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P62137 (PP1A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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. 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.8 Ref.10 Ref.11 Ref.12

Catalytic activity

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

Cofactor

Binds 1 iron ion per subunit By similarity.

Binds 2 manganese ions 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. Component of the MLL5-L complex, at least composed of KMT2E/MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with PPP1R9A, PPP1R9B and PPP1R7. Interacts with PPP1R15A; the interaction mediates binding to EIF2S1. Interacts with YLPM1. 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 PPP1R15B; the interaction mediates binding to EIF2S1. Part of a complex containing PPP1R15B, PP1 and NCK1/2. Interacts with NEK2. Interacts with FER; this promotes phosphorylation at Thr-320 By similarity. Interacts with PHACTR4; which acts as an activator of PP1 activity. Ref.6 Ref.7 Ref.8

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 this protein to the nucleolus. In the presence of PPP1R8 relocalizes from the nucleus to nuclear speckles By similarity.

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 processBiological rhythms
Carbohydrate metabolism
Cell cycle
Cell division
Glycogen metabolism
   Cellular componentCytoplasm
Nucleus
   LigandManganese
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 mutant phenotype PubMed 15042703. Source: MGI

cellular process

Traceable author statement PubMed 7857673. Source: MGI

circadian regulation of gene expression

Inferred from direct assay Ref.11. Source: UniProtKB

entrainment of circadian clock by photoperiod

Inferred from mutant phenotype Ref.10. Source: UniProtKB

female meiotic division

Traceable author statement PubMed 9882488. Source: MGI

glycogen metabolic process

Traceable author statement PubMed 7736790. Source: MGI

lung development

Inferred from mutant phenotype PubMed 15042703. Source: MGI

positive regulation of extrinsic apoptotic signaling pathway in absence of ligand

Inferred from mutant phenotype PubMed 12115603. Source: MGI

protein dephosphorylation

Inferred from direct assay Ref.11. Source: UniProtKB

regulation of circadian rhythm

Inferred from direct assay Ref.11. Source: UniProtKB

regulation of glycogen biosynthetic process

Inferred from electronic annotation. Source: Ensembl

regulation of glycogen catabolic process

Inferred from electronic annotation. Source: Ensembl

regulation of translation

Traceable author statement PubMed 7736790. Source: MGI

   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 15042703PubMed 21471512PubMed 9882488. Source: MGI

dendritic spine

Inferred from electronic annotation. Source: Ensembl

glycogen granule

Inferred from electronic annotation. Source: Ensembl

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Inferred from direct assay PubMed 15042703PubMed 9882488. Source: MGI

nucleus

Inferred from direct assay PubMed 21471512. Source: MGI

perikaryon

Inferred from electronic annotation. Source: Ensembl

protein phosphatase type 1 complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphatase activity

Inferred from direct assay Ref.11. Source: UniProtKB

phosphoprotein phosphatase activity

Inferred from direct assay PubMed 14580336. Source: MGI

protein binding

Inferred from physical interaction PubMed 17274640PubMed 19581931PubMed 23555304. Source: IntAct

protein serine/threonine phosphatase activity

Inferred from direct assay PubMed 12115603PubMed 14640981. Source: MGI

ribonucleoprotein complex binding

Inferred from electronic annotation. Source: Ensembl

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_0000058775

Sites

Active site1251Proton donor By similarity
Metal binding641Manganese 1 By similarity
Metal binding661Manganese 1 By similarity
Metal binding921Manganese 1 By similarity
Metal binding921Manganese 2 By similarity
Metal binding1241Manganese 2 By similarity
Metal binding1731Manganese 2 By similarity
Metal binding2481Manganese 2 By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue3051N6-acetyllysine Ref.13
Modified residue3061Phosphotyrosine Ref.9
Modified residue3201Phosphothreonine By similarity

Experimental info

Mutagenesis641D → N: Dominant negatif, severely disrupts circadian rhythmicity of transcription. Ref.11
Mutagenesis951D → N: Dominant negatif, severely disrupts circadian rhythmicity of transcription. Ref.11

Sequences

Sequence LengthMass (Da)Tools
P62137 [UniParc].

