2A5G_MOUSE - dbPTM
2A5G_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID 2A5G_MOUSE
UniProt AC Q60996
Protein Name Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform
Gene Name Ppp2r5c
Organism Mus musculus (Mouse).
Sequence Length 524
Subcellular Localization Nucleus. Chromosome, centromere.
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. The PP2A-PPP2R5C holoenzyme may activate TP53 and play a role in DNA damage-induced inhibition of cell proliferation. PP2A-PPP2R5C may also regulate the ERK signaling pathway through ERK dephosphorylation (By similarity)..
Protein Sequence MLTCNKAGSGMVVDAASSNGPFQPVALLHIRDVPPADQEKLFIQKLRQCCVLFDFVSDPLSDLKWKEVKRAALSEMVEYITHNRNVITEPIYPEAVHMFAVNMFRTLPPSSNPTGAEFDPEEDEPTLEAAWPHLQLVYEFFLRFLESPDFQPNIAKKYIDQKFVLQLLELFDSEDPRERDFLKTTLHRIYGKFLGLRAYIRKQINNIFYRFIYETEHHNGIAELLEILGSIINGFALPLKEEHKIFLLKVLLPLHKVKSLSVYHPQLAYCVVQFLEKDSTLTEPVVMALLKYWPKTHSPKEVMFLNELEEILDVIEPSEFVKIMEPLFRQLAKCVSSPHFQVAERALYYWNNEYIMSLISDNAAKILPIMFPSLYRNSKTHWNKTIHGLIYNALKLFMEMNQKLFDDCTQQFKAEKLKEKLKMKEREEAWVKIENLAKANPQYAVYSQASAVSIPVAMETDGPQFEDVQMLKKTVSDEARQAQKELKKDRPLVRRKSELPQDPHTEKALEAHCRASELLSQDGR
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
1Acetylation-------MLTCNKAG
-------CCCCCCCC
6.71-
64UbiquitinationSDPLSDLKWKEVKRA
CCCHHHCCHHHHHHH
62.30-
192AcetylationTLHRIYGKFLGLRAY
HHHHHHHHHHCHHHH
22.0522826441
279PhosphorylationVQFLEKDSTLTEPVV
HHHHHCCCCCCHHHH
36.06-
333UbiquitinationPLFRQLAKCVSSPHF
HHHHHHHHHHCCCCH
43.70-
354PhosphorylationLYYWNNEYIMSLISD
HHHCCCHHHHHHHCC
12.21-
357PhosphorylationWNNEYIMSLISDNAA
CCCHHHHHHHCCCHH
17.00-
360PhosphorylationEYIMSLISDNAAKIL
HHHHHHHCCCHHHHH
30.06-
373PhosphorylationILPIMFPSLYRNSKT
HHHHCCHHHHHCCCC
27.1128285833
375PhosphorylationPIMFPSLYRNSKTHW
HHCCHHHHHCCCCHH
16.4628285833
385PhosphorylationSKTHWNKTIHGLIYN
CCCHHHHHHHHHHHH
18.2625521595
497PhosphorylationRPLVRRKSELPQDPH
CCCCCCHHCCCCCCH
42.4226824392
520PhosphorylationCRASELLSQDGR---
HHHHHHHCCCCC---
38.5630635358

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 2A5G_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of 2A5G_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 2A5G_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
2AAA_HUMANPPP2R1Aphysical
26496610
2AAB_HUMANPPP2R1Bphysical
26496610
U2AF2_HUMANU2AF2physical
26496610
ADNP2_HUMANADNP2physical
26496610
ELL2_HUMANELL2physical
26496610

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of 2A5G_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-497, AND MASSSPECTROMETRY.

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