CIBAR1
entrez
137392
canonical
uniprot
A1XBS5
canonical
ensembl
ENSG00000188343
resolver
ensp
ENSP00000401774
resolver
ensp
ENSP00000429367
resolver
ensp
ENSP00000768847
resolver
genesymbol
CIBAR1
resolver
genesymbol_syn
FAM92A
resolver
genesymbol_syn
FAM92A1
resolver
hgnc
HGNC:30452
resolver
uniprot
A1XBS4
resolver
uniprot
Q32ND3
resolver
uniprot
Q6AHW7
resolver
uniprot
Q8N8R1
resolver
uniprot
Q96L09
resolver
uniprot_entry
CBAR1_HUMAN
resolver
uniprot_sec
A1XBS4
resolver
uniprot_sec
Q32ND3
resolver
uniprot_sec
Q6AHW7
resolver
uniprot_sec
Q8N8R1
resolver
uniprot_sec
Q96L09
resolver
amino_acid_sequence
MMRRTLENRNAQTKQLQTAVSNVEKHFGELCQIFAAYVRKTARLRDKADLLVNEINAYAATETPHLKLGLMNFADEFAKLQDYRQAEVERLEAKVVEPLKTYGTIVKMKRDDLKATLTARNREAKQLTQLERTRQRNPSDRHVISQAETELQRAAMDASRTSRHLEETINNFERQKMKDIKTIFSEFITIEMLFHGKALEVYTAAYQNIQNIDEDEDLEVFRNSLYAPDYSSRLDIVRANSKSPLQRSLSAKCVSGTGQVSTCRLRKDQQAEDDEDDELDVTEEENFLK
uniprot
proteins
disease_involvement
DISEASE: Polydactyly, postaxial, A9 (PAPA9) [MIM:618219]: A form of postaxial polydactyly, a condition characterized by the occurrence of supernumerary digits in the upper and/or lower extremities. In postaxial polydactyly type A, the extra digit is well-formed and articulates with the fifth or a sixth metacarpal/metatarsal. PAPA9 is an autosomal recessive condition characterized by one or more posterior or postaxial digits. {ECO:0000269|PubMed:30395363}. Note=The disease may be caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Plays a critical role in regulating mitochondrial ultrastructure and function by maintaining the integrity of mitochondrial morphology, particularly the organization of cristae (PubMed:30404948). Preferentially binds to negatively charged phospholipids like cardiolipin and phosphatidylinositol 4,5-bisphosphate enhancing its interaction with mitochondrial membranes (PubMed:30404948). Induces membrane curvature and tubulation, which are critical for maintaining mitochondrial ultrastructure and the organization of cristae (PubMed:30404948). Plays a crucial role in ciliogenesis (PubMed:27528616, PubMed:30395363). May play a role in limb development through its role in ciliogenesis (PubMed:30395363). Plays a key role in the correct positioning of the annulus, a septin-based ring structure in the sperm flagellum, serving both as a physical barrier and a membrane diffusion barrier that separates the midpiece (MP) from the principal piece (PP) (By similarity). This positioning is essential for proper sperm motility and function (By similarity). Interacts with CBY3 to form a complex which localizes to the curved membrane region of the flagellar pocket (By similarity). By doing so, may provide stability and rigidity to the periannular membrane to prevent membrane deformation (By similarity). This function is crucial for halting annulus migration at the proximal end of the fibrous sheath-containing PP (By similarity). {ECO:0000250|UniProtKB:Q8BP22, ECO:0000269|PubMed:27528616, ECO:0000269|PubMed:30395363, ECO:0000269|PubMed:30404948}.
