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Protein

Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

Gene

Ppp1cc

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 Ca2+/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.By similarity

Catalytic activityi

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactori

Mn2+Note: Binds 2 manganese ions per subunit.

Enzyme regulationi

Inactivated by binding to URI1.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi64Manganese 1By similarity1
Metal bindingi66Manganese 1By similarity1
Metal bindingi92Manganese 1By similarity1
Metal bindingi92Manganese 21 Publication1
Metal bindingi124Manganese 21 Publication1
Active sitei125Proton donorBy similarity1
Metal bindingi173Manganese 21 Publication1
Metal bindingi248Manganese 21 Publication1

GO - Molecular functioni

  • lamin binding Source: RGD
  • metal ion binding Source: UniProtKB-KW
  • phosphatase activity Source: UniProtKB
  • poly(A) RNA binding Source: Ensembl
  • protein complex binding Source: RGD
  • protein C-terminus binding Source: RGD
  • protein domain specific binding Source: RGD
  • protein phosphatase 1 binding Source: RGD
  • protein phosphatase binding Source: RGD
  • protein serine/threonine phosphatase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Biological rhythms, Carbohydrate metabolism, Cell cycle, Cell division, Glycogen metabolism

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiR-RNO-163560. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
R-RNO-2467813. Separation of Sister Chromatids.
R-RNO-2500257. Resolution of Sister Chromatid Cohesion.
R-RNO-5663220. RHO GTPases Activate Formins.
R-RNO-68877. Mitotic Prometaphase.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase PP1-gamma catalytic subunit (EC:3.1.3.16)
Short name:
PP-1G
Alternative name(s):
Protein phosphatase 1C catalytic subunit
Gene namesi
Name:Ppp1cc
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 12

Organism-specific databases

RGDi3377. Ppp1cc.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity
  • Cleavage furrow By similarity
  • Nucleusnucleolus By similarity
  • Nucleusnucleoplasm By similarity
  • Chromosomecentromerekinetochore By similarity
  • Nucleus speckle By similarity
  • Midbody By similarity
  • Mitochondrion By similarity

  • Note: Rapidly exchanges between the nucleolar, nucleoplasmic and cytoplasmic compartments. Highly mobile in cells and can be relocalized through interaction with targeting subunits. In the presence of PPP1R8 relocalizes from the nucleolus to nuclear speckles. Shows a dynamic targeting to specific sites throughout the cell cycle. Highly concentrated in nucleoli of interphase cells and localizes at kinetochores early in mitosis. Relocalization to chromosome-containing regions occurs at the transition from early to late anaphase. Also accumulates at the cleavage furrow and midbody by telophase. Colocalizes with SPZ1 in the nucleus. Colocalizes with URI1 at mitochondrion (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Kinetochore, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000587892 – 323Serine/threonine-protein phosphatase PP1-gamma catalytic subunitAdd BLAST322

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei307PhosphothreonineBy similarity1
Modified residuei311PhosphothreonineBy similarity1

Post-translational modificationi

Phosphorylated by NEK2.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP63088.
PRIDEiP63088.

PTM databases

iPTMnetiP63088.
PhosphoSitePlusiP63088.

Expressioni

Gene expression databases

BgeeiENSRNOG00000001269.
ExpressionAtlasiP63088. differential.
GenevisibleiP63088. RN.

