Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Electronic Gene Ontology annotations created by ARBA machine learning models
Functional interactions between the ciliopathy-associated Meckel syndrome 1 (MKS1) protein and two novel MKS1-related (MKSR) proteins.
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Human B9 orthologs localize to basal bodies and cilia.
"This localization is evolutionarily conserved, because the human orthologues also localize to basal bodies, as well as cilia."
Nephrocystins and MKS proteins interact with IFT particle and facilitate transport of selected ciliary cargos.
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B9d2 binds IFT components and supports Inversin ciliary localization.
"Our studies demonstrate that IFT particle components, and a Meckel-Gruber syndrome 1 (MKS1)-related, B9 domain protein, B9d2, bind each other and contribute to the ciliary localization of Inversin (Nephrocystin 2)."
A ciliopathy complex at the transition zone protects the cilia as a privileged membrane domain.
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A nine-protein TZ complex restricts ciliary membrane diffusion.
"Strikingly, disruption of the complex increases the rate of diffusion into the ciliary membrane and the amount of plasma-membrane protein in the cilia."
A Dynamic Protein Interaction Landscape of the Human Centrosome-Cilium Interface.
An organelle-specific protein landscape identifies novel diseases and molecular mechanisms.
A reference map of the human binary protein interactome.
Formation of the B9-domain protein complex MKS1-B9D2-B9D1 is essential as a diffusion barrier for ciliary membrane proteins.
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MKS1-B9D2-B9D1 complex; interdependent TZ localization.
"We here demonstrate the interaction mode of these B9D proteins to be MKS1-B9D2-B9D1 and demonstrate their interdependent localization to the TZ."
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B9D2-KO cells lose ciliary GPR161; mild ciliogenesis defect.
"In striking contrast, GPR161 was not detectable on the ciliary membrane, even under basal conditions in MKS1-KO or B9D2-KO cells (Figure 3, B–E; also see Figure 3U)."
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Multimodal cell maps as a foundation for structural and functional genomics.
MAD2 converted to an inhibitory state via interaction with Mad1
MAD2 associates with the Mad1 kinetochore complex
Release of activated MAD2 from kinetochores
Phosphorylation of cohesin by PLK1 at centromeres
PP2A-B56 dephosphorylates centromeric cohesin
ESPL1 (Separase) cleaves centromeric cohesin
Separation of sister chromatids
CDK1 phosphorylates CDCA5 (Sororin) at centromeres
Kinetochore capture of astral microtubules
RAB3IP stimulates nucleotide exchange on RAB8A
Recruitment of transition zone proteins
CEP164 recruits RAB3IP-carrying Golgi-derived vesicles to the basal body
CDC42:GTP recruits DIAPH2-2 to kinetochores
AURKB phosphorylates DIAPH2-2 at kinetochores
Kinetochore capture of astral microtubules is positively regulated by CDC42:GTP:p-S196-DIAPH2-2
EML4 recruits NUDC to mitotic spindle
Disruption of a ciliary B9 protein complex causes Meckel syndrome.
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B9D2 S101R causes MKS and breaks MKS1 binding.
"We identified a homozygous c.301A>C (p.Ser101Arg) B9D2 mutation that segregates with MKS, affects an evolutionarily conserved residue, and is absent from controls."
Ciliopathy-related B9 protein complex regulates ciliary axonemal microtubule posttranslational modifications and initiation of ciliogenesis.
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The B9 complex anchors TMEM67 at the TZ membrane.
"We also found that the B9 complex interacts with and anchors TMEM67 to the TZ membrane, thereby stabilizing the MKS module and maintaining the integrity of the TZ diffusion barrier."
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B9 proteins act at the mother centriole to initiate ciliogenesis.
"During ciliogenesis, B9 proteins localize to the mother centriole, facilitate the docking of membrane vesicles to the distal appendages, and promote the removal of CP110 from the mother centriole, thus initiating cilia assembly."
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JBTS B9D2 variants impair axonemal MT modifications.
"We found that Joubert syndrome-associated B9D2 variants primarily affected axonemal microtubule modifications without disrupting ciliogenesis, whereas the Meckel syndrome-associated B9D2 variant disrupted both ciliogenesis and axonemal microtubule modifications."
UniProt entry Q9BPU9 (B9D2_HUMAN)
Affinage mechanistic annotation for B9D2 (human)