F16P1_HUMAN - dbPTM
F16P1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID F16P1_HUMAN
UniProt AC P09467
Protein Name Fructose-1,6-bisphosphatase 1
Gene Name FBP1
Organism Homo sapiens (Human).
Sequence Length 338
Subcellular Localization
Protein Description Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate in the presence of divalent cations, acting as a rate-limiting enzyme in gluconeogenesis. Plays a role in regulating glucose sensing and insulin secretion of pancreatic beta-cells. Appears to modulate glycerol gluconeogenesis in liver. Important regulator of appetite and adiposity; increased expression of the protein in liver after nutrient excess increases circulating satiety hormones and reduces appetite-stimulating neuropeptides and thus seems to provide a feedback mechanism to limit weight gain..
Protein Sequence MADQAPFDTDVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAVRKAGIAHLYGIAGSTNVTGDQVKKLDVLSNDLVMNMLKSSFATCVLVSEEDKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGIYRKKSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLAMDCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYARDFDPAVTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVYGGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTGKEAVLDVIPTDIHQRAPVILGSPDDVLEFLKVYEKHSAQ
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 Orthologous
Protein Cluster
2Acetylation------MADQAPFDT
------CCCCCCCCC
20.02-
28PhosphorylationEGRKARGTGELTQLL
CHHHCCCHHHHHHHH
23.1728258704
32PhosphorylationARGTGELTQLLNSLC
CCCHHHHHHHHHHHH
16.9328857561
58PhosphorylationKAGIAHLYGIAGSTN
HHCCCHHHCCCCCCC
9.1627642862
63PhosphorylationHLYGIAGSTNVTGDQ
HHHCCCCCCCCCCHH
14.05-
72AcetylationNVTGDQVKKLDVLSN
CCCCHHHHHHHHCCC
41.827744611
88PhosphorylationLVMNMLKSSFATCVL
HHHHHHHHHCCEEEE
27.08-
144PhosphorylationFGIYRKKSTDEPSEK
HEEEECCCCCCCCHH
44.0924719451
151SuccinylationSTDEPSEKDALQPGR
CCCCCCHHHCCCCCC
53.27-
151SuccinylationSTDEPSEKDALQPGR
CCCCCCHHHCCCCCC
53.27-
210PhosphorylationIKKKGKIYSLNEGYA
EEECCEEEECCCCCC
15.59-
216PhosphorylationIYSLNEGYARDFDPA
EEECCCCCCCCCCHH
7.7121253578
227PhosphorylationFDPAVTEYIQRKKFP
CCHHHHHHHHHCCCC
7.93-
232AcetylationTEYIQRKKFPPDNSA
HHHHHHCCCCCCCCC
66.3519813147
241PhosphorylationPPDNSAPYGARYVGS
CCCCCCCCCHHHHHH
24.1221712546
245PhosphorylationSAPYGARYVGSMVAD
CCCCCHHHHHHHHHC
14.5024275569
256PhosphorylationMVADVHRTLVYGGIF
HHHCHHHHHEECEEE
13.0028152594
259PhosphorylationDVHRTLVYGGIFLYP
CHHHHHEECEEEEEE
16.8528152594
265PhosphorylationVYGGIFLYPANKKSP
EECEEEEEECCCCCC
6.9128348404
269AcetylationIFLYPANKKSPNGKL
EEEEECCCCCCCCCE
57.657744623
271PhosphorylationLYPANKKSPNGKLRL
EEECCCCCCCCCEEE
25.8029457462
280PhosphorylationNGKLRLLYECNPMAY
CCCEEEEEEECCHHH
24.0328258704
297PhosphorylationEKAGGMATTGKEAVL
HHCCCCCCCCCCHHH
27.47-
298PhosphorylationKAGGMATTGKEAVLD
HCCCCCCCCCCHHHH
36.40-
321PhosphorylationRAPVILGSPDDVLEF
CCCEEECCHHHHHHH
23.0124719451
330AcetylationDDVLEFLKVYEKHSA
HHHHHHHHHHHHHCC
48.3620167786
334AcetylationEFLKVYEKHSAQ---
HHHHHHHHHCCC---
25.7727178108

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
63SPhosphorylationKinaseULK1O75385
PSP
88SPhosphorylationKinaseULK1O75385
PSP
-KUbiquitinationE3 ubiquitin ligaseTRIM28Q13263
PMID:28394358

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of F16P1_HUMAN !!

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 F16P1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PCX4_HUMANPCNXL4physical
16189514
FXR2_HUMANFXR2physical
16189514
RN183_HUMANRNF183physical
16189514
LNX1_HUMANLNX1physical
16189514
F16P1_HUMANFBP1physical
16189514
F16P1_HUMANFBP1physical
16169070
F16P1_HUMANFBP1physical
2164670
NKG2C_HUMANKLRC2physical
21988832
BIN1_HUMANBIN1physical
16275660
F16P1_HUMANFBP1physical
25416956
F16P2_HUMANFBP2physical
25416956
F16P1_HUMANFBP1physical
21516116

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
229700Fructose-1,6-bisphosphatase deficiency (FBPD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00131Adenosine monophosphate
Regulatory Network of F16P1_HUMAN

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Related Literatures of Post-Translational Modification

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