F16P2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: F16P2_HUMAN
• UniProt AC: O00757
• Protein Name: Fructose-1,6-bisphosphatase isozyme 2
• Gene Name: FBP2
• Organism: Homo sapiens (Human).
• Sequence Length: 339
• Subcellular Localization: Cell junction. Cytoplasm. Nucleus. Cytoplasm, myofibril, sarcomere, Z line. In neonatal cardiomyocytes, distributed throughout the cytosol, accumulating in the intercalated disks which occur at the Z line of cardiomyocytes and connect adjacent cells,
• Protein Description: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate in the presence of divalent cations and probably participates in glycogen synthesis from carbohydrate precursors, such as lactate..
• Protein Sequence: MTDRSPFETDMLTLTRYVMEKGRQAKGTGELTQLLNSMLTAIKAISSAVRKAGLAHLYGIAGSVNVTGDEVKKLDVLSNSLVINMVQSSYSTCVLVSEENKDAIITAKEKRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTSEDEPSEKDALQCGRNIVAAGYALYGSATLVALSTGQGVDLFMLDPALGEFVLVEKDVKIKKKGKIYSLNEGYAKYFDAATTEYVQKKKFPEDGSAPYGARYVGSMVADVHRTLVYGGIFLYPANQKSPKGKLRLLYECNPVAYIIEQAGGLATTGTQPVLDVKPEAIHQRVPLILGSPEDVQEYLTCVQKNQAGS

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
17	Phosphorylation	DMLTLTRYVMEKGRQ HHHHHHHHHHHHCCC	10.02	-
28	Phosphorylation	KGRQAKGTGELTQLL HCCCCCCHHHHHHHH	27.12	22673903
32	Phosphorylation	AKGTGELTQLLNSML CCCHHHHHHHHHHHH	16.93	22673903
40	Phosphorylation	QLLNSMLTAIKAISS HHHHHHHHHHHHHHH	20.07	-
63	Phosphorylation	HLYGIAGSVNVTGDE HHHCCCCEEECCCHH	11.07	30257219
143	Phosphorylation	IFAIYRKTSEDEPSE HEEEEECCCCCCCCH	28.49	26437602
149	Phosphorylation	KTSEDEPSEKDALQC CCCCCCCCHHHHHHH	56.05	26437602
210	Phosphorylation	IKKKGKIYSLNEGYA EEECCEEEECCCHHH	15.59	-
211	Phosphorylation	KKKGKIYSLNEGYAK EECCEEEECCCHHHH	28.35	28152594
216	Phosphorylation	IYSLNEGYAKYFDAA EEECCCHHHHHHHHH	8.17	21082442
219	Phosphorylation	LNEGYAKYFDAATTE CCCHHHHHHHHHHHH	9.87	19764811
231	Acetylation	TTEYVQKKKFPEDGS HHHHHHHCCCCCCCC	42.42	7978517
238	Phosphorylation	KKFPEDGSAPYGARY CCCCCCCCCCCCCHH	38.09	26437602
241	Phosphorylation	PEDGSAPYGARYVGS CCCCCCCCCCHHHHH	24.12	-
245	Phosphorylation	SAPYGARYVGSMVAD CCCCCCHHHHHHHHC	14.50	24275569
256	Phosphorylation	MVADVHRTLVYGGIF HHHCHHHHHEECEEE	13.00	-
259	Phosphorylation	DVHRTLVYGGIFLYP CHHHHHEECEEEEEE	16.85	22817900
265	Phosphorylation	VYGGIFLYPANQKSP EECEEEEEECCCCCC	6.91	22673903

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

Oops, there are no upstream regulatory protein records of F16P2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of F16P2_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 F16P2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CHD3_HUMAN	CHD3	physical	16169070
F16P2_HUMAN	FBP2	physical	25416956
F16P1_HUMAN	FBP1	physical	26186194
F16P1_HUMAN	FBP1	physical	28514442

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
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, AND MASSSPECTROMETRY.
PubMed: 18083107