PP1A_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PP1A_RAT
• UniProt AC: P62138
• Protein Name: Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
• Gene Name: Ppp1ca
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 330
• Subcellular Localization: Cytoplasm. Nucleus. Nucleus, nucleoplasm. Nucleus, nucleolus. Primarily nuclear and largely excluded from the nucleolus. Highly mobile in cells and can be relocalized through interaction with targeting subunits. NOM1 plays a role in targeting it to t
• Protein Description: Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca(2+)/calmodulin dependent protein kinase II. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. Regulates NEK2 function in terms of kinase activity and centrosome number and splitting, both in the presence and absence of radiation-induced DNA damage. Regulator of neural tube and optic fissure closure, and enteric neural crest cell (ENCCs) migration during development. In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E (By similarity). Dephosphorylates CENPA (By similarity). Dephosphorylates the 'Ser-139' residue of ATG16L1 causing dissociation of ATG12-ATG5-ATG16L1 complex, thereby inhibiting autophagy (By similarity)..
• Protein Sequence: MSDSEKLNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPADKNKGKYGQFSGLNPGGRPITPPRNSAKAKK

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
2	Phosphorylation	------MSDSEKLNL ------CCHHHHCCH	50.25	27097102
2	Acetylation	------MSDSEKLNL ------CCHHHHCCH	50.25	-
4	Phosphorylation	----MSDSEKLNLDS ----CCHHHHCCHHH	29.35	27097102
6	Acetylation	--MSDSEKLNLDSII --CCHHHHCCHHHHH	46.78	22902405
11	Phosphorylation	SEKLNLDSIIGRLLE HHHCCHHHHHHHHHH	21.19	23984901
22	Phosphorylation	RLLEVQGSRPGKNVQ HHHHHCCCCCCCCEE	20.43	-
26	Ubiquitination	VQGSRPGKNVQLTEN HCCCCCCCCEECCHH	57.54	-
42	Phosphorylation	IRGLCLKSREIFLSQ HHHHHHHCCHHHHCC	23.38	23984901
48	Phosphorylation	KSREIFLSQPILLEL HCCHHHHCCCEEEEE	24.14	23984901
129	Phosphorylation	RGNHECASINRIYGF CCCCHHHHHHHHEEE	31.86	29779826
134	Phosphorylation	CASINRIYGFYDECK HHHHHHHEEEHHHHH	9.65	-
147	Acetylation	CKRRYNIKLWKTFTD HHHHHCCCCCHHHHH	44.66	22902405
177	Phosphorylation	FCCHGGLSPDLQSME EECCCCCCCCHHHHH	21.46	23984901
260	Acetylation	DGYEFFAKRQLVTLF HCHHHHHHCCEEECC	35.20	22902405
305	Acetylation	PADKNKGKYGQFSGL CCCCCCCCCCCCCCC	48.06	-
306	Phosphorylation	ADKNKGKYGQFSGLN CCCCCCCCCCCCCCC	25.48	27097102
320	Phosphorylation	NPGGRPITPPRNSAK CCCCCCCCCCCCCCC	29.89	27097102
325	Phosphorylation	PITPPRNSAKAKK-- CCCCCCCCCCCCC--	32.21	23984901

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
320	T	Phosphorylation	Kinase	CDK1	P06493	PSP
320	T	Phosphorylation	Kinase	CDK5	Q03114	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
320	T	Phosphorylation	Dephosphorylated at Thr-320 in the presence of ionizing radiation (By similarity).	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of PP1A_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of PP1A_RAT !!

Drug and Disease Associations

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