CBAR2_HUMAN
ID CBAR2_HUMAN Reviewed; 304 AA.
AC Q6ZTR7; A0A0D9SG36;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=CBY1-interacting BAR domain-containing protein 2 {ECO:0000312|HGNC:HGNC:24781};
DE AltName: Full=Protein FAM92B;
GN Name=CIBAR2 {ECO:0000312|HGNC:HGNC:24781}; Synonyms=FAM92B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart, and Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INTERACTION WITH CBY1, SUBUNIT, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-105;
RP ARG-108; LYS-112; LYS-130; ARG-132 AND LYS-134, AND FUNCTION.
RX PubMed=27528616; DOI=10.1128/mcb.00160-16;
RA Li F.Q., Chen X., Fisher C., Siller S.S., Zelikman K., Kuriyama R.,
RA Takemaru K.I.;
RT "BAR domain-containing FAM92 proteins interact with chibby1 to facilitate
RT ciliogenesis.";
RL Mol. Cell. Biol. 36:2668-2680(2016).
CC -!- FUNCTION: May play a role in ciliogenesis (By similarity). In
CC cooperation with CBY1 may facilitate ciliogenesis likely by the
CC recruitment and fusion of endosomal vesicles at distal appendages
CC during early stages of ciliogenesis (PubMed:27528616).
CC {ECO:0000250|UniProtKB:A1XBS5, ECO:0000269|PubMed:27528616}.
CC -!- SUBUNIT: Homodimer (via BAR-like domain) (PubMed:27528616). Heterodimer
CC (via BAR-like domain) with FAM92A (PubMed:27528616). Interacts with
CC CBY1 (PubMed:27528616). {ECO:0000269|PubMed:27528616}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000250|UniProtKB:Q3V2J0}.
CC Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000250|UniProtKB:Q3V2J0}. Note=Extensive colocalization with CBY1
CC at mother centrioles. {ECO:0000250|UniProtKB:Q3V2J0}.
CC -!- TISSUE SPECIFICITY: Restricted to certain tissues, most prominently
CC expressed in multicilaited tissues. {ECO:0000269|PubMed:27528616}.
CC -!- DOMAIN: The BAR-like domain displays limited similarity to other BAR
CC domains. {ECO:0000250|UniProtKB:A1XBS5}.
CC -!- SIMILARITY: Belongs to the CIBAR family. {ECO:0000305}.
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DR EMBL; AK126284; BAC86515.1; -; mRNA.
DR EMBL; AC026469; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC093665; AAH93665.1; -; mRNA.
DR EMBL; BC111944; AAI11945.1; -; mRNA.
DR CCDS; CCDS32500.1; -.
DR RefSeq; NP_940893.1; NM_198491.2.
DR RefSeq; XP_011521365.1; XM_011523063.1.
DR AlphaFoldDB; Q6ZTR7; -.
DR SMR; Q6ZTR7; -.
DR BioGRID; 130832; 3.
DR IntAct; Q6ZTR7; 2.
DR MINT; Q6ZTR7; -.
DR STRING; 9606.ENSP00000443411; -.
DR iPTMnet; Q6ZTR7; -.
DR PhosphoSitePlus; Q6ZTR7; -.
DR BioMuta; FAM92B; -.
DR DMDM; 74738328; -.
DR jPOST; Q6ZTR7; -.
DR MassIVE; Q6ZTR7; -.
DR PaxDb; Q6ZTR7; -.
DR PeptideAtlas; Q6ZTR7; -.
DR PRIDE; Q6ZTR7; -.
DR ProteomicsDB; 68290; -.
DR Antibodypedia; 44888; 29 antibodies from 13 providers.
DR DNASU; 339145; -.
DR Ensembl; ENST00000629253.1; ENSP00000487117.1; ENSG00000153789.13.
DR GeneID; 339145; -.
DR KEGG; hsa:339145; -.
DR UCSC; uc059xyr.1; human.
DR CTD; 339145; -.
DR DisGeNET; 339145; -.
DR GeneCards; CIBAR2; -.
DR HGNC; HGNC:24781; CIBAR2.
DR HPA; ENSG00000153789; Tissue enriched (fallopian).
DR MIM; 617274; gene.
DR neXtProt; NX_Q6ZTR7; -.
DR OpenTargets; ENSG00000153789; -.
DR PharmGKB; PA142671826; -.
