Calcineurin subunit B type 1


NameCalcineurin subunit B type 1
SynonymsCNA2 CNB Protein phosphatase 2B regulatory subunit 1 Protein phosphatase 3 regulatory subunit B alpha isoform 1
Gene NamePPP3R1
OrganismHuman
Amino acid sequence
>lcl|BSEQ0010107|Calcineurin subunit B type 1
MGNEASYPLEMCSHFDADEIKRLGKRFKKLDLDNSGSLSVEEFMSLPELQQNPLVQRVID
IFDTDGNGEVDFKEFIEGVSQFSVKGDKEQKLRFAFRIYDMDKDGYISNGELFQVLKMMV
GNNLKDTQLQQIVDKTIINADKDGDGRISFEEFCAVVGGLDIHKKMVVDV
Number of residues170
Molecular Weight19299.785
Theoretical pI4.4
GO Classification
Functions
    calmodulin binding
    calcium ion binding
    protein domain specific binding
    calcium-dependent protein serine/threonine phosphatase activity
Processes
    Fc-epsilon receptor signaling pathway
    positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway
    apoptotic process
    positive regulation of transcription from RNA polymerase II promoter
    stimulatory C-type lectin receptor signaling pathway
    protein dephosphorylation
    programmed cell death
    intrinsic apoptotic signaling pathway
    calcineurin-NFAT signaling cascade
    innate immune response
    positive regulation of NFAT protein import into nucleus
Components
    sarcolemma
    calcineurin complex
    cytosol
    nucleoplasm
General FunctionProtein domain specific binding
Specific FunctionRegulatory subunit of calcineurin, a calcium-dependent, calmodulin stimulated protein phosphatase. Confers calcium sensitivity.
Transmembrane Regions
GenBank Protein ID180705
UniProtKB IDP63098
UniProtKB Entry NameCANB1_HUMAN
Cellular LocationCytoplasm
Gene sequence
>lcl|BSEQ0010108|Calcineurin subunit B type 1 (PPP3R1)
ATGGGAAATGAGGCAAGTTATCCTTTGGAAATGTGCTCACACTTTGATGCGGATGAAATT
AAAAGGCTAGGAAAGAGATTTAAGAAGCTTGATTTGGACAATTCTGGTTCTTTGAGTGTG
GAAGAGTTCATGTCTCTGCCTGAGTTACAACAGAATCCTTTAGTACAGCGAGTAATAGAT
ATATTCGACACAGATGGGAATGGAGAAGTAGACTTTAAAGAATTCATTGAGGGCGTCTCT
CAGTTCAGTGTCAAAGGAGATAAGGAGCAGAAATTGAGGTTTGCTTTCCGTATCTATGAC
ATGGATAAAGATGGCTATATTTCCAATGGGGAACTCTTCCAGGTATTGAAGATGATGGTG
GGGAACAATCTGAAAGATACACAGTTACAGCAAATTGTAGACAAAACCATAATAAATGCA
GATAAGGATGGAGATGGAAGAATATCCTTTGAAGAATTCTGTGCTGTTGTAGGTGGCCTA
GATATCCACAAAAAGATGGTGGTAGATGTGTGA
GenBank Gene IDM30773
GeneCard IDNone
GenAtlas IDPPP3R1
HGNC IDHGNC:9317
Chromosome Location2
Locus2p15
References
  1. Guerini D, Krinks MH, Sikela JM, Hahn WE, Klee CB: Isolation and sequence of a cDNA clone for human calcineurin B, the Ca2+-binding subunit of the Ca2+/calmodulin-stimulated protein phosphatase. DNA. 1989 Nov;8(9):675-82.[2558868 ]
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  4. Thinon E, Serwa RA, Broncel M, Brannigan JA, Brassat U, Wright MH, Heal WP, Wilkinson AJ, Mann DJ, Tate EW: Global profiling of co- and post-translationally N-myristoylated proteomes in human cells. Nat Commun. 2014 Sep 26;5:4919. doi: 10.1038/ncomms5919.[25255805 ]
  5. 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.[8524402 ]
  6. Huai Q, Kim HY, Liu Y, Zhao Y, Mondragon A, Liu JO, Ke H: Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes. Proc Natl Acad Sci U S A. 2002 Sep 17;99(19):12037-42. Epub 2002 Sep 6.[12218175 ]
  7. Jin L, Harrison SC: Crystal structure of human calcineurin complexed with cyclosporin A and human cyclophilin. Proc Natl Acad Sci U S A. 2002 Oct 15;99(21):13522-6. Epub 2002 Sep 30.[12357034 ]
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