UniProt ID | PP1G_HUMAN | |
---|---|---|
UniProt AC | P36873 | |
Protein Name | Serine/threonine-protein phosphatase PP1-gamma catalytic subunit | |
Gene Name | PPP1CC | |
Organism | Homo sapiens (Human). | |
Sequence Length | 323 | |
Subcellular Localization | Cytoplasm . Nucleus. Nucleus, nucleolus . Nucleus, nucleoplasm . Nucleus speckle . Chromosome, centromere, kinetochore . Cleavage furrow . Midbody . Mitochondrion . Colocalizes with SPZ1 in the nucleus (By similarity). Colocalizes with URI1 at mitoch | |
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. Dephosphorylates RPS6KB1. 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. 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 | MADLDKLNIDSIIQRLLEVRGSKPGKNVQLQENEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVLGWGENDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAEKKKPNATRPVTPPRGMITKQAKK | |
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 | ------MADLDKLNI ------CCCHHHCCH | 26.52 | 25944712 | |
6 | Ubiquitination | --MADLDKLNIDSII --CCCHHHCCHHHHH | 51.21 | - | |
6 | Acetylation | --MADLDKLNIDSII --CCCHHHCCHHHHH | 51.21 | 25038526 | |
6 (in isoform 2) | Ubiquitination | - | 51.21 | 21890473 | |
11 | Phosphorylation | LDKLNIDSIIQRLLE HHHCCHHHHHHHHHH | 20.14 | 30622161 | |
22 | Phosphorylation | RLLEVRGSKPGKNVQ HHHHHHCCCCCCCCC | 25.72 | 23186163 | |
23 (in isoform 1) | Ubiquitination | - | 61.69 | 21890473 | |
23 (in isoform 2) | Ubiquitination | - | 61.69 | 21890473 | |
23 | Ubiquitination | LLEVRGSKPGKNVQL HHHHHCCCCCCCCCC | 61.69 | 21906983 | |
26 (in isoform 1) | Ubiquitination | - | 63.57 | 21890473 | |
26 | Ubiquitination | VRGSKPGKNVQLQEN HHCCCCCCCCCCCCC | 63.57 | 21906983 | |
26 (in isoform 2) | Ubiquitination | - | 63.57 | 21890473 | |
36 | Methylation | QLQENEIRGLCLKSR CCCCCHHHHHHHHCH | 26.33 | 115488427 | |
41 | Ubiquitination | EIRGLCLKSREIFLS HHHHHHHHCHHHHHC | 46.61 | - | |
41 | Acetylation | EIRGLCLKSREIFLS HHHHHHHHCHHHHHC | 46.61 | 25953088 | |
42 | Phosphorylation | IRGLCLKSREIFLSQ HHHHHHHCHHHHHCC | 23.38 | 28450419 | |
48 | Phosphorylation | KSREIFLSQPILLEL HCHHHHHCCCEEEEE | 24.14 | 28450419 | |
60 | Ubiquitination | LELEAPLKICGDIHG EEEHHHHHHCCCCCC | 34.59 | - | |
69 | Phosphorylation | CGDIHGQYYDLLRLF CCCCCCHHHHHHHHH | 11.98 | 28152594 | |
70 | Phosphorylation | GDIHGQYYDLLRLFE CCCCCHHHHHHHHHH | 7.70 | 28152594 | |
93 | Phosphorylation | NYLFLGDYVDRGKQS CEEECHHHCHHCHHH | 11.49 | - | |
98 | Ubiquitination | GDYVDRGKQSLETIC HHHCHHCHHHHHHHH | 37.29 | 22053931 | |
98 (in isoform 2) | Ubiquitination | - | 37.29 | 21890473 | |
98 (in isoform 1) | Ubiquitination | - | 37.29 | 21890473 | |
113 | Acetylation | LLLAYKIKYPENFFL HHHHHHCCCCCCEEE | 51.07 | 26051181 | |
113 (in isoform 2) | Ubiquitination | - | 51.07 | 21890473 | |
113 | Ubiquitination | LLLAYKIKYPENFFL HHHHHHCCCCCCEEE | 51.07 | 21890473 | |
113 (in isoform 1) | Ubiquitination | - | 51.07 | 21890473 | |
114 | Phosphorylation | LLAYKIKYPENFFLL HHHHHCCCCCCEEEE | 21.17 | 28152594 | |
122 | Methylation | PENFFLLRGNHECAS CCCEEEECCCCHHHH | 46.12 | - | |
127 | S-nitrosylation | LLRGNHECASINRIY EECCCCHHHHHHHHE | 2.53 | 19483679 | |
127 | S-nitrosocysteine | LLRGNHECASINRIY EECCCCHHHHHHHHE | 2.53 | - | |
129 | Phosphorylation | RGNHECASINRIYGF CCCCHHHHHHHHEEC | 31.86 | 30576142 | |
132 | Methylation | HECASINRIYGFYDE CHHHHHHHHEECHHH | 23.10 | - | |
134 | Phosphorylation | CASINRIYGFYDECK HHHHHHHEECHHHHH | 9.65 | 28152594 | |
137 | Phosphorylation | INRIYGFYDECKRRY HHHHEECHHHHHHHH | 13.38 | 28152594 | |
140 | Glutathionylation | IYGFYDECKRRYNIK HEECHHHHHHHHCCC | 3.67 | 22555962 | |
141 (in isoform 2) | Ubiquitination | - | 37.55 | 21890473 | |
