P30304 · MPIP1_HUMAN
- ProteinM-phase inducer phosphatase 1
- GeneCDC25A
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids524 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Directly dephosphorylates CDK1 and stimulates its kinase activity (PubMed:20360007).
Also dephosphorylates CDK2 in complex with cyclin-E, in vitro (PubMed:20360007).
Catalytic activity
- H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphateThis reaction proceeds in the forward direction.
Activity regulation
Stimulated by PIM1-mediated phosphorylation (PubMed:16356754).
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 431 | |||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | phosphoprotein phosphatase activity | |
Molecular Function | protein kinase binding | |
Molecular Function | protein tyrosine phosphatase activity | |
Molecular Function | protein-folding chaperone binding | |
Biological Process | cell division | |
Biological Process | cell population proliferation | |
Biological Process | cellular response to UV | |
Biological Process | G1/S transition of mitotic cell cycle | |
Biological Process | G2/M transition of mitotic cell cycle | |
Biological Process | positive regulation of DNA replication | |
Biological Process | positive regulation of G2/M transition of mitotic cell cycle | |
Biological Process | positive regulation of G2/MI transition of meiotic cell cycle | |
Biological Process | regulation of cyclin-dependent protein serine/threonine kinase activity | |
Biological Process | response to radiation |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameM-phase inducer phosphatase 1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP30304
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 76 | Abolishes ubiquitination and impairs CHEK1-dependent degradation following checkpoint activation. | ||||
Sequence: S → A | ||||||
Mutagenesis | 79 | Abrogates interactions with BTRC and FBXW11 and prevents ubiquitination. | ||||
Sequence: S → A | ||||||
Mutagenesis | 81 | Abrogates interactions with BTRC and FBXW11 and prevents ubiquitination. | ||||
Sequence: D → A | ||||||
Mutagenesis | 82 | Abrogates interactions with BTRC and FBXW11 and prevents ubiquitination. | ||||
Sequence: S → A | ||||||
Natural variant | VAR_020932 | 88 | in dbSNP:rs3731499 | |||
Sequence: S → F | ||||||
Mutagenesis | 124 | Abrogates phosphorylation by CHEK2 and infrared-induced degradation. Increases basal stability and impairs CHEK1-dependent degradation following checkpoint activation; when associated with A-178; A-279 and A-293. | ||||
Sequence: S → A | ||||||
Mutagenesis | 141-143 | Prevents ubiquitination and subsequent degradation by the APC/C ubiquitin ligase complex. | ||||
Sequence: KEN → AAA | ||||||
Mutagenesis | 178 | Increases basal stability and impairs CHEK1-dependent degradation following checkpoint activation; when associated with A-124; A-279 and A-293. Abrogates 14-3-3 protein binding. | ||||
Sequence: S → A | ||||||
Natural variant | VAR_023532 | 182 | in dbSNP:rs6771386 | |||
Sequence: R → G | ||||||
Natural variant | VAR_023533 | 182 | in dbSNP:rs6771386 | |||
Sequence: R → W | ||||||
Mutagenesis | 279 | Increases basal stability and impairs CHEK1-dependent degradation following checkpoint activation; when associated with A-124; A-178 and A-293. | ||||
Sequence: S → A | ||||||
Mutagenesis | 293 | Increases basal stability and impairs CHEK1-dependent degradation following checkpoint activation; when associated with A-124; A-178 and A-279. | ||||
Sequence: S → A | ||||||
Mutagenesis | 431 | Abolishes phosphatase activity. | ||||
Sequence: C → S | ||||||
Mutagenesis | 507 | Abrogates 14-3-3 protein binding; increases binding to cyclin B1. | ||||
Sequence: T → A | ||||||
Mutagenesis | 513 | Increased stability following IR treatment. | ||||
Sequence: S → A | ||||||
Mutagenesis | 513 | Mimicks phosphorylation state, leading to promote degradation following IR treatment. | ||||
Sequence: S → D | ||||||
Mutagenesis | 514 | Abrogates binding to CCNB1; when associated with L-520. | ||||
Sequence: K → L | ||||||
Mutagenesis | 519 | Increased stability following IR treatment. | ||||
Sequence: S → A | ||||||
Mutagenesis | 519 | Mimicks phosphorylation state, leading to promote degradation following IR treatment. | ||||
Sequence: S → D | ||||||
Mutagenesis | 520 | Abrogates binding to CCNB1; when associated with L-514. | ||||
Sequence: R → L |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 448 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000198641 | 1-524 | UniProt | M-phase inducer phosphatase 1 | |||
