| 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 | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 12 | Phosphorylation | CGESELKSADGEEAA CCHHHCCCCCCCHHC | 44.19 | 30266825 | |
| 45 | Phosphorylation | PEPGLDLSLSPRPDS CCCCCCCCCCCCCCC | 26.85 | 29255136 | |
| 47 | Phosphorylation | PGLDLSLSPRPDSPQ CCCCCCCCCCCCCCC | 18.58 | 29255136 | |
| 52 | Phosphorylation | SLSPRPDSPQPRHGS CCCCCCCCCCCCCCC | 28.28 | 29255136 | |
| 59 | Phosphorylation | SPQPRHGSPGRRKGR CCCCCCCCCCCHHCH | 20.32 | 26329039 | |
| 84 | Phosphorylation | RQVRFRLTPPSPVRS HEEEEEECCCCCCCC | 28.97 | 22167270 | |
| 87 | Phosphorylation | RFRLTPPSPVRSEPQ EEEECCCCCCCCCCC | 36.91 | 23401153 | |
| 91 | Phosphorylation | TPPSPVRSEPQPAVP CCCCCCCCCCCCCCC | 54.59 | 22617229 | |
| 128 | Ubiquitination | GSHFDAAKAVEEQLR CCCHHHHHHHHHHHH | 55.47 | 29967540 | |
| 137 | Phosphorylation | VEEQLRKSFQIRCGL HHHHHHHHHCHHCCC | 18.89 | 23828894 | |
| 147 | Phosphorylation | IRCGLEESVSEGLNV HHCCCCHHHHCCCCC | 22.90 | 23828894 | |
| 149 | Phosphorylation | CGLEESVSEGLNVPR CCCCHHHHCCCCCCH | 34.91 | 23828894 | |
| 157 | Phosphorylation | EGLNVPRSKRLFRDL CCCCCCHHHHHHHHH | 18.96 | 23828894 | |
| 182 | Ubiquitination | LNAALREKLALLPPQ HHHHHHHHHCCCCCC | 32.40 | - | |
| 216 | Phosphorylation | CDPETLFYESPHLTL ECHHHCEECCCCCCC | 20.71 | 27642862 | |
| 241 | Phosphorylation | RPRPSEDTFLMHRTL CCCCCCCCCHHHHHH | 18.02 | 24719451 | |
| 247 | Phosphorylation | DTFLMHRTLRRWEA- CCCHHHHHHHHHCC- | 15.22 | 24719451 |
| 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 !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PPR35_HUMAN !! | ||||||
* 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 !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| EDC4_HUMAN | EDC4 | physical | 26496610 | |
| PR40A_HUMAN | PRPF40A | physical | 26496610 | |
| DCP1A_HUMAN | DCP1A | physical | 26496610 | |
| EDC3_HUMAN | EDC3 | physical | 26496610 | |
| DCP2_HUMAN | DCP2 | physical | 26496610 |
| 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. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "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. | |