P62139

PR
Gene name
PPP1CA (PPP1A)
Protein name
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
Names
PP-1A
Species
Oryctolagus cuniculus (Rabbit)
KEGG Pathway
ocu:100009298
EC number
3.1.3.16: Phosphoric monoester hydrolases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

283-330 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

3 structures for P62139

Entry ID Method Resolution Chain Position Source
1FJM X-ray 210 A A/B 1-330 PDB
7NZM EM 396 A B 7-300 PDB
AF-P62139-F1 Predicted AlphaFoldDB

No variants for P62139

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P62139

No associated diseases with P62139

3 regional properties for P62139

Type Name Position InterPro Accession
domain Calcineurin-like phosphoesterase domain, ApaH type 60 - 250 IPR004843
domain Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase 30 - 300 IPR006186
domain Serine-threonine protein phosphatase, N-terminal 9 - 56 IPR031675

Functions

Description
EC Number 3.1.3.16 Phosphoric monoester hydrolases
Subcellular Localization
  • Cytoplasm
  • Nucleus
  • Nucleus, nucleoplasm
  • Nucleus, nucleolus
  • 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)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
nucleolus A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome.
nucleoplasm That part of the nuclear content other than the chromosomes or the nucleolus.
protein phosphatase type 1 complex A protein complex that possesses magnesium-dependent protein serine/threonine phosphatase (AMD phosphatase) activity, and consists of a catalytic subunit and one or more regulatory subunits that dictates the phosphatase's substrate specificity, function, and activity.
PTW/PP1 phosphatase complex A protein serine/threonine phosphatase complex that contains a catalytic subunit (PPP1CA, PPP1CB or PPP1CC) and the regulatory subunits PPP1R10 (PNUTS), TOX4 and WDR82, and plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase.

7 GO annotations of molecular function

Name Definition
fatty acid derivative binding Binding to fatty acid derivative.
metal ion binding Binding to a metal ion.
myosin phosphatase activity Catalysis of the reaction: phosphomyosin + H2O = myosin + phosphate.
phosphatase activity Catalysis of the hydrolysis of phosphoric monoesters, releasing inorganic phosphate.
phosphoprotein phosphatase activity Catalysis of the reaction: a phosphoprotein + H2O = a protein + phosphate. Together with protein kinases, these enzymes control the state of phosphorylation of cellular proteins and thereby provide an important mechanism for regulating cellular activity.
protein phosphatase activator activity Binds to and increases the activity of a protein phosphatase, an enzyme which catalyzes of the removal of a phosphate group from a protein substrate molecule.
protein serine/threonine phosphatase activity Catalysis of the reaction: protein serine phosphate + H2O = protein serine + phosphate, and protein threonine phosphate + H2O = protein threonine + phosphate.

12 GO annotations of biological process

Name Definition
beta-catenin destruction complex disassembly The disaggregation of a beta-catenin destruction complex into its constituent components.
cell cycle The progression of biochemical and morphological phases and events that occur in a cell during successive cell replication or nuclear replication events. Canonically, the cell cycle comprises the replication and segregation of genetic material followed by the division of the cell, but in endocycles or syncytial cells nuclear replication or nuclear division may not be followed by cell division.
cell division The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells.
circadian regulation of gene expression Any process that modulates the frequency, rate or extent of gene expression such that an expression pattern recurs with a regularity of approximately 24 hours.
entrainment of circadian clock by photoperiod The synchronization of a circadian rhythm to photoperiod, the intermittent cycle of light (day) and dark (night).
glycogen metabolic process The chemical reactions and pathways involving glycogen, a polydisperse, highly branched glucan composed of chains of D-glucose residues in alpha-(1->4) glycosidic linkage, joined together by alpha-(1->6) glycosidic linkages.
negative regulation of protein binding Any process that stops, prevents, or reduces the frequency, rate or extent of protein binding.
peptidyl-serine dephosphorylation The removal of phosphoric residues from peptidyl-O-phospho-L-serine to form peptidyl-serine.
positive regulation of canonical Wnt signaling pathway Any process that increases the rate, frequency, or extent of the Wnt signaling pathway through beta-catenin, the series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell, followed by propagation of the signal via beta-catenin, and ending with a change in transcription of target genes.
protein dephosphorylation The process of removing one or more phosphoric residues from a protein.
regulation of circadian rhythm Any process that modulates the frequency, rate or extent of a circadian rhythm. A circadian rhythm is a biological process in an organism that recurs with a regularity of approximately 24 hours.
regulation of translational initiation by eIF2 alpha dephosphorylation Any process that modulates the frequency, rate or extent of translation initiation in response to stress by the dephosphorylation of eIF2 alpha.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
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
KNKGKYGQFS GLNPGGRPIT PPRNSAKAKK