Last modified June 21, 2004. Version 1.
Checksum: 8FBFD158A52282E0

FASTA33037,540
        10         20         30         40         50         60 
MSDSEKLNLD SIIGRLLEVQ GSRPGKNVQL TENEIRGLCL KSREIFLSQP ILLELEAPLK 

        70         80         90        100        110        120 
ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS LETICLLLAY KIRYPENFFL 

       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]Ortiz J.M., Lorenzo M.L., Eguiraun A., Andres I., Sangrador A., Allshire R., Hastie N.D.
Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and DBA/2.
Tissue: Extraembryonic tissue, Liver, Pancreas and Placenta.
[3]"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: Kidney.
[4]Lubec G., Klug S.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 44-74; 114-122 AND 247-260, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Hippocampus.
[5]"Molecular cloning of a protein serine/threonine phosphatase containing a putative regulatory tetratricopeptide repeat domain."
Becker W., Kentrup H., Klumpp S., Schultz J.E., Joost H.G.
J. Biol. Chem. 269:22586-22592(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 69-90.
[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]"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.
[8]"Phactr4 regulates neural tube and optic fissure closure by controlling PP1-, Rb-, and E2F1-regulated cell-cycle progression."
Kim T.H., Goodman J., Anderson K.V., Niswander L.
Dev. Cell 13:87-102(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PHACTR4.
[9]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-306, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[10]"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.
[11]"The period of the circadian oscillator is primarily determined by the balance between casein kinase 1 and protein phosphatase 1."
Lee H.M., Chen R., Kim H., Etchegaray J.P., Weaver D.R., Lee C.
Proc. Natl. Acad. Sci. U.S.A. 108:16451-16456(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CIRCADIAN CLOCK, MUTAGENESIS OF ASP-64 AND ASP-95.
[12]"Phactr4 regulates directional migration of enteric neural crest through PP1, integrin signaling, and cofilin activity."
Zhang Y., Kim T.H., Niswander L.
Genes Dev. 26:69-81(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-305, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Web resources

Protein Spotlight

The things we forget - Issue 32 of March 2003

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U25809 mRNA. Translation: AAC99814.1.
AK007932 mRNA. Translation: BAB25358.1.
AK028392 mRNA. Translation: BAC25928.1.
AK090070 mRNA. Translation: BAC41078.1.
AK151582 mRNA. Translation: BAE30522.1.
AK152667 mRNA. Translation: BAE31402.1.
AK153517 mRNA. Translation: BAE32060.1.
AK159575 mRNA. Translation: BAE35196.1.
AK167244 mRNA. Translation: BAE39365.1.
AK167538 mRNA. Translation: BAE39605.1.
AK167880 mRNA. Translation: BAE39893.1.
AK167981 mRNA. Translation: BAE39973.1.
BC014828 mRNA. Translation: AAH14828.1.
CCDSCCDS29421.1.
RefSeqNP_114074.1. NM_031868.2.
UniGeneMm.1970.
Mm.474260.

3D structure databases

ProteinModelPortalP62137.
SMRP62137. Positions 7-299.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202335. 30 interactions.
IntActP62137. 28 interactions.
MINTMINT-4108290.

PTM databases

PhosphoSiteP62137.

Proteomic databases

MaxQBP62137.
PaxDbP62137.
PRIDEP62137.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000046094; ENSMUSP00000039109; ENSMUSG00000040385.
ENSMUST00000180575; ENSMUSP00000137997; ENSMUSG00000096994.
GeneID19045.
KEGGmmu:19045.
UCSCuc008fzg.1. mouse.

Organism-specific databases

CTD5499.
MGIMGI:103016. Ppp1ca.

Phylogenomic databases

eggNOGCOG0639.
GeneTreeENSGT00530000062911.
HOGENOMHOG000172697.
HOVERGENHBG000216.
InParanoidP62137.
KOK06269.
OMAMGDVMNI.
OrthoDBEOG7TJ3K3.
PhylomeDBP62137.
TreeFamTF354243.

Gene expression databases

BgeeP62137.
GenevestigatorP62137.

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

ChiTaRSPPP1CA. mouse.
NextBio21272.
PROP62137.
SOURCESearch...

Entry information

Entry namePP1A_MOUSE
AccessionPrimary (citable) accession number: P62137
Secondary accession number(s): P08129 expand/collapse secondary AC list , P20653, P22802, Q3U7G7, Q9Z1G2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: June 21, 2004
Last modified: July 9, 2014
This is version 110 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot