Required for renal function. Homooligomer (By similarity). Central component of a complex containing at least ANKS6, INVS, NEK8 and NPHP3 (PubMed:23793029). ANKS6 may organize complex assembly by linking INVS and NPHP3 to NEK8 and INVS may target the complex to the proximal ciliary axoneme (PubMed:23793029). Interacts (via SAM domain) with BICC1 (via KH domains) in an RNA-dependent manner (By similarity). Interacts (via SAM domain) with ANKS3 (via SAM domain) (PubMed:24998259). Localizes to the proximal region of the primary cilium in the presence of INVS. The ankyrin repeats are necessary and sufficient for NEK8-binding. The SAM domain mediates interaction with the SAM domain of ANKS3. Hydroxylated at Asn-138, most probably by HIF1AN. This hydroxylation results in decreased NEK8-binding. The disease is caused by variants affecting the gene represented in this entry. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus.