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P62138 (PP1A_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit

Short name=PP-1A
EC=3.1.3.16
Gene names
Name:Ppp1ca
Synonyms:Ppp1a
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length330 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. 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. Regulates NEK2 function in terms of kinase activity and centrosome number and splitting, both in the presence and absence of radiation-induced DNA damage. Regulator of neural tube and optic fissure closure, and enteric neural crest cell (ENCCs) migration during development By similarity.

Catalytic activity

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactor

Binds 1 iron ion per subunit By similarity.

Binds 1 manganese ion per subunit 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. Interacts with PPP1R15A and PPP1R15B; the interactions mediate binding to EIF2S1. Part of a complex containing PPP1R15B, PP1 and NCK1/2. Component of the MLL5-L complex, at least composed of KMT2E/MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with PPP1R7. Forms a complex with ILF2, ILF3, YLPM1, KHDRBS1, RBMX and NCOA5. Interacts with NOM1 and PPP1R8. Interacts with PPP1R16B. Interacts with RPSA only in the presence of PPP1R16B. Component of the PTW/PP1 phosphatase complex, composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or PPP1CC. Interacts with PPP1R10/PNUTS and PPP1R8. Interacts with WDR82 in the presence of PPP1R10/PNUTS. Interacts with PPP1R39. Interacts with TRIM28; the interaction dephosphorylates TRIM28 on 'Ser-824' and forms a complex at the p21 promoter site By similarity. Interacts with PPP1R9A, PPP1R9B and YLPM1. Interacts with NEK2. Interacts with PHACTR4; which acts as an activator of PP1 activity. Interacts with FER; this promotes phosphorylation at Thr-320 By similarity. Ref.5 Ref.7

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. Nucleusnucleoplasm By similarity. Nucleusnucleolus By similarity. Note: Primarily nuclear and largely excluded from the nucleolus. Highly mobile in cells and can be relocalized through interaction with targeting subunits. NOM1 plays a role in targeting it to the nucleolus. In the presence of PPP1R8 relocalizes from the nucleus to nuclear speckles By similarity.

Tissue specificity

Widely expressed. Ref.3

Post-translational modification

Phosphorylated. Dephosphorylated at Thr-320 in the presence of ionizing radiation By similarity.

Sequence similarities

Belongs to the PPP phosphatase family. PP-1 subfamily.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cell cycle
Cell division
Glycogen metabolism
   Cellular componentCytoplasm
Nucleus
   LigandIron
Manganese
Metal-binding
   Molecular functionHydrolase
Protein phosphatase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbranching morphogenesis of an epithelial tube

Inferred from electronic annotation. Source: Ensembl

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

lung development

Inferred from electronic annotation. Source: Ensembl

positive regulation of extrinsic apoptotic signaling pathway in absence of ligand

Inferred from electronic annotation. Source: Ensembl

protein dephosphorylation

Inferred from direct assay PubMed 7720853. Source: RGD

regulation of glycogen biosynthetic process

Inferred from direct assay PubMed 7720853. Source: RGD

regulation of glycogen catabolic process

Inferred from direct assay PubMed 7720853. Source: RGD

   Cellular_componentMLL5-L complex

Inferred from electronic annotation. Source: Ensembl

PTW/PP1 phosphatase complex

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 12065664. Source: RGD

cytosol

Traceable author statement. Source: Reactome

dendritic spine

Inferred from direct assay PubMed 7724573. Source: RGD

glycogen granule

Inferred from direct assay PubMed 7720853. Source: RGD

neuron projection

Inferred from direct assay PubMed 12065664. Source: RGD

neuronal cell body

Inferred from direct assay PubMed 12065664. Source: RGD

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay PubMed 7724573. Source: RGD

perikaryon

Inferred from direct assay PubMed 7724573. Source: RGD

protein phosphatase type 1 complex

Inferred from direct assay PubMed 7720853. Source: RGD

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoprotein phosphatase activity

Inferred from direct assay PubMed 7720853. Source: RGD

protein serine/threonine phosphatase activity

Inferred from electronic annotation. Source: Ensembl

ribonucleoprotein complex binding

Inferred from physical interaction PubMed 12065664. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 330329Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
PRO_0000058777

Sites

Active site1251Proton donor By similarity
Metal binding641Iron By similarity
Metal binding661Iron By similarity
Metal binding921Iron By similarity
Metal binding921Manganese By similarity
Metal binding1241Manganese By similarity
Metal binding1731Manganese By similarity
Metal binding2481Manganese By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue3051N6-acetyllysine By similarity
Modified residue3061Phosphotyrosine By similarity
Modified residue3201Phosphothreonine By similarity

Sequences

Sequence LengthMass (Da)Tools
P62138 [UniParc].

