UniProt ID | PP1B_HUMAN | |
---|---|---|
UniProt AC | P62140 | |
Protein Name | Serine/threonine-protein phosphatase PP1-beta catalytic subunit | |
Gene Name | PPP1CB | |
Organism | Homo sapiens (Human). | |
Sequence Length | 327 | |
Subcellular Localization | Cytoplasm . Nucleus . Nucleus, nucleoplasm . Nucleus, nucleolus . Highly mobile in cells and can be relocalized through interaction with targeting subunits. In the presence of PPP1R8 relocalizes from the nucleus to nuclear speckles. | |
Protein Description | Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase (PP1) is essential for cell division, it participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. 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. 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] | |
Protein Sequence | MADGELNVDSLITRLLEVRGCRPGKIVQMTEAEVRGLCIKSREIFLSQPILLELEAPLKICGDIHGQYTDLLRLFEYGGFPPEANYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRFNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDTGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVSKFLNRHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGGMMSVDETLMCSFQILKPSEKKAKYQYGGLNSGRPVTPPRTANPPKKR | |
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 | Acetylation | ------MADGELNVD ------CCCCCCCHH | 33.25 | 22223895 | |
10 | Phosphorylation | DGELNVDSLITRLLE CCCCCHHHHHHHHHH | 19.86 | 24719451 | |
13 | Phosphorylation | LNVDSLITRLLEVRG CCHHHHHHHHHHHCC | 22.13 | 24961811 | |
19 | Methylation | ITRLLEVRGCRPGKI HHHHHHHCCCCCCCE | 29.17 | 115488403 | |
25 | Acetylation | VRGCRPGKIVQMTEA HCCCCCCCEEEEEHH | 42.24 | 23954790 | |
25 | Ubiquitination | VRGCRPGKIVQMTEA HCCCCCCCEEEEEHH | 42.24 | - | |
25 | Malonylation | VRGCRPGKIVQMTEA HCCCCCCCEEEEEHH | 42.24 | 26320211 | |
29 | Sulfoxidation | RPGKIVQMTEAEVRG CCCCEEEEEHHHHHC | 2.24 | 21406390 | |
35 | Methylation | QMTEAEVRGLCIKSR EEEHHHHHCCEECCC | 24.70 | 115488395 | |
40 | Ubiquitination | EVRGLCIKSREIFLS HHHCCEECCCCHHHC | 42.33 | - | |
41 | Phosphorylation | VRGLCIKSREIFLSQ HHCCEECCCCHHHCC | 18.42 | 28450419 | |
47 | Phosphorylation | KSREIFLSQPILLEL CCCCHHHCCCEEEEE | 24.14 | 28450419 | |
59 | Ubiquitination | LELEAPLKICGDIHG EEEHHHHHHCCCCCC | 34.59 | - | |
92 | Phosphorylation | NYLFLGDYVDRGKQS CEEEHHHHCHHCHHH | 11.49 | - | |
97 | Ubiquitination | GDYVDRGKQSLETIC HHHCHHCHHHHHHHH | 37.29 | 21890473 | |
112 | Ubiquitination | LLLAYKIKYPENFFL HHHHHHCCCCCCEEE | 51.07 | 21890473 | |
113 | Phosphorylation | LLAYKIKYPENFFLL HHHHHCCCCCCEEEE | 21.17 | 28152594 | |
121 | Methylation | PENFFLLRGNHECAS CCCEEEECCCCHHHH | 46.12 | - | |
128 | Phosphorylation | RGNHECASINRIYGF CCCCHHHHHHHHEEC | 31.86 | 30576142 | |
131 | Methylation | HECASINRIYGFYDE CHHHHHHHHEECHHH | 23.10 | - | |
133 | Phosphorylation | CASINRIYGFYDECK HHHHHHHEECHHHHH | 9.65 | 28152594 | |
136 | Phosphorylation | INRIYGFYDECKRRF HHHHEECHHHHHHHH | 13.38 | 28152594 | |
140 | Malonylation | YGFYDECKRRFNIKL EECHHHHHHHHCCCH | 44.56 | 26320211 | |
140 | Acetylation | YGFYDECKRRFNIKL EECHHHHHHHHCCCH | 44.56 | 23954790 | |
140 | Ubiquitination | YGFYDECKRRFNIKL EECHHHHHHHHCCCH | 44.56 | 21890473 | |
146 | Ubiquitination | CKRRFNIKLWKTFTD HHHHHCCCHHHHHHH | 49.77 | 21890473 | |
146 | Acetylation | CKRRFNIKLWKTFTD HHHHHCCCHHHHHHH | 49.77 | 23749302 | |
146 | Malonylation | CKRRFNIKLWKTFTD HHHHHCCCHHHHHHH | 49.77 | 26320211 | |
149 | Acetylation | RFNIKLWKTFTDCFN HHCCCHHHHHHHHCC | 44.17 | 26051181 | |
149 | Ubiquitination | RFNIKLWKTFTDCFN HHCCCHHHHHHHHCC | 44.17 | - | |
149 | Malonylation | RFNIKLWKTFTDCFN HHCCCHHHHHHHHCC | 44.17 | 26320211 | |
176 | Phosphorylation | FCCHGGLSPDLQSME EECCCCCCCCHHHHH | 21.46 | 30622161 | |
181 | Phosphorylation | GLSPDLQSMEQIRRI CCCCCHHHHHHHHHH | 31.42 | 26437602 | |
210 | Ubiquitination | LLWSDPDKDVQGWGE HHCCCCCCCCCCCCC | 66.25 | - | |
233 | Ubiquitination | FGADVVSKFLNRHDL ECHHHHHHHHCHHCH | 42.11 | 21890473 | |
254 | Phosphorylation | HQVVEDGYEFFAKRQ HHHHHHCHHHHHHCC | 23.14 | 28796482 | |
259 | Malonylation | DGYEFFAKRQLVTLF HCHHHHHHCCEEECC | 35.20 | 26320211 | |
259 | Acetylation | DGYEFFAKRQLVTLF HCHHHHHHCCEEECC | 35.20 | 19809617 | |
259 | Ubiquitination | DGYEFFAKRQLVTLF HCHHHHHHCCEEECC | 35.20 | 21890473 | |
298 | Phosphorylation | SFQILKPSEKKAKYQ EEEECCCCCCCCCCC | 61.53 | 26074081 | |
303 | Acetylation | KPSEKKAKYQYGGLN CCCCCCCCCCCCCCC | 41.59 | 23236377 | |
303 | Ubiquitination | KPSEKKAKYQYGGLN CCCCCCCCCCCCCCC | 41.59 | 21890473 | |
304 | Phosphorylation | PSEKKAKYQYGGLNS CCCCCCCCCCCCCCC | 16.30 | 21945579 | |
306 | Phosphorylation | EKKAKYQYGGLNSGR CCCCCCCCCCCCCCC | 15.29 | 21945579 | |
311 | Phosphorylation | YQYGGLNSGRPVTPP CCCCCCCCCCCCCCC | 41.02 | 21945579 | |
316 | Phosphorylation | LNSGRPVTPPRTANP CCCCCCCCCCCCCCC | 30.20 | 25159151 | |
320 | Phosphorylation | RPVTPPRTANPPKKR CCCCCCCCCCCCCCC | 36.24 | 23403867 |
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 PP1B_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PP1B_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 PP1B_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. |
loading...
Acetylation | |
Reference | PubMed |
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-316, AND MASS SPECTROMETRY. | |
"Exploring proteomes and analyzing protein processing by massspectrometric identification of sorted N-terminal peptides."; Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,Thomas G.R., Vandekerckhove J.; Nat. Biotechnol. 21:566-569(2003). Cited for: PROTEIN SEQUENCE OF 2-14, AND ACETYLATION AT ALA-2. | |
Phosphorylation | |
Reference | PubMed |
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-47, 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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-316, 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 THR-316, AND MASSSPECTROMETRY. | |
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-306, AND MASSSPECTROMETRY. |