| Category | Specific Function/Feature | Evidence Type | Key Findings |
|---|---|---|---|
| Protein Structure/Domains | G-patch domain | Domain/family review; patient mutation analysis | GPATCH11 is a human G-patch protein with a conserved glycine-rich G-patch motif, a hallmark domain that in the broader family typically regulates DEAH/RHA RNA helicases. In GPATCH11, a recurrent pathogenic splice variant removes 14 aa from the G-patch region, supporting functional importance of this domain (pqac-00000008, pqac-00000009, pqac-00000006). |
| Protein Structure/Domains | Coiled-coil/CCDC region | Sequence/domain annotation; CRISPR deletion functional study | GPATCH11 is also known as CCDC75, reflecting a coiled-coil domain. Deletion of the CCDC-encoding region in hTERT-RPE1 cells did not alter nucleo-centrosomal localization, suggesting the coiled-coil region is not solely responsible for targeting to those compartments (pqac-00000001, pqac-00000006). |
| Protein Structure/Domains | DUF4187 and overall domain architecture | Domain annotation; human G-patch family review | The UniProt-linked protein architecture includes G-patch, coiled-coil, and DUF4187-related features; reviews emphasize that human G-patch proteins commonly combine the G-patch with additional RNA-binding or interaction modules, consistent with multifunctional RNA-metabolism roles (pqac-00000001, pqac-00000004, pqac-00000009). |
| Molecular Function | RNA metabolism regulator | Human disease paper; family review | Zanetti et al. describe GPATCH11 as a lesser-known regulator of RNA metabolism. Their genetic, transcriptomic, and proteomic data support roles in RNA processing, splicing, and transcriptional regulation rather than enzymatic catalysis (pqac-00000001, pqac-00000015, pqac-00000017). |
| Molecular Function | Putative RNA helicase cofactor via G-patch domain | Mechanistic reviews; inference from family biology | Reviews of G-patch proteins state that the core function of the G-patch motif is to bind and stimulate DEAH/RHA-box RNA helicases, enhancing ATPase/helicase activity and RNA remodeling. Although GPATCH11’s direct helicase partner remains unconfirmed, its function is plausibly analogous by family logic (pqac-00000008, pqac-00000009). |
| Molecular Function | Pre-mRNA splicing regulator | Mouse retina transcriptomics; proteomics; discussion synthesis | Mutant Gpatch11 mouse retina showed 299 altered splicing events in 178 genes, and GPATCH11-associated proteins included spliceosomal/RNA-metabolism factors, strongly supporting a role in splicing regulation (pqac-00000012, pqac-00000013, pqac-00000016). |
| Molecular Function | Transcriptional regulation | Proteomics and protein interaction analysis | GPATCH11-associated proteins included factors involved in transcription regulation, and the authors argue GPATCH11 likely influences both splicing and transcription, analogous to other GPATCH family members with multifunctional nuclear roles (pqac-00000013, pqac-00000016, pqac-00000017). |
| Subcellular Localization | Nucleoplasmic localization | Immunocytochemistry/confocal microscopy in human fibroblasts | GPATCH11 shows diffuse nucleoplasmic distribution in control fibroblasts and is proximal to SC-35-positive speckles and H3K9me3-marked heterochromatin, consistent with nuclear RNA-processing machinery (pqac-00000002, pqac-00000005, pqac-00000016). |
| Subcellular Localization | Centrosomal localization | Confocal/STED microscopy | GPATCH11 localizes to the centrosome linker region and basal-body-associated structures, including association with Rootletin/CROCC-marked linker fibers, supporting a nucleo-centrosomal distribution (pqac-00000002, pqac-00000005, pqac-00000016). |
| Subcellular Localization | Not centromeric/kinetochore despite alias CENP-Y | Mitotic-stage imaging in human cells | Despite the historical alias “CENP-Y,” Zanetti et al. found GPATCH11 exclusively at centrosomes during mitosis, with no detectable localization at centromeres or kinetochores in their assays (pqac-00000002, pqac-00000006). |
| Subcellular Localization | Retinal and brain nuclear expression | Mouse immunohistochemistry | In mouse tissue, GPATCH11 protein was detected in all retinal nuclear layers and strongly in the hippocampus and broader brain, supporting roles in retinal and neural physiology (pqac-00000011). |
