Reviewed,
UniProtKB/Swiss-Prot P20651 (PP2BB_RAT)
Last modified
November 3, 2009.
Version 77.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform EC=3.1.3.16 Alternative name(s): Calmodulin-dependent calcineurin A subunit beta isoform CAM-PRP catalytic subunit | ||
| Gene names |
| ||
| Organism | Rattus norvegicus (Rat) | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 525 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin. |
| Catalytic activity | A phosphoprotein + H2O = a protein + phosphate. |
| Cofactor | Binds 1 Fe3+ ion per subunit By similarity. Binds 1 zinc ion per subunit By similarity. |
| Subunit structure | Composed of two components (A and B), the A component is the catalytic subunit and the B component confers calcium sensitivity. |
| Sequence similarities | Belongs to the PPP phosphatase family. PP-2B subfamily. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Calmodulin-binding Iron Metal-binding Zinc |
| Molecular function | Hydrolase Protein phosphatase |
| Gene Ontology (GO) | |
| Biological process | muscle homeostasis Inferred from expression pattern. Source: RGD protein amino acid dephosphorylationInferred from direct assay. Source: RGD response to amphetamineInferred from expression pattern. Source: RGD |
| Cellular component | insoluble fraction Inferred from direct assay. Source: RGD protein complexInferred from direct assay. Source: RGD soluble fractionInferred from direct assay. Source: RGD |
| Molecular function | calcium-dependent protein serine/threonine phosphatase activity Inferred from direct assay. Source: RGD calmodulin bindingInferred from direct assay. Source: RGD iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW protein heterodimerization activityInferred from direct assay. Source: RGD zinc ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 525 | 525 | Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform | PRO_0000058827 | |||||
Regions | |||||||||
| Region | 1 – 310 | 310 | Catalytic | ||||||
| Region | 256 – 262 | 7 | Calcineurin B binding-site 1 Potential | ||||||
| Region | 305 – 310 | 6 | Calcineurin B binding-site 2 Potential | ||||||
| Region | 402 – 424 | 23 | Calmodulin-binding Potential | ||||||
| Region | 475 – 497 | 23 | Inhibitory domain | ||||||
| Compositional bias | 11 – 20 | 10 | Poly-Pro | ||||||
Sites | |||||||||
| Active site | 160 | 1 | Proton donor By similarity | ||||||
| Metal binding | 99 | 1 | Iron By similarity | ||||||
| Metal binding | 101 | 1 | Iron By similarity | ||||||
| Metal binding | 127 | 1 | Iron By similarity | ||||||
| Metal binding | 127 | 1 | Zinc By similarity | ||||||
| Metal binding | 159 | 1 | Zinc By similarity | ||||||
| Metal binding | 208 | 1 | Zinc By similarity | ||||||
| Metal binding | 290 | 1 | Zinc By similarity | ||||||
Sequences
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References
| [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(1989) [PubMed: 2558657] [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(1990) [PubMed: 2174876] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 245-315. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| M31809 mRNA. Translation: AAA40848.1. D90036 mRNA. Translation: BAA14084.1. M58441 mRNA. Translation: AAA41915.1. | |
| IPI | IPI00201407. |
| PIR | A33794. |
| RefSeq | NP_058738.1. |
| UniGene | Rn.11063 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1AUI based on UniProtKB Q08209. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP:66N. |
| STRING | P20651. |
PTM databases | |
| PhosphoSite | P20651. |
Genome annotation databases | |
| Ensembl | ENSRNOT00000010476; ENSRNOP00000010476; ENSRNOG00000007757; Rattus norvegicus. [Genome view] |
| GeneID | 24675. |
| KEGG | rno:24675. |
Organism-specific databases | |
| CTD | 24675. |
| RGD | 3383. Ppp3cb. |
Phylogenomic databases | |
| HOVERGEN | P20651. |
Enzyme and pathway databases | |
| BRENDA | 3.1.3.16. 248. |
Gene expression databases | |
| Genevestigator | P20651. |
| GermOnline | ENSRNOG00000007757. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR004843. M-pesterase. IPR006186. Ser/Thr-sp_prot-phosphatase. [Graphical view] |
| PANTHER | PTHR11668. T_phtase_apaH. 1 hit. |
| Pfam | PF00149. Metallophos. 1 hit. [Graphical view] |
| PRINTS | PR00114. STPHPHTASE. |
| ProDom | PD000252. T_phtase_apaH. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| SMART | SM00156. PP2Ac. 1 hit. [Graphical view] |
| PROSITE | PS00125. SER_THR_PHOSPHATASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 604059. |
Entry information
| Entry name | PP2BB_RAT | ||||||||
| Accession | Primary (citable) accession number: P20651 Secondary accession number(s): Q6LDJ7 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

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