Q27889 · PP2B2_DROME
- ProteinSerine/threonine-protein phosphatase 2B catalytic subunit 2
- GenePp2B-14D
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids570 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin.
Catalytic activity
- H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 Fe3+ ion per subunit.
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 156 | Fe cation (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 158 | Fe cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 184 | Fe cation (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 184 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 216 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Active site | 217 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 265 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 347 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | calcineurin complex | |
Cellular Component | cytoplasm | |
Molecular Function | calcium-dependent protein serine/threonine phosphatase activity | |
Molecular Function | calmodulin binding | |
Molecular Function | calmodulin-dependent protein phosphatase activity | |
Molecular Function | metal ion binding | |
Molecular Function | myosin phosphatase activity | |
Molecular Function | protein serine/threonine phosphatase activity | |
Biological Process | calcineurin-mediated signaling | |
Biological Process | female meiotic nuclear division | |
Biological Process | meiotic cell cycle | |
Biological Process | regulation of embryonic development | |
Biological Process | sleep | |
Biological Process | wing disc development |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerine/threonine-protein phosphatase 2B catalytic subunit 2
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionQ27889
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000058831 | 1-570 | Serine/threonine-protein phosphatase 2B catalytic subunit 2 | |||
Sequence: MSSNNQSSSVAQAATSARTVSAGSAEATDANSTASNNNNNSSSTAAAGNNSDNSSPTTGTGTGASTGKLHGGHTAVNTKERVVDSVPFPPSHKLTLAEVFDQRTGKPNHELLKQHFILEGRIEEAPALKIIQDGAALLRQEKTMIDIEAPVTVCGDIHGQFYDLMKLFEVGGSPASTKYLFLGDYVDRGYFSIECVLYLWSLKITYPQTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMDAFDCLPLAALMNQQFLCVHGGLSPEIHELEDIRRLDRFKEPPAFGPMCDLLWSDPLEDFGNEKNSDFYTHNSVRGCSYFYSYAACCDFLQNNNLLSIIRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTEMLVNVLNICSDDELMTEESEEPLSDDEAALRKEVIRNKIRAIGKMARVFSVLREESESVLQLKGLTPTGALPLGALSGGKQSLKNAMQGFSPNHKITSFAEAKGLDAVNERMPPRRDQPPTPSEDPNQHSQQGGKNGAGHG |
Proteomic databases
Expression
Tissue specificity
Expressed in CNS and PNS.
Developmental stage
Expressed both maternally and zygotically in embryos, larvae and adults.
Gene expression databases
Interaction
Subunit
Interacts with sra in a complex that contains CanA-14F.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q27889 | euc Q9VE19 | 4 | EBI-132663, EBI-9936648 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-67 | Polar residues | ||||
Sequence: MSSNNQSSSVAQAATSARTVSAGSAEATDANSTASNNNNNSSSTAAAGNNSDNSSPTTGTGTGASTG | ||||||
Region | 1-88 | Disordered | ||||
Sequence: MSSNNQSSSVAQAATSARTVSAGSAEATDANSTASNNNNNSSSTAAAGNNSDNSSPTTGTGTGASTGKLHGGHTAVNTKERVVDSVPF | ||||||
Region | 530-570 | Disordered | ||||
Sequence: EAKGLDAVNERMPPRRDQPPTPSEDPNQHSQQGGKNGAGHG |
Sequence similarities
Belongs to the PPP phosphatase family. PP-2B subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length570
- Mass (Da)63,101
- Last updated2005-08-30 v2
- Checksum4A5429A620C0C275
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
M9NE01 | M9NE01_DROME | Pp2B-14D | 570 |
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-67 | Polar residues | ||||
Sequence: MSSNNQSSSVAQAATSARTVSAGSAEATDANSTASNNNNNSSSTAAAGNNSDNSSPTTGTGTGASTG | ||||||
Sequence conflict | 111 | in Ref. 2 | ||||
Sequence: Missing | ||||||
Sequence conflict | 133 | in Ref. 1; CAA54807 | ||||
Sequence: D → E | ||||||
Sequence conflict | 175 | in Ref. 1; CAA54807 and 2; AAB29893 | ||||
Sequence: A → Q | ||||||
Sequence conflict | 323-333 | in Ref. 1; CAA54807 | ||||
Sequence: SYFYSYAACCD → CY | ||||||
Sequence conflict | 407 | in Ref. 1; CAA54807 | ||||
Sequence: Y → I | ||||||
Sequence conflict | 459 | in Ref. 1; CAA54807 | ||||
Sequence: L → V | ||||||
Sequence conflict | 491 | in Ref. 1; CAA54807 | ||||
Sequence: Missing |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X77768 EMBL· GenBank· DDBJ | CAA54807.1 EMBL· GenBank· DDBJ | mRNA | ||
S68806 EMBL· GenBank· DDBJ | AAB29893.1 EMBL· GenBank· DDBJ | mRNA | ||
AE014298 EMBL· GenBank· DDBJ | AAF48622.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT010083 EMBL· GenBank· DDBJ | AAQ22552.1 EMBL· GenBank· DDBJ | mRNA |