141 | Malonylation | YGFYDECKRRYNIKL EECHHHHHHHHCCCC | 37.55 | 26320211 | |
141 (in isoform 1) | Ubiquitination | - | 37.55 | 21890473 | |
141 | Acetylation | YGFYDECKRRYNIKL EECHHHHHHHHCCCC | 37.55 | 25825284 | |
141 | Ubiquitination | YGFYDECKRRYNIKL EECHHHHHHHHCCCC | 37.55 | - | |
147 (in isoform 1) | Ubiquitination | - | 44.66 | 21890473 | |
147 (in isoform 2) | Ubiquitination | - | 44.66 | 21890473 | |
147 | Acetylation | CKRRYNIKLWKTFTD HHHHHCCCCCHHHHH | 44.66 | 23749302 | |
147 | Ubiquitination | CKRRYNIKLWKTFTD HHHHHCCCCCHHHHH | 44.66 | - | |
150 (in isoform 2) | Ubiquitination | - | 44.17 | - | |
150 | Malonylation | RYNIKLWKTFTDCFN HHCCCCCHHHHHHCC | 44.17 | 26320211 | |
150 | Ubiquitination | RYNIKLWKTFTDCFN HHCCCCCHHHHHHCC | 44.17 | - | |
155 | S-nitrosylation | LWKTFTDCFNCLPIA CCHHHHHHCCCCHHH | 2.10 | 19483679 | |
155 | S-nitrosocysteine | LWKTFTDCFNCLPIA CCHHHHHHCCCCHHH | 2.10 | - | |
158 | S-nitrosylation | TFTDCFNCLPIAAIV HHHHHCCCCHHHHHC | 2.10 | 19483679 | |
158 | S-nitrosocysteine | TFTDCFNCLPIAAIV HHHHHCCCCHHHHHC | 2.10 | - | |
158 | Glutathionylation | TFTDCFNCLPIAAIV HHHHHCCCCHHHHHC | 2.10 | 22555962 | |
177 | Phosphorylation | FCCHGGLSPDLQSME EECCCCCCCCHHHHH | 21.46 | 30622161 | |
182 | Phosphorylation | GLSPDLQSMEQIRRI CCCCCHHHHHHHHHH | 31.42 | 26437602 | |
183 | Sulfoxidation | LSPDLQSMEQIRRIM CCCCHHHHHHHHHHH | 2.57 | 30846556 | |
238 (in isoform 2) | Ubiquitination | - | 40.75 | 21890473 | |
238 | Acetylation | VVAKFLHKHDLDLIC HHHHHHCCCCHHHHH | 40.75 | 25825284 | |
238 | Ubiquitination | VVAKFLHKHDLDLIC HHHHHHCCCCHHHHH | 40.75 | - | |
238 (in isoform 1) | Ubiquitination | - | 40.75 | 21890473 | |
245 | S-nitrosocysteine | KHDLDLICRAHQVVE CCCHHHHHHHHHHHH | 4.01 | - | |
245 | Glutathionylation | KHDLDLICRAHQVVE CCCHHHHHHHHHHHH | 4.01 | 22555962 | |
245 | S-nitrosylation | KHDLDLICRAHQVVE CCCHHHHHHHHHHHH | 4.01 | 19483679 | |
255 | Phosphorylation | HQVVEDGYEFFAKRQ HHHHHHCHHHHHHCC | 23.14 | 28796482 | |
260 | Acetylation | DGYEFFAKRQLVTLF HCHHHHHHCCEEECC | 35.20 | 23954790 | |
260 | Ubiquitination | DGYEFFAKRQLVTLF HCHHHHHHCCEEECC | 35.20 | 21890473 | |
260 (in isoform 1) | Ubiquitination | - | 35.20 | 21890473 | |
260 (in isoform 2) | Ubiquitination | - | 35.20 | 21890473 | |
303 (in isoform 1) | Ubiquitination | - | 55.35 | 21890473 | |
303 (in isoform 2) | Ubiquitination | - | 55.35 | 21890473 | |
303 | Ubiquitination | LKPAEKKKPNATRPV CCHHHCCCCCCCCCC | 55.35 | 2190698 | |
307 | Phosphorylation | EKKKPNATRPVTPPR HCCCCCCCCCCCCCC | 41.99 | 30266825 | |
311 (in isoform 2) | Phosphorylation | - | 30.20 | 28985074 | |
311 | Phosphorylation | PNATRPVTPPRGMIT CCCCCCCCCCCCCCC | 30.20 | 30266825 | |
317 (in isoform 2) | Phosphorylation | - | 4.91 | 30622161 | |
318 | Phosphorylation | TPPRGMITKQAKK-- CCCCCCCCCCCCC-- | 14.28 | 10880350 | |
319 | Acetylation | PPRGMITKQAKK--- CCCCCCCCCCCC--- | 37.02 | 25953088 | |
319 | Ubiquitination | PPRGMITKQAKK--- CCCCCCCCCCCC--- | 37.02 | - | |
322 | Methylation | GMITKQAKK------ CCCCCCCCC------ | 57.43 | 116252267 | |
336 (in isoform 2) | Phosphorylation | - | 27642862 |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PP1G_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 PP1G_HUMAN !! |
Kegg Disease | ||||||
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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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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, AND MASS SPECTROMETRY. | |
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-147, AND MASS SPECTROMETRY. | |
Phosphorylation | |
Reference | PubMed |
"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-307, AND MASSSPECTROMETRY. |