PP1R7_MOUSE - dbPTM
PP1R7_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PP1R7_MOUSE
UniProt AC Q3UM45
Protein Name Protein phosphatase 1 regulatory subunit 7
Gene Name Ppp1r7
Organism Mus musculus (Mouse).
Sequence Length 361
Subcellular Localization Nucleus.
Protein Description Regulatory subunit of protein phosphatase 1..
Protein Sequence MAAERGAGQQQSQEMMEVDRRVESEESGDEEGKKHGGGGIVANLSEQSLKDGVDRGAEDPEEEHELAVDMETINLDRDAEDVDLTHYRIGKIEGLEVLKKVKSLCLRQNLIKCIENLEELQSLRELDLYDNQIKKIENLEALTELEVLDISFNMLRNIEGIDKLTQLKKLFLVNNKINKIENISNLHQLQMLELGSNRIRAIENIDTLTNLESLFLGKNKITKLQNLDALTNLTVLSVQSNRLAKIEGLQSLVNLRELYLSNNGIEVIEGLENNNKLTMLDIASNRIKKIENISHLTELQEFWMNDNLLESWSDLDELKGARSLETVYLERNPLQKDPQYRRKVMLALPSVRQIDATYVRF
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------MAAERGAGQ
------CCCCCCCCH
20.31-
12PhosphorylationRGAGQQQSQEMMEVD
CCCCHHHHHHHHHHH
24.6225521595
23UbiquitinationMEVDRRVESEESGDE
HHHHHHHHHCHHCCC
51.0927667366
24PhosphorylationEVDRRVESEESGDEE
HHHHHHHHCHHCCCC
43.7527087446
27PhosphorylationRRVESEESGDEEGKK
HHHHHCHHCCCCCCC
47.7127087446
45PhosphorylationGGIVANLSEQSLKDG
CCHHCCCCHHHHHCC
33.1425521595
48PhosphorylationVANLSEQSLKDGVDR
HCCCCHHHHHCCCCC
33.0825521595
134AcetylationDLYDNQIKKIENLEA
CCCHHHHHHHHCHHH
37.6223236377
134MalonylationDLYDNQIKKIENLEA
CCCHHHHHHHHCHHH
37.6226320211
163UbiquitinationRNIEGIDKLTQLKKL
CCCCCHHHHHHHHHH
52.0622790023
169UbiquitinationDKLTQLKKLFLVNNK
HHHHHHHHHHHHCCC
53.7322790023
176UbiquitinationKLFLVNNKINKIENI
HHHHHCCCCCHHHHC
42.3122790023
183UbiquitinationKINKIENISNLHQLQ
CCCHHHHCCCHHHHH
1.5527667366
184PhosphorylationINKIENISNLHQLQM
CCHHHHCCCHHHHHH
44.9428464351
190UbiquitinationISNLHQLQMLELGSN
CCCHHHHHHHHHCCC
28.0427667366
218UbiquitinationLESLFLGKNKITKLQ
HHHHHCCCCCCHHHC
58.1622790023
231PhosphorylationLQNLDALTNLTVLSV
HCCHHHHHCCEEEEC
29.87-
323PhosphorylationDELKGARSLETVYLE
HHHCCCCCCCEEEEC
29.9827742792
326PhosphorylationKGARSLETVYLERNP
CCCCCCCEEEECCCC
21.5326643407
328PhosphorylationARSLETVYLERNPLQ
CCCCCEEEECCCCCC
15.4026643407
336MalonylationLERNPLQKDPQYRRK
ECCCCCCCCHHHHHH
78.1630639696
336UbiquitinationLERNPLQKDPQYRRK
ECCCCCCCCHHHHHH
78.1627667366
343UbiquitinationKDPQYRRKVMLALPS
CCHHHHHHHHHHCCC
24.0127667366
350PhosphorylationKVMLALPSVRQIDAT
HHHHHCCCCEECCCE
30.6821454597
357PhosphorylationSVRQIDATYVRF---
CCEECCCEEECC---
20.8521454597
358PhosphorylationVRQIDATYVRF----
CEECCCEEECC----
7.4321454597

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 PP1R7_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PP1R7_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 PP1R7_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PP1A_HUMANPPP1CAphysical
26496610
PP1B_HUMANPPP1CBphysical
26496610
PP1G_HUMANPPP1CCphysical
26496610
PP1RB_HUMANPPP1R11physical
26496610

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PP1R7_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-24 AND SER-27, AND MASSSPECTROMETRY.

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