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P62139 (PP1A_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 94. 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·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-alpha catalytic subunit

Short name=PP-1A
EC=3.1.3.16
Gene names
Name:PPP1CA
Synonyms:PPP1A
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

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 By similarity.

Catalytic activity

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

Cofactor

Binds 2 manganese ions per subunit. Ref.6

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 PPP1R9A, PPP1R9B and PPP1R7. 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 TRIM28; the interaction dephosphorylates TRIM28 on 'Ser-824' and forms a complex at the p21 promoter site By similarity. Interacts with PPP1R39. 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

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.

Tissue specificity

Detected in skeletal muscle (at protein level). Detected in skeletal muscle. Ref.1

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
   Coding sequence diversityAlternative splicing
   LigandManganese
Metal-binding
   Molecular functionHydrolase
Protein phosphatase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

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

protein dephosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of circadian rhythm

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentPTW/PP1 phosphatase complex

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

phosphoprotein phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.5. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

GRIN2BQ132242EBI-2008988,EBI-2256942From a different organism.
PPP1R11O609272EBI-2008988,EBI-1048104From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 2 (identifier: P62139-1)

Also known as: 1-alpha-2;

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 1 (identifier: P62139-2)

Also known as: 1-alpha-1;

The sequence of this isoform differs from the canonical sequence as follows:
     2-33: SDSEKLNLDSIIGRLLEVQGSRPGKNVQLTEN → MVTIMTTSEYLSGY
Note: No experimental confirmation available.

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_0000058776

Sites

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

Amino acid modifications

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

Natural variations

Alternative sequence2 – 3332SDSEK…QLTEN → MVTIMTTSEYLSGY in isoform 1.
VSP_010642

Experimental info

Sequence conflict3091F → L in CAA68693. Ref.1
Sequence conflict3091F → L in CAA30645. Ref.3

Secondary structure

...................................................... 330
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 2 (1-alpha-2) [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

Isoform 1 (1-alpha-1) [UniParc] [UniParc].

Checksum: F8F24487D1110507
Show »

FASTA31235,597

References

[1]"Isolation and sequence analysis of a cDNA clone encoding a type-1 protein phosphatase catalytic subunit: homology with protein phosphatase 2A."
Berndt N., Campbell D.G., Caudwell F.B., Cohen P., da Cruz e Silva E.F., da Cruz e Silva O.B., Cohen P.T.W.
FEBS Lett. 223:340-346(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, TISSUE SPECIFICITY.
Strain: New Zealand white.
Tissue: Skeletal muscle.
[2]"Molecular cloning of a cDNA for the catalytic subunit of rabbit muscle phosphorylase phosphatase."
Bai G., Zhang Z., Amin J., Deans-Zirattu S.A., Lee E.Y.C.
FASEB J. 2:3010-3016(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Muscle.
[3]"Two isoforms of protein phosphatase 1 may be produced from the same gene."
Cohen P.T.W.
FEBS Lett. 232:17-23(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Strain: New Zealand white.
Tissue: Skeletal muscle.
[4]"The major type-1 protein phosphatase catalytic subunits are the same gene products in rabbit skeletal muscle and rabbit liver."
Cohen P.T.W., Schelling D.L., da Cruz e Silva O.B., Barker H.M., Cohen P.
Biochim. Biophys. Acta 1008:125-128(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Strain: New Zealand white.
Tissue: Liver.
[5]"FLJ23654 encodes a heart protein phosphatase 1-binding protein (Hepp1)."
Chen C.Y., Lai N.S., Yang J.J., Huang H.L., Hung W.C., Li C., Lin T.H., Huang H.B.
Biochem. Biophys. Res. Commun. 391:698-702(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PPP1R39.
[6]"Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1."
Goldberg J., Huang H.B., Kwon Y.G., Greengard P., Nairn A.C., Kuriyan J.
Nature 376:745-753(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS, COFACTOR.

Web resources

Protein Spotlight

The things we forget - Issue 32 of March 2003

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00701 mRNA. Translation: CAA68693.1.
X07798 mRNA. Translation: CAA30645.1.
X14832 mRNA. Translation: CAA32941.1.
PIRPARB11. S04335.
RefSeqNP_001095176.1. NM_001101706.1.
UniGeneOcu.2075.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FJMX-ray2.10A/B1-330[»]
ProteinModelPortalP62139.
SMRP62139. Positions 7-299.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid1172319. 78 interactions.
IntActP62139. 3 interactions.
MINTMINT-106725.

Chemistry

BindingDBP62139.

Proteomic databases

PRIDEP62139.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100009298.

Organism-specific databases

CTD5499.

Phylogenomic databases

eggNOGCOG0639.
HOVERGENHBG000216.

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

EvolutionaryTraceP62139.

Entry information

Entry namePP1A_RABIT
AccessionPrimary (citable) accession number: P62139
Secondary accession number(s): P08128 expand/collapse secondary AC list , P08129, P20653, P22802
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: June 21, 2004
Last modified: July 9, 2014
This is version 94 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references