P63088 (PP1G_RAT) 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

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. 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.
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 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 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 By similarity. Ref.3 Ref.4 Ref.5 Ref.6
Subcellular location	Cytoplasm By similarity. Nucleus By similarity. Nucleus › nucleolus 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. 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 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 Nucleus
Coding sequence diversity	Alternative splicing
Ligand	Iron Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure 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
Cellular component	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 cytosol Traceable author statement. Source: Reactome dendritic spine Inferred from direct assay. Source: RGD midbody Inferred from electronic annotation. Source: UniProtKB-SubCell 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 phosphoprotein phosphatase activity Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Gamma-1 (identifier: P63088-1)

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: P63088-2)

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_0000058789

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

147

1

N6-acetyllysine By similarity

Modified residue

307

1

Phosphothreonine By similarity

Natural variations

Alternative sequence

315 – 323

9

GMITKQAKK → VGSGLNPSIQKASNYRNNTV LYE in isoform Gamma-2.

VSP_011566

Secondary structure

1

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323

Helix Strand Turn

Details...

Helix

9 – 17

9

Turn

18 – 21

4

Helix

32 – 48

17

Beta strand

51 – 55

5

Beta strand

59 – 62

4

Helix

69 – 79

11

Beta strand

87 – 89

3

Beta strand

94 – 98

5

Helix

100 – 113

14

Turn

115 – 117

3

Beta strand

118 – 120

3

Helix

128 – 131

4

Helix

136 – 143

8

Helix

146 – 156

11

Beta strand

162 – 165

4

Turn

166 – 168

3

Beta strand

169 – 174

6

Helix

184 – 187

4

Beta strand

197 – 199

3

Helix

200 – 206

7

Beta strand

214 – 218

5

Beta strand

222 – 227

6

Helix

229 – 239

11

Beta strand

242 – 246

5

Beta strand

253 – 258

6

Turn

259 – 262

4

Beta strand

263 – 267

5

Helix

272 – 274

3

Beta strand

279 – 285

7

Beta strand

290 – 296

7

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

[1]	"Identification of members of the protein phosphatase 1 gene family in the rat and enhanced expression of protein phosphatase 1 alpha gene in rat hepatocellular carcinomas." Sasaki K., Shima H., Kitagawa Y., Irino S., Sugimura T., Nagao M. Jpn. J. Cancer Res. 81:1272-1280(1990) [PubMed: 2177460] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS GAMMA-1 AND GAMMA-2), ALTERNATIVE SPLICING.
[2]	Erratum Sasaki K., Shima H., Kitagawa Y., Irino S., Sugimura T., Nagao M. Jpn. J. Cancer Res. 82:873-873(1991) [PubMed: 1653777] [Abstract]
[3]	"Regulation of neurabin I interaction with protein phosphatase 1 by phosphorylation." McAvoy T., Allen P.B., Obaishi H., Nakanishi H., Takai Y., Greengard P., Nairn A.C., Hemmings H.C. Jr. Biochemistry 38:12943-12949(1999) [PubMed: 10504266] [Abstract] Cited for: PROTEIN SEQUENCE OF 42-58 AND 212-234, INTERACTION WITH PPP1R9A. Strain: Sprague-Dawley.
[4]	"Purification of the hepatic glycogen-associated form of protein phosphatase-1 by microcystin-Sepharose affinity chromatography." Moorhead G., MacKintosh C., Morrice N., Cohen P. FEBS Lett. 362:101-105(1995) [PubMed: 7720853] [Abstract] Cited for: INTERACTION WITH PPP1R3B.
[5]	"Identification of the separate domains in the hepatic glycogen-targeting subunit of protein phosphatase 1 that interact with phosphorylase a, glycogen and protein phosphatase 1." Armstrong C.G., Doherty M.J., Cohen P.T.W. Biochem. J. 336:699-704(1998) [PubMed: 9841883] [Abstract] Cited for: INTERACTION WITH PPP1R3B.
[6]	"Brain actin-associated protein phosphatase 1 holoenzymes containing spinophilin, neurabin, and selected catalytic subunit isoforms." MacMillan L.B., Bass M.A., Cheng N., Howard E.F., Tamura M., Strack S., Wadzinski B.E., Colbran R.J. J. Biol. Chem. 274:35845-35854(1999) [PubMed: 10585469] [Abstract] Cited for: SUBUNIT.
[7]	"Structural basis for regulation of protein phosphatase 1 by inhibitor-2." Hurley T.D., Yang J., Zhang L., Goodwin K.D., Zou Q., Cortese M., Dunker A.K., DePaoli-Roach A.A. J. Biol. Chem. 282:28874-28883(2007) [PubMed: 17636256] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-323 IN COMPLEX WITH MANGANESE AND M.MUSCULUS INHIBITOR PPP1R2.
+	Additional computationally mapped references.

Web resources

Protein Spotlight

The things we forget - Issue 32 of March 2003

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D90165 mRNA. Translation: BAA14196.1.
D90166 mRNA. Translation: BAA14197.1. Sequence problems.

IPI

IPI00203358.
IPI00231715.

PIR

I76572.
I76573.

RefSeq

NP_071943.1. NM_022498.1.

UniGene

Rn.1495.
Rn.202940.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2O8A	X-ray	2.61	A/B	2-323	[»]
2O8G	X-ray	2.50	A/B	2-323	[»]

ProteinModelPortal

P63088.

SMR

P63088. Positions 6-299.

ModBase

Search...

Protein-protein interaction databases

IntAct

P63088. 2 interactions.

STRING

P63088.

PTM databases

PhosphoSite

P63088.

Proteomic databases

PRIDE

P63088.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000001711; ENSRNOP00000001711; ENSRNOG00000001269.
ENSRNOT00000048851; ENSRNOP00000047912; ENSRNOG00000001269.

GeneID

24669.

KEGG

rno:24669.

UCSC

NM_022498. rat.

Organism-specific databases

CTD

5501.

RGD

3377. Ppp1cc.

Phylogenomic databases

eggNOG

maNOG06431.

HOVERGEN

HBG000216.

OMA

VGWSEND.

PhylomeDB

P63088.

Enzyme and pathway databases

Reactome

REACT_105988. Metabolism of lipids and lipoproteins.

Gene expression databases

ArrayExpress

P63088.

Genevestigator

P63088.

GermOnline

ENSRNOG00000001269. Rattus norvegicus.

Family and domain databases

InterPro

IPR004843. Metallo_PEstase_dom.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]

KO

K06269.

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

NextBio

604038.

Entry information

Entry name

PP1G_RAT

Accession

Primary (citable) accession number: P63088
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:	December 14, 2011
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program