A7MBD1 (MPIP1_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified April 3, 2013. Version 45. History...
Names and origin
|Protein names||Recommended name:|
M-phase inducer phosphatase 1
Dual specificity phosphatase Cdc25A
|Organism||Bos taurus (Bovine) [Reference proteome]|
|Taxonomic identifier||9913 [NCBI]|
|Taxonomic lineage||Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos|
|Sequence length||525 AA.|
|Protein existence||Evidence at transcript level|
General annotation (Comments)
Tyrosine protein phosphatase which functions as a dosage-dependent inducer of mitotic progression. Directly dephosphorylates CDK1 and stimulates its kinase activity. Also dephosphorylates CDK2 in complex with cyclin E, in vitro By similarity.
Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
Stimulated by B-type cyclins By similarity. Stimulated by PIM1-mediated phosphorylation By similarity.
Interacts with CCNB1/cyclin B1. Interacts with YWHAE/14-3-3 epsilon when phosphorylated. Interacts with CUL1 specifically when CUL1 is neddylated and active. Interacts with BTRC/BTRCP1 and FBXW11/BTRCP2. Interactions with CUL1, BTRC and FBXW11 are enhanced upon DNA damage By similarity. Interacts with PIM1 By similarity.
The phosphodegron motif mediates interaction with specific F-box proteins when phosphorylated. Putative phosphorylation sites at Ser-78 and Ser-81 appear to be essential for this interaction By similarity.
Phosphorylated by CHEK1 on Ser-75, Ser-123, Ser-177, Ser-279, Ser-293 and Thr-508 during checkpoint mediated cell cycle arrest. Also phosphorylated by CHEK2 on Ser-123, Ser-279, and Ser-293 during checkpoint mediated cell cycle arrest. Phosphorylation on Ser-177 and Thr-508 creates binding sites for YWHAE/14-3-3 epsilon which inhibits CDC25A. Phosphorylation on Ser-75, Ser-123, Ser-177, Ser-279 and Ser-293 may also promote ubiquitin-dependent proteolysis of CDC25A by the SCF complex. Phosphorylation of CDC25A at Ser-75 by CHEK1 primes it for subsequent phosphorylation at Ser-78, Ser-81 and Ser-87 by NEK11. Phosphorylation by NEK11 is required for BTRC-mediated polyubiquitination and degradation. Phosphorylation by PIM1 leads to an increase in phosphatase activity. Phosphorylated by PLK3 following DNA damage, leading to promote its ubiquitination and degradation By similarity.
Ubiquitinated by the anaphase promoting complex/cyclosome (APC/C) ubiquitin ligase complex that contains FZR1/CDH1 during G1 phase leading to its degradation by the proteasome. Ubiquitinated by a SCF complex containing BTRC and FBXW11 during S phase leading to its degradation by the proteasome. Deubiquitination by USP17L2/DUB3 leads to its stabilization By similarity.
Belongs to the MPI phosphatase family.
Contains 1 rhodanese domain.
|Biological process||Cell cycle|
|Technical term||Complete proteome|
|Gene Ontology (GO)|
Inferred from electronic annotation. Source: UniProtKB-KWcellular response to UV
Inferred from electronic annotation. Source: Comparamitosis
Inferred from electronic annotation. Source: UniProtKB-KWpeptidyl-tyrosine dephosphorylation
Inferred from electronic annotation. Source: GOCresponse to radiation
Inferred from sequence or structural similarity. Source: UniProtKB
Inferred from electronic annotation. Source: Comparanucleus
Inferred from electronic annotation. Source: Compara
|Molecular_function||protein tyrosine phosphatase activity|
Inferred from electronic annotation. Source: EC
|Complete GO annotation...|
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Chain||1 – 525||525||M-phase inducer phosphatase 1||PRO_0000365161|
|Domain||377 – 483||107||Rhodanese|
|Motif||73 – 83||11||Phosphodegron|
|Motif||140 – 142||3||KEN box|
|Active site||432||1||By similarity|
Amino acid modifications
|Modified residue||75||1||Phosphoserine; by CHEK1 By similarity|
|Modified residue||78||1||Phosphoserine; by NEK11 By similarity|
|Modified residue||81||1||Phosphoserine; by NEK11 By similarity|
|Modified residue||87||1||Phosphoserine; by NEK11 By similarity|
|Modified residue||123||1||Phosphoserine; by CHEK1 and CHEK2 By similarity|
|Modified residue||177||1||Phosphoserine; by CHEK1 By similarity|
|Modified residue||279||1||Phosphoserine; by CHEK1 and CHEK2 By similarity|
|Modified residue||293||1||Phosphoserine; by CHEK1 and CHEK2 By similarity|
|Modified residue||508||1||Phosphothreonine; by CHEK1 By similarity|
|Modified residue||514||1||Phosphoserine; by PLK3 By similarity|
|Modified residue||520||1||Phosphoserine; by PLK3 By similarity|
|BC151493 mRNA. Translation: AAI51494.1.|
|RefSeq||NP_001094570.1. NM_001101100.2. |
3D structure databases
|SMR||A7MBD1. Positions 338-497. |
Protein-protein interaction databases
Protocols and materials databases
Genome annotation databases
|Ensembl||ENSBTAT00000012611; ENSBTAP00000012611; ENSBTAG00000009586. |
Family and domain databases
|Gene3D||126.96.36.199. 1 hit. |
|InterPro||IPR000751. MPI_Phosphatase. |
|PANTHER||PTHR10828. PTHR10828. 1 hit. |
|Pfam||PF06617. M-inducer_phosp. 1 hit. |
PF00581. Rhodanese. 1 hit.
|PRINTS||PR00716. MPIPHPHTASE. |
|SMART||SM00450. RHOD. 1 hit. |
|SUPFAM||SSF52821. Rhodanese-like. 1 hit. |
|PROSITE||PS50206. RHODANESE_3. 1 hit. |
|Accession||Primary (citable) accession number: A7MBD1|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Chordata Protein Annotation Program|
Index of protein domains and families