Sequence: MELGPEPPHRRRLLFACSPPPASQPVVKALFGASAAGGLSPVTNLTVTMDQLQGLGSDYEQPLEVKNNSNLQRMGSSESTDSGFCLDSPGPLDSKENLENPMRRIHSLPQKLLGCSPALKRSHSDSLDHDIFQLIDPDENKENEAFEFKKPVRPVSRGCLHSHGLQEGKDLFTQRQNSAPARMLSSNERDSSEPGNFIPLFTPQSPVTATLSDEDDGFVDLLDGENLKNEEETPSCMASLWTAPLVMRTTNLDNRCKLFDSPSLCSSSTRSVLKRPERSQEESPPGSTKRRKSMSGASPKESTNPEKAHETLHQSLSLASSPKGTIENILDNDPRDLIGDFSKGYLFHTVAGKHQDLKYISPEIMASVLNGKFANLIKEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKKPIVPTDGKRVIVVFHCEFSSERGPRMCRYVRERDRLGNEYPKLHYPELYVLKGGYKEFFMKCQSYCEPPSYRPMHHEDFKEDLKKFRTKSRTWAGEKSKREMYSRLKKL | |||||||
Modified residue (large scale data) | 18 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 76 | UniProt | Phosphoserine; by CHEK1 | ||||
Sequence: S | |||||||
Modified residue | 79 | UniProt | Phosphoserine; by NEK11 | ||||
Sequence: S | |||||||
Modified residue | 82 | UniProt | Phosphoserine; by NEK11 | ||||
Sequence: S | |||||||
Modified residue | 88 | UniProt | Phosphoserine; by NEK11 | ||||
Sequence: S | |||||||
Modified residue | 107 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 116 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 124 | UniProt | Phosphoserine; by CHEK1 and CHEK2 | ||||
Sequence: S | |||||||
Modified residue | 178 | UniProt | Phosphoserine; by CHEK1 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 178 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 261 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 267 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 279 | UniProt | Phosphoserine; by CHEK1 and CHEK2 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 283 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 293 | UniProt | Phosphoserine; by CHEK1 and CHEK2 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 320 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 321 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 321 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 507 | UniProt | Phosphothreonine; by CHEK1 | ||||
Sequence: T | |||||||
Modified residue | 513 | UniProt | Phosphoserine; by PLK3 | ||||
Sequence: S | |||||||
Modified residue | 519 | UniProt | Phosphoserine; by PLK3 | ||||
Sequence: S |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P30304 | NAA11 Q9BSU3 | 3 | EBI-747671, EBI-2585120 | |
BINARY | P30304 | RAF1 P04049 | 4 | EBI-747671, EBI-365996 | |
BINARY | P30304 | YWHAB P31946 | 10 | EBI-747671, EBI-359815 | |
BINARY | P30304 | YWHAE P62258 | 3 | EBI-747671, EBI-356498 | |
BINARY | P30304 | YWHAQ P27348 | 3 | EBI-747671, EBI-359854 | |
BINARY | P30304 | YWHAZ P63104 | 3 | EBI-747671, EBI-347088 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for motif, region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 74-84 | Phosphodegron | ||||
Sequence: MGSSESTDSGF | ||||||
Motif | 141-143 | KEN box | ||||
Sequence: KEN | ||||||
Region | 264-317 | Disordered | ||||
Sequence: LCSSSTRSVLKRPERSQEESPPGSTKRRKSMSGASPKESTNPEKAHETLHQSLS | ||||||
Compositional bias | 274-288 | Basic and acidic residues | ||||
Sequence: KRPERSQEESPPGST | ||||||
Domain | 376-482 | Rhodanese | ||||
Sequence: LIKEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKKPIVPTDGKRVIVVFHCEFSSERGPRMCRYVRERDRLGNEYPKLHYPELYVLKGGYKEFFMKCQSYCE |
Domain
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
P30304-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- SynonymsCDC25A1
- Length524
- Mass (Da)59,087
- Last updated2004-07-19 v2
- ChecksumB2F6B792D4E6122B
P30304-2
- Name2
- SynonymsCDC25A2
- Differences from canonical
- 144-183: Missing
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Features
Showing features for sequence conflict, alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 6-10 | in Ref. 1; AAA58415 | ||||
Sequence: EPPHR → SPAP | ||||||
Alternative sequence | VSP_000860 | 144-183 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 180-181 | in Ref. 1; AAA58415 | ||||
Sequence: PA → QL | ||||||
Compositional bias | 274-288 | Basic and acidic residues | ||||
Sequence: KRPERSQEESPPGST |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M81933 EMBL· GenBank· DDBJ | AAA58415.1 EMBL· GenBank· DDBJ | mRNA | ||
AY137580 EMBL· GenBank· DDBJ | AAN11305.1 EMBL· GenBank· DDBJ | mRNA | ||
AF527417 EMBL· GenBank· DDBJ | AAM77917.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC007401 EMBL· GenBank· DDBJ | AAH07401.1 EMBL· GenBank· DDBJ | mRNA | ||
BC018642 EMBL· GenBank· DDBJ | AAH18642.1 EMBL· GenBank· DDBJ | mRNA | ||
AF277722 EMBL· GenBank· DDBJ | AAG41884.1 EMBL· GenBank· DDBJ | mRNA |