P63087 (PP1G_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
Short name=PP-1G
EC=3.1.3.16

Alternative name(s):
Protein phosphatase 1C catalytic subunit

Gene names

Name:

Ppp1cc

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	323 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Catalytic activity	A phosphoprotein + H2O = a protein + phosphate.
Cofactor	Binds 1 iron ion per subunit By similarity. Binds 1 manganese ion per subunit By similarity.
Enzyme regulation	Inactivated by binding to URI1 By similarity.
Subunit structure	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 MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with PPP1R3B, PPP1R7 and CDCA2 By similarity. Isoform gamma-2 interacts 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 2 interacts with PPP1R42; the interaction is direct. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10
Subcellular location	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.
Post-translational modification	Phosphorylated by NEK2 By similarity.
Sequence similarities	Belongs to the PPP phosphatase family. PP-1 subfamily.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cell cycle Cell division Glycogen metabolism
Cellular component	Centromere Chromosome Cytoplasm Kinetochore Mitochondrion Nucleus
Coding sequence diversity	Alternative splicing
Ligand	Iron Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW glycogen metabolic process Inferred from electronic annotation. Source: UniProtKB-KW neuron differentiation Inferred from sequence or structural similarity PubMed 17202132. Source: MGI protein dephosphorylation Inferred from direct assay PubMed 14640981PubMed 17369396. Source: MGI regulation of nucleocytoplasmic transport Inferred from mutant phenotype PubMed 17369396. Source: MGI
Cellular_component	MLL5-L complex Inferred from electronic annotation. Source: Compara PTW/PP1 phosphatase complex Inferred from sequence or structural similarity. Source: UniProtKB cleavage furrow Inferred from electronic annotation. Source: UniProtKB-SubCell condensed chromosome kinetochore Inferred from electronic annotation. Source: UniProtKB-SubCell midbody Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial outer membrane Inferred from direct assay PubMed 12931191. Source: MGI nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine phosphatase activity Inferred from direct assay PubMed 14640981PubMed 17369396. Source: MGI
Complete GO annotation...

Alternative products

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
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 323	322	Serine/threonine-protein phosphatase PP1-gamma catalytic subunit		PRO_0000058788
Sites
	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
Natural variations
	Alternative sequence	315 – 323	9	GMITKQAKK → VGSGLNPSIQKASNYRNNTV LYE in isoform Gamma-2.		VSP_005095
Experimental info
	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

Sequences

	Sequence		Length	Mass (Da)
	Isoform Gamma-1 [UniParc]. Last modified September 13, 2004. Version 1. Checksum: 4E28412C16898615	FASTA	323	36,984
	10 20 30 40 50 60 MADIDKLNID SIIQRLLEVR GSKPGKNVQL QENEIRGLCL KSREIFLSQP ILLELEAPLK 70 80 90 100 110 120 ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS LETICLLLAY KIKYPENFFL 130 140 150 160 170 180 LRGNHECASI NRIYGFYDEC KRRYNIKLWK TFTDCFNCLP IAAIVDEKIF CCHGGLSPDL 190 200 210 220 230 240 QSMEQIRRIM RPTDVPDQGL LCDLLWSDPD KDVLGWGEND RGVSFTFGAE VVAKFLHKHD 250 260 270 280 290 300 LDLICRAHQV VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAE 310 320 KKKPNATRPV TPPRGMITKQ AKK
	Isoform Gamma-2 [UniParc]. Checksum: E6F271155E0E67D7	FASTA	337	38,504
	10 20 30 40 50 60 MADIDKLNID SIIQRLLEVR GSKPGKNVQL QENEIRGLCL KSREIFLSQP ILLELEAPLK 70 80 90 100 110 120 ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS LETICLLLAY KIKYPENFFL 130 140 150 160 170 180 LRGNHECASI NRIYGFYDEC KRRYNIKLWK TFTDCFNCLP IAAIVDEKIF CCHGGLSPDL 190 200 210 220 230 240 QSMEQIRRIM RPTDVPDQGL LCDLLWSDPD KDVLGWGEND RGVSFTFGAE VVAKFLHKHD 250 260 270 280 290 300 LDLICRAHQV VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAE 310 320 330 KKKPNATRPV TPPRVGSGLN PSIQKASNYR NNTVLYE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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). Tissue: Brain.
[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. Tissue: Embryo.
[3]	"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). Tissue: Brain.
[4]	"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.
[5]	Lubec G., Klug S. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 61-74 AND 114-122, MASS SPECTROMETRY. Tissue: Hippocampus.
[6]	"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.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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.

Web resources

Protein Spotlight

The things we forget - Issue 32 of March 2003

Cross-references

Sequence databases
EMBL GenBank DDBJ	M27071 mRNA. Translation: AAA37526.1. U53456 mRNA. Translation: AAC53383.1. U53276 , U53271, U53272, U53273, U53275 Genomic DNA. Translation: AAC53384.1. U53276 , U53271, U53272, U53273, 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.
IPI	IPI00123862. IPI00227773.
PIR	C32550.
RefSeq	NP_038664.2. NM_013636.3.
UniGene	Mm.280784. Mm.474554.
3D structure databases
ProteinModelPortal	P63087.
SMR	P63087. Positions 6-299.
ModBase	Search...
Protein-protein interaction databases
IntAct	P63087. 22 interactions.
PTM databases
PhosphoSite	P63087.
Proteomic databases
PaxDb	P63087.
PRIDE	P63087.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000086294; ENSMUSP00000083474; ENSMUSG00000004455. ENSMUST00000102528; ENSMUSP00000099587; ENSMUSG00000004455.
GeneID	19047.
KEGG	mmu:19047.
Organism-specific databases
CTD	5501.
MGI	MGI:104872. Ppp1cc.
Phylogenomic databases
eggNOG	COG0639.
GeneTree	ENSGT00530000062911.
HOGENOM	HOG000172697.
HOVERGEN	HBG000216.
KO	K06269.
OMA	VMGWGEN.
OrthoDB	EOG49GKGT.
Gene expression databases
ArrayExpress	P63087.
Bgee	P63087.
Genevestigator	P63087.
GermOnline	ENSMUSG00000044341. Mus musculus.
Family and domain databases
InterPro	IPR004843. Metallo_PEstase_dom. IPR006186. Ser/Thr-sp_prot-phosphatase. [Graphical view]
Pfam	PF00149. Metallophos. 1 hit. [Graphical view]
PRINTS	PR00114. STPHPHTASE.
SMART	SM00156. PP2Ac. 1 hit. [Graphical view]
PROSITE	PS00125. SER_THR_PHOSPHATASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChEMBL	CHEMBL3270.
ChiTaRS	PPP1CC. mouse.
NextBio	295513.
SOURCE	Search...

Entry information

Entry name

PP1G_MOUSE

Accession

Primary (citable) accession number: P63087
Secondary accession number(s): O09186 , O09189, P37139, Q64679

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2004
Last sequence update:	September 13, 2004
Last modified:	April 3, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program