Hmdb loader
Identification
HMDB Protein ID HMDBP07948
Secondary Accession Numbers
  • 13659
  • HMDBP10472
Name Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform
Synonyms
  1. CAM-PRP catalytic subunit
  2. Calmodulin-dependent calcineurin A subunit alpha isoform
Gene Name PPP3CA
Protein Type Unknown
Biological Properties
General Function Involved in hydrolase activity
Specific Function Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin. Dephosphorylates DNM1L, HSPB1 and SSH1.
Pathways
  • Alzheimer disease
  • Amphetamine addiction
  • Amyotrophic lateral sclerosis
  • Apoptosis
  • Axon guidance
  • B cell receptor signaling pathway
  • Calcium signaling pathway
  • Dopaminergic synapse
  • Glutamatergic synapse
  • Human T-cell leukemia virus 1 infection
  • Long-term potentiation
  • MAPK signaling pathway
  • Natural killer cell mediated cytotoxicity
  • Oocyte meiosis
  • Osteoclast differentiation
  • T cell receptor signaling pathway
  • Tuberculosis
  • VEGF signaling pathway
  • Wnt signaling pathway
Reactions
A phosphoprotein + Water → a protein + Phosphate details
GO Classification
Biological Process
skeletal muscle fiber development
cellular response to drug
response to stress
regulation of excitatory postsynaptic membrane potential
response to calcium ion
G1/S transition of mitotic cell cycle
cellular response to glucose stimulus
response to amphetamine
calcium ion transport
negative regulation of insulin secretion
positive regulation of transcription from RNA polymerase II promoter
calcineurin-NFAT signaling cascade
protein import into nucleus
regulation of synaptic transmission
transition between fast and slow fiber
T cell activation
protein dephosphorylation
Cellular Component
cytosol
mitochondrion
nucleus
membrane
calcineurin complex
Z disc
Function
catalytic activity
hydrolase activity
Molecular Function
enzyme binding
calcium ion binding
drug binding
calmodulin-dependent protein phosphatase activity
calmodulin binding
Cellular Location
  1. Cytoplasmic
  2. Nucleus
Gene Properties
Chromosome Location 4
Locus 4q24
SNPs PPP3CA
Gene Sequence
>1566 bp
ATGTCCGAGCCCAAGGCAATTGATCCCAAGTTGTCGACGACCGACAGGGTGGTGAAAGCT
GTTCCATTTCCTCCAAGTCACCGGCTTACAGCAAAAGAAGTGTTTGATAATGATGGAAAA
CCTCGTGTGGATATCTTAAAGGCGCATCTTATGAAGGAGGGAAGGCTGGAAGAGAGTGTT
GCATTGAGAATAATAACAGAGGGTGCATCAATTCTTCGACAGGAAAAAAATTTGCTGGAT
ATTGATGCGCCAGTCACTGTTTGTGGGGACATTCATGGACAATTCTTTGATTTGATGAAG
CTCTTTGAAGTCGGGGGATCTCCTGCCAACACTCGCTACCTCTTCTTAGGGGACTATGTT
GACAGAGGGTACTTCAGTATTGAATGTGTGCTGTATTTGTGGGCCTTGAAAATTCTCTAC
CCCAAAACACTGTTTTTACTTCGTGGAAATCATGAATGTAGACATCTAACAGAGTATTTC
ACATTTAAACAAGAATGTAAAATAAAGTATTCAGAACGAGTATATGATGCCTGTATGGAT
GCCTTTGACTGCCTTCCCCTGGCTGCCCTGATGAACCAACAGTTCCTGTGTGTGCATGGT
GGTTTGTCTCCAGAGATTAACACTTTAGATGATATCAGAAAATTAGACCGATTCAAAGAA
CCACCTGCATATGGACCTATGTGTGATATCCTGTGGTCAGACCCCCTGGAAGATTTTGGA
AATGAGAAGACTCAGGAACATTTCACTCACAACACAGTCAGGGGGTGTTCATACTTCTAC
AGTTACCCGGCTGTATGTGAATTCTTACAGCACAATAACTTGTTATCTATACTCCGAGCC
CACGAAGCCCAAGATGCAGGGTACCGCATGTACAGGAAAAGCCAAACAACAGGCTTCCCT
TCTCTAATTACAATTTTTTCAGCACCAAATTACTTAGATGTATACAATAACAAAGCTGCA
GTATTGAAGTATGAGAACAATGTTATGAATATCAGGCAATTCAACTGTTCTCCTCATCCA
TACTGGCTTCCAAATTTCATGGATGTTTTTACTTGGTCCCTTCCATTTGTTGGGGAAAAA
GTGACTGAGATGCTGGTAAATGTCCTCAACATCTGCTCAGATGATGAACTAGGGTCAGAA
GAAGATGGATTTGATGGTGCAACAGCTGCAGCCCGGAAAGAGGTGATAAGGAACAAGATC
CGAGCAATAGGCAAAATGGCCAGAGTGTTCTCAGTGCTCAGAGAAGAGAGTGAGAGTGTG
CTGACGCTGAAAGGCTTGACCCCAACTGGCATGCTCCCCAGCGGAGTACTTTCTGGAGGG
AAGCAAACCCTGCAAAGCGCTACTGTTGAGGCTATTGAGGCTGATGAAGCTATCAAAGGA
TTTTCACCACAACATAAGATCACTAGCTTCGAGGAAGCCAAGGGCTTAGACCGAATTAAT
GAGAGGATGCCGCCTCGCAGAGATGCCATGCCCTCTGACGCCAACCTTAACTCCATCAAC
AAGGCTCTCACCTCAGAGACTAACGGCACGGACAGCAATGGCAGTAATAGCAGCAATATT
CAGTGA
Protein Properties
Number of Residues 521
Molecular Weight 58687.27
Theoretical pI 5.864
