{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"A1XBS5","secondaryAccessions":["A1XBS4","Q32ND3","Q6AHW7","Q8N8R1","Q96L09"],"uniProtkbId":"CBAR1_HUMAN","entryAudit":{"firstPublicDate":"2007-05-15","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2008-09-23","entryVersion":131,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:30452"}],"value":"CBY1-interacting BAR domain-containing protein 1"}},"flag":"Precursor"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:30452"}],"value":"CIBAR1"},"synonyms":[{"value":"FAM92A"},{"value":"FAM92A1"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8BP22"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27528616"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30395363"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30404948"}],"value":"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)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27528616"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30395363"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38197861"}],"value":"Homodimer (via BAR-like domain) (PubMed:27528616, PubMed:30395363). Heterodimer with FAM92B (via BAR-like domains) (PubMed:27528616). Interacts (via BAR-like domain) with CBY1; this interaction is required for targeting FAM92A to centriole and cilium basal body (PubMed:27528616, PubMed:30395363). Interacts (via BAR-like domain) with CBY3; both proteins form a ninefold symmetric structure at the flagellar base; are recruited to the annulus in a mutually dependent manner and regulate annulus positioning (PubMed:38197861)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"A1XBS5","intActId":"EBI-2349888"},"interactantTwo":{"uniProtKBAccession":"Q9Y3M2","geneName":"CBY1","intActId":"EBI-947308"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"A1XBS5-3","intActId":"EBI-12348777"},"interactantTwo":{"uniProtKBAccession":"Q9Y3M2","geneName":"CBY1","intActId":"EBI-947308"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"A1XBS5-3","intActId":"EBI-12348777"},"interactantTwo":{"uniProtKBAccession":"Q8NA61-2","geneName":"CBY2","intActId":"EBI-11524851"},"numberOfExperiments":3,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8BP22"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27528616"}],"value":"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)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27528616"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30404948"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27528616"}],"value":"Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole","id":"SL-0046"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27528616"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30395363"}],"value":"Cytoplasm, cytoskeleton, cilium basal body","id":"SL-0087"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8BP22"}],"value":"Cell projection, cilium","id":"SL-0066"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30404948"}],"value":"Nucleus","id":"SL-0191"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30404948"}],"value":"Mitochondrion inner membrane","id":"SL-0168"},"topology":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30404948"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30404948"}],"value":"Matrix side","id":"SL-9913"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8BP22"}],"value":"Cell projection, cilium, flagellum","id":"SL-0117"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Isoform 3","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17646714"}],"value":"Nucleus","id":"SL-0191"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"17646714"}],"value":"FAM92A1-289"}],"isoformIds":["A1XBS5-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"17646714"}],"value":"FAM92A1-251"}],"isoformIds":["A1XBS5-2"],"sequenceIds":["VSP_025294"],"isoformSequenceStatus":"Described"},{"name":{"value":"3"},"isoformIds":["A1XBS5-3"],"sequenceIds":["VSP_025296"],"isoformSequenceStatus":"Described"},{"name":{"value":"4"},"isoformIds":["A1XBS5-4"],"sequenceIds":["VSP_025295"],"isoformSequenceStatus":"Described"},{"name":{"value":"5"},"isoformIds":["A1XBS5-5"],"sequenceIds":["VSP_025292","VSP_025293"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"27528616"}],"value":"The BAR-like domain displays limited similarity to other BAR domains"}],"commentType":"DOMAIN"},{"commentType":"DISEASE","disease":{"diseaseId":"Polydactyly, postaxial, A9","diseaseAccession":"DI-05433","acronym":"PAPA9","description":"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.","diseaseCrossReference":{"database":"MIM","id":"618219"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30395363"}]},"note":{"texts":[{"value":"The disease may be caused by variants affecting the gene represented in this entry"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the CIBAR family"}],"commentType":"SIMILARITY"},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Erroneous initiation","sequence":"AAH14598.2","note":"Extended N-terminus.","evidences":[{"evidenceCode":"ECO:0000305"}]},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Erroneous initiation","sequence":"AAI08708.1","note":"Extended N-terminus.","evidences":[{"evidenceCode":"ECO:0000305"}]}],"features":[{"type":"Transit peptide","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":47,"modifier":"EXACT"}},"description":"Mitochondrion","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30404948"}]},{"type":"Chain","location":{"start":{"value":48,"modifier":"EXACT"},"end":{"value":289,"modifier":"EXACT"}},"description":"CBY1-interacting BAR domain-containing protein 1","featureId":"PRO_0000287080"},{"type":"Region","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":220,"modifier":"EXACT"}},"description":"BAR-like","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"27528616"}]},{"type":"Region","location":{"start":{"value":265,"modifier":"EXACT"},"end":{"value":289,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Coiled coil","location":{"start":{"value":107,"modifier":"EXACT"},"end":{"value":178,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Compositional bias","location":{"start":{"value":271,"modifier":"EXACT"},"end":{"value":289,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Alternative sequence","location":{"start":{"value":89,"modifier":"EXACT"},"end":{"value":97,"modifier":"EXACT"}},"description":"in isoform 5","evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"17974005"}],"featureId":"VSP_025292","alternativeSequence":{"originalSequence":"ERLEAKVVE","alternativeSequences":["WSEITVSLL"]}},{"type":"Alternative sequence","location":{"start":{"value":98,"modifier":"EXACT"},"end":{"value":289,"modifier":"EXACT"}},"description":"in isoform 5","evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"17974005"}],"featureId":"VSP_025293","alternativeSequence":{}},{"type":"Alternative sequence","location":{"start":{"value":182,"modifier":"EXACT"},"end":{"value":219,"modifier":"EXACT"}},"description":"in isoform 2","evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"17646714"}],"featureId":"VSP_025294","alternativeSequence":{}},{"type":"Alternative sequence","location":{"start":{"value":220,"modifier":"EXACT"},"end":{"value":289,"modifier":"EXACT"}},"description":"in isoform 4","evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"14702039"}],"featureId":"VSP_025295","alternativeSequence":{"originalSequence":"VFRNSLYAPDYSSRLDIVRANSKSPLQRSLSAKCVSGTGQVSTCRLRKDQQAEDDEDDELDVTEEENFLK","alternativeSequences":["RWSFAMLPRLVLNSWGSSDPPALASQSVRFSEILCMHQIIHLV"]}},{"type":"Alternative sequence","location":{"start":{"value":260,"modifier":"EXACT"},"end":{"value":289,"modifier":"EXACT"}},"description":"in isoform 3","evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"15489334"}],"featureId":"VSP_025296","alternativeSequence":{"originalSequence":"VSTCRLRKDQQAEDDEDDELDVTEEENFLK","alternativeSequences":["EAGWAATCQTLI"]}},{"type":"Natural variant","location":{"start":{"value":160,"modifier":"EXACT"},"end":{"value":289,"modifier":"EXACT"}},"description":"in PAPA9; 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