PCNT

PCNT binds to calmodulin and is expressed in the centrosome. It is an integral component of the pericentriolar material (PCM). The protein contains a series of coiled-coil domains and a highly conserved PCM targeting motif called the PACT domain near its C-terminus. The protein interacts with the microtubule nucleation component gamma-tubulin and is likely important to normal functioning of the centrosomes, cytoskeleton, and cell-cycle progression. Mutations in this gene cause Seckel syndrome-4 and microcephalic osteodysplastic primordial dwarfism type II.

Pericentrin

Integral component of the filamentous matrix of the centrosome involved in the initial establishment of organized microtubule arrays in both mitosis and meiosis. Plays a role, together with DISC1, in the microtubule network formation. Is an integral component of the pericentriolar material (PCM). May play an important role in preventing premature centrosome splitting during interphase by inhibiting NEK2 kinase activity at the centrosome.

Cilium assemblyManual Assertion Based On ExperimentIDA:MGI
Microtubule cytoskeleton organizationManual Assertion Based On ExperimentIMP:UniProtKB
Mitotic spindle organizationManual Assertion Based On ExperimentIMP:GO_Central
Positive regulation of intracellular protein transportManual Assertion Based On ExperimentIMP:UniProtKB
Signal transductionIEA:InterPro

Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
Centrosomal at all stages of the cell cycle. Remains associated with centrosomes following microtubule depolymerization. Colocalized with DISC1 at the centrosome.

Microcephalic osteodysplastic primordial dwarfism 2 (MOPD2):
Adults with this rare inherited condition have an average height of 100 centimeters and a brain size comparable to that of a 3-month-old baby, but are of near-normal intelligence.

Cleaved during mitotis which leads to removal of CDK5RAP2 from the centrosome and promotes centriole disengagement and subsequent centriole separation (PubMed:22722493, PubMed:25503564).
The C-terminal fragment is rapidly degraded following cleavage (PubMed:22722493).