dbPTM

PP1B_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PP1B_MOUSE
UniProt AC	P62141
Protein Name	Serine/threonine-protein phosphatase PP1-beta catalytic subunit
Gene Name	Ppp1cb
Organism	Mus musculus (Mouse).
Sequence Length	327
Subcellular Localization	Cytoplasm . Nucleus . Nucleus, nucleoplasm . Nucleus, nucleolus . Highly mobile in cells and can be relocalized through interaction with targeting subunits. In the presence of PPP1R8 relocalizes from the nucleus to nuclear speckles.
Protein Description	Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase (PP1) is essential for cell division, it participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. 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. 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..
Protein Sequence	MADGELNVDSLITRLLEVRGCRPGKIVQMTEAEVRGLCIKSREIFLSQPILLELEAPLKICGDIHGQYTDLLRLFEYGGFPPEANYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRFNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDTGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVSKFLNRHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGGMMSVDETLMCSFQILKPSEKKAKYQYGGLNSGRPVTPPRTANPPKKR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MADGELNVD ------CCCCCCCHH	33.25	-
10	Phosphorylation	DGELNVDSLITRLLE CCCCCHHHHHHHHHH	19.86	20469934
13	Phosphorylation	LNVDSLITRLLEVRG CCHHHHHHHHHHHCC	22.13	20469934
25	Acetylation	VRGCRPGKIVQMTEA HCCCCCCCEEEEEHH	42.24	23236377
25	Malonylation	VRGCRPGKIVQMTEA HCCCCCCCEEEEEHH	42.24	26320211
25	Ubiquitination	VRGCRPGKIVQMTEA HCCCCCCCEEEEEHH	42.24	-
41	Phosphorylation	VRGLCIKSREIFLSQ HHCCEECCCCHHHCC	18.42	26745281
47	Phosphorylation	KSREIFLSQPILLEL CCCCHHHCCCEEEEE	24.14	26745281
97	Ubiquitination	GDYVDRGKQSLETIC HHHCHHCHHHHHHHH	37.29	-
112	Acetylation	LLLAYKIKYPENFFL HHHHHHCCCCCCEEE	51.07	22826441
112	Ubiquitination	LLLAYKIKYPENFFL HHHHHHCCCCCCEEE	51.07	22790023
128	Phosphorylation	RGNHECASINRIYGF CCCCHHHHHHHHEEC	31.86	23684622
136	Phosphorylation	INRIYGFYDECKRRF HHHHEECHHHHHHHH	13.38	-
140	Ubiquitination	YGFYDECKRRFNIKL EECHHHHHHHHCCCH	44.56	-
140	Acetylation	YGFYDECKRRFNIKL EECHHHHHHHHCCCH	44.56	68947
140	Malonylation	YGFYDECKRRFNIKL EECHHHHHHHHCCCH	44.56	26320211
146	Ubiquitination	CKRRFNIKLWKTFTD HHHHHCCCHHHHHHH	49.77	22790023
146	Acetylation	CKRRFNIKLWKTFTD HHHHHCCCHHHHHHH	49.77	22826441
149	Ubiquitination	RFNIKLWKTFTDCFN HHCCCHHHHHHHHCC	44.17	-
150	Phosphorylation	FNIKLWKTFTDCFNC HCCCHHHHHHHHCCC	21.86	23984901
152	Phosphorylation	IKLWKTFTDCFNCLP CCHHHHHHHHCCCCH	36.77	23984901
170	S-palmitoylation	IVDEKIFCCHGGLSP HCCCCEEECCCCCCC	1.58	28680068
171	S-palmitoylation	VDEKIFCCHGGLSPD CCCCEEECCCCCCCC	2.02	28680068
181	Phosphorylation	GLSPDLQSMEQIRRI CCCCCHHHHHHHHHH	31.42	28464351
192	Phosphorylation	IRRIMRPTDVPDTGL HHHHCCCCCCCCCCC	38.98	22817900
197	Phosphorylation	RPTDVPDTGLLCDLL CCCCCCCCCCHHHHH	24.53	22817900
206	Phosphorylation	LLCDLLWSDPDKDVQ CHHHHHCCCCCCCCC	38.95	19854140
233	Ubiquitination	FGADVVSKFLNRHDL ECHHHHHHHHCHHCH	42.11	-
259	Ubiquitination	DGYEFFAKRQLVTLF HCHHHHHHCCEEECC	35.20	-
259	Acetylation	DGYEFFAKRQLVTLF HCHHHHHHCCEEECC	35.20	19809623
303	Ubiquitination	KPSEKKAKYQYGGLN CCCCCCCCCCCCCCC	41.59	22790023
304	Phosphorylation	PSEKKAKYQYGGLNS CCCCCCCCCCCCCCC	16.30	28833060
306	Phosphorylation	EKKAKYQYGGLNSGR CCCCCCCCCCCCCCC	15.29	28833060
311	Phosphorylation	YQYGGLNSGRPVTPP CCCCCCCCCCCCCCC	41.02	26824392
316	Phosphorylation	LNSGRPVTPPRTANP CCCCCCCCCCCCCCC	30.20	26824392
320	Phosphorylation	RPVTPPRTANPPKKR CCCCCCCCCCCCCCC	36.24	25266776

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
Oops, there are no upstream regulatory protein records of PP1B_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PP1B_MOUSE !!

