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Showing Protein Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (HMDBP08684)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 6 metabolites
Identification
HMDB Protein ID HMDBP08684
Secondary Accession Numbers
  • 14405
  • HMDBP09427
Name Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
Synonyms
  1. PP-1A
Gene Name PPP1CA
Protein Type Unknown
Biological Properties
General Function Involved in hydrolase activity
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.
Pathways
  • Alcoholism
  • Amphetamine addiction
  • Dopaminergic synapse
  • Excitatory Neural Signalling Through 5-HTR 4 and Serotonin
  • Excitatory Neural Signalling Through 5-HTR 6 and Serotonin
  • Excitatory Neural Signalling Through 5-HTR 7 and Serotonin
  • Focal adhesion
  • Herpes simplex virus 1 infection
  • Hippo signaling pathway
  • Insulin signaling pathway
  • Intracellular Signalling Through FSH Receptor and Follicle Stimulating Hormone
  • Intracellular Signalling Through Histamine H2 Receptor and Histamine
  • Intracellular Signalling Through LHCGR Receptor and Luteinizing Hormone/Choriogonadotropin
  • Long-term potentiation
  • mRNA surveillance pathway
  • Oocyte meiosis
  • Proteoglycans in cancer
  • Regulation of actin cytoskeleton
  • Vascular smooth muscle contraction
Reactions
A phosphoprotein + Water → a protein + Phosphate details
GO Classification
Biological Process
small molecule metabolic process
cell cycle
cell division
branching morphogenesis of a tube
glycogen metabolic process
triglyceride catabolic process
negative regulation of transforming growth factor beta receptor signaling pathway
lung development
transforming growth factor beta receptor signaling pathway
regulation of glycogen biosynthetic process
regulation of glycogen catabolic process
protein dephosphorylation
Cellular Component
cytosol
nucleolus
perikaryon
dendritic spine
protein phosphatase type 1 complex
PTW/PP1 phosphatase complex
glycogen granule
MLL5-L complex
Function
catalytic activity
hydrolase activity
Molecular Function
protein serine/threonine phosphatase activity
metal ion binding
ribonucleoprotein complex binding
Cellular Location
  1. Cytoplasmic
  2. Nucleus
  3. Nucleus
  4. Nucleus
  5. Cytoplasm
  6. nucleolus
  7. nucleoplasm
Gene Properties
Chromosome Location 11
Locus 11q13
SNPs PPP1CA
Gene Sequence 
>993 bp
ATGTCCGACAGCGAGAAGCTCAACCTGGACTCGATCATCGGGCGCCTGCTGGAAGTGCAG
GGCTCGCGGCCTGGCAAGAATGTACAGCTGACAGAGAACGAGATCCGCGGTCTGTGCCTG
AAATCCCGGGAGATTTTTCTGAGCCAGCCCATTCTTCTGGAGCTGGAGGCACCCCTCAAG
ATCTGCGGTGACATACACGGCCAGTACTACGACCTTCTGCGACTATTTGAGTATGGCGGT
TTCCCTCCCGAGAGCAACTACCTCTTTCTGGGGGACTATGTGGACAGGGGCAAGCAGTCC
TTGGAGACCATCTGCCTGCTGCTGGCCTATAAGATCAAGTACCCCGAGAACTTCTTCCTG
CTCCGTGGGAACCACGAGTGTGCCAGCATCAACCGCATCTATGGTTTCTACGATGAGTGC
AAGAGACGCTACAACATCAAACTGTGGAAAACCTTCACTGACTGCTTCAACTGCCTGCCC
ATCGCGGCCATAGTGGACGAAAAGATCTTCTGCTGCCACGGAGGCCTGTCCCCGGACCTG
CAGTCTATGGAGCAGATTCGGCGGATCATGCGGCCCACAGATGTGCCTGACCAGGGCCTG
CTGTGTGACCTGCTGTGGTCTGACCCTGACAAGGACGTGCAGGGCTGGGGCGAGAACGAC
CGTGGCGTCTCTTTTACCTTTGGAGCCGAGGTGGTGGCCAAGTTCCTCCACAAGCACGAC
TTGGACCTCATCTGCCGAGCACACCAGGTGGTAGAAGACGGCTACGAGTTCTTTGCCAAG
CGGCAGCTGGTGACACTTTTCTCAGCTCCCAACTACTGTGGCGAGTTTGACAATGCTGGC
GCCATGATGAGTGTGGACGAGACCCTCATGTGCTCTTTCCAGATCCTCAAGCCCGCCGAC
AAGAACAAGGGGAAGTACGGGCAGTTCAGTGGCCTGAACCCTGGAGGCCGACCCATCACC
CCACCCCGCAATTCCGCCAAAGCCAAGAAATAG
Protein Properties
Number of Residues 330
Molecular Weight 38630.99
Theoretical pI 6.629
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence 
>Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
MSDSEKLNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQPILLELEAPLK
ICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFL
LRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDL
QSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHD
LDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAD
KNKGKYGQFSGLNPGGRPITPPRNSAKAKK
GenBank ID Protein 35451
UniProtKB/Swiss-Prot ID P62136
UniProtKB/Swiss-Prot Entry Name PP1A_HUMAN
PDB IDs
GenBank Gene ID X70848
GeneCard ID PPP1CA
GenAtlas ID PPP1CA
HGNC ID HGNC:9281
References
General References
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  3. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
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  8. Connor JH, Weiser DC, Li S, Hallenbeck JM, Shenolikar S: Growth arrest and DNA damage-inducible protein GADD34 assembles a novel signaling complex containing protein phosphatase 1 and inhibitor 1. Mol Cell Biol. 2001 Oct;21(20):6841-50. [PubMed:11564868 ]
  9. Ceulemans H, Vulsteke V, De Maeyer M, Tatchell K, Stalmans W, Bollen M: Binding of the concave surface of the Sds22 superhelix to the alpha 4/alpha 5/alpha 6-triangle of protein phosphatase-1. J Biol Chem. 2002 Dec 6;277(49):47331-7. Epub 2002 Sep 10. [PubMed:12226088 ]
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  14. 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. [PubMed:9023344 ]
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