uniprot
proteins
mass_dalton
33431
uniprot
proteins
mutagenesis
MUTAGEN 107; /note="K->A: Reduced membrane-binding and significant reduction in membrane remodeling activity; when associated with A-109 and A-110."; /evidence="ECO:0000269|PubMed:30404948"; MUTAGEN 107; /note="K->E: Abolishes ability to induce membrane remodeling in the presence of CBY1; when associated with E-110; E-114; E-132; E-134 and E-136."; /evidence="ECO:0000269|PubMed:27528616"; MUTAGEN 109; /note="K->A: Reduced membrane-binding and significant reduction in membrane remodeling activity; when associated with A-107 and A-110."; /evidence="ECO:0000269|PubMed:30404948"; MUTAGEN 110; /note="R->A: Reduced membrane-binding and significant reduction in membrane remodeling activity; when associated with A-107 and A-109."; /evidence="ECO:0000269|PubMed:30404948"; MUTAGEN 110; /note="R->E: Abolishes ability to induce membrane remodeling in the presence of CBY1; when associated with E-107;E-114; E-132; E-134 and E-136."; /evidence="ECO:0000269|PubMed:27528616"; MUTAGEN 114; /note="K->E: Abolishes ability to induce membrane remodeling in the presence of CBY1; when associated with E-107; E-110; E-132; E-134 and E-136."; /evidence="ECO:0000269|PubMed:27528616"; MUTAGEN 132; /note="R->A: Reduced membrane-binding and significant reduction in membrane remodeling activity; when associated with A-134 and A-136."; /evidence="ECO:0000269|PubMed:30404948"; MUTAGEN 132; /note="R->E: Abolishes ability to induce membrane remodeling in the presence of CBY1; when associated with E-107; E-110; E-114; E-134 and E-136."; /evidence="ECO:0000269|PubMed:27528616"; MUTAGEN 134; /note="R->A: Reduced membrane-binding and significant reduction in membrane remodeling activity; when associated with A-132 and A-136."; /evidence="ECO:0000269|PubMed:30404948"; MUTAGEN 134; /note="R->E: Abolishes ability to induce membrane remodeling in the presence of CBY1; when associated with E-107; E-110; E-114; E-132 and E-136."; /evidence="ECO:0000269|PubMed:27528616"; MUTAGEN 136; /note="R->A: Reduced membrane-binding and significant reduction in membrane remodeling activity; when associated with A-132 and A-134."; /evidence="ECO:0000269|PubMed:30404948"; MUTAGEN 136; /note="R->E: Abolishes ability to induce membrane remodeling in the presence of CBY1; when associated with E-107; E-110; E-114; E-132 and E-134."; /evidence="ECO:0000269|PubMed:27528616"; MUTAGEN 264; /note="R->A: Reduced membrane-binding and significant reduction in membrane remodeling activity; when associated with A-266 and A-267."; /evidence="ECO:0000269|PubMed:30404948"; MUTAGEN 266; /note="R->A: Reduced membrane-binding and significant reduction in membrane remodeling activity; when associated with A-264 and A-267."; /evidence="ECO:0000269|PubMed:30404948"; MUTAGEN 267; /note="K->A: Reduced membrane-binding and significant reduction in membrane remodeling activity; when associated with A-264 and A-266."; /evidence="ECO:0000269|PubMed:30404948
uniprot
proteins
protein_family
CIBAR family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16421571
uniprot
proteins
pubmed
17646714
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
27528616
uniprot
proteins
pubmed
30395363
uniprot
proteins
pubmed
30404948
uniprot
proteins
pubmed
38197861
uniprot
proteins
sequence_length
289
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27528616, ECO:0000269|PubMed:30404948}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:27528616}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:27528616, ECO:0000269|PubMed:30395363}. Cell projection, cilium {ECO:0000250|UniProtKB:Q8BP22}. Nucleus {ECO:0000269|PubMed:30404948}. Mitochondrion inner membrane {ECO:0000269|PubMed:30404948}; Peripheral membrane protein {ECO:0000269|PubMed:30404948}; Matrix side {ECO:0000269|PubMed:30404948}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q8BP22}. Note=Weak punctate vesicular distribution throughout the cytoplasm (PubMed:27528616). Localizes at the distal end of mother centrioles (PubMed:27528616). Extensive colocalization with CBY1 at mother centrioles (PubMed:27528616). Localizes to the annulus at the junction between the midpiece (MP) and principal piece (PP) of the sperm flagellum (By similarity). {ECO:0000250|UniProtKB:Q8BP22, ECO:0000269|PubMed:27528616}.; SUBCELLULAR LOCATION: [Isoform 3]: Nucleus {ECO:0000269|PubMed:17646714}.
uniprot
proteins