PTPA_MOUSE - dbPTM
PTPA_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PTPA_MOUSE
UniProt AC P58389
Protein Name Serine/threonine-protein phosphatase 2A activator
Gene Name Ptpa
Organism Mus musculus (Mouse).
Sequence Length 323
Subcellular Localization Cytoplasm. Nucleus.
Protein Description PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for serine/threonine-protein phosphatase 2A (PP2A) modulating its activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a proposed direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2A(i)) in presence of ATP and Mg(2+). Reversibly stimulates the variable phosphotyrosyl phosphatase activity of PP2A core heterodimer PP2A(D) in presence of ATP and Mg(2+) (in vitro). The phosphotyrosyl phosphatase activity is dependent of an ATPase activity of the PP2A(D):PPP2R4 complex. Is involved in apoptosis; the function appears to be independent from PP2A (By similarity)..
Protein Sequence MAEGERQPPPDSSEETPPTTQNFIIPKKEIHTVPDMGKWKRSQAYADYIGFILTLNEGVKGKKLTFDYKVSEAIEKLVALLDTLDRWIDETPPVDQPSRFGNKAYRTWYAKLDQEAENLVATVVPTHLAAAVPEVAVYLKEAVGNSTRIDYGTGHEAAFAAFLCCLCKIGVLRVDDQVAIVFKVFDRYLEVMRKLQKTYRMEPAGSQGVWGLDDFQFLPFIWGSSQLIDHPHLEPRHFVDEKAVSENHKDYMFLQCILFITEMKTGPFAEHSNQLWNISAVPSWSKVNQGLIRMYKAECLEKFPVIQHFKFGSLLPIHPVTSG
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MAEGERQPP
------CCCCCCCCC
33.24-
12PhosphorylationERQPPPDSSEETPPT
CCCCCCCCCCCCCCC
45.4825293948
13PhosphorylationRQPPPDSSEETPPTT
CCCCCCCCCCCCCCC
47.0025293948
16PhosphorylationPPDSSEETPPTTQNF
CCCCCCCCCCCCCCC
30.4325293948
19PhosphorylationSSEETPPTTQNFIIP
CCCCCCCCCCCCEEE
42.0725293948
20PhosphorylationSEETPPTTQNFIIPK
CCCCCCCCCCCEEEC
27.5625293948
103MalonylationQPSRFGNKAYRTWYA
CCCCCCCHHHHHHHH
47.3726320211
286AcetylationSAVPSWSKVNQGLIR
ECCCCHHHHCHHHHH
38.6623236377
296MalonylationQGLIRMYKAECLEKF
HHHHHHHHHHHHHHC
28.5026320211
296AcetylationQGLIRMYKAECLEKF
HHHHHHHHHHHHHHC
28.5022826441
302AcetylationYKAECLEKFPVIQHF
HHHHHHHHCCEEEEE
41.8622826441

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 PTPA_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PTPA_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 PTPA_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PTPA_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PTPA_MOUSE

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Related Literatures of Post-Translational Modification

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