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P61287

- PP1G_BOVIN

UniProt

P61287 - PP1G_BOVIN

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Protein

Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

Gene

PPP1CC

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript 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).By similarity

Catalytic activityi

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

Cofactori

Mn2+By similarityNote: Binds 2 manganese ions per subunit.By similarity

Enzyme regulationi

Inactivated by binding to URI1.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi64 – 641Manganese 1By similarity
Metal bindingi66 – 661Manganese 1By similarity
Metal bindingi92 – 921Manganese 1By similarity
Metal bindingi92 – 921Manganese 2By similarity
Metal bindingi124 – 1241Manganese 2By similarity
Active sitei125 – 1251Proton donorBy similarity
Metal bindingi173 – 1731Manganese 2By similarity
Metal bindingi248 – 2481Manganese 2By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. phosphatase activity Source: UniProtKB
  3. poly(A) RNA binding Source: Ensembl
  4. protein serine/threonine phosphatase activity Source: UniProtKB

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cell division Source: UniProtKB-KW
  3. circadian regulation of gene expression Source: UniProtKB
  4. entrainment of circadian clock by photoperiod Source: UniProtKB
  5. glycogen metabolic process Source: UniProtKB-KW
  6. protein dephosphorylation Source: UniProtKB
  7. regulation of circadian rhythm Source: UniProtKB
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

ReactomeiREACT_203101. Mitotic Prometaphase.
REACT_209545. Resolution of Sister Chromatid Cohesion.
REACT_212887. Separation of Sister Chromatids.
REACT_214027. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
REACT_225632. Downregulation of TGF-beta receptor signaling.

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 17

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

  1. kinetochore Source: UniProtKB-KW
  2. mitochondrion Source: UniProtKB
  3. MLL5-L complex Source: Ensembl
  4. nucleolus Source: Ensembl
  5. PTW/PP1 phosphatase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Kinetochore, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 323322Serine/threonine-protein phosphatase PP1-gamma catalytic subunitPRO_0000058785Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei307 – 3071PhosphothreonineBy similarity

Post-translational modificationi

Phosphorylated by NEK2.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP61287.
PRIDEiP61287.

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 liver), 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. 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. Interacts with NEK2. Interacts with PPP1R42; the interaction is direct. Interacts with URI1; the interaction is phosphorylation-dependent and occurs in a growth factor-dependent manner (By similarity).By similarity

Protein-protein interaction databases

BioGridi159580. 1 interaction.
STRINGi9913.ENSBTAP00000014873.

Structurei

3D structure databases

ProteinModelPortaliP61287.
SMRiP61287. Positions 6-299.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00530000062911.
HOGENOMiHOG000172697.
HOVERGENiHBG000216.
InParanoidiP61287.
KOiK06269.
OMAiPRSMITK.
OrthoDBiEOG7TJ3K3.
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.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P61287-1 [UniParc]FASTAAdd to Basket

« 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:May 10, 2004 - v1
Checksum:i4E28412C16898615
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ429235 mRNA. Translation: CAD22157.1.
BC123502 mRNA. Translation: AAI23503.1.
RefSeqiNP_777006.1. NM_174581.3.
UniGeneiBt.9578.

Genome annotation databases

EnsembliENSBTAT00000057594; ENSBTAP00000048567; ENSBTAG00000011198.
GeneIDi282318.
KEGGibta:282318.

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
AJ429235 mRNA. Translation: CAD22157.1 .
BC123502 mRNA. Translation: AAI23503.1 .
RefSeqi NP_777006.1. NM_174581.3.
UniGenei Bt.9578.

3D structure databases

ProteinModelPortali P61287.
SMRi P61287. Positions 6-299.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 159580. 1 interaction.
STRINGi 9913.ENSBTAP00000014873.

Proteomic databases

PaxDbi P61287.
PRIDEi P61287.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000057594 ; ENSBTAP00000048567 ; ENSBTAG00000011198 .
GeneIDi 282318.
KEGGi bta:282318.

Organism-specific databases

CTDi 5501.

Phylogenomic databases

eggNOGi COG0639.
GeneTreei ENSGT00530000062911.
HOGENOMi HOG000172697.
HOVERGENi HBG000216.
InParanoidi P61287.
KOi K06269.
OMAi PRSMITK.
OrthoDBi EOG7TJ3K3.
TreeFami TF354243.

Enzyme and pathway databases

Reactomei REACT_203101. Mitotic Prometaphase.
REACT_209545. Resolution of Sister Chromatid Cohesion.
REACT_212887. Separation of Sister Chromatids.
REACT_214027. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
REACT_225632. Downregulation of TGF-beta receptor signaling.

Miscellaneous databases

NextBioi 20806115.

Family and domain databases

Gene3Di 3.60.21.10. 1 hit.
InterProi IPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view ]
Pfami PF00149. Metallophos. 1 hit.
[Graphical view ]
PRINTSi PR00114. STPHPHTASE.
SMARTi SM00156. PP2Ac. 1 hit.
[Graphical view ]
SUPFAMi SSF56300. SSF56300. 1 hit.
PROSITEi PS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The metabotropic glutamate receptor mGluR7b binds to the catalytic gamma-subunit of protein phosphatase 1."
    Enz R.
    J. Neurochem. 81:1130-1140(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Retina.
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Brain cortex.

Entry informationi

Entry nameiPP1G_BOVIN
AccessioniPrimary (citable) accession number: P61287
Secondary accession number(s): Q08DZ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: November 26, 2014
This is version 97 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

Complete proteome, Reference proteome

Documents

  1. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3