Ppp3cb
entrez
19056
canonical
uniprot
P48453
canonical
ensembl
ENSMUSG00000021816
resolver
ensp
ENSMUSP00000022355
resolver
ensp
ENSMUSP00000125630
resolver
ensp
ENSMUSP00000125722
resolver
ensp
ENSMUSP00000244084
resolver
ensp
ENSMUSP00000244085
resolver
ensp
ENSMUSP00000244086
resolver
ensp
ENSMUSP00000244091
resolver
enst
ENSMUST00000022355
resolver
enst
ENSMUST00000161445
resolver
genesymbol
Ppp3cb
resolver
genesymbol_syn
Calnb
resolver
uniprot
A0A6B9EQU3
resolver
uniprot
E0CZ78
resolver
uniprot
G3X8U7
resolver
uniprot
Q6NZR4
resolver
uniprot_entry
A0A6B9EQU3_MOUSE
resolver
uniprot_entry
E0CZ78_MOUSE
resolver
uniprot_entry
G3X8U7_MOUSE
resolver
uniprot_entry
PP2BB_MOUSE
resolver
uniprot_sec
Q6NZR4
resolver
activity_regulation
ACTIVITY REGULATION: Activated by Ca(2+)-bound calmodulin following an increase in intracellular Ca(2+). At low Ca(2+) concentrations, the catalytic subunit (also known as calcineurin A) is inactive and is bound to the regulatory subunit (also known as calcineurin B) in which only two high-affinity binding sites are occupied by Ca(2+). In response to elevated calcium levels, the occupancy of the low-affinity sites on calcineurin B by Ca(2+) causes a conformational change of the C-terminal regulatory domain of calcineurin A, resulting in the exposure of the calmodulin-binding domain and in the partial activation of calcineurin A. The subsequent binding of Ca(2+)-bound calmodulin leads to the displacement of the autoinhibitory domain from the active site and possibly of the autoinhibitory segment from the substrate binding site which fully activates calcineurin A. {ECO:0000250|UniProtKB:P16298}.
uniprot
proteins
amino_acid_sequence
MAAPEPARAAPPPPPPPPPPLGADRVVKAVPFPPTHRLTSEEVFDMDGIPRVDVLKNHLVKEGRVDEEIALRIINEGAAILRREKTMIEVEAPITVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWVLKILYPSTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYEACMEAFDSLPLAALLNQQFLCVHGGLSPEIHTLDDIRRLDRFKEPPAFGPMCDLLWSDPSEDFGNEKSQEHFSHNTVRGCSYFYNYPAVCEFLQNNNLLSIIRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTEMLVNVLSICSDDELMTEGEDQFDVGSAAARKEIIRNKIRAIGKMARVFSVLREESESVLTLKGLTPTGMLPSGVLAGGRQTLQSATVEAIEAEKAIRGFSPPHRICSFEEAKGLDRINERMPPRKDAVQQDGFNSLNTAHTTENHGTGNHSAQ
uniprot
proteins
ec_number
3.1.3.16
uniprot
proteins
function
FUNCTION: Calcium-dependent, calmodulin-stimulated protein phosphatase which plays an essential role in the transduction of intracellular Ca(2+)-mediated signals (By similarity). Dephosphorylates TFEB in response to lysosomal Ca(2+) release, resulting in TFEB nuclear translocation and stimulation of lysosomal biogenesis (By similarity). Dephosphorylates and activates transcription factor NFATC1 (By similarity). Dephosphorylates and inactivates transcription factor ELK1 (By similarity). Dephosphorylates DARPP32 (By similarity). Negatively regulates MAP3K14/NIK signaling via inhibition of nuclear translocation of the transcription factors RELA and RELB (PubMed:26029823). May play a role in skeletal muscle fiber type specification (PubMed:12773574). {ECO:0000250|UniProtKB:P16298, ECO:0000269|PubMed:12773574, ECO:0000269|PubMed:26029823}.
uniprot
proteins
mass_dalton
59173
uniprot
proteins
protein_family
PP-2B subfamily
uniprot
proteins
protein_family
PPP phosphatase family
uniprot
proteins
pubmed
10200317
uniprot
proteins
pubmed
12773574
uniprot
proteins
pubmed
1328240
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15509543
uniprot
proteins
pubmed
1659808
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21435446
uniprot
proteins
pubmed
25967121
uniprot
proteins
pubmed
26029823
uniprot
proteins
pubmed
31696965
uniprot
proteins
sequence_length
525
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P16298}.
uniprot
proteins