Centrosomal protein of 162 kDa; Required to promote assembly of the transition zone in primary cilia. Acts by specifically recognizing and binding the axonemal microtubule. Localizes to the distal ends of centrioles before ciliogenesis and directly binds to axonemal microtubule, thereby promoting and restricting transition zone formation specifically at the cilia base. Required to mediate CEP290 association with microtubules. Belongs to the CEP162 family.

Dual specificity phosphatase 28; Has phosphatase activity with the synthetic substrate 6,8- difluoro-4-methylumbelliferyl phosphate (in vitro). Has almost no detectable activity with phosphotyrosine, even less activity with phosphothreonine and displays complete lack of activity with phosphoserine. The poor activity with phosphotyrosine may be due to steric hindrance by bulky amino acid sidechains that obstruct access to the active site ; Belongs to the protein-tyrosine phosphatase family. Non- receptor class dual specificity subfamily.

Dual specificity phosphatase 28; Has phosphatase activity with the synthetic substrate 6,8- difluoro-4-methylumbelliferyl phosphate (in vitro). Has almost no detectable activity with phosphotyrosine, even less activity with phosphothreonine and displays complete lack of activity with phosphoserine. The poor activity with phosphotyrosine may be due to steric hindrance by bulky amino acid sidechains that obstruct access to the active site ; Belongs to the protein-tyrosine phosphatase family. Non- receptor class dual specificity subfamily.

Centrosomal protein of 162 kDa; Required to promote assembly of the transition zone in primary cilia. Acts by specifically recognizing and binding the axonemal microtubule. Localizes to the distal ends of centrioles before ciliogenesis and directly binds to axonemal microtubule, thereby promoting and restricting transition zone formation specifically at the cilia base. Required to mediate CEP290 association with microtubules. Belongs to the CEP162 family.

Dual specificity phosphatase 28; Has phosphatase activity with the synthetic substrate 6,8- difluoro-4-methylumbelliferyl phosphate (in vitro). Has almost no detectable activity with phosphotyrosine, even less activity with phosphothreonine and displays complete lack of activity with phosphoserine. The poor activity with phosphotyrosine may be due to steric hindrance by bulky amino acid sidechains that obstruct access to the active site ; Belongs to the protein-tyrosine phosphatase family. Non- receptor class dual specificity subfamily.

Josephin-2; Cleaves 'Lys-63'-linked poly-ubiquitin chains, and with lesser efficiency 'Lys-48'-linked poly-ubiquitin chains (in vitro). May act as a deubiquitinating enzyme.

Dual specificity phosphatase 28; Has phosphatase activity with the synthetic substrate 6,8- difluoro-4-methylumbelliferyl phosphate (in vitro). Has almost no detectable activity with phosphotyrosine, even less activity with phosphothreonine and displays complete lack of activity with phosphoserine. The poor activity with phosphotyrosine may be due to steric hindrance by bulky amino acid sidechains that obstruct access to the active site ; Belongs to the protein-tyrosine phosphatase family. Non- receptor class dual specificity subfamily.

Protein LMBR1L; Plays an essential role in lymphocyte development by negatively regulating the canonical Wnt signaling pathway (By similarity). In association with UBAC2 and E3 ubiquitin-protein ligase AMFR, promotes the ubiquitin-mediated degradation of CTNNB1 and Wnt receptors FZD6 and LRP6 (By similarity). LMBR1L stabilizes the beta- catenin destruction complex that is required for regulating CTNNB1 levels (By similarity). Acts as a LCN1 receptor and can mediate its endocytosis. Belongs to the LIMR family.

Dual specificity phosphatase 28; Has phosphatase activity with the synthetic substrate 6,8- difluoro-4-methylumbelliferyl phosphate (in vitro). Has almost no detectable activity with phosphotyrosine, even less activity with phosphothreonine and displays complete lack of activity with phosphoserine. The poor activity with phosphotyrosine may be due to steric hindrance by bulky amino acid sidechains that obstruct access to the active site ; Belongs to the protein-tyrosine phosphatase family. Non- receptor class dual specificity subfamily.

Methyltransferase-like protein 22; Protein N-lysine methyltransferase. In vitro methylates KIN. Belongs to the methyltransferase superfamily. METTL22 family.

Dual specificity phosphatase 28; Has phosphatase activity with the synthetic substrate 6,8- difluoro-4-methylumbelliferyl phosphate (in vitro). Has almost no detectable activity with phosphotyrosine, even less activity with phosphothreonine and displays complete lack of activity with phosphoserine. The poor activity with phosphotyrosine may be due to steric hindrance by bulky amino acid sidechains that obstruct access to the active site ; Belongs to the protein-tyrosine phosphatase family. Non- receptor class dual specificity subfamily.

