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P36873

- PP1G_HUMAN

UniProt

P36873 - PP1G_HUMAN

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Protein
Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
Gene
PPP1CC
Organism
Homo sapiens (Human)
Status
Reviewed - 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.3 Publications

Catalytic activityi

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.1 Publication

Cofactori

Binds 2 manganese ions per subunit.2 Publications

Enzyme regulationi

Inactivated by binding to URI1. The phosphatase activity of the PPP1R15A-PP1 complex toward EIF2S1 is specifically inhibited by Salubrinal, a drug that protects cells from endoplasmic reticulum stress.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi64 – 641Manganese 1
Metal bindingi66 – 661Manganese 1
Metal bindingi92 – 921Manganese 1
Metal bindingi92 – 921Manganese 2
Metal bindingi124 – 1241Manganese 2
Active sitei125 – 1251Proton donor
Metal bindingi173 – 1731Manganese 2
Metal bindingi248 – 2481Manganese 2
Sitei273 – 2731Inhibition by microcystin toxin binding

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. phosphatase activity Source: UniProtKB
  3. phosphoprotein phosphatase activity Source: Reactome
  4. poly(A) RNA binding Source: UniProtKB
  5. protein N-terminus binding Source: MGI
  6. protein binding Source: IntAct
  7. protein kinase binding Source: UniProtKB
  8. protein serine/threonine phosphatase activity Source: UniProtKB

GO - Biological processi

  1. cell division Source: UniProtKB-KW
  2. circadian regulation of gene expression Source: UniProtKB
  3. entrainment of circadian clock by photoperiod Source: UniProtKB
  4. glycogen metabolic process Source: UniProtKB-KW
  5. mitotic cell cycle Source: Reactome
  6. negative regulation of transforming growth factor beta receptor signaling pathway Source: Reactome
  7. protein dephosphorylation Source: UniProtKB
  8. regulation of circadian rhythm Source: UniProtKB
  9. regulation of nucleocytoplasmic transport Source: Ensembl
  10. small molecule metabolic process Source: Reactome
  11. transforming growth factor beta receptor signaling pathway Source: Reactome
  12. triglyceride catabolic process Source: Reactome
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_120727. Downregulation of TGF-beta receptor signaling.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_494. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
REACT_682. Mitotic Prometaphase.
SignaLinkiP36873.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:9283. PPP1CC.

Subcellular locationi

Cytoplasm. Nucleus. Nucleusnucleolus. Nucleusnucleoplasm. Nucleus speckle. Chromosomecentromerekinetochore. Cleavage furrow. Midbody. Mitochondrion
Note: Colocalizes with SPZ1 in the nucleus By similarity. Colocalizes with URI1 at mitochondrion. 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.4 Publications

GO - Cellular componenti

  1. MLL5-L complex Source: UniProtKB
  2. PTW/PP1 phosphatase complex Source: UniProtKB
  3. cleavage furrow Source: UniProtKB-SubCell
  4. condensed chromosome kinetochore Source: UniProtKB-SubCell
  5. cytoplasm Source: UniProtKB
  6. cytosol Source: Reactome
  7. midbody Source: UniProtKB-SubCell
  8. mitochondrial outer membrane Source: Ensembl
  9. mitochondrion Source: UniProtKB
  10. nuclear speck Source: UniProtKB-SubCell
  11. nucleolus Source: UniProtKB
  12. nucleus Source: UniProtKB
  13. protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Kinetochore, Mitochondrion, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi125 – 1251H → A: Loss of activity. 1 Publication
Mutagenesisi273 – 2731C → A, S or L: Abolishes interaction with microcystin toxin. 1 Publication

Organism-specific databases

PharmGKBiPA33611.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 323322Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
PRO_0000058787Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei307 – 3071Phosphothreonine1 Publication

Post-translational modificationi

Phosphorylated by NEK2.1 Publication

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiP36873.
PaxDbiP36873.
PRIDEiP36873.

PTM databases

PhosphoSiteiP36873.

Expressioni

Gene expression databases

ArrayExpressiP36873.
BgeeiP36873.
CleanExiHS_PPP1CC.
GenevestigatoriP36873.

Organism-specific databases

HPAiCAB022645.
HPA013661.

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. Interacts with cyanobacterial toxin microcystin; disulfide-linked. Interacts with PPP1R3B and PPP1R7. Isoform gamma-2 interacts with SPZ1 By similarity. Component of the MLL5-L complex, at least composed of KMT2E/MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with CDCA2. PPP1R15A and PPP1R15B mediate binding to EIF2S1. Part of a complex containing PPP1R15B, PP1 and NCK1/2. Interacts with IKFZ1; the interaction targets PPP1CC to pericentromeric heterochromatin, dephosphorylates IKAROS, stabilizes it and prevents it from degradation. Interacts with PPP1R42; the interaction is direct By similarity. 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 isoform 1 and isoform 4 NEK2. Interacts with URI1; the interaction is phosphorylation-dependent and occurs in a growth factor-dependent manner.12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
A1DRY32EBI-3964623,EBI-4311408
BRCA1P383982EBI-356283,EBI-349905
ClockO087852EBI-356283,EBI-79859From a different organism.
PPP1R2P412364EBI-356283,EBI-1056517
PPP1R32Q7Z5V64EBI-3964623,EBI-4311771
RANBP9Q96S593EBI-3964623,EBI-636085
TCTEX1D4Q5JR983EBI-3964623,EBI-4311709
TP53P046372EBI-356289,EBI-366083
TP53BP2Q136256EBI-356283,EBI-77642
URI1O947636EBI-356283,EBI-357067

Protein-protein interaction databases

BioGridi111495. 191 interactions.
DIPiDIP-749N.
IntActiP36873. 145 interactions.
MINTiMINT-190765.
STRINGi9606.ENSP00000335084.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 179
Turni18 – 214
Helixi32 – 4817
Beta strandi51 – 555
Beta strandi57 – 626
Helixi69 – 7911
Beta strandi87 – 893
Beta strandi94 – 985
Helixi100 – 11314
Turni115 – 1173
Beta strandi118 – 1203
Helixi128 – 1314
Turni132 – 1354
Helixi136 – 1438
Helixi146 – 15611
Beta strandi162 – 1654
Turni166 – 1683
Beta strandi169 – 1746
Helixi183 – 1875
Beta strandi197 – 1993
Helixi200 – 2067
Beta strandi214 – 2185
Beta strandi222 – 2276
Helixi229 – 23810
Beta strandi242 – 2465
Beta strandi254 – 2585
Turni259 – 2624
Beta strandi263 – 2675
Helixi272 – 2743
Beta strandi280 – 2856
Beta strandi291 – 2966

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IT6X-ray2.00A/B1-323[»]
1JK7X-ray1.90A1-323[»]
1U32X-ray2.00A6-298[»]
2BCDX-ray2.10A1-323[»]
2BDXX-ray2.30A1-323[»]
ProteinModelPortaliP36873.
SMRiP36873. Positions 6-299.

Miscellaneous databases

EvolutionaryTraceiP36873.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0639.
HOGENOMiHOG000172697.
HOVERGENiHBG000216.
KOiK06269.
OMAiPRSMITK.
OrthoDBiEOG7TJ3K3.
PhylomeDBiP36873.
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]

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. Align

Isoform Gamma-1 (identifier: P36873-1) [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

MADLDKLNID SIIQRLLEVR GSKPGKNVQL QENEIRGLCL KSREIFLSQP    50
ILLELEAPLK ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS 100
LETICLLLAY KIKYPENFFL LRGNHECASI NRIYGFYDEC KRRYNIKLWK 150
TFTDCFNCLP IAAIVDEKIF CCHGGLSPDL QSMEQIRRIM RPTDVPDQGL 200
LCDLLWSDPD KDVLGWGEND RGVSFTFGAE VVAKFLHKHD LDLICRAHQV 250
VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAE 300
KKKPNATRPV TPPRGMITKQ AKK 323
Length:323
Mass (Da):36,984
Last modified:June 1, 1994 - v1
Checksum:i0EEEF0E842188536
GO
Isoform Gamma-2 (identifier: P36873-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:337
Mass (Da):38,518
Checksum:i9731E5A6C8EEBF46
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti152 – 1521F → S.
Corresponds to variant rs11558237 [ dbSNP | Ensembl ].
VAR_051734

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei315 – 3239GMITKQAKK → VASGLNPSIQKASNYRNNTV LYE in isoform Gamma-2.
VSP_005094

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X74008 mRNA. Translation: CAA52169.1.
BC014073 mRNA. Translation: AAH14073.1.
L07395 mRNA. Translation: AAA19823.1.
CCDSiCCDS58279.1. [P36873-2]
CCDS9150.1. [P36873-1]
PIRiS35699.
S35700.
RefSeqiNP_001231903.1. NM_001244974.1. [P36873-2]
NP_002701.1. NM_002710.3. [P36873-1]
UniGeneiHs.79081.

