHPO
• UniProt AC: O14027
• Protein Name: Probable pyridoxal 5'-phosphate synthase subunit PDX1
• Gene Name: snz1
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 296
• Protein Description: Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by PDX2. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively. Also plays an indirect role in resistance to singlet oxygen-generating photosensitizers..
• Protein Sequence: MSAEIKGSTQVKAGLAQMLKGGVIMDVVNAEQARIAEAAGACAVMALERVPADIRAQGGVARMSDPSMIKEIQAAVSIPVMAKVRIGHFVEAQILESIGVDYIDESEVLTPADDINHIEKSKFTVPFVCGSRNLGEALRRISEGAAMIRTKGEAGTGDVVEAVRHTRQMQGELRRVKSMSPDELYTYAKEIAAPIDLVKECAQLGRLPVVNFAAGGVATPADAALMMQLGCDGVFVGSGIFLSGDPAKRARAIVRAVTHYNDPKILAEVSENLGAAMVGRSVSSLEEKEKLATRGW

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
2	Phosphorylation	------MSAEIKGST ------CCCCCCCHH	34.31	29996109
8	Phosphorylation	MSAEIKGSTQVKAGL CCCCCCCHHHHHHHH	15.63	29996109
9	Phosphorylation	SAEIKGSTQVKAGLA CCCCCCHHHHHHHHH	46.15	29996109
121	Phosphorylation	DINHIEKSKFTVPFV HCCCHHHCCCCCEEE	21.88	25720772
131	Phosphorylation	TVPFVCGSRNLGEAL CCEEEECCCCHHHHH	16.93	25720772
142	Phosphorylation	GEALRRISEGAAMIR HHHHHHHHHCCCEEE	28.32	25720772
150	Phosphorylation	EGAAMIRTKGEAGTG HCCCEEEECCCCCCC	32.26	25720772
156	Phosphorylation	RTKGEAGTGDVVEAV EECCCCCCCCHHHHH	36.94	25720772
178	Phosphorylation	GELRRVKSMSPDELY HHHHHHHCCCHHHHH	22.95	28889911
180	Phosphorylation	LRRVKSMSPDELYTY HHHHHCCCHHHHHHH	35.97	28889911
281	Phosphorylation	GAAMVGRSVSSLEEK CHHHCCCCCCCHHHH	22.03	21712547
283	Phosphorylation	AMVGRSVSSLEEKEK HHCCCCCCCHHHHHH	30.38	28889911
284	Phosphorylation	MVGRSVSSLEEKEKL HCCCCCCCHHHHHHH	37.33	24763107

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

Oops, there are no upstream regulatory protein records of PDX1_SCHPO !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PDX1_SCHPO !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of PDX1_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MEI3_SCHPO	mei3	physical	23695164
PDX1_SCHPO	snz1	physical	23695164
PDX1_SCHPO	snz1	physical	26771498
YF75_SCHPO	spa2	physical	26771498
MEI3_SCHPO	mei3	physical	26771498
IMA2_SCHPO	imp1	physical	26771498

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Phosphoproteome analysis of fission yeast.";
Wilson-Grady J.T., Villen J., Gygi S.P.;
J. Proteome Res. 7:1088-1097(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; SER-180 ANDSER-283, AND MASS SPECTROMETRY.
PubMed: 18257517