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Reviewed, UniProtKB/Swiss-Prot P62137 (PP1A_MOUSE)

Last modified July 7, 2009. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

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 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.

Catalytic activity

A phosphoprotein + H2O = a protein + 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, PPP1R3B, PPP1R3C and PPP1R3D mediate binding to glycogen. Component of the MLL5-L complex, at least composed of MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with PPP1R9A, PPP1R9B and PPP1R7 By similarity. PPP1R15A and PPP1R15B mediate binding to EIF2S1. Part of a complex containing PPP1R15B, PP1 and NCK1/2.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

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

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 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 residue3061Phosphotyrosine
Modified residue3201Phosphothreonine By similarity

Sequences

Sequence LengthMass (Da)Tools
P62137-1 [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: 16141072] [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: 15489334] [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, 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: 8077208] [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: 14638860] [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: 16835242] [Abstract]
Cited for: IDENTIFICATION IN COMPLEX WITH PPP1R15B AND NCK1.
[8]"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: 19131326] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-306, MASS SPECTROMETRY.
+Additional computationally mapped references.

Web resources

Protein Spotlight

The things we forget - Issue 32 of March 2003

Cross-references

Sequence databases

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.
IPIIPI00130185.
RefSeqNP_114074.1.
UniGeneMm.1970
Mm.474260

3D structure databases

HSSPHSSP built from PDB template 1FJM based on UniProtKB P08129.
SMRP62137. Positions 7-300.
ModBaseSearch...

Protein-protein interaction databases

IntActP62137. 19 interactions.

PTM databases

PhosphoSiteP62137.

Proteomic databases

PRIDEP62137.

Genome annotation databases

EnsemblENSMUSG00000040385. Mus musculus. [Contig view]
GeneID19045.
KEGGmmu:19045.

Organism-specific databases

MGIMGI:103016. Ppp1ca.

Phylogenomic databases

HOGENOMP62137.
HOVERGENP62137.
OMAP62137. FFSKRQL.

Enzyme and pathway databases

BRENDA3.1.3.16. 244.

Gene expression databases

ArrayExpressP62137.
BgeeP62137.
GermOnlineENSMUSG00000040385. Mus musculus.

Family and domain databases

InterProIPR004843. M-pesterase.
IPR006186. T_phtase_apaH.
[Graphical view]
PANTHERPTHR11668. T_phtase_apaH. 1 hit.
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR00114. STPHPHTASE.
ProDomPD000252. T_phtase_apaH. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00156. PP2Ac. 1 hit.
[Graphical view]
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio295505.
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 7, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents