P36873 (PP1G_HUMAN) 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

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

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. 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. Ref.16 Ref.20 Ref.22
Catalytic activity	[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate. Ref.26
Cofactor	Binds 2 manganese ions per subunit. Ref.25 Ref.26
Enzyme regulation	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. Ref.13 Ref.16
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. Interacts with cyanobacterial toxin microcystin; disulfide-linked. Interacts with PPP1R3B and PPP1R7. Isoform gamma-2interacts 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 1and isoform 4NEK2. Interacts with URI1; the interaction is phosphorylation-dependent and occurs in a growth factor-dependent manner. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20
Subcellular location	Cytoplasm. Nucleus. Nucleus › nucleolus. Nucleus › nucleoplasm. Nucleus speckle. Chromosome › centromere › kinetochore. 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. Ref.8 Ref.11 Ref.16 Ref.17
Post-translational modification	Phosphorylated by NEK2. Ref.12
Miscellaneous	Microcystin toxin is bound to Cys-273 through a thioether bond.
Sequence similarities	Belongs to the PPP phosphatase family. PP-1 subfamily.

Ontologies

Keywords
Biological process	Biological rhythms Carbohydrate metabolism Cell cycle Cell division Glycogen metabolism
Cellular component	Centromere Chromosome Cytoplasm Kinetochore Mitochondrion Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
PTM	Acetylation Disulfide bond Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW circadian regulation of gene expression Inferred from sequence or structural similarity. Source: UniProtKB entrainment of circadian clock by photoperiod Inferred from sequence or structural similarity. Source: UniProtKB glycogen metabolic process Inferred from electronic annotation. Source: UniProtKB-KW mitotic cell cycle Traceable author statement. Source: Reactome negative regulation of transforming growth factor beta receptor signaling pathway Traceable author statement. Source: Reactome protein dephosphorylation Inferred from sequence or structural similarity. Source: UniProtKB regulation of circadian rhythm Inferred from mutant phenotype Ref.22. Source: UniProtKB regulation of nucleocytoplasmic transport Inferred from electronic annotation. Source: Ensembl small molecule metabolic process Traceable author statement. Source: Reactome transforming growth factor beta receptor signaling pathway Traceable author statement. Source: Reactome triglyceride catabolic process Traceable author statement. Source: Reactome
Cellular_component	MLL5-L complex Inferred from direct assay Ref.19. Source: UniProtKB PTW/PP1 phosphatase complex Inferred from direct assay Ref.20. Source: UniProtKB cleavage furrow Inferred from electronic annotation. Source: UniProtKB-SubCell condensed chromosome kinetochore Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from direct assay Ref.8. Source: UniProtKB cytosol Traceable author statement. Source: Reactome midbody Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial outer membrane Inferred from electronic annotation. Source: Ensembl mitochondrion Inferred from direct assay Ref.16. Source: UniProtKB nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus Inferred from direct assay Ref.8. Source: UniProtKB nucleus Inferred from direct assay Ref.8. Source: UniProtKB protein complex Inferred from mutant phenotype PubMed 10880350. Source: UniProtKB
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphatase activity Inferred from sequence or structural similarity. Source: UniProtKB phosphoprotein phosphatase activity Traceable author statement. Source: Reactome poly(A) RNA binding Inferred from direct assay PubMed 22681889. Source: UniProtKB protein N-terminus binding Inferred from physical interaction PubMed 23789093. Source: MGI protein binding Inferred from physical interaction PubMed 17274640PubMed 21382349PubMed 21382349. Source: IntAct protein kinase binding Inferred from physical interaction PubMed 10880350. Source: UniProtKB protein serine/threonine phosphatase activity Inferred from mutant phenotype PubMed 10880350Ref.16. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	A1DRY3	2	EBI-3964623,EBI-4311408
BRCA1	P38398	2	EBI-356283,EBI-349905
Clock	O08785	2	EBI-356283,EBI-79859	From a different organism.
PPP1R2	P41236	4	EBI-356283,EBI-1056517
PPP1R32	Q7Z5V6	4	EBI-3964623,EBI-4311771
RANBP9	Q96S59	3	EBI-3964623,EBI-636085
TCTEX1D4	Q5JR98	3	EBI-3964623,EBI-4311709
TP53	P04637	2	EBI-356289,EBI-366083
TP53BP2	Q13625	6	EBI-356283,EBI-77642
URI1	O94763	6	EBI-356283,EBI-357067

Alternative products

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

Isoform Gamma-1 (identifier: P36873-1)

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: P36873-2)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.3 Ref.4

Chain

2 – 323

322

Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

PRO_0000058787

Sites

Active site

125

1

Proton donor

Metal binding

64

1

Manganese 1

Metal binding

66

1

Manganese 1

Metal binding

92

1

Manganese 1

Metal binding

92

1

Manganese 2

Metal binding

124

1

Manganese 2

Metal binding

173

1

Manganese 2

Metal binding

248

1

Manganese 2

Site

273

1

Inhibition by microcystin toxin binding

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.3 Ref.4 Ref.23

Modified residue

307

1

Phosphothreonine Ref.18

Natural variations

Alternative sequence

315 – 323

9

GMITKQAKK → VASGLNPSIQKASNYRNNTV LYE in isoform Gamma-2.