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform
MSEPKAIDPKLSTTDRVVKAVPFPPSHRLTAKEVFDNDGKPRVDILKAHLMKEGRLEESV
ALRIITEGASILRQEKNLLDIDAPVTVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYV
DRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMD
AFDCLPLAALMNQQFLCVHGGLSPEINTLDDIRKLDRFKEPPAYGPMCDILWSDPLEDFG
NEKTQEHFTHNTVRGCSYFYSYPAVCEFLQHNNLLSILRAHEAQDAGYRMYRKSQTTGFP
SLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEK
VTEMLVNVLNICSDDELGSEEDGFDGATAAARKEVIRNKIRAIGKMARVFSVLREESESV
LTLKGLTPTGMLPSGVLSGGKQTLQSATVEAIEADEAIKGFSPQHKITSFEEAKGLDRIN
ERMPPRRDAMPSDANLNSINKALTSETNGTDSNGSNSSNIQ
GenBank ID Protein 306477
UniProtKB/Swiss-Prot ID Q08209
UniProtKB/Swiss-Prot Entry Name PP2BA_HUMAN
PDB IDs
GenBank Gene ID L14778
GeneCard ID PPP3CA
GenAtlas ID PPP3CA
HGNC ID HGNC:9314
References
General References
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  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed:17974005 ]
  4. Goshima N, Kawamura Y, Fukumoto A, Miura A, Honma R, Satoh R, Wakamatsu A, Yamamoto J, Kimura K, Nishikawa T, Andoh T, Iida Y, Ishikawa K, Ito E, Kagawa N, Kaminaga C, Kanehori K, Kawakami B, Kenmochi K, Kimura R, Kobayashi M, Kuroita T, Kuwayama H, Maruyama Y, Matsuo K, Minami K, Mitsubori M, Mori M, Morishita R, Murase A, Nishikawa A, Nishikawa S, Okamoto T, Sakagami N, Sakamoto Y, Sasaki Y, Seki T, Sono S, Sugiyama A, Sumiya T, Takayama T, Takayama Y, Takeda H, Togashi T, Yahata K, Yamada H, Yanagisawa Y, Endo Y, Imamoto F, Kisu Y, Tanaka S, Isogai T, Imai J, Watanabe S, Nomura N: Human protein factory for converting the transcriptome into an in vitro-expressed proteome,. Nat Methods. 2008 Dec;5(12):1011-7. [PubMed:19054851 ]
  5. Screaton RA, Conkright MD, Katoh Y, Best JL, Canettieri G, Jeffries S, Guzman E, Niessen S, Yates JR 3rd, Takemori H, Okamoto M, Montminy M: The CREB coactivator TORC2 functions as a calcium- and cAMP-sensitive coincidence detector. Cell. 2004 Oct 1;119(1):61-74. [PubMed:15454081 ]
  6. Frey N, Olson EN: Calsarcin-3, a novel skeletal muscle-specific member of the calsarcin family, interacts with multiple Z-disc proteins. J Biol Chem. 2002 Apr 19;277(16):13998-4004. Epub 2002 Feb 12. [PubMed:11842093 ]
  7. Kissinger CR, Parge HE, Knighton DR, Lewis CT, Pelletier LA, Tempczyk A, Kalish VJ, Tucker KD, Showalter RE, Moomaw EW, et al.: Crystal structures of human calcineurin and the human FKBP12-FK506-calcineurin complex. Nature. 1995 Dec 7;378(6557):641-4. [PubMed:8524402 ]
  8. Muramatsu T, Kincaid RL: Molecular cloning of a full-length cDNA encoding the catalytic subunit of human calmodulin-dependent protein phosphatase (calcineurin A alpha). Biochim Biophys Acta. 1993 Jul 28;1178(1):117-20. [PubMed:8392375 ]
  9. Frey N, Richardson JA, Olson EN: Calsarcins, a novel family of sarcomeric calcineurin-binding proteins. Proc Natl Acad Sci U S A. 2000 Dec 19;97(26):14632-7. [PubMed:11114196 ]
  10. Wang Y, Shibasaki F, Mizuno K: Calcium signal-induced cofilin dephosphorylation is mediated by Slingshot via calcineurin. J Biol Chem. 2005 Apr 1;280(13):12683-9. Epub 2005 Jan 24. [PubMed:15671020 ]
  11. Cereghetti GM, Stangherlin A, Martins de Brito O, Chang CR, Blackstone C, Bernardi P, Scorrano L: Dephosphorylation by calcineurin regulates translocation of Drp1 to mitochondria. Proc Natl Acad Sci U S A. 2008 Oct 14;105(41):15803-8. doi: 10.1073/pnas.0808249105. Epub 2008 Oct 6. [PubMed:18838687 ]
  12. Chiocco MJ, Zhu X, Walther D, Pletnikova O, Troncoso JC, Uhl GR, Liu QR: Fine mapping of calcineurin (PPP3CA) gene reveals novel alternative splicing patterns, association of 5'UTR trinucleotide repeat with addiction vulnerability, and differential isoform expression in Alzheimer's disease. Subst Use Misuse. 2010 Sep;45(11):1809-26. doi: 10.3109/10826084.2010.482449. [PubMed:20590401 ]