DR VEuPathDB; HostDB:ENSG00000153789; -.
DR eggNOG; ENOG502QT9N; Eukaryota.
DR GeneTree; ENSGT00390000010285; -.
DR HOGENOM; CLU_072172_2_0_1; -.
DR InParanoid; Q6ZTR7; -.
DR OrthoDB; 1324464at2759; -.
DR PhylomeDB; Q6ZTR7; -.
DR TreeFam; TF324316; -.
DR PathwayCommons; Q6ZTR7; -.
DR SignaLink; Q6ZTR7; -.
DR BioGRID-ORCS; 339145; 15 hits in 1011 CRISPR screens.
DR GenomeRNAi; 339145; -.
DR Pharos; Q6ZTR7; Tdark.
DR PRO; PR:Q6ZTR7; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q6ZTR7; protein.
DR Bgee; ENSG00000153789; Expressed in right uterine tube and 80 other tissues.
DR ExpressionAtlas; Q6ZTR7; baseline and differential.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0036064; C:ciliary basal body; IBA:GO_Central.
DR GO; GO:0035869; C:ciliary transition zone; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR CDD; cd07598; BAR_FAM92; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR035590; BAR_CBAR1/2.
DR InterPro; IPR009602; CBAR/FAM92.
DR PANTHER; PTHR21223; PTHR21223; 1.
DR Pfam; PF06730; FAM92; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton;
KW Reference proteome.
FT CHAIN 1..304
FT /note="CBY1-interacting BAR domain-containing protein 2"
FT /id="PRO_0000333004"
FT REGION 6..217
FT /note="BAR-like"
FT /evidence="ECO:0000250|UniProtKB:A1XBS5"
FT VARIANT 22
FT /note="E -> K (in dbSNP:rs9934891)"
FT /id="VAR_043035"
FT MUTAGEN 105
FT /note="K->E: Abolishes ability to induce membrane
FT remodeling in the presence of CBY1; when associated with E-
FT 108; E-112; E-130; E-132 and E-134."
FT /evidence="ECO:0000269|PubMed:27528616"
FT MUTAGEN 108
FT /note="R->E: Abolishes ability to induce membrane
FT remodeling in the presence of CBY1; when associated with E-
FT 105; E-112; E-130; E-132 and E-134."
FT /evidence="ECO:0000269|PubMed:27528616"
FT MUTAGEN 112
FT /note="K->E: Abolishes ability to induce membrane
FT remodeling in the presence of CBY1; when associated with E-
FT 105; E-108; E-130; E-132 and E-134."
FT /evidence="ECO:0000269|PubMed:27528616"
FT MUTAGEN 130
FT /note="K->E: Abolishes ability to induce membrane
FT remodeling in the presence of CBY1; when associated with E-
FT 105; E-108; E-112; E-132 and E-134."
FT /evidence="ECO:0000269|PubMed:27528616"
FT MUTAGEN 132
FT /note="R->E: Abolishes ability to induce membrane
FT remodeling in the presence of CBY1; when associated with E-
FT 105; E-108; E-112; E-130 and E-134."
FT /evidence="ECO:0000269|PubMed:27528616"
FT MUTAGEN 134
FT /note="K->E: Abolishes ability to induce membrane
FT remodeling in the presence of CBY1; when associated with E-
FT 105; E-108; E-1112; E-130 and E-132."
FT /evidence="ECO:0000269|PubMed:27528616"
FT CONFLICT 143
FT /note="G -> S (in Ref. 1; BAC86515 and 3; AAH93665/
FT AAI11945)"
SQ SEQUENCE 304 AA; 34755 MW; 8126DCC535375296 CRC64;
MNIVFSRDSQ VRVMENTVAN TEKYFGQFCS LLAAYTRKTA RLRDKADQLV KQLIDFANSE
NPELRATMRG FAEDLAKVQD YRQAQVERLE TKVVNPLKLY GAQIKQTRAE IKKFKHVQNH
EIKQLEKLEK LRQKSPSDQQ MIGQAETRVQ RAAVDSSRTT LQLEETVDGF QRQKLKDLQK
FFCDFVTIEM VFHAKAVEVY SSAFQTLEKY DLERDLLDFR AKMQGVYGHY DTRLLANTSP
PPSVLQSLAS QGTLQVQLSR ANEDPEHPHA NHGRFSLCEW VVKGQPAHCV CGQGGHLMLP
GHSL
