dbPTM

PP2B3_DROME - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PP2B3_DROME
UniProt AC	Q9VXF1
Protein Name	Serine/threonine-protein phosphatase 2B catalytic subunit 3
Gene Name	CanA-14F {ECO:0000312\|EMBL:AAF48623.4, ECO:0000312\|FlyBase:FBgn0267912}
Organism	Drosophila melanogaster (Fruit fly).
Sequence Length	584
Subcellular Localization
Protein Description	Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin..
Protein Sequence	MSSPAAQSNSSSSQSQSAAQQQQQQNQKANVNNTHDNKNAAATTGTAAGSGSGGAAGSAGTQQQGQGGTGTSSGPSSPTKRSTISTKERVIDSVAFPPSRKLTCADVFDARTGKPQHDVLKQHFILEGRIEESAALRIIQEGATLLRTEKTMIDIEAPVTVCGDIHGQFYDLMKLFEIGGSPATTKYLFLGDYVDRGYFSIECVLYLWSLKITYPQTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMDAFDCLPLAALMNQQFLCVHGGLSPEIHELEDIRRLDRFKEPPAFGPMCDLLWSDPLEDFGNEKNSDFYTHNSVRGCSYFYSYAACCDFLQNNNLLSIIRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTEMLVNVLNICSDDELMTEESEEPLSDDEAALRKEVIRNKIRAIGKMARVFSVLREESESVLQLKGLTPTGALPLGALSGGKQSLKNAMQGFSPNHKITSFAEAKGLDAVNERMPPRRDATPSPAEEGQKSLSAAAAAAANANANSING

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSSPAAQSN ------CCCHHHCCC	45.06	28490779
3	Phosphorylation	-----MSSPAAQSNS -----CCCHHHCCCC	19.77	28490779
61	Phosphorylation	GAAGSAGTQQQGQGG CCCCCCCCCCCCCCC	23.95	18327897
73	Phosphorylation	QGGTGTSSGPSSPTK CCCCCCCCCCCCCCC	55.34	28490779
76	Phosphorylation	TGTSSGPSSPTKRST CCCCCCCCCCCCCCC	53.10	28490779
77	Phosphorylation	GTSSGPSSPTKRSTI CCCCCCCCCCCCCCC	39.46	27794539
83	Phosphorylation	SSPTKRSTISTKERV CCCCCCCCCCCCCHH	23.99	22817900
461	Phosphorylation	EESEEPLSDDEAALR CCCCCCCCCCHHHHH	54.45	27794539
487	Phosphorylation	GKMARVFSVLREESE HHHHHHHHHHHHHCC	19.86	21082442
503	Phosphorylation	VLQLKGLTPTGALPL HHHHCCCCCCCCCCC	27.72	21082442
519	Phosphorylation	ALSGGKQSLKNAMQG HHCCHHHHHHHHHCC	44.81	21082442
528	Phosphorylation	KNAMQGFSPNHKITS HHHHCCCCCCCCCCC	31.45	30478224

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 PP2B3_DROME !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PP2B3_DROME !!

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 PP2B3_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
SRA_DROME	sra	genetic	21900555

Drug and Disease Associations

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

Regulatory Network of PP2B3_DROME

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphoproteome analysis of Drosophila melanogaster embryos."; Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.; J. Proteome Res. 7:1675-1682(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-61, AND MASSSPECTROMETRY.	18327897 [Abstract]