dbPTM

ALF_SCHPO - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ALF_SCHPO
UniProt AC	P36580
Protein Name	Fructose-bisphosphate aldolase
Gene Name	fba1
Organism	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length	358
Subcellular Localization
Protein Description	Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis..
Protein Sequence	MGILDIVPTGVITGDNVLKLFTYAREHGFAIPAINVTSSSTAIAALEAAREARSPIILQTSNGGAHFFAGKESSNEGQKASIAGSIAAAHYIRSIAPFFGVPVVMHSDHCAKKLLPWMDGMFEADEAYFKIHGEPLFSSHMLDLSEEPKKENIAQVKEYCKRAVPMKIWIEMEIGITGGEEDGVDNSHVSHTELYTQPEDIWDVYRELSSVTPYFSIAAAFGNVHGVYKPGNVKLQPALLGQHQAYVKEQLKTTNDKPVFFVFHGGSGSSVNEFRTGIKCGVVKVNIDTDTQFAYVEGVRDYVLKYKDYLMTPVGNPEGADKPNKKKFDPRVWIHEGEKTMTKRVLTALEDFYTVNTL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
39	Phosphorylation	PAINVTSSSTAIAAL EEEEECCCHHHHHHH	23.49	25720772
40	Phosphorylation	AINVTSSSTAIAALE EEEECCCHHHHHHHH	22.94	25720772
41	Phosphorylation	INVTSSSTAIAALEA EEECCCHHHHHHHHH	24.83	25720772
54	Phosphorylation	EAAREARSPIILQTS HHHHHCCCCEEEEEC	27.74	25720772
61	Phosphorylation	SPIILQTSNGGAHFF CCEEEEECCCCCEEE	22.10	25720772
73	Phosphorylation	HFFAGKESSNEGQKA EEECCCCCCCCCHHH	41.78	25720772
267	Phosphorylation	FFVFHGGSGSSVNEF EEEEECCCCCCHHHH	39.84	25720772
269	Phosphorylation	VFHGGSGSSVNEFRT EEECCCCCCHHHHHC	32.58	25720772
270	Phosphorylation	FHGGSGSSVNEFRTG EECCCCCCHHHHHCC	32.27	25720772
289	Phosphorylation	VVKVNIDTDTQFAYV EEEEEECCCCCEEEE	36.83	28889911
291	Phosphorylation	KVNIDTDTQFAYVEG EEEECCCCCEEEEEC	27.90	25720772
306	Phosphorylation	VRDYVLKYKDYLMTP CHHHHHHECCEEECC	12.63	25720772
309	Phosphorylation	YVLKYKDYLMTPVGN HHHHECCEEECCCCC	8.33	25720772
312	Phosphorylation	KYKDYLMTPVGNPEG HECCEEECCCCCCCC	16.54	28889911
340	Phosphorylation	WIHEGEKTMTKRVLT EEECCCCHHHHHHHH	26.27	28889911
342	Phosphorylation	HEGEKTMTKRVLTAL ECCCCHHHHHHHHHH	22.41	28889911

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 ALF_SCHPO !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ALF_SCHPO !!

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 ALF_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of ALF_SCHPO !!

Drug and Disease Associations

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

Regulatory Network of ALF_SCHPO

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 THR-289; THR-312; THR-340AND THR-342, AND MASS SPECTROMETRY.	18257517 [Abstract]