dbPTM

F262_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	F262_MOUSE
UniProt AC	P70265
Protein Name	6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2
Gene Name	Pfkfb2
Organism	Mus musculus (Mouse).
Sequence Length	519
Subcellular Localization
Protein Description	Synthesis and degradation of fructose 2,6-bisphosphate..
Protein Sequence	MSENSTFSTEDSCNSSYKPHASNLRRAGKTCSWASYMTNSPTLIVMIGLPARGKTYVSKKLTRYLNWIGVPTKVFNLGVYRREAVKSYQSYDFFRHDNEEAMKIRKQCALVALEDVKAYFTEESGQIAVFDATNTTRERRDMILNFAKQNAFKVFFVESVCDDPDVIAANILEVKVSSPDYPERNRENVMEDFLKRIECYKVTYQPLDPDNYDKDLSFIKVMNVGQRFLVNRVQDYIQSKIVYYLMNIHVHPRTIYLCRHGESEFNLLGKIGGDSGLSVRGKQFAHALKKFLEEQEIQDLKVWTSQLKRTIQTAESLGVTYEQWKILNEIDAGVCEEMTYSEIEQRYPEEFALRDQEKYLYRYPGGESYQDLVQRLEPVIMELERQGNILVISHQAVMRCLLAYFLDKGADELPYLRCPLHIIFKLTPVAYGCKVETITLNVDAVDTHRDKPTHNFPKSQTPVRMRRNSFTPLSSSNTIRRPRNYSVGSRPLKPLSPLRALDMQEGADQPKTQVSIPVV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSENSTFST ------CCCCCCCCC	45.55	-
32	Phosphorylation	RRAGKTCSWASYMTN HHCCCCCCHHHHHCC	30.79	-
178	Phosphorylation	ILEVKVSSPDYPERN EEEEEECCCCCCHHC	25.44	-
195	Acetylation	NVMEDFLKRIECYKV HHHHHHHHHHCEEEE	51.85	7613079
461	Phosphorylation	HNFPKSQTPVRMRRN CCCCCCCCCCEECCC	30.73	-
469	Phosphorylation	PVRMRRNSFTPLSSS CCEECCCCCCCCCCC	28.78	26824392
471	Phosphorylation	RMRRNSFTPLSSSNT EECCCCCCCCCCCCC	24.12	27742792
474	Phosphorylation	RNSFTPLSSSNTIRR CCCCCCCCCCCCCCC	32.68	28833060
475	Phosphorylation	NSFTPLSSSNTIRRP CCCCCCCCCCCCCCC	34.98	28833060
476	Phosphorylation	SFTPLSSSNTIRRPR CCCCCCCCCCCCCCC	34.32	28833060
478	Phosphorylation	TPLSSSNTIRRPRNY CCCCCCCCCCCCCCC	20.15	28833060
485	Phosphorylation	TIRRPRNYSVGSRPL CCCCCCCCCCCCCCC	13.15	26239621
486	Phosphorylation	IRRPRNYSVGSRPLK CCCCCCCCCCCCCCC	24.45	26824392
489	Phosphorylation	PRNYSVGSRPLKPLS CCCCCCCCCCCCCCC	28.68	26239621
496	Phosphorylation	SRPLKPLSPLRALDM CCCCCCCCCCEEHHH	30.34	26824392

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
32	S	Phosphorylation	Kinase	PKA	-	Uniprot
469	S	Phosphorylation	Kinase	AMPK-FAMILY	-	GPS
469	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
478	T	Phosphorylation	Kinase	PKC	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of F262_MOUSE !!

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 F262_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of F262_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of F262_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-469 AND SER-496, ANDMASS SPECTROMETRY.	19367708 [Abstract]