UniProt ID: A0A0R4IVA4
FUNCTION: Dual-specificity phosphatase. Required for centrosome separation and productive cytokinesis during cell division. Dephosphorylates SIRT2 around early anaphase. May dephosphorylate the APC subunit FZR1/CDH1, thereby promoting APC-FZR1 dependent degradation of mitotic cyclins and subsequent exit from mitosis. {ECO:0000250|UniProtKB:Q9UNH5}.
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044};
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000250|UniProtKB:Q9UNH5};
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl- [protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA- COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; Evidence={ECO:0000250|UniProtKB:Q9UNH5};
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UNH5}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9UNH5}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q9UNH5}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9UNH5}. Cell projection, kinocilium {ECO:0000250|UniProtKB:Q6GQT0}. Note=Centrosomal during interphase, released into the cytoplasm at the onset of mitosis. Subsequently localizes to the mitotic spindle pole and at the central spindle (By similarity). Present along both the transient kinocilia of developing cochlear hair cells and the persistent kinocilia of vestibular hair cells (By similarity). {ECO:0000250|UniProtKB:Q6GQT0, ECO:0000250|UniProtKB:Q9UNH5}.
DOMAIN: Composed of two structurally equivalent A and B domains that adopt a dual specificity protein phosphatase (DSP) fold. {ECO:0000250|UniProtKB:Q9UNH5}.
DISRUPTION PHENOTYPE: Morpholino knockdown of the protein causes a shortening of the hair cell kinocilia in a larvae at 3 dpf. There are no other gross morphological defects in the inner ear. {ECO:0000269|PubMed:27259055}.
SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-receptor class CDC14 subfamily. {ECO:0000305}.
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