Interactioni

Subunit structurei

PP1 comprises 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, PPP1R12B and PPP1R12C mediate binding to myosin. PPP1R3A (in skeletal muscle), PPP1R3B (in sliver), PPP1R3C, PPP1R3D and PPP1R3F (in brain) mediate binding to glycogen. PPP1R15A and PPP1R15B mediate binding to EIF2S1. Part of a complex containing PPP1R15B, PP1 and NCK1/2. Component of the MLL5-L complex, at least composed of KMT2E/MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with PPP1R3B, PPP1R7 and CDCA2. Isoform gamma-2 interacts with SPZ1. Interacts with IKFZ1; the interaction targets PPP1CC to pericentromeric heterochromatin, dephosphorylates IKAROS, stabilizes it and prevents it from degradation. Interacts with NOM1 and PPP1R8. Component of the PTW/PP1 phosphatase complex, composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or PPP1CC. Interacts with PPP1R8 (By similarity). Interacts with NEK2. Interacts with URI1; the interaction is phosphorylation-dependent and occurs in a growth factor-dependent manner (By similarity). Interacts with FOXP3 (By similarity). Interacts with TMEM225 (via RVxF motif) (By similarity). Interacts with MKI67 (By similarity).By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Grm1P2338515EBI-80049,EBI-4410410
Grm5P3142419EBI-80049,EBI-2902734
Grm7P354004EBI-80049,EBI-6936416
Grm7Q6333711EBI-80049,EBI-6935714
Ppp1r9aO358672EBI-80049,EBI-7092421
Ppp1r9bO352743EBI-80049,EBI-80022

GO - Molecular functioni

  • lamin binding Source: RGD
  • protein complex binding Source: RGD
  • protein C-terminus binding Source: RGD
  • protein domain specific binding Source: RGD
  • protein phosphatase 1 binding Source: RGD
  • protein phosphatase binding Source: RGD

Protein-protein interaction databases

IntActiP63088. 7 interactors.
MINTiMINT-4591365.
STRINGi10116.ENSRNOP00000047912.

Structurei

Secondary structure

1323
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 17Combined sources9
Turni18 – 21Combined sources4
Helixi32 – 48Combined sources17
Beta strandi51 – 55Combined sources5
Beta strandi57 – 62Combined sources6
Helixi69 – 79Combined sources11
Beta strandi87 – 89Combined sources3
Beta strandi94 – 98Combined sources5
Helixi100 – 113Combined sources14
Turni115 – 117Combined sources3
Beta strandi118 – 120Combined sources3
Helixi128 – 131Combined sources4
Helixi136 – 143Combined sources8
Helixi146 – 156Combined sources11
Beta strandi162 – 165Combined sources4
Turni166 – 168Combined sources3
Beta strandi169 – 174Combined sources6
Helixi183 – 187Combined sources5
Beta strandi197 – 199Combined sources3
Helixi200 – 206Combined sources7
Beta strandi214 – 218Combined sources5
Beta strandi222 – 227Combined sources6
Helixi229 – 239Combined sources11
Beta strandi242 – 246Combined sources5
Beta strandi253 – 258Combined sources6
Turni259 – 262Combined sources4
Beta strandi263 – 267Combined sources5
Helixi272 – 274Combined sources3
Beta strandi279 – 285Combined sources7
Beta strandi290 – 296Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2O8AX-ray2.61A/B2-323[»]
2O8GX-ray2.50A/B2-323[»]
ProteinModelPortaliP63088.
SMRiP63088.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP63088.

Family & Domainsi

Sequence similaritiesi

Belongs to the PPP phosphatase family. PP-1 subfamily.Curated

Phylogenomic databases

eggNOGiENOG410IN85. Eukaryota.
ENOG410XPVF. LUCA.
GeneTreeiENSGT00530000062911.
HOGENOMiHOG000172697.
HOVERGENiHBG000216.
InParanoidiP63088.
KOiK06269.
OMAiIQRLLEX.
OrthoDBiEOG091G0EKF.
TreeFamiTF354243.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_ApaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
IPR031675. STPPase_N.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
PF16891. STPPase_N. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Gamma-1 (identifier: P63088-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MADIDKLNID SIIQRLLEVR GSKPGKNVQL QENEIRGLCL KSREIFLSQP
60 70 80 90 100
ILLELEAPLK ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS
110 120 130 140 150
LETICLLLAY KIKYPENFFL LRGNHECASI NRIYGFYDEC KRRYNIKLWK
160 170 180 190 200
TFTDCFNCLP IAAIVDEKIF CCHGGLSPDL QSMEQIRRIM RPTDVPDQGL
210 220 230 240 250
LCDLLWSDPD KDVLGWGEND RGVSFTFGAE VVAKFLHKHD LDLICRAHQV
260 270 280 290 300
VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAE
310 320
KKKPNATRPV TPPRGMITKQ AKK
Length:323
Mass (Da):36,984
Last modified:September 13, 2004 - v1
Checksum:i4E28412C16898615
GO
Isoform Gamma-2 (identifier: P63088-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     315-323: GMITKQAKK → VGSGLNPSIQKASNYRNNTVLYE

Show »
Length:337
Mass (Da):38,504
Checksum:iE6F271155E0E67D7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Isoform Gamma-2 (identifier: P63088-2)
Sequence conflicti214L → F in BAA14197 (PubMed:2177460).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_011566315 – 323GMITKQAKK → VGSGLNPSIQKASNYRNNTV LYE in isoform Gamma-2. 1 Publication9

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90165 mRNA. Translation: BAA14196.1.
D90166 mRNA. Translation: BAA14197.1.
PIRiI76572.
I76573.
RefSeqiNP_071943.1. NM_022498.2. [P63088-1]
UniGeneiRn.1495.
Rn.234216.

Genome annotation databases

EnsembliENSRNOT00000048851; ENSRNOP00000047912; ENSRNOG00000001269. [P63088-2]
ENSRNOT00000078761; ENSRNOP00000071829; ENSRNOG00000001269. [P63088-1]
GeneIDi24669.
KEGGirno:24669.
UCSCiRGD:3377. rat. [P63088-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Protein Spotlight

The things we forget - Issue 32 of March 2003

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90165 mRNA. Translation: BAA14196.1.
D90166 mRNA. Translation: BAA14197.1.
PIRiI76572.
I76573.
RefSeqiNP_071943.1. NM_022498.2. [P63088-1]
UniGeneiRn.1495.
Rn.234216.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2O8AX-ray2.61A/B2-323[»]
2O8GX-ray2.50A/B2-323[»]
ProteinModelPortaliP63088.
SMRiP63088.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP63088. 7 interactors.
MINTiMINT-4591365.
STRINGi10116.ENSRNOP00000047912.

PTM databases

iPTMnetiP63088.
PhosphoSitePlusiP63088.

Proteomic databases

PaxDbiP63088.
PRIDEiP63088.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000048851; ENSRNOP00000047912; ENSRNOG00000001269. [P63088-2]
ENSRNOT00000078761; ENSRNOP00000071829; ENSRNOG00000001269. [P63088-1]
GeneIDi24669.
KEGGirno:24669.
UCSCiRGD:3377. rat. [P63088-1]

Organism-specific databases

CTDi5501.
RGDi3377. Ppp1cc.

Phylogenomic databases

eggNOGiENOG410IN85. Eukaryota.
ENOG410XPVF. LUCA.
GeneTreeiENSGT00530000062911.
HOGENOMiHOG000172697.
HOVERGENiHBG000216.
InParanoidiP63088.
KOiK06269.
OMAiIQRLLEX.
OrthoDBiEOG091G0EKF.
TreeFamiTF354243.

Enzyme and pathway databases

ReactomeiR-RNO-163560. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
R-RNO-2467813. Separation of Sister Chromatids.
R-RNO-2500257. Resolution of Sister Chromatid Cohesion.
R-RNO-5663220. RHO GTPases Activate Formins.
R-RNO-68877. Mitotic Prometaphase.

Miscellaneous databases

EvolutionaryTraceiP63088.
PROiP63088.

Gene expression databases

BgeeiENSRNOG00000001269.
ExpressionAtlasiP63088. differential.
GenevisibleiP63088. RN.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_ApaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
IPR031675. STPPase_N.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
PF16891. STPPase_N. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPP1G_RAT
AccessioniPrimary (citable) accession number: P63088
Secondary accession number(s): O09186
, O09189, P37139, Q64679
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: September 13, 2004
Last modified: November 30, 2016
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.