Q80TL0 · PPM1E_MOUSE
- ProteinProtein phosphatase 1E
- GenePpm1e
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids749 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Protein phosphatase that inactivates multifunctional CaM kinases such as CAMK4 and CAMK2. Dephosphorylates and inactivates PAK. May play a role in the inhibition of actin fiber stress breakdown and in morphological changes driven by TNK2/CDC42 (By similarity).
Dephosphorylates PRKAA2
Dephosphorylates PRKAA2
Catalytic activity
- H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Cofactor
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Note: Binds 2 magnesium or manganese ions per subunit.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nucleolus | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | protein-containing complex | |
Molecular Function | metal ion binding | |
Molecular Function | myosin phosphatase activity | |
Molecular Function | protein serine/threonine phosphatase activity | |
Biological Process | cellular response to lipopolysaccharide | |
Biological Process | cellular response to xenobiotic stimulus | |
Biological Process | positive regulation of stress fiber assembly | |
Biological Process | protein dephosphorylation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein phosphatase 1E
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ80TL0
- Secondary accessions
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000286821 | 1-749 | Protein phosphatase 1E | |||
Sequence: MAGCIPEEKTYRRFLELFLGEFRGPCGGGEPEPEPESEPEPEPEAELVAAEAAEASGEEPGEDAATVEATEEGEQDQDPEPEDEAVEEETATEGEEEEEEEAAAPGHSAVPPPPQPQLPPLPPLPRPLSERITREEVEGESLDLCLQQLYKYNCPSFLAAALARATSDEVLQSDLSAHCIPKETDGTEGTVEIETVKLARSVFSKLHEICCSWVKDFPLRRRPQIYYETSIHAIKNMRRKMEDKHVCIPDFNMLFNLEDQEEQAYFAVFDGHGGVDAAIYASVHLHVNLVRQEMFPHDPAEALCRAFRVTDERFVQKAARESLRCGTTGVVTFIRGNMLHVAWVGDSQVMLVRKGQAVELMKPHKPDREDEKQRIEALGGCVVWFGAWRVNGSLSVSRAIGDAEHKPYICGDADSASTVLDGTEDYLILACDGFYDTVNPDEAVKVVSDHLKENNGDSSMVAHKLVASARDAGSSDNITVIVVFLRDMNKAVNVSEESEWTENSFQGGQEDGGDDKETHGECKRPWPQHQCSAPADLGYEGRVDSFTDRTSLSPGPQINVLEDPDYLDLTQIEASKPHSTQFLPPVEMIGPGAPKKDLNELIMEERSVKSSLPERSGAGEPRVSFNLGSTGQQICRMENLSPVSSGLENEQFKSRGKTASRLYHLRHHYSKRQRGFRFNPKFYSFLSAREPSHKIGISLSSLTRSGKRNKMLRSSLPWRENSWEGYSGNVKIRKRNDIPCPDFPWSYKI | ||||||
Modified residue | 532 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 545 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, repeat, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 21-128 | Disordered | ||||
Sequence: EFRGPCGGGEPEPEPESEPEPEPEAELVAAEAAEASGEEPGEDAATVEATEEGEQDQDPEPEDEAVEEETATEGEEEEEEEAAAPGHSAVPPPPQPQLPPLPPLPRPL | ||||||
Repeat | 31-32 | 1 | ||||
Sequence: PE | ||||||
Region | 31-44 | 7 X 2 AA tandem repeats of P-E | ||||
Sequence: PEPEPESEPEPEPE | ||||||
Repeat | 33-34 | 2 | ||||
Sequence: PE | ||||||
Compositional bias | 33-47 | Acidic residues | ||||
Sequence: PEPESEPEPEPEAEL | ||||||
Repeat | 35-36 | 3 | ||||
Sequence: PE | ||||||
Repeat | 37-38 | 4; approximate | ||||
Sequence: SE | ||||||
Repeat | 39-40 | 5 | ||||
Sequence: PE | ||||||
Repeat | 41-42 | 6 | ||||
Sequence: PE | ||||||
Repeat | 43-44 | 7 | ||||
Sequence: PE | ||||||
Compositional bias | 64-102 | Acidic residues | ||||
Sequence: AATVEATEEGEQDQDPEPEDEAVEEETATEGEEEEEEEA | ||||||
Compositional bias | 107-127 | Pro residues | ||||
Sequence: HSAVPPPPQPQLPPLPPLPRP | ||||||
Domain | 224-485 | PPM-type phosphatase | ||||
Sequence: QIYYETSIHAIKNMRRKMEDKHVCIPDFNMLFNLEDQEEQAYFAVFDGHGGVDAAIYASVHLHVNLVRQEMFPHDPAEALCRAFRVTDERFVQKAARESLRCGTTGVVTFIRGNMLHVAWVGDSQVMLVRKGQAVELMKPHKPDREDEKQRIEALGGCVVWFGAWRVNGSLSVSRAIGDAEHKPYICGDADSASTVLDGTEDYLILACDGFYDTVNPDEAVKVVSDHLKENNGDSSMVAHKLVASARDAGSSDNITVIVVFL | ||||||
Region | 495-537 | Disordered | ||||
Sequence: SEESEWTENSFQGGQEDGGDDKETHGECKRPWPQHQCSAPADL | ||||||
Compositional bias | 509-524 | Basic and acidic residues | ||||
Sequence: QEDGGDDKETHGECKR | ||||||
Region | 608-627 | Disordered | ||||
Sequence: VKSSLPERSGAGEPRVSFNL |
Sequence similarities
Belongs to the PP2C family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length749
- Mass (Da)83,419
- Last updated2007-05-15 v2
- ChecksumC59BC6CAC3E268B0
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 33-47 | Acidic residues | ||||
Sequence: PEPESEPEPEPEAEL | ||||||
Compositional bias | 64-102 | Acidic residues | ||||
Sequence: AATVEATEEGEQDQDPEPEDEAVEEETATEGEEEEEEEA | ||||||
Sequence conflict | 107 | in Ref. 1; BAC29490 | ||||
Sequence: H → D | ||||||
Compositional bias | 107-127 | Pro residues | ||||
Sequence: HSAVPPPPQPQLPPLPPLPRP | ||||||
Compositional bias | 509-524 | Basic and acidic residues | ||||
Sequence: QEDGGDDKETHGECKR |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK036583 EMBL· GenBank· DDBJ | BAC29490.1 EMBL· GenBank· DDBJ | mRNA | ||
AK046962 EMBL· GenBank· DDBJ | BAC32927.1 EMBL· GenBank· DDBJ | mRNA | ||
AK053696 EMBL· GenBank· DDBJ | BAC35479.1 EMBL· GenBank· DDBJ | mRNA | ||
AL596130 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AK122434 EMBL· GenBank· DDBJ | BAC65716.1 EMBL· GenBank· DDBJ | mRNA |