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Protein

Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform

Gene

Ppp3cb

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin.

Catalytic activityi

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactori

Protein has several cofactor binding sites:
  • Fe3+By similarityNote: Binds 1 Fe3+ ion per subunit.By similarity
  • Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi99 – 991IronBy similarity
Metal bindingi101 – 1011IronBy similarity
Metal bindingi127 – 1271IronBy similarity
Metal bindingi127 – 1271ZincBy similarity
Metal bindingi159 – 1591ZincBy similarity
Active sitei160 – 1601Proton donorBy similarity
Metal bindingi208 – 2081ZincBy similarity
Metal bindingi290 – 2901ZincBy similarity

GO - Molecular functioni

  1. calcium-dependent protein serine/threonine phosphatase activity Source: RGD
  2. calcium ion binding Source: UniProtKB
  3. calmodulin binding Source: RGD
  4. calmodulin-dependent protein phosphatase activity Source: UniProtKB
  5. drug binding Source: UniProtKB
  6. enzyme binding Source: UniProtKB
  7. protein heterodimerization activity Source: RGD
  8. protein phosphatase 2B binding Source: UniProtKB
  9. protein serine/threonine phosphatase activity Source: Reactome

GO - Biological processi

  1. calcium ion-dependent exocytosis Source: UniProtKB
  2. cellular response to drug Source: UniProtKB
  3. muscle cell cellular homeostasis Source: RGD
  4. positive regulation of insulin secretion involved in cellular response to glucose stimulus Source: UniProtKB
  5. protein dephosphorylation Source: RGD
  6. protein phosphorylation Source: UniProtKB
  7. regulation of insulin secretion Source: UniProtKB
  8. response to amphetamine Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Calmodulin-binding, Iron, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_348359. DARPP-32 events.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform (EC:3.1.3.16)
Alternative name(s):
CAM-PRP catalytic subunit
Calmodulin-dependent calcineurin A subunit beta isoform
Gene namesi
Name:Ppp3cb
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3383. Ppp3cb.

Subcellular locationi

GO - Cellular componenti

  1. calcineurin complex Source: UniProtKB
  2. cytosol Source: Reactome
  3. plasma membrane Source: UniProtKB
  4. protein complex Source: RGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 525524Serine/threonine-protein phosphatase 2B catalytic subunit beta isoformPRO_0000058827Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP20651.
PRIDEiP20651.

PTM databases

PhosphoSiteiP20651.

Expressioni

Gene expression databases

GenevestigatoriP20651.

Interactioni

Subunit structurei

Composed of two components (A and B), the A component is the catalytic subunit and the B component confers calcium sensitivity.

Binary interactionsi

WithEntry#Exp.IntActNotes
Akap6Q9WVC72EBI-7400670,EBI-7559840

Protein-protein interaction databases

BioGridi246807. 1 interaction.
DIPiDIP-66N.
IntActiP20651. 4 interactions.
MINTiMINT-4589009.
STRINGi10116.ENSRNOP00000010476.

Structurei

3D structure databases

ProteinModelPortaliP20651.
SMRiP20651. Positions 24-381.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 310309CatalyticAdd
BLAST
Regioni256 – 2627Calcineurin B binding-site 1Sequence Analysis
Regioni305 – 3106Calcineurin B binding-site 2Sequence Analysis
Regioni402 – 42423Calmodulin-bindingSequence AnalysisAdd
BLAST
Regioni475 – 49723Inhibitory domainAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi11 – 2010Poly-Pro

Sequence similaritiesi

Belongs to the PPP phosphatase family. PP-2B subfamily.Curated

Phylogenomic databases

eggNOGiCOG0639.
HOGENOMiHOG000172699.
HOVERGENiHBG002819.
InParanoidiP20651.
KOiK04348.
PhylomeDBiP20651.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P20651-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAPEPARAA PPPPPPPPPP LGADRVVKAV PFPPTHRLTS EEVFDMDGIP
60 70 80 90 100
RVDVLKNHLV KEGRVDEEIA LRIINEGAAI LRREKTMIEV EAPITVCGDI
110 120 130 140 150
HGQFFDLMKL FEVGGSPANT RYLFLGDYVD RGYFSIECVL YLWVLKILYP
160 170 180 190 200
STLFLLRGNH ECRHLTEYFT FKQECKIKYS ERVYEACMEA FDSLPLAALL
210 220 230 240 250
NQQFLCVHGG LSPEIHTLDD IRRLDRFKEP PAFGPMCDLL WSDPSEDFGN
260 270 280 290 300
EKSQEHFSHN TVRGCSYFYN YPAVCEFLQN NNLLSIIRAH EAQDAGYRMY
310 320 330 340 350
RKSQTTGFPS LITIFSAPNY LDVYNNKAAV LKYENNVMNI RQFNCSPHPY
360 370 380 390 400
WLPNFMDVFT WSLPFVGEKV TEMLVNVLSI CSDDELMTEG EDQFDVGSAA
410 420 430 440 450
ARKEIIRNKI RAIGKMARVF SVLREESESV LTLKGLTPTG MLPSGVLAGG
460 470 480 490 500
RQTLQSATVE AIEAEKAIRG SSPPHRICSF EEAKGLDRIN ERMPPRKDAV
510 520
QQDGFNSLNT AHTTENHGTG NHSAQ
Length:525
Mass (Da):59,113
Last modified:February 1, 1991 - v1
Checksum:i5E66AF3100BE3987
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31809 mRNA. Translation: AAA40848.1.
D90036 mRNA. Translation: BAA14084.1.
M58441 mRNA. Translation: AAA41915.1.
PIRiA33794.
RefSeqiNP_058738.1. NM_017042.2.
UniGeneiRn.11063.

Genome annotation databases

GeneIDi24675.
KEGGirno:24675.
UCSCiRGD:3383. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31809 mRNA. Translation: AAA40848.1.
D90036 mRNA. Translation: BAA14084.1.
M58441 mRNA. Translation: AAA41915.1.
PIRiA33794.
RefSeqiNP_058738.1. NM_017042.2.
UniGeneiRn.11063.

3D structure databases

ProteinModelPortaliP20651.
SMRiP20651. Positions 24-381.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246807. 1 interaction.
DIPiDIP-66N.
IntActiP20651. 4 interactions.
MINTiMINT-4589009.
STRINGi10116.ENSRNOP00000010476.

PTM databases

PhosphoSiteiP20651.

Proteomic databases

PaxDbiP20651.
PRIDEiP20651.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24675.
KEGGirno:24675.
UCSCiRGD:3383. rat.

Organism-specific databases

CTDi5532.
RGDi3383. Ppp3cb.

Phylogenomic databases

eggNOGiCOG0639.
HOGENOMiHOG000172699.
HOVERGENiHBG002819.
InParanoidiP20651.
KOiK04348.
PhylomeDBiP20651.

Enzyme and pathway databases

ReactomeiREACT_348359. DARPP-32 events.

Miscellaneous databases

NextBioi604059.

Gene expression databases

GenevestigatoriP20651.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Evidence for a second isoform of the catalytic subunit of calmodulin-dependent protein phosphatase (calcineurin A)."
    Kuno T., Takeda T., Hirai M., Ito A., Mukai H., Tanaka C.
    Biochem. Biophys. Res. Commun. 165:1352-1358(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Multiplicity of protein serine-threonine phosphatases in PC12 pheochromocytoma and FTO-2B hepatoma cells."
    Wadzinski B.E., Heasley L.E., Johnson G.L.
    J. Biol. Chem. 265:21504-21508(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 245-315.

Entry informationi

Entry nameiPP2BB_RAT
AccessioniPrimary (citable) accession number: P20651
Secondary accession number(s): Q6LDJ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: April 1, 2015
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.