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
Subcellular localization of ALMS1 supports involvement of centrosome and basal body dysfunction in the pathogenesis of obesity, insulin resistance, and type 2 diabetes.
Centriolar association of ALMS1 and likely centrosomal functions of the ALMS motif-containing proteins C10orf90 and KIAA1731.
Novel asymmetrically localizing components of human centrosomes identified by complementary proteomics methods.
The Alström syndrome protein, ALMS1, interacts with α-actinin and components of the endosome recycling pathway.
Defective adaptive thermogenesis contributes to metabolic syndrome and liver steatosis in obese mice.
HENA, heterogeneous network-based data set for Alzheimer's disease.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
AJUBA facilitates AURKA autophosphorylation
AJUBA binds centrosome-associated AURKA
AURKA phosphorylates PLK1
BORA binds PLK1 and AURKA
Plk1-mediated phosphorylation of Nlp
Recruitment of additional gamma tubulin/ gamma TuRC to the centrosome
Loss of C-Nap-1 from centrosomes
Dissociation of Phospho-Nlp from the centrosome
Recruitment of Plk1 to centrosomes
Association of NuMA with microtubules
Recruitment of CDK11p58 to the centrosomes
Translocation of NuMA to the centrosomes
RAB3IP stimulates nucleotide exchange on RAB8A
C2CD3 binds the mother centriole
C2CD3 and OFD1 recruit 5 distal appendage proteins to the centriole
CP110 and CEP97 dissociate from the centriole
The distal appendage proteins recruit TTBK2
Recruitment of transition zone proteins
MARK4 binds ODF2 in the centriole
CEP164 recruits RAB3IP-carrying Golgi-derived vesicles to the basal body
TPX2 binds AURKA at centrosomes
TPX2 promotes AURKA autophosphorylation
Cep164, a novel centriole appendage protein required for primary cilium formation.
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ALMS1 depletion in human hTERT-RPE1 cells produces morphologically abnormal, stunted cilia without substantially lowering the fraction of ciliated cells. This separates ciliary morphology from the CEP164-dependent ciliogenesis-frequency phenotype in the same screen.
"the depletion of Cep57 or ALMS1 led to the formation of morphologically abnormal, stunted cilia without considerably reducing the efficiency of ciliogenesis"
Drosophila Alms1 proteins regulate centriolar cartwheel assembly by enabling Plk4-Ana2 amplification loop.
Author Correction: Drosophila Alms1 proteins regulate centriolar cartwheel assembly by enabling Plk4-Ana2 amplification loop.