Last modified June 21, 2004. Version 1.
Checksum: 60C37E1AD9831DAC

FASTA33037,512
        10         20         30         40         50         60 
MSDSEKLNLD SIIGRLLEVQ GSRPGKNVQL TENEIRGLCL 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 KDVQGWGEND RGVSFTFGAE VVAKFLHKHD 

       250        260        270        280        290        300 
LDLICRAHQV VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAD 

       310        320        330 
KNKGKYGQFS GLNPGGRPIT PPRNSAKAKK 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and sequence analysis of cDNA for the catalytic subunit 1 alpha of rat kidney type 1 protein phosphatase, and detection of the gene expression at high levels in hepatoma cells and regenerating livers as compared to rat livers."
Kitamura K., Mizuno Y., Sasaki A., Yasui A., Tsuiki S., Kikuchi K.
J. Biochem. 109:307-310(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.
[2]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Differential expression of protein phosphatase 1 isoforms in mammalian brain."
da Cruz e Silva E.F., Fox C.A., Ouimet C.C., Gustafson E., Watson S.J., Greengard P.
J. Neurosci. 15:3375-3389(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
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].
Tissue: Heart.
[5]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 7-26 AND 212-234, INTERACTION WITH PPP1R9A AND PPP1R9B.
Strain: Sprague-Dawley.
[6]Lubec G., Afjehi-Sadat L.
Submitted (NOV-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 44-60 AND 112-122, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Spinal cord.
[7]"The nuclear PP1 interacting protein ZAP3 (ZAP) is a putative nucleoside kinase that complexes with SAM68, CIA, NF110/45, and HNRNP-G."
Ulke-Lemee A., Trinkle-Mulcahy L., Chaulk S., Bernstein N.K., Morrice N., Glover M., Lamond A.I., Moorhead G.B.G.
Biochim. Biophys. Acta 1774:1339-1350(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH YLPM1.
+Additional computationally mapped references.

Web resources

Protein Spotlight

The things we forget - Issue 32 of March 2003

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D00859 mRNA. Translation: BAA00732.1.
D90163 mRNA. Translation: BAA14194.1.
BC070517 mRNA. Translation: AAH70517.1.
PIRJX0157.
RefSeqNP_113715.1. NM_031527.1.
UniGeneRn.2024.

3D structure databases

ProteinModelPortalP62138.
SMRP62138. Positions 7-299.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid246800. 2 interactions.
IntActP62138. 1 interaction.

Chemistry

BindingDBP62138.

PTM databases

PhosphoSiteP62138.

Proteomic databases

PaxDbP62138.
PRIDEP62138.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000025282; ENSRNOP00000025282; ENSRNOG00000018708.
GeneID24668.
KEGGrno:24668.
UCSCRGD:3375. rat.

Organism-specific databases

CTD5499.
RGD3375. Ppp1ca.

Phylogenomic databases

eggNOGCOG0639.
GeneTreeENSGT00530000062911.
HOGENOMHOG000172697.
HOVERGENHBG000216.
InParanoidP62138.
KOK06269.
OMALEHEIRY.
OrthoDBEOG7TJ3K3.
PhylomeDBP62138.
TreeFamTF354243.

Gene expression databases

ArrayExpressP62138.
GenevestigatorP62138.

Family and domain databases

InterProIPR004843. Calcineurin-like_PHP_apaH.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
[Graphical view]
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio604034.
PROP62138.

Entry information

Entry namePP1A_RAT
AccessionPrimary (citable) accession number: P62138
Secondary accession number(s): P08129, P20653, P22802
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: June 21, 2004
Last modified: April 16, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries