P63087 (PP1G_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified April 16, 2014. Version 109. History...
Names and origin
|Protein names||Recommended name:|
Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
Protein phosphatase 1C catalytic subunit
|Organism||Mus musculus (Mouse) [Reference proteome]|
|Taxonomic identifier||10090 [NCBI]|
|Taxonomic lineage||Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus|
|Sequence length||323 AA.|
|Sequence processing||The displayed sequence is further processed into a mature form.|
|Protein existence||Evidence at protein level|
General annotation (Comments)
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 By similarity.
[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.
Binds 1 iron ion per subunit By similarity.
Binds 1 manganese ion per subunit By similarity.
Inactivated by binding to URI1 By similarity.
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. 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 By similarity. Isoform gamma-2interacts with SPZ1. This interaction can prevent SPZ1 binding to the E-box and inhibits PPP1CC activity. 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 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 NEK2. Interacts with URI1; the interaction is phosphorylation-dependent and occurs in a growth factor-dependent manner By similarity. Isoform 2interacts with PPP1R42; the interaction is direct. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10
Cytoplasm By similarity. Nucleus By similarity. Cleavage furrow By similarity. Nucleus › nucleolus By similarity. Nucleus › nucleoplasm By similarity. Chromosome › centromere › kinetochore 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.
Phosphorylated by NEK2 By similarity.
|This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]|
|Isoform Gamma-1 (identifier: P63087-1) |
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.
|Isoform Gamma-2 (identifier: P63087-2) |
The sequence of this isoform differs from the canonical sequence as follows:
315-323: GMITKQAKK → VGSGLNPSIQKASNYRNNTVLYE
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Initiator methionine||1||1||Removed By similarity|
|Chain||2 – 323||322||Serine/threonine-protein phosphatase PP1-gamma catalytic subunit||PRO_0000058788|
|Active site||125||1||Proton donor By similarity|
|Metal binding||64||1||Iron By similarity|
|Metal binding||66||1||Iron By similarity|
|Metal binding||92||1||Iron By similarity|
|Metal binding||92||1||Manganese By similarity|
|Metal binding||124||1||Manganese By similarity|
|Metal binding||173||1||Manganese By similarity|
|Metal binding||248||1||Manganese By similarity|
Amino acid modifications
|Modified residue||2||1||N-acetylalanine By similarity|
|Modified residue||307||1||Phosphothreonine By similarity|
|Alternative sequence||315 – 323||9||GMITKQAKK → VGSGLNPSIQKASNYRNNTV LYE in isoform Gamma-2.||VSP_005095|
|Sequence conflict||316 – 317||2||MI → IV in AAC53383. Ref.2|
|Sequence conflict||316 – 317||2||MI → IV in AAC53384. Ref.2|
|Sequence conflict||316 – 317||2||MI → IV in BAA19729. Ref.3|
|||"The fission yeast dis2+ gene required for chromosome disjoining encodes one of two putative type 1 protein phosphatases."|
Ohkura H., Kinoshita N., Miyatani S., Toda T., Yanagida M.
Cell 57:997-1007(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GAMMA-2).
|||"Genomic organization and functional analysis of the murine protein phosphatase 1c gamma (Ppp1cc) gene."|
Okano K., Heng H., Trevisanato S., Tyers M., Varmuza S.
Genomics 45:211-215(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS GAMMA-1 AND GAMMA-2), ALTERNATIVE SPLICING.
Strain: 129 and CD-1.
|||"Tertially complex among Pim-1 kinase, protein phosphatase 1 gamma, and PAP-1."|
Harada Y., Sato E., Izumi F., Imamura Y., Ariga H., Iguchi-Ariga S.
Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GAMMA-1).
|||"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).
Strain: C57BL/6, C57BL/6J and NOD.
Tissue: Brain and Thymus.
|||Lubec G., Klug S.|
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 61-74 AND 114-122, IDENTIFICATION BY MASS SPECTROMETRY.
|||"Inhibition of a constitutive translation initiation factor 2alpha phosphatase, CReP, promotes survival of stressed cells."|
Jousse C., Oyadomari S., Novoa I., Lu P., Zhang Y., Harding H.P., Ron D.
J. Cell Biol. 163:767-775(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PPP1R15B.
|||"Identification of the spermatogenic zip protein Spz1 as a putative protein phosphatase-1 (PP1) regulatory protein that specifically binds the PP1cgamma2 splice variant in mouse testis."|
Hrabchak C., Varmuza S.
J. Biol. Chem. 279:37079-37086(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SPZ1.
|||"Nck in a complex containing the catalytic subunit of protein phosphatase 1 regulates eukaryotic initiation factor 2alpha signaling and cell survival to endoplasmic reticulum stress."|
Latreille M., Larose L.
J. Biol. Chem. 281:26633-26644(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN COMPLEX WITH PPP1R15B AND NCK1.
|||"TLRR (lrrc67) interacts with PP1 and is associated with a cytoskeletal complex in the testis."|
Wang R., Kaul A., Sperry A.O.
Biol. Cell 102:173-189(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PPP1R42.
|||"Ikaros stability and pericentromeric localization are regulated by protein phosphatase 1."|
Popescu M., Gurel Z., Ronni T., Song C., Hung K.Y., Payne K.J., Dovat S.
J. Biol. Chem. 284:13869-13880(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IKFZ1.
|+||Additional computationally mapped references.|
|Protein Spotlight |
The things we forget - Issue 32 of March 2003
|M27071 mRNA. Translation: AAA37526.1.|
U53456 mRNA. Translation: AAC53383.1.
U53276 U53275 Genomic DNA. Translation: AAC53384.1.
U53276 U53275 Genomic DNA. Translation: AAC53385.1.
D85137 mRNA. Translation: BAA19729.1.
BC010613 mRNA. Translation: AAH10613.1.
BC021646 mRNA. Translation: AAH21646.1.
BC085496 mRNA. Translation: AAH85496.1.
|RefSeq||NP_038664.2. NM_013636.3. |
3D structure databases
|SMR||P63087. Positions 6-299. |
Protein-protein interaction databases
|BioGrid||202337. 33 interactions.|
|IntAct||P63087. 22 interactions.|
Protocols and materials databases
Genome annotation databases
|Ensembl||ENSMUST00000086294; ENSMUSP00000083474; ENSMUSG00000004455. [P63087-2]|
ENSMUST00000102528; ENSMUSP00000099587; ENSMUSG00000004455. [P63087-1]
|UCSC||uc008zks.1. mouse. [P63087-1]|
uc008zkt.1. mouse. [P63087-2]
|MGI||MGI:104872. Ppp1cc. |
Gene expression databases
Family and domain databases
|InterPro||IPR004843. Calcineurin-like_PHP_apaH. |
|Pfam||PF00149. Metallophos. 1 hit. |
|PRINTS||PR00114. STPHPHTASE. |
|SMART||SM00156. PP2Ac. 1 hit. |
|PROSITE||PS00125. SER_THR_PHOSPHATASE. 1 hit. |
|ChiTaRS||PPP1CC. mouse. |
|Accession||Primary (citable) accession number: P63087|
Secondary accession number(s): O09186 Q64679
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Chordata Protein Annotation Program|