Genome annotation databases

EnsembliENST00000335007; ENSP00000335084; ENSG00000186298. [P36873-1]
ENST00000340766; ENSP00000341779; ENSG00000186298. [P36873-2]
GeneIDi5501.
KEGGihsa:5501.
UCSCiuc001tru.3. human. [P36873-1]
uc021rdx.1. human. [P36873-2]

Polymorphism databases

DMDMi548573.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Protein Spotlight

The things we forget - Issue 32 of March 2003

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X74008 mRNA. Translation: CAA52169.1 .
BC014073 mRNA. Translation: AAH14073.1 .
L07395 mRNA. Translation: AAA19823.1 .
CCDSi CCDS58279.1. [P36873-2 ]
CCDS9150.1. [P36873-1 ]
PIRi S35699.
S35700.
RefSeqi NP_001231903.1. NM_001244974.1. [P36873-2 ]
NP_002701.1. NM_002710.3. [P36873-1 ]
UniGenei Hs.79081.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1IT6 X-ray 2.00 A/B 1-323 [» ]
1JK7 X-ray 1.90 A 1-323 [» ]
1U32 X-ray 2.00 A 6-298 [» ]
2BCD X-ray 2.10 A 1-323 [» ]
2BDX X-ray 2.30 A 1-323 [» ]
ProteinModelPortali P36873.
SMRi P36873. Positions 6-299.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111495. 191 interactions.
DIPi DIP-749N.
IntActi P36873. 145 interactions.
MINTi MINT-190765.
STRINGi 9606.ENSP00000335084.

Chemistry

BindingDBi P36873.
ChEMBLi CHEMBL4438.

PTM databases

PhosphoSitei P36873.

Polymorphism databases

DMDMi 548573.

Proteomic databases

MaxQBi P36873.
PaxDbi P36873.
PRIDEi P36873.

Protocols and materials databases

DNASUi 5501.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000335007 ; ENSP00000335084 ; ENSG00000186298 . [P36873-1 ]
ENST00000340766 ; ENSP00000341779 ; ENSG00000186298 . [P36873-2 ]
GeneIDi 5501.
KEGGi hsa:5501.
UCSCi uc001tru.3. human. [P36873-1 ]
uc021rdx.1. human. [P36873-2 ]

Organism-specific databases

CTDi 5501.
GeneCardsi GC12M111157.
HGNCi HGNC:9283. PPP1CC.
HPAi CAB022645.
HPA013661.
MIMi 176914. gene.
neXtProti NX_P36873.
PharmGKBi PA33611.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0639.
HOGENOMi HOG000172697.
HOVERGENi HBG000216.
KOi K06269.
OMAi PRSMITK.
OrthoDBi EOG7TJ3K3.
PhylomeDBi P36873.
TreeFami TF354243.

Enzyme and pathway databases

Reactomei REACT_120727. Downregulation of TGF-beta receptor signaling.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_494. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
REACT_682. Mitotic Prometaphase.
SignaLinki P36873.

Miscellaneous databases

ChiTaRSi PPP1CC. human.
EvolutionaryTracei P36873.
GeneWikii PPP1CC.
GenomeRNAii 5501.
NextBioi 21286.
PROi P36873.
SOURCEi Search...

Gene expression databases

ArrayExpressi P36873.
Bgeei P36873.
CleanExi HS_PPP1CC.
Genevestigatori P36873.