VSP_005094

Natural variant

152

1

F → S.
Corresponds to variant rs11558237 [ dbSNP | Ensembl ].

VAR_051734

Experimental info

Mutagenesis

125

1

H → A: Loss of activity. Ref.8

Mutagenesis

273

1

C → A, S or L: Abolishes interaction with microcystin toxin. Ref.6

Secondary structure

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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

57 – 62

6

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

Turn

132 – 135

4

Helix

136 – 143

8

Helix

146 – 156

11

Beta strand

162 – 165

4

Turn

166 – 168

3

Beta strand

169 – 174

6

Helix

183 – 187

5

Beta strand

197 – 199

3

Helix

200 – 206

7

Beta strand

214 – 218

5

Beta strand

222 – 227

6

Helix

229 – 238

10

Beta strand

242 – 246

5

Beta strand

254 – 258

5

Turn

259 – 262

4

Beta strand

263 – 267

5

Helix

272 – 274

3

Beta strand

280 – 285

6

Beta strand

291 – 296

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform Gamma-1 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 0EEEF0E842188536	FASTA	323	36,984
	10 20 30 40 50 60 MADLDKLNID 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: 9731E5A6C8EEBF46	FASTA	337	38,518
	10 20 30 40 50 60 MADLDKLNID 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 TPPRVASGLN PSIQKASNYR NNTVLYE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"NOM1 targets protein phosphatase I to the nucleolus." Gunawardena S.R., Ruis B.L., Meyer J.A., Kapoor M., Conklin K.F. J. Biol. Chem. 283:398-404(2008) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NOM1.
[18]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] 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]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] 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]	"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB." Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R. Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Web resources

Protein Spotlight

The things we forget - Issue 32 of March 2003

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X74008 mRNA. Translation: CAA52169.1.
BC014073 mRNA. Translation: AAH14073.1.
L07395 mRNA. Translation: AAA19823.1.

CCDS

CCDS58279.1. [P36873-2]
CCDS9150.1. [P36873-1]

PIR

S35699.
S35700.

RefSeq

NP_001231903.1. NM_001244974.1. [P36873-2]
NP_002701.1. NM_002710.3. [P36873-1]

UniGene

Hs.79081.

3D structure databases

PDBe
RCSB-PDB
PDBj

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	[»]

ProteinModelPortal

P36873.

SMR

P36873. Positions 6-299.

ModBase

Search...

MobiDB

Search...

Protein-protein interaction databases

BioGrid

111495. 191 interactions.

DIP

DIP-749N.

IntAct

P36873. 145 interactions.

MINT

MINT-190765.

STRING

9606.ENSP00000335084.

Chemistry

BindingDB

P36873.

ChEMBL

CHEMBL4438.

PTM databases

PhosphoSite

P36873.

Polymorphism databases

DMDM

548573.

Proteomic databases

MaxQB

P36873.

PaxDb

P36873.

PRIDE

P36873.

Protocols and materials databases

DNASU

5501.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000335007; ENSP00000335084; ENSG00000186298. [P36873-1]
ENST00000340766; ENSP00000341779; ENSG00000186298. [P36873-2]

GeneID

5501.

KEGG

hsa:5501.

UCSC

uc001tru.3. human. [P36873-1]
uc021rdx.1. human. [P36873-2]

Organism-specific databases

CTD

5501.

GeneCards

GC12M111157.

HGNC

HGNC:9283. PPP1CC.

HPA

CAB022645.
HPA013661.

MIM

176914. gene.

neXtProt

NX_P36873.

PharmGKB

PA33611.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0639.

HOGENOM

HOG000172697.

HOVERGEN

HBG000216.

KO

K06269.

OMA

PRSMITK.

OrthoDB

EOG7TJ3K3.

PhylomeDB

P36873.

TreeFam

TF354243.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_21300. Mitotic M-M/G1 phases.

SignaLink

P36873.

Gene expression databases

ArrayExpress

P36873.

Bgee

P36873.

CleanEx

HS_PPP1CC.

Genevestigator

P36873.

Family and domain databases

Gene3D

3.60.21.10. 1 hit.

InterPro

IPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
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]

SUPFAM

SSF56300. SSF56300. 1 hit.

PROSITE

PS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

PPP1CC. human.

EvolutionaryTrace

P36873.

GeneWiki

PPP1CC.

GenomeRNAi

5501.

NextBio

21286.

PRO

P36873.

SOURCE

Search...

Entry information

Entry name

PP1G_HUMAN

Accession

Primary (citable) accession number: P36873

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	July 9, 2014
This is version 172 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.