dbPTM

PP2BA_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PP2BA_MOUSE
UniProt AC	P63328
Protein Name	Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform
Gene Name	Ppp3ca
Organism	Mus musculus (Mouse).
Sequence Length	521
Subcellular Localization	Cytoplasm . Cell membrane Peripheral membrane protein . Cell membrane, sarcolemma . Cytoplasm, myofibril, sarcomere, Z line . Cell projection, dendritic spine . Colocalizes with ACTN1 and MYOZ2 at the Z line in heart and skeletal muscle. Recruited
Protein Description	Calcium-dependent, calmodulin-stimulated protein phosphatase which plays an essential role in the transduction of intracellular Ca(2+)-mediated signals. [PubMed: 7791792]
Protein Sequence	MSEPKAIDPKLSTTDRVVKAVPFPPSHRLTAKEVFDNDGKPRVDILKAHLMKEGRLEESVALRIITEGASILRQEKNLLDIDAPVTVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMDAFDCLPLAALMNQQFLCVHGGLSPEINTLDDIRKLDRFKEPPAYGPMCDILWSDPLEDFGNEKTQEHFTHNTVRGCSYFYSYPAVCDFLQHNNLLSILRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTEMLVNVLNICSDDELGSEEDGFDGATAAARKEVIRNKIRAIGKMARVFSVLREESESVLTLKGLTPTGMLPSGVLSGGKQTLQSATVEAIEADEAIKGFSPQHKITSFEEAKGLDRINERMPPRRDAMPSDANLNSINKALASETNGTDSNGSNSSNIQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSEPKAIDP ------CCCCCCCCC	63.71	-
2	Phosphorylation	------MSEPKAIDP ------CCCCCCCCC	63.71	-
10 (in isoform 2)	Ubiquitination	-	51.85	22790023
10	Ubiquitination	EPKAIDPKLSTTDRV CCCCCCCCCCCCCCE	51.85	22790023
32	Methylation	PSHRLTAKEVFDNDG CCCCCCHHHHCCCCC	49.53	-
32 (in isoform 2)	Ubiquitination	-	49.53	22790023
32	Ubiquitination	PSHRLTAKEVFDNDG CCCCCCHHHHCCCCC	49.53	22790023
59	Phosphorylation	KEGRLEESVALRIIT HCCCCCHHHHHHHHH	11.87	22817900
66	Phosphorylation	SVALRIITEGASILR HHHHHHHHHHHHHHH	26.45	21454597
70	Phosphorylation	RIITEGASILRQEKN HHHHHHHHHHHHHCC	32.77	21454597
107	Phosphorylation	KLFEVGGSPANTRYL HHHCCCCCCCCCEEE	18.21	22817900
142 (in isoform 2)	Ubiquitination	-	44.28	22790023
142	Ubiquitination	ALKILYPKTLFLLRG HHHHHCCHHHHHHCC	44.28	22790023
143	Phosphorylation	LKILYPKTLFLLRGN HHHHCCHHHHHHCCC	20.45	29899451
224	Nitrated tyrosine	RFKEPPAYGPMCDIL HCCCCCCCCCCCCEE	27.77	-
224	Nitration	RFKEPPAYGPMCDIL HCCCCCCCCCCCCEE	27.77	16800626
224	Nitration	RFKEPPAYGPMCDIL HCCCCCCCCCCCCEE	27.77	16800626
228	S-palmitoylation	PPAYGPMCDILWSDP CCCCCCCCCEEECCC	3.11	28680068
288	Phosphorylation	HEAQDAGYRMYRKSQ HHHHHHCCCCHHHHC	8.23	29899451
323 (in isoform 2)	Ubiquitination	-	43.87	22790023
323	Ubiquitination	NNKAAVLKYENNVMN CCCEEEEEEECCEEC	43.87	22790023
362	Phosphorylation	PFVGEKVTEMLVNVL CCCCHHHHHHHHHHH	27.09	30635358
373	Phosphorylation	VNVLNICSDDELGSE HHHHHHCCCCCCCCC	44.28	30635358
379	Phosphorylation	CSDDELGSEEDGFDG CCCCCCCCCCCCCCH	50.89	30635358
388	Phosphorylation	EDGFDGATAAARKEV CCCCCHHHHHHHHHH	23.51	30635358
411	Phosphorylation	GKMARVFSVLREESE HHHHHHHHHHHHHCC	19.86	22324799