| Biological Processes/Pathways | Alternative splicing and spliceosome-linked regulation | Transcriptomics; family reviews | GPATCH11 perturbation alters splicing broadly, while G-patch protein reviews place such proteins centrally in spliceosome remodeling through RNA helicase regulation. Together these support GPATCH11 as a spliceosome-associated regulatory factor (pqac-00000012, pqac-00000008, pqac-00000009). |
| Biological Processes/Pathways | Gene expression control in photoreceptors | Differential expression analysis in mutant mouse retina | Mutant retina showed 160 differentially expressed genes enriched for visual perception, photoreceptor development, response to light stimulus, and non-motile cilium categories, indicating GPATCH11 is important for retinal gene-expression homeostasis (pqac-00000012). |
| Biological Processes/Pathways | Ciliary/centrosomal biology | Localization studies; pathway enrichment | Centrosomal/basal body localization plus retinal transcriptomic enrichment for cilium-associated genes suggests participation in cilia-related biology, although direct ciliogenesis defects were not seen in fibroblasts (pqac-00000001, pqac-00000005, pqac-00000017). |
| Biological Processes/Pathways | Synaptic plasticity and neuronal function | Retina proteomics and interaction proteomics | Proteomic analyses suggested additional roles in synaptic plasticity, synaptogenesis, neurotransmission, and neuronal maintenance, potentially explaining memory phenotypes in the mouse model (pqac-00000001, pqac-00000013, pqac-00000017). |
| Biological Processes/Pathways | Stress-response and neuroprotection-linked pathways | Interaction proteomics; discussion | GPATCH11-associated proteins included stress-response and nuclear homeostasis factors, and the paper discusses possible links to neuroprotective pathways relevant to retinal degeneration (pqac-00000013, pqac-00000016, pqac-00000017). |
| Protein Partners | RNA/splicing factors | Immunoprecipitation-mass spectrometry | GPATCH11-associated proteins included DDX23, PRPF31, PPIL1 and other RNA-metabolism factors; about 23% of interactors were involved in RNA metabolism, reinforcing a splicing/transcription role (pqac-00000013, pqac-00000016). |
| Protein Partners | Centrosomal linker factor Rootletin/CROCC | Microscopy colocalization | STED/confocal imaging placed GPATCH11 with Rootletin in the centrosome linker region, suggesting functional coupling to centrosomal organization (pqac-00000002, pqac-00000016). |
| Protein Partners | Transcription/stress-associated proteins | Immunoprecipitation-mass spectrometry | GPATCH11 pull-downs recovered proteins such as IRF2BPL, ZFP287, FGF2, SAP18, and NMNAT1, linking GPATCH11 to transcriptional control, nuclear repression, and stress-response/neuroprotection networks (pqac-00000013, pqac-00000016). |
| Disease Association | Autosomal recessive syndromic retinal dystrophy with neurological impairment | Human genetics; clinical cohort | Biallelic GPATCH11 variants were identified in 12 affected individuals from 6 families, causing early-onset retinal dystrophy with intellectual/neurological impairment and craniofacial/skeletal features (pqac-00000001, pqac-00000000, pqac-00000010). |
| Disease Association | Mutation classes and molecular consequences | RNA/protein analysis in patient cells | Reported pathogenic alleles included splice-site and nonsense variants; c.328+1G>T caused in-frame exon 4 skipping and a shorter protein lacking part of the G-patch domain, while other variants caused intron retention or likely nonsense-mediated decay (pqac-00000002, pqac-00000006). |
| Disease Association | Mouse model recapitulates core phenotype | CRISPR mouse model; ERG/behavioral assays | Gpatch11Δ5/Δ5 mice were viable but developed progressive retinal degeneration, memory deficits, and male infertility, supporting a causal role for GPATCH11 dysfunction and highlighting tissue-specific physiological importance (pqac-00000007, pqac-00000011). |


*Table: This table summarizes current evidence on GPATCH11 structure, function, localization, pathways, partners, and disease relevance. It is useful as a compact evidence map grounded in the key GPATCH11 disease study and authoritative G-patch protein reviews.*