MYCBP-associated protein; May play a role in spermatogenesis. May be involved in synaptic processes (By similarity).

Dual specificity phosphatase 28; Has phosphatase activity with the synthetic substrate 6,8- difluoro-4-methylumbelliferyl phosphate (in vitro). Has almost no detectable activity with phosphotyrosine, even less activity with phosphothreonine and displays complete lack of activity with phosphoserine. The poor activity with phosphotyrosine may be due to steric hindrance by bulky amino acid sidechains that obstruct access to the active site ; Belongs to the protein-tyrosine phosphatase family. Non- receptor class dual specificity subfamily.

Protein pitchfork; During primary cilia disassembly, involved in cilia disassembly. Required specifically to control cilia retraction as well as the liberation and duplication of the basal body/centrosome. May act by stimulating AURKA activity at the basal body in a cell cycle- dependent manner.

Josephin-2; Cleaves 'Lys-63'-linked poly-ubiquitin chains, and with lesser efficiency 'Lys-48'-linked poly-ubiquitin chains (in vitro). May act as a deubiquitinating enzyme.

Dual specificity phosphatase 28; Has phosphatase activity with the synthetic substrate 6,8- difluoro-4-methylumbelliferyl phosphate (in vitro). Has almost no detectable activity with phosphotyrosine, even less activity with phosphothreonine and displays complete lack of activity with phosphoserine. The poor activity with phosphotyrosine may be due to steric hindrance by bulky amino acid sidechains that obstruct access to the active site ; Belongs to the protein-tyrosine phosphatase family. Non- receptor class dual specificity subfamily.

Protein LMBR1L; Plays an essential role in lymphocyte development by negatively regulating the canonical Wnt signaling pathway (By similarity). In association with UBAC2 and E3 ubiquitin-protein ligase AMFR, promotes the ubiquitin-mediated degradation of CTNNB1 and Wnt receptors FZD6 and LRP6 (By similarity). LMBR1L stabilizes the beta- catenin destruction complex that is required for regulating CTNNB1 levels (By similarity). Acts as a LCN1 receptor and can mediate its endocytosis. Belongs to the LIMR family.

Dual specificity phosphatase 28; Has phosphatase activity with the synthetic substrate 6,8- difluoro-4-methylumbelliferyl phosphate (in vitro). Has almost no detectable activity with phosphotyrosine, even less activity with phosphothreonine and displays complete lack of activity with phosphoserine. The poor activity with phosphotyrosine may be due to steric hindrance by bulky amino acid sidechains that obstruct access to the active site ; Belongs to the protein-tyrosine phosphatase family. Non- receptor class dual specificity subfamily.

Methyltransferase-like protein 22; Protein N-lysine methyltransferase. In vitro methylates KIN. Belongs to the methyltransferase superfamily. METTL22 family.

Dual specificity phosphatase 28; Has phosphatase activity with the synthetic substrate 6,8- difluoro-4-methylumbelliferyl phosphate (in vitro). Has almost no detectable activity with phosphotyrosine, even less activity with phosphothreonine and displays complete lack of activity with phosphoserine. The poor activity with phosphotyrosine may be due to steric hindrance by bulky amino acid sidechains that obstruct access to the active site ; Belongs to the protein-tyrosine phosphatase family. Non- receptor class dual specificity subfamily.

MYCBP-associated protein; May play a role in spermatogenesis. May be involved in synaptic processes (By similarity).

Dual specificity phosphatase 28; Has phosphatase activity with the synthetic substrate 6,8- difluoro-4-methylumbelliferyl phosphate (in vitro). Has almost no detectable activity with phosphotyrosine, even less activity with phosphothreonine and displays complete lack of activity with phosphoserine. The poor activity with phosphotyrosine may be due to steric hindrance by bulky amino acid sidechains that obstruct access to the active site ; Belongs to the protein-tyrosine phosphatase family. Non- receptor class dual specificity subfamily.

Protein pitchfork; During primary cilia disassembly, involved in cilia disassembly. Required specifically to control cilia retraction as well as the liberation and duplication of the basal body/centrosome. May act by stimulating AURKA activity at the basal body in a cell cycle- dependent manner.

Dual specificity phosphatase 28; Has phosphatase activity with the synthetic substrate 6,8- difluoro-4-methylumbelliferyl phosphate (in vitro). Has almost no detectable activity with phosphotyrosine, even less activity with phosphothreonine and displays complete lack of activity with phosphoserine. The poor activity with phosphotyrosine may be due to steric hindrance by bulky amino acid sidechains that obstruct access to the active site ; Belongs to the protein-tyrosine phosphatase family. Non- receptor class dual specificity subfamily.