UniProt ID | PP1A_HUMAN | |
---|---|---|
UniProt AC | P62136 | |
Protein Name | Serine/threonine-protein phosphatase PP1-alpha catalytic subunit | |
Gene Name | PPP1CA | |
Organism | Homo sapiens (Human). | |
Sequence Length | 330 | |
Subcellular Localization | Cytoplasm. Nucleus. Nucleus, nucleoplasm. Nucleus, nucleolus. Primarily nuclear and largely excluded from the nucleolus. Highly mobile in cells and can be relocalized through interaction with targeting subunits. NOM1 plays a role in targeting this pr | |
Protein Description | Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca(2+)/calmodulin dependent protein kinase II. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. Regulates NEK2 function in terms of kinase activity and centrosome number and splitting, both in the presence and absence of radiation-induced DNA damage. Regulator of neural tube and optic fissure closure, and enteric neural crest cell (ENCCs) migration during development. In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E. Dephosphorylates the 'Ser-418' residue of FOXP3 in regulatory T-cells (Treg) from patients with rheumatoid arthritis, thereby inactivating FOXP3 and rendering Treg cells functionally defective. [PubMed: 23396208 Dephosphorylates CENPA] | |
Protein Sequence | MSDSEKLNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPADKNKGKYGQFSGLNPGGRPITPPRNSAKAKK | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSDSEKLNL ------CCHHHHCCH | 50.25 | 22617229 | |
2 | Acetylation | ------MSDSEKLNL ------CCHHHHCCH | 50.25 | 22814378 | |
4 | Phosphorylation | ----MSDSEKLNLDS ----CCHHHHCCHHH | 29.35 | 28464451 | |
6 | Ubiquitination | --MSDSEKLNLDSII --CCHHHHCCHHHHH | 46.78 | - | |
11 | Phosphorylation | SEKLNLDSIIGRLLE HHHCCHHHHHHHHHH | 21.19 | 20164059 | |
22 | Phosphorylation | RLLEVQGSRPGKNVQ HHHHHCCCCCCCCEE | 20.43 | 20068231 | |
25 (in isoform 3) | Phosphorylation | - | 32.81 | 27732954 | |
26 | Ubiquitination | VQGSRPGKNVQLTEN HCCCCCCCCEECCHH | 57.54 | 21890473 | |
26 | Malonylation | VQGSRPGKNVQLTEN HCCCCCCCCEECCHH | 57.54 | 26320211 | |
26 (in isoform 3) | Phosphorylation | - | 57.54 | 27732954 | |
26 | Acetylation | VQGSRPGKNVQLTEN HCCCCCCCCEECCHH | 57.54 | 26051181 | |
36 | Methylation | QLTENEIRGLCLKSR ECCHHHHHHHHHHCC | 26.33 | 115488367 | |
41 | Ubiquitination | EIRGLCLKSREIFLS HHHHHHHHCCHHHHC | 46.61 | - | |
42 | Phosphorylation | IRGLCLKSREIFLSQ HHHHHHHCCHHHHCC | 23.38 | 28450419 | |
48 | Phosphorylation | KSREIFLSQPILLEL HCCHHHHCCCEEEEE | 24.14 | 28450419 | |
54 | Ubiquitination | LSQPILLELEAPLKI HCCCEEEEEHHHHHH | 40.91 | 21890473 | |
59 | Phosphorylation | LLELEAPLKICGDIH EEEEHHHHHHCCCCC | 8.23 | 27251275 | |
60 | Ubiquitination | LELEAPLKICGDIHG EEEHHHHHHCCCCCC | 34.59 | - | |
69 | Phosphorylation | CGDIHGQYYDLLRLF CCCCCCHHHHHHHHH | 11.98 | 28152594 | |
69 | Ubiquitination | CGDIHGQYYDLLRLF CCCCCCHHHHHHHHH | 11.98 | 21890473 | |
70 | Phosphorylation | GDIHGQYYDLLRLFE CCCCCHHHHHHHHHH | 7.70 | 28152594 | |
93 | Phosphorylation | NYLFLGDYVDRGKQS CEEECHHHCHHCHHH | 11.49 | - | |
98 | Ubiquitination | GDYVDRGKQSLETIC HHHCHHCHHHHHHHH | 37.29 | 21890473 | |
103 | Acetylation | RGKQSLETICLLLAY HCHHHHHHHHHHHHH | 23.45 | 19608861 | |
103 | Ubiquitination | RGKQSLETICLLLAY HCHHHHHHHHHHHHH | 23.45 | 19608861 | |
103 | Ubiquitination | RGKQSLETICLLLAY HCHHHHHHHHHHHHH | 23.45 | 21890473 | |
109 | Ubiquitination | ETICLLLAYKIKYPE HHHHHHHHHHCCCCC | 11.98 | 21890473 | |
113 | Ubiquitination | LLLAYKIKYPENFFL HHHHHHCCCCCCEEE | 51.07 | 21890473 | |
114 | Phosphorylation | LLAYKIKYPENFFLL HHHHHCCCCCCEEEE | 21.17 | 28152594 | |
122 | Methylation | PENFFLLRGNHECAS CCCEEEECCCCHHHH | 46.12 | - | |
124 | Ubiquitination | NFFLLRGNHECASIN CEEEECCCCHHHHHH | 22.73 | 21890473 | |
129 | Phosphorylation | RGNHECASINRIYGF CCCCHHHHHHHHEEE | 31.86 | 30576142 | |
132 | Methylation | HECASINRIYGFYDE CHHHHHHHHEEEHHH | 23.10 | - | |
134 | Phosphorylation | CASINRIYGFYDECK HHHHHHHEEEHHHHH | 9.65 | 28152594 | |
137 | Phosphorylation | INRIYGFYDECKRRY HHHHEEEHHHHHHHH | 13.38 | 28152594 | |
140 | Glutathionylation | IYGFYDECKRRYNIK HEEEHHHHHHHHCCC | 3.67 | 22555962 | |
141 | Ubiquitination | YGFYDECKRRYNIKL EEEHHHHHHHHCCCC | 37.55 | 21906983 | |
141 | Acetylation | YGFYDECKRRYNIKL EEEHHHHHHHHCCCC | 37.55 | 68941 | |
147 | Ubiquitination | CKRRYNIKLWKTFTD HHHHHCCCCCHHHHH | 44.66 | 19608861 | |
147 | Acetylation | CKRRYNIKLWKTFTD HHHHHCCCCCHHHHH | 44.66 | 22637287 | |
150 | Ubiquitination | RYNIKLWKTFTDCFN HHCCCCCHHHHHHCC | 44.17 | - | |
158 | Glutathionylation | TFTDCFNCLPIAAIV HHHHHCCCCHHHHHC | 2.10 | 22555962 | |
158 | Ubiquitination | TFTDCFNCLPIAAIV HHHHHCCCCHHHHHC | 2.10 | 21890473 | |
177 | Phosphorylation | FCCHGGLSPDLQSME EECCCCCCCCHHHHH | 21.46 | 30622161 | |
182 | Phosphorylation | GLSPDLQSMEQIRRI CCCCCHHHHHHHHHH | 31.42 | 26437602 | |
194 | Ubiquitination | RRIMRPTDVPDQGLL HHHHCCCCCCCCCCC | 53.27 | 21890473 | |
216 | Ubiquitination | PDKDVQGWGENDRGV CCCCCCCCCCCCCCC | 8.20 | 21890473 | |
238 | Acetylation | VVAKFLHKHDLDLIC HHHHHHCCCCHHHHH | 40.75 | 44499823 | |
238 | Ubiquitination | VVAKFLHKHDLDLIC HHHHHHCCCCHHHHH | 40.75 | 21890473 | |
245 | Glutathionylation | KHDLDLICRAHQVVE CCCHHHHHHHHHHHH | 4.01 | 22555962 | |
249 | Ubiquitination | DLICRAHQVVEDGYE HHHHHHHHHHHHCHH | 39.71 | 21890473 | |
255 | Phosphorylation | HQVVEDGYEFFAKRQ HHHHHHCHHHHHHCC | 23.14 | 28796482 | |