417	Phosphorylation	FSVLREESESVLTLK HHHHHHHCCCEEEEC	30.34	20415495
419	Phosphorylation	VLREESESVLTLKGL HHHHHCCCEEEECCC	31.54	20415495
422	Phosphorylation	EESESVLTLKGLTPT HHCCCEEEECCCCCC	25.03	20415495
427	Phosphorylation	VLTLKGLTPTGMLPS EEEECCCCCCCCCCC	27.72	22324799
429	Phosphorylation	TLKGLTPTGMLPSGV EECCCCCCCCCCCCC	29.95	22324799
434	Phosphorylation	TPTGMLPSGVLSGGK CCCCCCCCCCCCCCC	37.26	25777480
438	Phosphorylation	MLPSGVLSGGKQTLQ CCCCCCCCCCCHHHH	42.99	25777480
443	Phosphorylation	VLSGGKQTLQSATVE CCCCCCHHHHHCEEE	30.19	25777480
446	Phosphorylation	GGKQTLQSATVEAIE CCCHHHHHCEEEEHH	29.08	25777480
448	Phosphorylation	KQTLQSATVEAIEAD CHHHHHCEEEEHHHH	24.91	25777480
452 (in isoform 2)	Phosphorylation	-	2.58	27841257
456 (in isoform 2)	Ubiquitination	-	60.38	-
459 (in isoform 2)	Phosphorylation	-	62.03	29514104
462	Phosphorylation	DEAIKGFSPQHKITS HHHHCCCCCCCCCCC	32.11	25521595
466	Ubiquitination	KGFSPQHKITSFEEA CCCCCCCCCCCHHHH	42.29	22790023
466 (in isoform 2)	Ubiquitination	-	42.29	22790023
468	Phosphorylation	FSPQHKITSFEEAKG CCCCCCCCCHHHHCC	31.97	22324799
469	Phosphorylation	SPQHKITSFEEAKGL CCCCCCCCHHHHCCH	33.85	25521595
492	Phosphorylation	PRRDAMPSDANLNSI CCCCCCCCCCCHHHH	35.95	25521595
498	Phosphorylation	PSDANLNSINKALAS CCCCCHHHHHHHHHH	30.61	25521595
505	Phosphorylation	SINKALASETNGTDS HHHHHHHHHCCCCCC	45.89	30635358
507	Phosphorylation	NKALASETNGTDSNG HHHHHHHCCCCCCCC	36.13	30635358
510	Phosphorylation	LASETNGTDSNGSNS HHHHCCCCCCCCCCC	38.02	30635358
512	Phosphorylation	SETNGTDSNGSNSSN HHCCCCCCCCCCCCC	42.82	30635358
515	Phosphorylation	NGTDSNGSNSSNIQ- CCCCCCCCCCCCCC-	37.48	30635358
517	Phosphorylation	TDSNGSNSSNIQ--- CCCCCCCCCCCC---	26.85	30635358
518	Phosphorylation	DSNGSNSSNIQ---- CCCCCCCCCCC----	42.05	30635358

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
-	K	Ubiquitination	E3 ubiquitin ligase	Nedd4l	Q8CFI0	PMID:31357244

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PP2BA_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 PP2BA_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GBRG2_MOUSE	Gabrg2	physical	12574411
GBRB2_MOUSE	Gabrb2	physical	12574411
GBRA1_MOUSE	Gabra1	physical	12574411

Drug and Disease Associations

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

Regulatory Network of PP2BA_MOUSE

Related Literatures of Post-Translational Modification

Nitration
Reference	PubMed
"Endogenously nitrated proteins in mouse brain: links toneurodegenerative disease."; Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H.,Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J.,Squier T.C., Bigelow D.J.; Biochemistry 45:8009-8022(2006). Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-224, AND MASS SPECTROMETRY.	16800626 [Abstract]
Phosphorylation
Reference	PubMed
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-469, AND MASSSPECTROMETRY.	17114649 [Abstract]