dbPTM

2A5A_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	2A5A_MOUSE
UniProt AC	Q6PD03
Protein Name	Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform
Gene Name	Ppp2r5a
Organism	Mus musculus (Mouse).
Sequence Length	486
Subcellular Localization	Cytoplasm. Nucleus. Chromosome, centromere. From mitotic prophase to metaphase, localizes at the inner centromere between a pair of sister kinetochores. Decreased expression at the onset of anaphase (By similarity)..
Protein Description	The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment..
Protein Sequence	MSSPSPPAPVACAAISASEKVDGFTRKSVRKAQRQKRSQGSSQFRSQGSQAELHPLPQLKDATSNEQQELFCQKLQQCCVLFDFMDSVSDLKSKEIKRATLNELVEYVSTNRGVIVESAYSDIVKMISANIFRTLPPSDNPDFDPEEDEPTLEASWPHIQLVYEFFLRFLESPDFQPSIAKRYIDQKFVQQLLELFDSEDPRERDFLKTVLHRIYGKFLGLRAFIRKQINNIFLRFIYETEHFNGVAELLEILGSIINGFALPLKAEHKQFLMKVLIPMHTAKGLALFHAQLAYCVVQFLEKDTTLTEPVIRGLLKFWPKTCSQKEVMFLGEIEEILDVIEPTQFKKIEEPLFKQISKCVSSSHFQVAERALYFWNNEYILSLIEENIDKILPIMFASLYKISKEHWNQTIVALVYNVLKTLMEMNGKLFDDLTSSYKAERQREKKKELEREELWKKLEELQLKKALEKQNNAYNMHSIRSSTSAK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSSPSPPAP ------CCCCCCCCC	51.46	-
2	Phosphorylation	------MSSPSPPAP ------CCCCCCCCC	51.46	24759943
3	Phosphorylation	-----MSSPSPPAPV -----CCCCCCCCCC	28.26	24759943
5	Phosphorylation	---MSSPSPPAPVAC ---CCCCCCCCCCHH	45.52	26643407
25	Phosphorylation	SEKVDGFTRKSVRKA HHCCCCCCHHHHHHH	42.59	24719451
28	Phosphorylation	VDGFTRKSVRKAQRQ CCCCCHHHHHHHHHH	24.70	29514104
38	Phosphorylation	KAQRQKRSQGSSQFR HHHHHHHHCCCHHHH	46.02	27087446
41	Phosphorylation	RQKRSQGSSQFRSQG HHHHHCCCHHHHHCC	17.21	27087446
42	Phosphorylation	QKRSQGSSQFRSQGS HHHHCCCHHHHHCCC	39.91	27087446
46	Phosphorylation	QGSSQFRSQGSQAEL CCCHHHHHCCCCCEE	39.93	26239621
49	Phosphorylation	SQFRSQGSQAELHPL HHHHHCCCCCEECCC	20.69	27742792
181	Malonylation	DFQPSIAKRYIDQKF CCCHHHHHHHCCHHH	44.03	26320211
227	Ubiquitination	GLRAFIRKQINNIFL CHHHHHHHHHHHHHH	51.19	-
474	Phosphorylation	LEKQNNAYNMHSIRS HHHHCCCCCHHHCCC	18.36	25367039
478	Phosphorylation	NNAYNMHSIRSSTSA CCCCCHHHCCCCCCC	14.66	19060867

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 2A5A_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of 2A5A_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 2A5A_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of 2A5A_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of 2A5A_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 SER-41 AND SER-42, AND MASSSPECTROMETRY.	19367708 [Abstract]