Serine/threonine-protein phosphatase PP1-alpha catalytic subunit

Details

Name
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
Synonyms
  • 3.1.3.16
  • PP-1A
  • PPP1A
Gene Name
PPP1CA
Organism
Humans
Amino acid sequence
>lcl|BSEQ0007306|Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
MSDSEKLNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQPILLELEAPLK
ICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFL
LRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDL
QSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHD
LDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAD
KNKGKYGQFSGLNPGGRPITPPRNSAKAKK
Number of residues
330
Molecular Weight
37511.695
Theoretical pI
6.25
GO Classification
Functions
metal ion binding / phosphatase activity / protein serine/threonine phosphatase activity / ribonucleoprotein complex binding
Processes
branching morphogenesis of an epithelial tube / cell cycle / cell division / circadian regulation of gene expression / dephosphorylation / entrainment of circadian clock by photoperiod / glycogen metabolic process / lung development / negative regulation of transforming growth factor beta receptor signaling pathway / positive regulation of extrinsic apoptotic signaling pathway in absence of ligand / protein dephosphorylation / regulation of circadian rhythm / regulation of glycogen biosynthetic process / regulation of glycogen catabolic process / regulation of translational initiation by eIF2 alpha dephosphorylation / small molecule metabolic process / transforming growth factor beta receptor signaling pathway / triglyceride catabolic process
Components
cytoplasm / cytosol / dendritic spine / extracellular exosome / glycogen granule / MLL5-L complex / nucleolus / nucleoplasm / nucleus / perikaryon / plasma membrane / protein phosphatase type 1 complex / PTW/PP1 phosphatase complex
General Function
Ribonucleoprotein complex binding
Specific 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 Ca(2+)/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. Dephosphorylates the 'Ser-418' residue of FOXP3 in regulatory T-cells (Treg) from patients with rheumatoid arthritis, thereby inactivating FOXP3 and rendering Treg cells functionally defective (PubMed:23396208).
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0021365|Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (PPP1CA)
ATGTCCGACAGCGAGAAGCTCAACCTGGACTCGATCATCGGGCGCCTGCTGGAAGGGTCC
AGGGTCCTGACACCCCATTGCGCCCCAGTGCAGGGCTCGCGGCCTGGCAAGAATGTACAG
CTGACAGAGAACGAGATCCGCGGTCTGTGCCTGAAATCCCGGGAGATTTTTCTGAGCCAG
CCCATTCTTCTGGAGCTGGAGGCACCCCTCAAGATCTGCGGTGACATACACGGCCAGTAC
TACGACCTTCTGCGACTATTTGAGTATGGCGGTTTCCCTCCCGAGAGCAACTACCTCTTT
CTGGGGGACTATGTGGACAGGGGCAAGCAGTCCTTGGAGACCATCTGCCTGCTGCTGGCC
TATAAGATCAAGTACCCCGAGAACTTCTTCCTGCTCCGTGGGAACCACGAGTGTGCCAGC
ATCAACCGCATCTATGGTTTCTACGATGAGTGCAAGAGACGCTACAACATCAAACTGTGG
AAAACCTTCACTGACTGCTTCAACTGCCTGCCCATCGCGGCCATAGTGGACGAAAAGATC
TTCTGCTGCCACGGAGGCCTGTCCCCGGACCTGCAGTCTATGGAGCAGATTCGGCGGATC
ATGCGGCCCACAGATGTGCCTGACCAGGGCCTGCTGTGTGACCTGCTGTGGTCTGACCCT
GACAAGGACGTGCAGGGCTGGGGCGAGAACGACCGTGGCGTCTCTTTTACCTTTGGAGCC
GAGGTGGTGGCCAAGTTCCTCCACAAGCACGACTTGGACCTCATCTGCCGAGCACACCAG
GTGGTAGAAGACGGCTACGAGTTCTTTGCCAAGCGGCAGCTGGTGACACTTTTCTCAGCT
CCCAACTACTGTGGCGAGTTTGACAATGCTGGCGCCATGATGAGTGTGGACGAGACCCTC
ATGTGCTCTTTCCAGATCCTCAAGCCCGCCGACAAGAACAAGGGGAAGTACGGGCAGTTC
AGTGGCCTGAACCCTGGAGGCCGACCCATCACCCCACCCCGCAATTCCGCCAAAGCCAAG
AAATAG
Chromosome Location
11
Locus
11q13
External Identifiers
ResourceLink
UniProtKB IDP62136
UniProtKB Entry NamePP1A_HUMAN
GenBank Protein ID35451
GenBank Gene IDX70848
HGNC IDHGNC:9281
General References
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  7. He B, Gross M, Roizman B: The gamma(1)34.5 protein of herpes simplex virus 1 complexes with protein phosphatase 1alpha to dephosphorylate the alpha subunit of the eukaryotic translation initiation factor 2 and preclude the shutoff of protein synthesis by double-stranded RNA-activated protein kinase. Proc Natl Acad Sci U S A. 1997 Feb 4;94(3):843-8. [Article]
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Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB025062,6,8-Trimethyl-3-Amino-9-Benzyl-9-Methoxynonanoic AcidexperimentalunknownDetails