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. "Sequence of human protein serine/threonine phosphatase 1 gamma and localization of the gene (PPP1CC) encoding it to chromosome bands 12q24.1-q24.2."
    Barker H.M., Craig S.P., Spurr N.K., Cohen P.T.W.
    Biochim. Biophys. Acta 1178:228-233(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS GAMMA-1 AND GAMMA-2).
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GAMMA-1).
    Tissue: Placenta.
  3. Bienvenut W.V., Waridel P., Quadroni M.
    Submitted (MAR-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-15; 44-60; 99-122; 151-168 AND 247-260, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryonic kidney.
  4. Bienvenut W.V., Bilsland A.E., Keith W.N.
    Submitted (JAN-2010) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-15; 27-36; 44-60; 99-111; 133-141; 151-187 AND 239-260, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Colon carcinoma.
  5. "Molecular cloning and chromosomal localization of a human skeletal muscle PP-1 gamma 1 cDNA."
    Norman S.A., Mott D.M.
    Mamm. Genome 5:41-45(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-323 (ISOFORM GAMMA-1).
    Tissue: Skeletal muscle.
  6. "The cyanobacterial toxin microcystin binds covalently to cysteine-273 on protein phosphatase 1."
    MacKintosh R.W., Dalby K.N., Campbell D.G., Cohen P.T.W., Cohen P., MacKintosh C.
    FEBS Lett. 371:236-240(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MICROCYSTIN, MUTAGENESIS OF CYS-273.
  7. "PPP1R6, a novel member of the family of glycogen-targeting subunits of protein phosphatase 1."
    Armstrong C.G., Browne G.J., Cohen P., Cohen P.T.W.
    FEBS Lett. 418:210-214(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PPP1R3D.
  8. "Dynamic targeting of protein phosphatase 1 within the nuclei of living mammalian cells."
    Trinkle-Mulcahy L., Sleeman J.E., Lamond A.I.
    J. Cell Sci. 114:4219-4228(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PPP1R8, MUTAGENESIS OF HIS-125.
  9. "Growth arrest and DNA damage-inducible protein GADD34 assembles a novel signaling complex containing protein phosphatase 1 and inhibitor 1."
    Connor J.H., Weiser D.C., Li S., Hallenbeck J.M., Shenolikar S.
    Mol. Cell. Biol. 21:6841-6850(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PPP1R15A.
  10. "Binding of the concave surface of the Sds22 superhelix to the alpha 4/alpha 5/alpha 6-triangle of protein phosphatase-1."
    Ceulemans H., Vulsteke V., De Maeyer M., Tatchell K., Stalmans W., Bollen M.
    J. Biol. Chem. 277:47331-47337(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PPP1R7.
  11. "Time-lapse imaging reveals dynamic relocalization of PP1gamma throughout the mammalian cell cycle."
    Trinkle-Mulcahy L., Andrews P.D., Wickramasinghe S., Sleeman J., Prescott A., Lam Y.W., Lyon C., Swedlow J.R., Lamond A.I.
    Mol. Biol. Cell 14:107-117(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  12. "Alternatively spliced protein variants as potential therapeutic targets for male infertility and contraception."
    Fardilha M., Wu W., Sa R., Fidalgo S., Sousa C., Mota C., da Cruz e Silva O.A., da Cruz e Silva E.F.
    Ann. N. Y. Acad. Sci. 1030:468-478(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NEK2, PHOSPHORYLATION.
  13. "A selective inhibitor of eIF2alpha dephosphorylation protects cells from ER stress."
    Boyce M., Bryant K.F., Jousse C., Long K., Harding H.P., Scheuner D., Kaufman R.J., Ma D., Coen D.M., Ron D., Yuan J.
    Science 307:935-939(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  14. "Repo-Man recruits PP1 gamma to chromatin and is essential for cell viability."
    Trinkle-Mulcahy L., Andersen J., Lam Y.W., Moorhead G., Mann M., Lamond A.I.
    J. Cell Biol. 172:679-692(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDCA2.
  15. "Protein phosphatase-1alpha regulates centrosome splitting through Nek2."
    Mi J., Guo C., Brautigan D.L., Larner J.M.
    Cancer Res. 67:1082-1089(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NEK2.
  16. "S6K1-mediated disassembly of mitochondrial URI/PP1gamma complexes activates a negative feedback program that counters S6K1 survival signaling."
    Djouder N., Metzler S.C., Schmidt A., Wirbelauer C., Gstaiger M., Aebersold R., Hess D., Krek W.
    Mol. Cell 28:28-40(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DEPHOSPHORYLATION OF RPS6KB1, ENZYME REGULATION, INTERACTION WITH URI1, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  17. Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NOM1.
  18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-307, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. "GlcNAcylation of a histone methyltransferase in retinoic-acid-induced granulopoiesis."
    Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G., Kitagawa H., Kato S.
    Nature 459:455-459(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MLL5-L COMPLEX.
  20. "Identification and characterization of a novel human PP1 phosphatase complex."
    Lee J.H., You J., Dobrota E., Skalnik D.G.
    J. Biol. Chem. 285:24466-24476(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE PTW/PP1 PHOSPHATASE COMPLEX, FUNCTION, INTERACTION WITH PPP1R8.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "Protein phosphatase 1 (PP1) is a post-translational regulator of the mammalian circadian clock."
    Schmutz I., Wendt S., Schnell A., Kramer A., Mansuy I.M., Albrecht U.
    PLoS ONE 6:E21325-E21325(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CIRCADIAN CLOCK.
  23. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate."
    Egloff M.-P., Cohen P.T.W., Reinemer P., Barford D.
    J. Mol. Biol. 254:942-959(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
  25. "Crystal structure of the tumor-promoter okadaic acid bound to protein phosphatase-1."
    Maynes J.T., Bateman K.S., Cherney M.M., Das A.K., Luu H.A., Holmes C.F., James M.N.
    J. Biol. Chem. 276:44078-44082(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH MANGANESE, COFACTOR.
  26. "Crystal structure and mutagenesis of a protein phosphatase-1:calcineurin hybrid elucidate the role of the beta12-beta13 loop in inhibitor binding."
    Maynes J.T., Perreault K.R., Cherney M.M., Luu H.A., James M.N., Holmes C.F.
    J. Biol. Chem. 279:43198-43206(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 6-298 IN COMPLEX WITH MANGANESE, CATALYTIC ACTIVITY, COFACTOR.

Entry informationi

Entry nameiPP1G_HUMAN
AccessioniPrimary (citable) accession number: P36873
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: September 3, 2014
This is version 173 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Microcystin toxin is bound to Cys-273 through a thioether bond.

Keywords - Technical termi

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

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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