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 PP1B_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CCNB1_MOUSE	Ccnb1	physical	17274640
CCND3_MOUSE	Ccnd3	physical	17274640
HS71B_MOUSE	Hspa1b	physical	17274640
AP2A1_HUMAN	AP2A1	physical	26496610
CAZA2_HUMAN	CAPZA2	physical	26496610
CD59_HUMAN	CD59	physical	26496610
AP2M1_HUMAN	AP2M1	physical	26496610
CLCA_HUMAN	CLTA	physical	26496610
CLCB_HUMAN	CLTB	physical	26496610
CLH1_HUMAN	CLTC	physical	26496610
DAB2_HUMAN	DAB2	physical	26496610
DREB_HUMAN	DBN1	physical	26496610
DHX9_HUMAN	DHX9	physical	26496610
DSG2_HUMAN	DSG2	physical	26496610
FLII_HUMAN	FLII	physical	26496610
GELS_HUMAN	GSN	physical	26496610
PLAK_HUMAN	JUP	physical	26496610
ABLM1_HUMAN	ABLIM1	physical	26496610
MYO1B_HUMAN	MYO1B	physical	26496610
MYO1C_HUMAN	MYO1C	physical	26496610
MYO1E_HUMAN	MYO1E	physical	26496610
MYO5A_HUMAN	MYO5A	physical	26496610
MYPT1_HUMAN	PPP1R12A	physical	26496610
MYPT2_HUMAN	PPP1R12B	physical	26496610
PP1A_HUMAN	PPP1CA	physical	26496610
IPP2_HUMAN	PPP1R2	physical	26496610
PP1R8_HUMAN	PPP1R8	physical	26496610
PP1RA_HUMAN	PPP1R10	physical	26496610
TWF1_HUMAN	TWF1	physical	26496610
SPTN1_HUMAN	SPTAN1	physical	26496610
SPTB2_HUMAN	SPTBN1	physical	26496610
SSFA2_HUMAN	SSFA2	physical	26496610
SVIL_HUMAN	SVIL	physical	26496610
TMOD1_HUMAN	TMOD1	physical	26496610
YES_HUMAN	YES1	physical	26496610
LUZP1_HUMAN	LUZP1	physical	26496610
SRBS2_HUMAN	SORBS2	physical	26496610
PABP4_HUMAN	PABPC4	physical	26496610
LRRF2_HUMAN	LRRFIP2	physical	26496610
TOX4_HUMAN	TOX4	physical	26496610
RBM6_HUMAN	RBM6	physical	26496610
IASPP_HUMAN	PPP1R13L	physical	26496610
TARA_HUMAN	TRIOBP	physical	26496610
SYNPO_HUMAN	SYNPO	physical	26496610
AAK1_HUMAN	AAK1	physical	26496610
MPRIP_HUMAN	MPRIP	physical	26496610
COBL_HUMAN	COBL	physical	26496610
CYTSA_HUMAN	SPECC1L	physical	26496610
SCRIB_HUMAN	SCRIB	physical	26496610
RAI14_HUMAN	RAI14	physical	26496610
ZN638_HUMAN	ZNF638	physical	26496610
PACN3_HUMAN	PACSIN3	physical	26496610
TMOD3_HUMAN	TMOD3	physical	26496610
PP12C_HUMAN	PPP1R12C	physical	26496610
UACA_HUMAN	UACA	physical	26496610
RIF1_HUMAN	RIF1	physical	26496610
BMP2K_HUMAN	BMP2K	physical	26496610
YLPM1_HUMAN	YLPM1	physical	26496610
PARD3_HUMAN	PARD3	physical	26496610
AFAP1_HUMAN	AFAP1	physical	26496610
SH24A_HUMAN	SH2D4A	physical	26496610
AHNK_HUMAN	AHNAK	physical	26496610
KI18A_HUMAN	KIF18A	physical	26496610
ANTR1_HUMAN	ANTXR1	physical	26496610
PP16A_HUMAN	PPP1R16A	physical	26496610
STON2_HUMAN	STON2	physical	26496610
CYTSB_HUMAN	SPECC1	physical	26496610
MISP_HUMAN	MISP	physical	26496610
KI18B_HUMAN	KIF18B	physical	26496610
MY18A_HUMAN	MYO18A	physical	26496610
WDR92_HUMAN	WDR92	physical	26496610

Drug and Disease Associations

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

Regulatory Network of PP1B_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-316, AND MASSSPECTROMETRY.	19367708 [Abstract]