PPR35_HUMAN - dbPTM
PPR35_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PPR35_HUMAN
UniProt AC Q8TAP8
Protein Name Protein phosphatase 1 regulatory subunit 35
Gene Name PPP1R35
Organism Homo sapiens (Human).
Sequence Length 253
Subcellular Localization
Protein Description Inhibits PPP1CA phosphatase activity..
Protein Sequence MMMGCGESELKSADGEEAAAVPGPPPEPQVPQLRAPVPEPGLDLSLSPRPDSPQPRHGSPGRRKGRAERRGAARQRRQVRFRLTPPSPVRSEPQPAVPQELEMPVLKSSLALGLELRAAAGSHFDAAKAVEEQLRKSFQIRCGLEESVSEGLNVPRSKRLFRDLVSLQVPEEQVLNAALREKLALLPPQARAPHPKEPPGPGPDMTILCDPETLFYESPHLTLDGLPPLRLQLRPRPSEDTFLMHRTLRRWEA
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
12PhosphorylationCGESELKSADGEEAA
CCHHHCCCCCCCHHC
44.1930266825
45PhosphorylationPEPGLDLSLSPRPDS
CCCCCCCCCCCCCCC
26.8529255136
47PhosphorylationPGLDLSLSPRPDSPQ
CCCCCCCCCCCCCCC
18.5829255136
52PhosphorylationSLSPRPDSPQPRHGS
CCCCCCCCCCCCCCC
28.2829255136
59PhosphorylationSPQPRHGSPGRRKGR
CCCCCCCCCCCHHCH
20.3226329039
84PhosphorylationRQVRFRLTPPSPVRS
HEEEEEECCCCCCCC
28.9722167270
87PhosphorylationRFRLTPPSPVRSEPQ
EEEECCCCCCCCCCC
36.9123401153
91PhosphorylationTPPSPVRSEPQPAVP
CCCCCCCCCCCCCCC
54.5922617229
128UbiquitinationGSHFDAAKAVEEQLR
CCCHHHHHHHHHHHH
55.4729967540
137PhosphorylationVEEQLRKSFQIRCGL
HHHHHHHHHCHHCCC
18.8923828894
147PhosphorylationIRCGLEESVSEGLNV
HHCCCCHHHHCCCCC
22.9023828894
149PhosphorylationCGLEESVSEGLNVPR
CCCCHHHHCCCCCCH
34.9123828894
157PhosphorylationEGLNVPRSKRLFRDL
CCCCCCHHHHHHHHH
18.9623828894
182UbiquitinationLNAALREKLALLPPQ
HHHHHHHHHCCCCCC
32.40-
216PhosphorylationCDPETLFYESPHLTL
ECHHHCEECCCCCCC
20.7127642862
241PhosphorylationRPRPSEDTFLMHRTL
CCCCCCCCCHHHHHH
18.0224719451
247PhosphorylationDTFLMHRTLRRWEA-
CCCHHHHHHHHHCC-
15.2224719451

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 PPR35_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PPR35_HUMAN !!

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 PPR35_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EDC4_HUMANEDC4physical
26496610
PR40A_HUMANPRPF40Aphysical
26496610
DCP1A_HUMANDCP1Aphysical
26496610
EDC3_HUMANEDC3physical
26496610
DCP2_HUMANDCP2physical
26496610

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PPR35_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND SER-52, AND MASSSPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-47 AND SER-52,AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-47; SER-52;THR-84 AND SER-87, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 AND SER-52, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-47 AND SER-52,AND MASS SPECTROMETRY.

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