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Protein Page:
PPP1CC (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
PPP1CC is a catalytic subunit of protein phosphatase 1 (PP1), a ubiquitous cytosolic serine-threonine phosphatase. Composed a catalytic subunit (PPP1CA, PPP1CB or PPP1CC) which is folded into its native form by inhibitor 2 and glycogen synthetase kinase 3, and then complexed to one or several targeting (or regulatory) subunits: PPP1R12A and PPP1R12B mediate binding to myosin; PPP1R3A, PPP1R3B, PPP1R3C and PPP1R3D mediate binding to glycogen; and PPP1R15A and PPP1R15B mediate binding to EIF2S1. PP1 is essential for cell division, plays critical roles in many cellular processes including glycogen metabolism, muscle contractility and protein synthesis, and is involved in the regulation of ionic conductances and long-term synaptic plasticity. Inhibits the synthesis of proteins involved in synaptic plasticity. Binds to the transcription factor cyclic AMP-dependent response element binding (CREB) and dephosphorylates it. May regulate chromatin condensation through regulation of histone H3 phosphorylation. Differentially expressed in gastric cancer. May participate in the neurodegenerative progress in Alzheimer's disease. Down-regulated in lung squamous cell carcinoma. Note: This description may include information from UniProtKB.
Protein type: EC 3.1.3.16; Motility/polarity/chemotaxis; Protein phosphatase, Ser/Thr (non-receptor)
Cellular Component: mitochondrial outer membrane; protein complex; mitochondrion; cytoplasm; nucleolus; nuclear speck; midbody; nucleus; cytosol; cleavage furrow
Molecular Function: protein binding; metal ion binding; protein serine/threonine phosphatase activity; protein kinase binding; phosphoprotein phosphatase activity
Biological Process: glycogen metabolic process; cell division; transforming growth factor beta receptor signaling pathway; regulation of nucleocytoplasmic transport; triacylglycerol catabolic process; mitotic cell cycle; negative regulation of transforming growth factor beta receptor signaling pathway; protein amino acid dephosphorylation
Reference #:  P36873 (UniProtKB)
Alt. Names/Synonyms: PP-1G; PP1G; PP1gamma; PPP1CC; PPP1G; protein phosphatase 1, catalytic subunit, gamma isoform; protein phosphatase 1, catalytic subunit, gamma isozyme; Protein phosphatase 1C catalytic subunit; serine/threonine phosphatase 1 gamma; Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
Gene Symbols: PPP1CC
Molecular weight: 36,984 Da
Basal Isoelectric point: 6.12  Predict pI for various phosphorylation states
CST Pathways:  Growth And Differentiation Control by MAPKs  |  Insulin Receptor Signaling  |  Parkinson's Disease  |  Translation: eIF2
Select Structure to View Below

PPP1CC

Protein Structure Not Found.


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Sites Implicated In
enzymatic activity, inhibited: T307‑p, T311‑p, T318‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 1 K6-u __MADLDkLNIDSII
0 1 S22-p RLLEVRGskPGkNVQ
0 1 K23-u LLEVRGskPGkNVQL
0 2 K26-u VRGskPGkNVQLQEN
0 2 K60-u LELEAPLkICGDIHG
0 22 K98-u GDYVDRGkQSLETIC
0 4 K113-u LLLAYKIkYPENFFL
0 23 Y137-p INRIYGFyDECkRRY
0 18 K141-a YGFyDECkRRYNIkL
0 14 K141-u YGFyDECkRRYNIkL
0 3 K147-u CkRRYNIkLWkTFTD
0 4 K150-u RYNIkLWkTFTDCFN
0 5 K260-a DGYEFFAkRQLVTLF
0 34 K260-u DGYEFFAkRQLVTLF
0 1 K303-u LKPAEKKkPNAtRPV
1 5 T307-p EKKkPNAtRPVtPPR
1 22 T311-p PNAtRPVtPPRGMIt
1 0 T318-p tPPRGMItKQAKK__
  PPP1CC iso2  
K6 __MADLDKLNIDSII
S22 RLLEVRGSKPGKNVQ
K23 LLEVRGSKPGKNVQL
K26 VRGSKPGKNVQLQEN
K60 LELEAPLKICGDIHG
K98 GDYVDRGKQSLETIC
K113 LLLAYKIKYPENFFL
Y137 INRIYGFYDECKRRY
K141 YGFYDECKRRYNIKL
K141 YGFYDECKRRYNIKL
K147 CKRRYNIKLWKTFTD
K150 RYNIKLWKTFTDCFN
K260 DGYEFFAKRQLVTLF
K260 DGYEFFAKRQLVTLF
K303 LKPAEKKKPNATRPV
T307 EKKKPNATRPVTPPR
T311 PNATRPVTPPRVASG
- gap
  mouse

► Hide Isoforms
 
K6 __MADIDKLNIDSII
S22 RLLEVRGSKPGkNVQ
K23 LLEVRGSKPGkNVQL
K26-u VRGSKPGkNVQLQEN
K60 LELEAPLKICGDIHG
K98-u GDYVDRGkQSLETIC
K113-u LLLAYKIkYPENFFL
Y137-p INRIYGFyDECkRRY
K141-a YGFyDECkRRYNIkL
K141-u YGFyDECkRRYNIkL
K147-u CkRRYNIkLWkTFTD
K150-u RYNIkLWkTFTDCFN
K260-a DGYEFFAkRQLVTLF
K260-u DGYEFFAkRQLVTLF
K303 LKPAEKKKPNAtRPV
T307-p EKKKPNAtRPVtPPR
T311-p PNAtRPVtPPRGMIT
T318 tPPRGMITKQAKK__
  PPP1CC iso2  
K6 __MADIDKLNIDSII
S22 RLLEVRGSKPGKNVQ
K23 LLEVRGSKPGKNVQL
K26 VRGSKPGKNVQLQEN
K60 LELEAPLKICGDIHG
K98 GDYVDRGKQSLETIC
K113 LLLAYKIKYPENFFL
Y137 INRIYGFYDECKRRY
K141 YGFYDECKRRYNIKL
K141 YGFYDECKRRYNIKL
K147 CKRRYNIKLWKTFTD
K150 RYNIKLWKTFTDCFN
K260 DGYEFFAKRQLVTLF
K260 DGYEFFAKRQLVTLF
K303 LKPAEKKKPNATRPV
T307 EKKKPNATRPVTPPR
T311 PNATRPVTPPRVGSG
- gap
  rat

 
K6 __MADIDKLNIDSII
S22 RLLEVRGSKPGKNVQ
K23 LLEVRGSKPGKNVQL
K26 VRGSKPGKNVQLQEN
K60 LELEAPLKICGDIHG
K98 GDYVDRGKQSLETIC
K113 LLLAYKIKYPENFFL
Y137 INRIYGFYDECKRRY
K141 YGFYDECKRRYNIKL
K141 YGFYDECKRRYNIKL
K147 CKRRYNIKLWKTFTD
K150 RYNIKLWKTFTDCFN
K260 DGYEFFAKRQLVTLF
K260 DGYEFFAKRQLVTLF
K303 LKPAEKKKPNATRPV
T307 EKKKPNATRPVTPPR
T311 PNATRPVTPPRGMIT
T318 TPPRGMITKQAKK__
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