255 | Nitration | HQVVEDGYEFFAKRQ HHHHHHCHHHHHHCC | 23.14 | - | |
260 | Acetylation | DGYEFFAKRQLVTLF HCHHHHHHCCEEECC | 35.20 | 19809605 | |
260 | Ubiquitination | DGYEFFAKRQLVTLF HCHHHHHHCCEEECC | 35.20 | 21890473 | |
261 | Ubiquitination | GYEFFAKRQLVTLFS CHHHHHHCCEEECCC | 31.47 | 21890473 | |
271 | Ubiquitination | VTLFSAPNYCGEFDN EECCCCCCCCCCCCC | 44.43 | 21890473 | |
305 | Malonylation | PADKNKGKYGQFSGL CCCCCCCCCCCCCCC | 48.06 | 26320211 | |
305 | Ubiquitination | PADKNKGKYGQFSGL CCCCCCCCCCCCCCC | 48.06 | 21890473 | |
305 | Acetylation | PADKNKGKYGQFSGL CCCCCCCCCCCCCCC | 48.06 | 23749302 | |
306 | Phosphorylation | ADKNKGKYGQFSGLN CCCCCCCCCCCCCCC | 25.48 | 21945579 | |
310 | Phosphorylation | KGKYGQFSGLNPGGR CCCCCCCCCCCCCCC | 34.19 | 21945579 | |
316 | Ubiquitination | FSGLNPGGRPITPPR CCCCCCCCCCCCCCC | 33.19 | 21890473 | |
317 | Phosphorylation | SGLNPGGRPITPPRN CCCCCCCCCCCCCCC | 25.93 | 27642862 | |
320 | Dephosphorylation | NPGGRPITPPRNSAK CCCCCCCCCCCCCCC | 29.89 | 17274640 | |
320 | Phosphorylation | NPGGRPITPPRNSAK CCCCCCCCCCCCCCC | 29.89 | 29255136 | |
325 | Phosphorylation | PITPPRNSAKAKK-- CCCCCCCCCCCCC-- | 32.21 | 22617229 | |
329 | Methylation | PRNSAKAKK------ CCCCCCCCC------ | 59.31 | - | |
331 | Phosphorylation | NSAKAKK-------- CCCCCCC-------- | 27251275 | ||
336 | Phosphorylation | KK------------- CC------------- | 27251275 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
320 | T | Phosphorylation | Kinase | AKT1 | P31749 | PSP |
320 | T | Phosphorylation | Kinase | CDK1 | P06493 | PSP |
320 | T | Phosphorylation | Kinase | CDK2 | P24941 | PSP |
320 | T | Phosphorylation | Kinase | CDK5 | Q02399 | PSP |
320 | T | Phosphorylation | Kinase | CDK5 | Q00535 | PSP |
320 | T | Phosphorylation | Kinase | LMTK2 | Q8IWU2 | GPS |
320 | T | Phosphorylation | Kinase | CDK-FAMILY | - | GPS |
320 | T | Phosphorylation | Kinase | CDK_GROUP | - | PhosphoELM |
Modified Location | Modified Residue | Modification | Function | Reference |
---|---|---|---|---|
320 | T | Phosphorylation |
| 16732323 |
* 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 PP1A_HUMAN !! |
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 THR-320, AND MASSSPECTROMETRY. | |
"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 THR-320, AND MASSSPECTROMETRY. | |
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-320, AND MASSSPECTROMETRY. | |
"Downregulation of Fer induces PP1 activation and cell-cycle arrest inmalignant cells."; Pasder O., Shpungin S., Salem Y., Makovsky A., Vilchick S.,Michaeli S., Malovani H., Nir U.; Oncogene 25:4194-4206(2006). Cited for: INTERACTION WITH FER, AND PHOSPHORYLATION AT THR-320. |