Reviewed,
UniProtKB/Swiss-Prot P48454 (PP2BC_HUMAN)
Last modified
November 25, 2008.
Version 69.
History...
Clusters with 100%,
90%,
50% identity |
Documents (4) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Serine/threonine-protein phosphatase 2B catalytic subunit gamma isoform EC=3.1.3.16 Alternative name(s): Calmodulin-dependent calcineurin A subunit gamma isoform Calcineurin, testis-specific catalytic subunit CAM-PRP catalytic subunit | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 502 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 + H(2)O = a protein + phosphate. |
| Cofactor | Binds 1 Fe(3+) 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. |
| Tissue specificity | Testis. |
| 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 | activation of pro-apoptotic gene products Inferred from Experiment. Source: Reactome |
| Cellular component | cytosol Inferred from Experiment. Source: Reactome |
| Molecular function | calmodulin binding Inferred from electronic annotation. Source: UniProtKB-KW iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW phosphoprotein phosphatase activityInferred from electronic annotation. Source: UniProtKB-KW 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 – 502 | 502 | Serine/threonine-protein phosphatase 2B catalytic subunit gamma isoform | PRO_0000058828 | |||||
Sites | |||||||||
| Active site | 147 | 1 | Proton donor By similarity | ||||||
| Metal binding | 86 | 1 | Iron By similarity | ||||||
| Metal binding | 88 | 1 | Iron By similarity | ||||||
| Metal binding | 114 | 1 | Iron By similarity | ||||||
| Metal binding | 114 | 1 | Zinc By similarity | ||||||
| Metal binding | 146 | 1 | Zinc By similarity | ||||||
| Metal binding | 195 | 1 | Zinc By similarity | ||||||
| Metal binding | 277 | 1 | Zinc By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 475 – 476 | 2 | HA → YP in AAB23769. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Molecular cloning and chromosomal mapping of the human gene for the testis-specific catalytic subunit of calmodulin-dependent protein phosphatase (calcineurin A)." Muramatsu T., Kincaid R.L. Biochem. Biophys. Res. Commun. 188:265-271(1992) [PubMed: 1339277] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Testis. |
| [2] | "Isoform specific expression of calcineurin in endothelial cells." Bako E., Aydonian A., Verin A.D., Garcia J.G.N. Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Endothelial cell. |
| [3] | Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C.Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| S46622 mRNA. Translation: AAB23769.1. AY007249 mRNA. Translation: AAG02563.1. CH471080 Genomic DNA. Translation: EAW63679.1. | |
| PIR | JC1283. |
| UniGene | Hs.655661 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1AUI based on UniProtKB Q08209. |
| SMR | P48454. Positions 11-381. |
| ModBase | Search... |
PTM databases | |
| PhosphoSite | P48454. |
Genome annotation databases | |
| Ensembl | ENSG00000120910. Homo sapiens. [Contig view] |
Organism-specific databases | |
| HGNC | HGNC:9316. PPP3CC. |
| MIM | 114107. gene. |
| PharmGKB | PA33680. |
| GenAtlas | Search... |
| GeneCards | Search... |
Phylogenomic databases | |
| HOVERGEN | P48454. |
Enzyme and pathway databases | |
| Reactome | REACT_578. Apoptosis. |
Gene expression databases | |
| ArrayExpress | P48454. |
| CleanEx | HS_PPP3CC. |
| GermOnline | ENSG00000120910. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR004843. M-pesterase. IPR006186. T_phtase_apaH. [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 | |
| SOURCE | Search... |
Entry information
| Entry name | PP2BC_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P48454 Secondary accession number(s): Q9H4M5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Human chromosome 8 Human chromosome 8: entries, gene names and cross-references to MIM |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| UniProtKB secondary accession numbers Index of UniProtKB secondary accession numbers |
| SIMILARITY comments Index of protein domains and families |

Clusters with


