dbPTM

PP1A_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PP1A_MOUSE
UniProt AC	P62137
Protein Name	Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
Gene Name	Ppp1ca
Organism	Mus musculus (Mouse).
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 this pr
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. 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	MSDSEKLNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIRYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPADKNKGKYGQFSGLNPGGRPITPPRNSAKAKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSDSEKLNL ------CCHHHHCCH	50.25	-
2	Phosphorylation	------MSDSEKLNL ------CCHHHHCCH	50.25	23527152
4	Phosphorylation	----MSDSEKLNLDS ----CCHHHHCCHHH	29.35	25266776
11	Phosphorylation	SEKLNLDSIIGRLLE HHHCCHHHHHHHHHH	21.19	28066266
22	Phosphorylation	RLLEVQGSRPGKNVQ HHHHHCCCCCCCCEE	20.43	26824392
26	Ubiquitination	VQGSRPGKNVQLTEN HCCCCCCCCEECCHH	57.54	27667366
26	Malonylation	VQGSRPGKNVQLTEN HCCCCCCCCEECCHH	57.54	26320211
42	Phosphorylation	IRGLCLKSREIFLSQ HHHHHHHCCHHHHCC	23.38	26745281
48	Phosphorylation	KSREIFLSQPILLEL HCCHHHHCCCEEEEE	24.14	26745281
98	Ubiquitination	GDYVDRGKQSLETIC HHHCHHCHHHHHHHH	37.29	-
129	Phosphorylation	RGNHECASINRIYGF CCCCHHHHHHHHEEE	31.86	23684622
137	Phosphorylation	INRIYGFYDECKRRY HHHHEEEHHHHHHHH	13.38	-
141	Acetylation	YGFYDECKRRYNIKL EEEHHHHHHHHCCCC	37.55	23806337
141	Ubiquitination	YGFYDECKRRYNIKL EEEHHHHHHHHCCCC	37.55	-
141	Malonylation	YGFYDECKRRYNIKL EEEHHHHHHHHCCCC	37.55	26320211
147	Acetylation	CKRRYNIKLWKTFTD HHHHHCCCCCHHHHH	44.66	22826441
147	Ubiquitination	CKRRYNIKLWKTFTD HHHHHCCCCCHHHHH	44.66	22790023
150	Ubiquitination	RYNIKLWKTFTDCFN HHCCCCCHHHHHHCC	44.17	-
151	Phosphorylation	YNIKLWKTFTDCFNC HCCCCCHHHHHHCCC	21.86	23984901
153	Phosphorylation	IKLWKTFTDCFNCLP CCCCHHHHHHCCCCH	36.77	23984901
155	Glutathionylation	LWKTFTDCFNCLPIA CCHHHHHHCCCCHHH	2.10	24333276
155	S-palmitoylation	LWKTFTDCFNCLPIA CCHHHHHHCCCCHHH	2.10	28526873
171	Glutathionylation	IVDEKIFCCHGGLSP HCCCCEEECCCCCCC	1.58	24333276
171	S-palmitoylation	IVDEKIFCCHGGLSP HCCCCEEECCCCCCC	1.58	28680068
172	S-palmitoylation	VDEKIFCCHGGLSPD CCCCEEECCCCCCCC	2.02	28680068
182	Phosphorylation	GLSPDLQSMEQIRRI CCCCCHHHHHHHHHH	31.42	28464351
207	Phosphorylation	LLCDLLWSDPDKDVQ CCCHHHCCCCCCCCC	38.95	22817900
238	Acetylation	VVAKFLHKHDLDLIC HHHHHHCCCCHHHHH	40.75	22826441
245	S-palmitoylation	KHDLDLICRAHQVVE CCCHHHHHHHHHHHH	4.01	28526873
260	Ubiquitination	DGYEFFAKRQLVTLF HCHHHHHHCCEEECC	35.20	22790023
260	Acetylation	DGYEFFAKRQLVTLF HCHHHHHHCCEEECC	35.20	23236377
305	Acetylation	PADKNKGKYGQFSGL CCCCCCCCCCCCCCC	48.06	23806337
305	Ubiquitination	PADKNKGKYGQFSGL CCCCCCCCCCCCCCC	48.06	27667366
306	Phosphorylation	ADKNKGKYGQFSGLN CCCCCCCCCCCCCCC	25.48	28833060
310	Phosphorylation	KGKYGQFSGLNPGGR CCCCCCCCCCCCCCC	34.19	28833060
320	Phosphorylation	NPGGRPITPPRNSAK CCCCCCCCCCCCCCC	29.89	16888006
325	Phosphorylation	PITPPRNSAKAKK-- CCCCCCCCCCCCC--	32.21	21082442

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	P11440	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
320	T	Phosphorylation		21183079
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.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of PP1A_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ATM_MOUSE	Atm	physical	17274640
BCL2_MOUSE	Bcl2	physical	17274640
EIF2A_MOUSE	Eif2a	physical	17274640
FAK1_MOUSE	Ptk2	physical	17274640
LBR_MOUSE	Lbr	physical	17274640
TAU_MOUSE	Mapt	physical	17274640
NEK2_MOUSE	Nek2	physical	17274640
CDN2A_MOUSE	Cdkn2a	physical	17274640
ARF_MOUSE	Cdkn2a	physical	17274640
UB2R1_MOUSE	Cdc34	physical	17274640
CCNB1_MOUSE	Ccnb1	physical	17274640
CCND3_MOUSE	Ccnd3	physical	17274640
HS71B_MOUSE	Hspa1b	physical	17274640
SKP1_MOUSE	Skp1a	physical	17274640
PCNA_MOUSE	Pcna	physical	17274640
APAF_MOUSE	Apaf1	physical	17274640
CCNA1_MOUSE	Ccna1	physical	17274640
PTPA_MOUSE	Ppp2r4	physical	17274640
CCNE1_MOUSE	Ccne1	physical	17274640
TSC1_MOUSE	Tsc1	physical	17274640
ID2_MOUSE	Id2	physical	17274640
PER2_HUMAN	PER2	physical	16813562

Drug and Disease Associations

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

Regulatory Network of PP1A_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 THR-320, AND MASSSPECTROMETRY.	19367708 [Abstract]
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-306, AND MASSSPECTROMETRY.	19131326 [Abstract]

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