PPR3B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PPR3B_HUMAN
• UniProt AC: Q86XI6
• Protein Name: Protein phosphatase 1 regulatory subunit 3B
• Gene Name: PPP1R3B
• Organism: Homo sapiens (Human).
• Sequence Length: 285
• Protein Description: Acts as a glycogen-targeting subunit for phosphatase PP1. Facilitates interaction of the PP1 with enzymes of the glycogen metabolism and regulates its activity. Suppresses the rate at which PP1 dephosphorylates (inactivates) glycogen phosphorylase and enhances the rate at which it activates glycogen synthase and therefore limits glycogen breakdown. Its activity is inhibited by PYGL, resulting in inhibition of the glycogen synthase and glycogen phosphorylase phosphatase activities of PP1. Dramatically increases basal and insulin-stimulated glycogen synthesis upon overexpression in hepatocytes (By similarity)..
• Protein Sequence: MMAVDIEYRYNCMAPSLRQERFAFKISPKPSKPLRPCIQLSSKNEASGMVAPAVQEKKVKKRVSFADNQGLALTMVKVFSEFDDPLDMPFNITELLDNIVSLTTAESESFVLDFSQPSADYLDFRNRLQADHVCLENCVLKDKAIAGTVKVQNLAFEKTVKIRMTFDTWKSYTDFPCQYVKDTYAGSDRDTFSFDISLPEKIQSYERMEFAVYYECNGQTYWDSNRGKNYRIIRAELKSTQGMTKPHSGPDLGISFDQFGSPRCSYGLFPEWPSYLGYEKLGPYY

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
31	Phosphorylation	FKISPKPSKPLRPCI EECCCCCCCCCCCEE	53.70	24719451
57	Acetylation	VAPAVQEKKVKKRVS CCHHHHHHCHHCCCC	45.86	19819195
58	Ubiquitination	APAVQEKKVKKRVSF CHHHHHHCHHCCCCC	59.54	-
141	Ubiquitination	CLENCVLKDKAIAGT EEECCEECCCCEECE	36.46	-
143	Ubiquitination	ENCVLKDKAIAGTVK ECCEECCCCEECEEE	39.85	-
148	Phosphorylation	KDKAIAGTVKVQNLA CCCCEECEEEEEEEE	14.24	-
150	Ubiquitination	KAIAGTVKVQNLAFE CCEECEEEEEEEEEE	37.63	29967540
158	Ubiquitination	VQNLAFEKTVKIRMT EEEEEEEEEEEEEEE	52.76	29967540
165	Phosphorylation	KTVKIRMTFDTWKSY EEEEEEEEECCHHHC	14.44	22210691
168	Phosphorylation	KIRMTFDTWKSYTDF EEEEEECCHHHCCCC	30.51	22210691
172	Phosphorylation	TFDTWKSYTDFPCQY EECCHHHCCCCCCCE	13.45	-
181	Ubiquitination	DFPCQYVKDTYAGSD CCCCCEEEECCCCCC	39.14	29967540
184	Phosphorylation	CQYVKDTYAGSDRDT CCEEEECCCCCCCCE	21.06	-
213	Phosphorylation	ERMEFAVYYECNGQT CEEEEEEEEEECCEE	7.07	-
214	Phosphorylation	RMEFAVYYECNGQTY EEEEEEEEEECCEEE	13.86	-
230	Phosphorylation	DSNRGKNYRIIRAEL ECCCCCCEEEEEEEE	13.48	18083107
239	Phosphorylation	IIRAELKSTQGMTKP EEEEEEECCCCCCCC	38.29	24275569
244	Phosphorylation	LKSTQGMTKPHSGPD EECCCCCCCCCCCCC	48.53	24275569
248	Phosphorylation	QGMTKPHSGPDLGIS CCCCCCCCCCCCCCC	61.62	28857561
255	Phosphorylation	SGPDLGISFDQFGSP CCCCCCCCCHHCCCC	22.44	24275569
261	Phosphorylation	ISFDQFGSPRCSYGL CCCHHCCCCCCCCCC	15.51	25159151
285	Phosphorylation	YEKLGPYY------- CCCCCCCC-------	18.40	17870073

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

Oops, there are no upstream regulatory protein records of PPR3B_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PPR3B_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
57	Acetylation	48 (9)	G ⇒ E	rs3748140	Alzheimer's disease	22832961

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PP1G_HUMAN	PPP1CC	physical	26186194
PP1A_HUMAN	PPP1CA	physical	26186194
NIPS2_HUMAN	GBAS	physical	26186194
GLYG_HUMAN	GYG1	physical	26186194
GYS2_HUMAN	GYS2	physical	26186194
GYS1_HUMAN	GYS1	physical	26186194
TYY1_HUMAN	YY1	physical	26186194
PP1G_HUMAN	PPP1CC	physical	28514442
TYY1_HUMAN	YY1	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.