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P36873 (PP1G_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 172. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length323 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. 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. 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 processBiological rhythms
Carbohydrate metabolism
Cell cycle
Cell division
Glycogen metabolism
   Cellular componentCentromere
Chromosome
Cytoplasm
Kinetochore
Mitochondrion
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandManganese
Metal-binding
   Molecular functionHydrolase
Protein phosphatase
   PTMAcetylation
Disulfide bond
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell 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_componentMLL5-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_functionmetal 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...

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3 Ref.4
Chain2 – 323322Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
PRO_0000058787

Sites

Active site1251Proton donor
Metal binding641Manganese 1
Metal binding661Manganese 1
Metal binding921Manganese 1
Metal binding921Manganese 2
Metal binding1241Manganese 2
Metal binding1731Manganese 2
Metal binding2481Manganese 2
Site2731Inhibition by microcystin toxin binding

Amino acid modifications

Modified residue21N-acetylalanine Ref.3 Ref.4 Ref.23
Modified residue3071Phosphothreonine Ref.18

Natural variations

Alternative sequence315 – 3239GMITKQAKK → VASGLNPSIQKASNYRNNTV LYE in isoform Gamma-2.
VSP_005094
Natural variant1521F → S.
Corresponds to variant rs11558237 [ dbSNP | Ensembl ].
VAR_051734

Experimental info

Mutagenesis1251H → A: Loss of activity. Ref.8
Mutagenesis2731C → A, S or L: Abolishes interaction with microcystin toxin. Ref.6

Secondary structure

...................................................... 323
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Gamma-1 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 0EEEF0E842188536

FASTA32336,984
        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 

« Hide

Isoform Gamma-2 [UniParc].

Checksum: 9731E5A6C8EEBF46
Show »

FASTA33738,518

References

« Hide '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.
CCDSCCDS58279.1. [P36873-2]
CCDS9150.1. [P36873-1]
PIRS35699.
S35700.
RefSeqNP_001231903.1. NM_001244974.1. [P36873-2]
NP_002701.1. NM_002710.3. [P36873-1]
UniGeneHs.79081.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IT6X-ray2.00A/B1-323[»]
1JK7X-ray1.90A1-323[»]
1U32X-ray2.00A6-298[»]
2BCDX-ray2.10A1-323[»]
2BDXX-ray2.30A1-323[»]
ProteinModelPortalP36873.
SMRP36873. Positions 6-299.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111495. 191 interactions.
DIPDIP-749N.
IntActP36873. 145 interactions.
MINTMINT-190765.
STRING9606.ENSP00000335084.

Chemistry

BindingDBP36873.
ChEMBLCHEMBL4438.

PTM databases

PhosphoSiteP36873.

Polymorphism databases

DMDM548573.

Proteomic databases

MaxQBP36873.
PaxDbP36873.
PRIDEP36873.

Protocols and materials databases

DNASU5501.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000335007; ENSP00000335084; ENSG00000186298. [P36873-1]
ENST00000340766; ENSP00000341779; ENSG00000186298. [P36873-2]
GeneID5501.
KEGGhsa:5501.
UCSCuc001tru.3. human. [P36873-1]
uc021rdx.1. human. [P36873-2]

Organism-specific databases

CTD5501.
GeneCardsGC12M111157.
HGNCHGNC:9283. PPP1CC.
HPACAB022645.
HPA013661.
MIM176914. gene.
neXtProtNX_P36873.
PharmGKBPA33611.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0639.
HOGENOMHOG000172697.
HOVERGENHBG000216.
KOK06269.
OMAPRSMITK.
OrthoDBEOG7TJ3K3.
PhylomeDBP36873.
TreeFamTF354243.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_21300. Mitotic M-M/G1 phases.
SignaLinkP36873.

Gene expression databases

ArrayExpressP36873.
BgeeP36873.
CleanExHS_PPP1CC.
GenevestigatorP36873.

Family and domain databases

Gene3D3.60.21.10. 1 hit.
InterProIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMSSF56300. SSF56300. 1 hit.
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPPP1CC. human.
EvolutionaryTraceP36873.
GeneWikiPPP1CC.
GenomeRNAi5501.
NextBio21286.
PROP36873.
SOURCESearch...

Entry information

Entry namePP1G_HUMAN
AccessionPrimary (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 statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM