ID BBS2_HUMAN Reviewed; 721 AA. AC Q9BXC9; Q96CM0; Q96SN9; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 23-FEB-2022, sequence version 2. DT 27-MAR-2024, entry version 186. DE RecName: Full=Bardet-Biedl syndrome 2 protein {ECO:0000305}; GN Name=BBS2 {ECO:0000312|HGNC:HGNC:967}; 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 [MRNA], VARIANT BBS2 GLY-75, AND VARIANTS ASN-70 AND RP VAL-123. RX PubMed=11285252; DOI=10.1093/hmg/10.8.865; RA Nishimura D.Y., Searby C.C., Carmi R., Elbedour K., Van Maldergem L., RA Fulton A.B., Lam B.L., Powell B.R., Swiderski R.E., Bugge K.E., RA Haider N.B., Kwitek-Black A.E., Ying L., Duhl D.M., Gorman S.M., Heon E., RA Iannaccone A., Bonneau D., Biesecker L.G., Jacobson S.G., Stone E.M., RA Sheffield V.C.; RT "Positional cloning of a novel gene on chromosome 16q causing Bardet-Biedl RT syndrome (BBS2)."; RL Hum. Mol. Genet. 10:865-874(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASN-70. 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ASN-70 AND VAL-122. RC TISSUE=Placenta; 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 INVOLVEMENT IN BBS2, AND VARIANT BBS2 VAL-139. RX PubMed=16823392; DOI=10.1038/sj.ejhg.5201688; RA Laurier V., Stoetzel C., Muller J., Thibault C., Corbani S., Jalkh N., RA Salem N., Chouery E., Poch O., Licaire S., Danse J.M., Amati-Bonneau P., RA Bonneau D., Megarbane A., Mandel J.L., Dollfus H.; RT "Pitfalls of homozygosity mapping: an extended consanguineous Bardet-Biedl RT syndrome family with two mutant genes (BBS2, BBS10), three mutations, but RT no triallelism."; RL Eur. J. Hum. Genet. 14:1195-1203(2006). RN [5] RP INTERACTION WITH CCDC28B. RX PubMed=16327777; DOI=10.1038/nature04370; RA Badano J.L., Leitch C.C., Ansley S.J., May-Simera H., Lawson S., RA Lewis R.A., Beales P.L., Dietz H.C., Fisher S., Katsanis N.; RT "Dissection of epistasis in oligogenic Bardet-Biedl syndrome."; RL Nature 439:326-330(2006). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, FUNCTION, AND SUBCELLULAR RP LOCATION. RX PubMed=17574030; DOI=10.1016/j.cell.2007.03.053; RA Nachury M.V., Loktev A.V., Zhang Q., Westlake C.J., Peraenen J., Merdes A., RA Slusarski D.C., Scheller R.H., Bazan J.F., Sheffield V.C., Jackson P.K.; RT "A core complex of BBS proteins cooperates with the GTPase Rab8 to promote RT ciliary membrane biogenesis."; RL Cell 129:1201-1213(2007). RN [7] RP INTERACTION WITH ALDOB. RX PubMed=18000879; DOI=10.1002/cm.20250; RA Oeffner F., Moch C., Neundorf A., Hofmann J., Koch M., Grzeschik K.H.; RT "Novel interaction partners of Bardet-Biedl syndrome proteins."; RL Cell Motil. Cytoskeleton 65:143-155(2008). RN [8] RP INTERACTION WITH BBS7 AND MKKS. RX PubMed=20080638; DOI=10.1073/pnas.0910268107; RA Seo S., Baye L.M., Schulz N.P., Beck J.S., Zhang Q., Slusarski D.C., RA Sheffield V.C.; RT "BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family chaperonins and RT mediate BBSome assembly."; RL Proc. Natl. Acad. Sci. U.S.A. 107:1488-1493(2010). RN [9] RP FUNCTION, FUNCTION OF THE BBSOME COMPLEX, IDENTIFICATION IN THE BBSOME RP COMPLEX, AND SUBCELLULAR LOCATION. RX PubMed=22072986; DOI=10.1371/journal.pgen.1002358; RA Seo S., Zhang Q., Bugge K., Breslow D.K., Searby C.C., Nachury M.V., RA Sheffield V.C.; RT "A novel protein LZTFL1 regulates ciliary trafficking of the BBSome and RT Smoothened."; RL PLoS Genet. 7:E1002358-E1002358(2011). RN [10] RP INTERACTION WITH DLEC1. RX PubMed=33144677; DOI=10.1038/s41598-020-75957-y; RA Okitsu Y., Nagano M., Yamagata T., Ito C., Toshimori K., Dohra H., RA Fujii W., Yogo K.; RT "Dlec1 is required for spermatogenesis and male fertility in mice."; RL Sci. Rep. 10:18883-18883(2020). RN [11] RP INVOLVEMENT IN RP74, AND VARIANTS RP74 ASP-33; ALA-104; ARG-134 AND RP PRO-632. RX PubMed=25541840; DOI=10.1001/jamaophthalmol.2014.5251; RA Shevach E., Ali M., Mizrahi-Meissonnier L., McKibbin M., El-Asrag M., RA Watson C.M., Inglehearn C.F., Ben-Yosef T., Blumenfeld A., Jalas C., RA Banin E., Sharon D.; RT "Association between missense mutations in the BBS2 gene and nonsyndromic RT retinitis pigmentosa."; RL JAMA Ophthalmol. 133:312-318(2015). RN [12] RP VARIANTS BBS2 ALA-104; GLN-315; TRP-315; ILE-558 AND PRO-632. RX PubMed=11567139; DOI=10.1126/science.1063525; RA Katsanis N., Ansley S.J., Badano J.L., Eichers E.R., Lewis R.A., RA Hoskins B.E., Scambler P.J., Davidson W.S., Beales P.L., Lupski J.R.; RT "Triallelic inheritance in Bardet-Biedl syndrome, a Mendelian recessive RT disorder."; RL Science 293:2256-2259(2001). RN [13] RP VARIANTS BBS2 GLN-315 AND TRP-349. RX PubMed=12677556; DOI=10.1086/375178; RA Beales P.L., Badano J.L., Ross A.J., Ansley S.J., Hoskins B.E., Kirsten B., RA Mein C.A., Froguel P., Scambler P.J., Lewis R.A., Lupski J.R., Katsanis N.; RT "Genetic interaction of BBS1 mutations with alleles at other BBS loci can RT result in non-Mendelian Bardet-Biedl syndrome."; RL Am. J. Hum. Genet. 72:1187-1199(2003). RN [14] RP VARIANT BBS2 GLU-174. RX PubMed=12872256; DOI=10.1002/humu.10241; RA Hoskins B.E., Thorn A., Scambler P.J., Beales P.L.; RT "Evaluation of multiplex capillary heteroduplex analysis: a rapid and RT sensitive mutation screening technique."; RL Hum. Mutat. 22:151-157(2003). RN [15] RP VARIANT BBS2 HIS-643. RX PubMed=12920096; DOI=10.1136/jmg.40.8.e104; RA Fauser S., Munz M., Besch D.; RT "Further support for digenic inheritance in Bardet-Biedl syndrome."; RL J. Med. Genet. 40:E104-E104(2003). RN [16] RP VARIANT BBS2 PRO-23, AND VARIANT VAL-123. RX PubMed=15666242; DOI=10.1086/428679; RA Karmous-Benailly H., Martinovic J., Gubler M.-C., Sirot Y., Clech L., RA Ozilou C., Auge J., Brahimi N., Etchevers H., Detrait E., Esculpavit C., RA Audollent S., Goudefroye G., Gonzales M., Tantau J., Loget P., Joubert M., RA Gaillard D., Jeanne-Pasquier C., Delezoide A.-L., Peter M.-O., Plessis G., RA Simon-Bouy B., Dollfus H., Le Merrer M., Munnich A., Encha-Razavi F., RA Vekemans M., Attie-Bitach T.; RT "Antenatal presentation of Bardet-Biedl syndrome may mimic Meckel RT syndrome."; RL Am. J. Hum. Genet. 76:493-504(2005). RN [17] RP VARIANT VAL-123. RX PubMed=15770229; DOI=10.1038/sj.ejhg.5201372; RA Hichri H., Stoetzel C., Laurier V., Caron S., Sigaudy S., Sarda P., RA Hamel C., Martin-Coignard D., Gilles M., Leheup B., Holder M., Kaplan J., RA Bitoun P., Lacombe D., Verloes A., Bonneau D., Perrin-Schmitt F., RA Brandt C., Besancon A.-F., Mandel J.-L., Cossee M., Dollfus H.; RT "Testing for triallelism: analysis of six BBS genes in a Bardet-Biedl RT syndrome family cohort."; RL Eur. J. Hum. Genet. 13:607-616(2005). RN [18] RP VARIANT LYS-629. RX PubMed=20120035; DOI=10.1002/humu.21204; RA Hjortshoj T.D., Gronskov K., Philp A.R., Nishimura D.Y., Riise R., RA Sheffield V.C., Rosenberg T., Brondum-Nielsen K.; RT "Bardet-Biedl syndrome in Denmark -- report of 13 novel sequence variations RT in six genes."; RL Hum. Mutat. 31:429-436(2010). RN [19] RP VARIANTS BBS2 CYS-81; ALA-104; ARG-125; PRO-136; TRP-307; CYS-317 AND RP PRO-632. RX PubMed=21344540; DOI=10.1002/humu.21480; RA Deveault C., Billingsley G., Duncan J.L., Bin J., Theal R., Vincent A., RA Fieggen K.J., Gerth C., Noordeh N., Traboulsi E.I., Fishman G.A., RA Chitayat D., Knueppel T., Millan J.M., Munier F.L., Kennedy D., RA Jacobson S.G., Innes A.M., Mitchell G.A., Boycott K., Heon E.; RT "BBS genotype-phenotype assessment of a multiethnic patient cohort calls RT for a revision of the disease definition."; RL Hum. Mutat. 32:610-619(2011). CC -!- FUNCTION: The BBSome complex is thought to function as a coat complex CC required for sorting of specific membrane proteins to the primary CC cilia. The BBSome complex is required for ciliogenesis but is CC dispensable for centriolar satellite function. This ciliogenic function CC is mediated in part by the Rab8 GDP/GTP exchange factor, which CC localizes to the basal body and contacts the BBSome. Rab8(GTP) enters CC the primary cilium and promotes extension of the ciliary membrane. CC Firstly the BBSome associates with the ciliary membrane and binds to CC RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the CC Rab8-GTP localizes to the cilium and promotes docking and fusion of CC carrier vesicles to the base of the ciliary membrane. The BBSome CC complex, together with the LTZL1, controls SMO ciliary trafficking and CC contributes to the sonic hedgehog (SHH) pathway regulation. Required CC for proper BBSome complex assembly and its ciliary localization. CC {ECO:0000269|PubMed:17574030, ECO:0000269|PubMed:22072986}. CC -!- SUBUNIT: Part of BBSome complex, that contains BBS1, BBS2, BBS4, BBS5, CC BBS7, BBS8/TTC8, BBS9 and BBIP10. Interacts (via C-terminus) with BBS7. CC Interacts (via coiled coil domain) with MKKS. Interacts with CCDC28B CC and ALDOB. Interacts with DLEC1 (PubMed:33144677). CC {ECO:0000269|PubMed:16327777, ECO:0000269|PubMed:17574030, CC ECO:0000269|PubMed:18000879, ECO:0000269|PubMed:20080638, CC ECO:0000269|PubMed:22072986, ECO:0000269|PubMed:33144677}. CC -!- INTERACTION: CC Q9BXC9; P05062: ALDOB; NbExp=4; IntAct=EBI-748297, EBI-1045507; CC Q9BXC9; Q8NFJ9: BBS1; NbExp=7; IntAct=EBI-748297, EBI-1805484; CC Q9BXC9; Q6ZW61: BBS12; NbExp=2; IntAct=EBI-748297, EBI-6128352; CC Q9BXC9; Q8IWZ6: BBS7; NbExp=13; IntAct=EBI-748297, EBI-1806001; CC Q9BXC9; Q8IWZ6-2: BBS7; NbExp=6; IntAct=EBI-748297, EBI-20947190; CC Q9BXC9; Q3SYG4: BBS9; NbExp=14; IntAct=EBI-748297, EBI-2826852; CC Q9BXC9; Q53EP0-3: FNDC3B; NbExp=3; IntAct=EBI-748297, EBI-10242151; CC Q9BXC9; P52597: HNRNPF; NbExp=3; IntAct=EBI-748297, EBI-352986; CC Q9BXC9; Q15051: IQCB1; NbExp=8; IntAct=EBI-748297, EBI-2805823; CC Q9BXC9; P61968: LMO4; NbExp=3; IntAct=EBI-748297, EBI-2798728; CC Q9BXC9; Q99750: MDFI; NbExp=7; IntAct=EBI-748297, EBI-724076; CC Q9BXC9; Q9NPJ1: MKKS; NbExp=3; IntAct=EBI-748297, EBI-721319; CC Q9BXC9; Q16656-4: NRF1; NbExp=3; IntAct=EBI-748297, EBI-11742836; CC Q9BXC9; P61289: PSME3; NbExp=7; IntAct=EBI-748297, EBI-355546; CC Q9BXC9; Q93062: RBPMS; NbExp=3; IntAct=EBI-748297, EBI-740322; CC -!- SUBCELLULAR LOCATION: Cell projection, cilium membrane. Cytoplasm. CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, CC centriolar satellite. CC -!- TISSUE SPECIFICITY: Widely expressed. CC -!- DISEASE: Bardet-Biedl syndrome 2 (BBS2) [MIM:615981]: A syndrome CC characterized by usually severe pigmentary retinopathy, early-onset CC obesity, polydactyly, hypogenitalism, renal malformation and CC intellectual disability. Secondary features include diabetes mellitus, CC hypertension and congenital heart disease. Bardet-Biedl syndrome CC inheritance is autosomal recessive, but three mutated alleles (two at CC one locus, and a third at a second locus) may be required for clinical CC manifestation of some forms of the disease. CC {ECO:0000269|PubMed:11285252, ECO:0000269|PubMed:11567139, CC ECO:0000269|PubMed:12677556, ECO:0000269|PubMed:12872256, CC ECO:0000269|PubMed:12920096, ECO:0000269|PubMed:15666242, CC ECO:0000269|PubMed:16823392, ECO:0000269|PubMed:21344540}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Retinitis pigmentosa 74 (RP74) [MIM:616562]: A retinal CC dystrophy belonging to the group of pigmentary retinopathies. Retinitis CC pigmentosa is characterized by retinal pigment deposits visible on CC fundus examination and primary loss of rod photoreceptor cells followed CC by secondary loss of cone photoreceptors. Patients typically have night CC vision blindness and loss of midperipheral visual field. As their CC condition progresses, they lose their far peripheral visual field and CC eventually central vision as well. {ECO:0000269|PubMed:25541840}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- WEB RESOURCE: Name=Mutations of the BBS2 gene; Note=Retina CC International's Scientific Newsletter; CC URL="https://www.retina-international.org/files/sci-news/bbs2mut.htm"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF342736; AAK28552.1; -; mRNA. DR EMBL; AK027635; BAB55252.1; -; mRNA. DR EMBL; BC014140; AAH14140.1; -; mRNA. DR CCDS; CCDS32451.1; -. DR RefSeq; NP_114091.3; NM_031885.3. DR RefSeq; XP_005256137.1; XM_005256080.2. DR AlphaFoldDB; Q9BXC9; -. DR SMR; Q9BXC9; -. DR BioGRID; 107059; 75. DR ComplexPortal; CPX-1908; BBSome complex. DR CORUM; Q9BXC9; -. DR DIP; DIP-46563N; -. DR IntAct; Q9BXC9; 47. DR STRING; 9606.ENSP00000245157; -. DR TCDB; 3.A.33.1.1; the bbsome complex (bbsome) family. DR GlyCosmos; Q9BXC9; 1 site, 1 glycan. DR GlyGen; Q9BXC9; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9BXC9; -. DR MetOSite; Q9BXC9; -. DR PhosphoSitePlus; Q9BXC9; -. DR BioMuta; BBS2; -. DR DMDM; 20454827; -. DR EPD; Q9BXC9; -. DR jPOST; Q9BXC9; -. DR MassIVE; Q9BXC9; -. DR MaxQB; Q9BXC9; -. DR PaxDb; 9606-ENSP00000245157; -. DR PeptideAtlas; Q9BXC9; -. DR ProteomicsDB; 79404; -. DR Pumba; Q9BXC9; -. DR Antibodypedia; 28577; 129 antibodies from 23 providers. DR DNASU; 583; -. DR Ensembl; ENST00000245157.11; ENSP00000245157.5; ENSG00000125124.14. DR Ensembl; ENST00000682047.1; ENSP00000507699.1; ENSG00000125124.14. DR Ensembl; ENST00000682205.1; ENSP00000508377.1; ENSG00000125124.14. DR Ensembl; ENST00000682470.1; ENSP00000507654.1; ENSG00000125124.14. DR Ensembl; ENST00000682855.1; ENSP00000507027.1; ENSG00000125124.14. DR GeneID; 583; -. DR KEGG; hsa:583; -. DR MANE-Select; ENST00000245157.11; ENSP00000245157.5; NM_031885.5; NP_114091.4. DR UCSC; uc002ejd.3; human. DR AGR; HGNC:967; -. DR CTD; 583; -. DR DisGeNET; 583; -. DR GeneCards; BBS2; -. DR GeneReviews; BBS2; -. DR HGNC; HGNC:967; BBS2. DR HPA; ENSG00000125124; Low tissue specificity. DR MalaCards; BBS2; -. DR MIM; 606151; gene. DR MIM; 615981; phenotype. DR MIM; 616562; phenotype. DR neXtProt; NX_Q9BXC9; -. DR OpenTargets; ENSG00000125124; -. DR Orphanet; 110; Bardet-Biedl syndrome. DR Orphanet; 791; Retinitis pigmentosa. DR PharmGKB; PA25276; -. DR VEuPathDB; HostDB:ENSG00000125124; -. DR eggNOG; ENOG502QPWU; Eukaryota. DR GeneTree; ENSGT00390000017113; -. DR InParanoid; Q9BXC9; -. DR OMA; AMYTIPH; -. DR OrthoDB; 1327990at2759; -. DR PhylomeDB; Q9BXC9; -. DR TreeFam; TF313236; -. DR PathwayCommons; Q9BXC9; -. DR Reactome; R-HSA-5620922; BBSome-mediated cargo-targeting to cilium. DR SignaLink; Q9BXC9; -. DR SIGNOR; Q9BXC9; -. DR BioGRID-ORCS; 583; 13 hits in 1155 CRISPR screens. DR ChiTaRS; BBS2; human. DR GeneWiki; BBS2; -. DR GenomeRNAi; 583; -. DR Pharos; Q9BXC9; Tbio. DR PRO; PR:Q9BXC9; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q9BXC9; Protein. DR Bgee; ENSG00000125124; Expressed in adrenal tissue and 179 other cell types or tissues. DR ExpressionAtlas; Q9BXC9; baseline and differential. DR GO; GO:0034464; C:BBSome; IDA:UniProtKB. DR GO; GO:0034451; C:centriolar satellite; IEA:UniProtKB-SubCell. DR GO; GO:0036064; C:ciliary basal body; IDA:BHF-UCL. DR GO; GO:0060170; C:ciliary membrane; IDA:ComplexPortal. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0005902; C:microvillus; IEA:Ensembl. DR GO; GO:0031514; C:motile cilium; IDA:BHF-UCL. DR GO; GO:0043005; C:neuron projection; IBA:GO_Central. DR GO; GO:0032420; C:stereocilium; IEA:Ensembl. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:MGI. DR GO; GO:0030534; P:adult behavior; ISS:BHF-UCL. DR GO; GO:0014824; P:artery smooth muscle contraction; IEA:Ensembl. DR GO; GO:0048854; P:brain morphogenesis; ISS:BHF-UCL. DR GO; GO:0051216; P:cartilage development; IEA:Ensembl. DR GO; GO:0021987; P:cerebral cortex development; ISS:BHF-UCL. DR GO; GO:0060271; P:cilium assembly; ISS:BHF-UCL. DR GO; GO:0045444; P:fat cell differentiation; ISS:BHF-UCL. DR GO; GO:0010467; P:gene expression; IEA:Ensembl. DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IMP:MGI. DR GO; GO:0021766; P:hippocampus development; ISS:BHF-UCL. DR GO; GO:0032402; P:melanosome transport; ISS:BHF-UCL. DR GO; GO:0038108; P:negative regulation of appetite by leptin-mediated signaling pathway; ISS:BHF-UCL. DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl. DR GO; GO:0040015; P:negative regulation of multicellular organism growth; ISS:BHF-UCL. DR GO; GO:1905515; P:non-motile cilium assembly; IEA:Ensembl. DR GO; GO:0045494; P:photoreceptor cell maintenance; ISS:BHF-UCL. DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:Ensembl. DR GO; GO:0008104; P:protein localization; ISS:BHF-UCL. DR GO; GO:0033365; P:protein localization to organelle; ISS:BHF-UCL. DR GO; GO:0060296; P:regulation of cilium beat frequency involved in ciliary motility; ISS:BHF-UCL. DR GO; GO:0007288; P:sperm axoneme assembly; ISS:BHF-UCL. DR GO; GO:0021756; P:striatum development; ISS:BHF-UCL. DR GO; GO:0042311; P:vasodilation; IEA:Ensembl. DR GO; GO:0007601; P:visual perception; IMP:UniProtKB. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1. DR InterPro; IPR016616; Bardet-Biedl_syndrome_2_prot. DR InterPro; IPR029333; BBS2_C. DR InterPro; IPR029429; BBS2_Mid. DR InterPro; IPR029430; BBS2_N. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR PANTHER; PTHR32465; BARDET-BIEDL SYNDROME 2 PROTEIN; 1. DR PANTHER; PTHR32465:SF0; BARDET-BIEDL SYNDROME 2 PROTEIN; 1. DR Pfam; PF14782; BBS2_C; 1. DR Pfam; PF14783; BBS2_Mid; 1. DR Pfam; PF14781; BBS2_N; 1. DR PIRSF; PIRSF013684; BBS2; 1. DR SUPFAM; SSF50978; WD40 repeat-like; 1. DR Genevisible; Q9BXC9; HS. PE 1: Evidence at protein level; KW Bardet-Biedl syndrome; Cell membrane; Cell projection; Ciliopathy; Cilium; KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton; KW Disease variant; Intellectual disability; Membrane; Obesity; KW Protein transport; Reference proteome; Retinitis pigmentosa; KW Sensory transduction; Transport; Vision. FT CHAIN 1..721 FT /note="Bardet-Biedl syndrome 2 protein" FT /id="PRO_0000064843" FT COILED 325..369 FT /evidence="ECO:0000255" FT VARIANT 23 FT /note="R -> P (in BBS2)" FT /evidence="ECO:0000269|PubMed:15666242" FT /id="VAR_038889" FT VARIANT 33 FT /note="A -> D (in RP74; dbSNP:rs797045155)" FT /evidence="ECO:0000269|PubMed:25541840" FT /id="VAR_075726" FT VARIANT 70 FT /note="S -> N (in dbSNP:rs4784677)" FT /evidence="ECO:0000269|PubMed:11285252, FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334" FT /id="VAR_013162" FT VARIANT 75 FT /note="V -> G (in BBS2; in linkage disequilibrium with FT V-123 in a Bedouin kindred; dbSNP:rs121908174)" FT /evidence="ECO:0000269|PubMed:11285252" FT /id="VAR_013163" FT VARIANT 81 FT /note="G -> C (in BBS2; dbSNP:rs750506474)" FT /evidence="ECO:0000269|PubMed:21344540" FT /id="VAR_066280" FT VARIANT 104 FT /note="D -> A (in BBS2 and RP74; dbSNP:rs121908179)" FT /evidence="ECO:0000269|PubMed:11567139, FT ECO:0000269|PubMed:21344540, ECO:0000269|PubMed:25541840" FT /id="VAR_013164" FT VARIANT 122 FT /note="A -> V (in dbSNP:rs17856449)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_029747" FT VARIANT 123 FT /note="I -> V (in dbSNP:rs11373)" FT /evidence="ECO:0000269|PubMed:11285252, FT ECO:0000269|PubMed:15666242, ECO:0000269|PubMed:15770229" FT /id="VAR_013165" FT VARIANT 125 FT /note="L -> R (in BBS2)" FT /evidence="ECO:0000269|PubMed:21344540" FT /id="VAR_066281" FT VARIANT 134 FT /note="P -> R (in RP74; dbSNP:rs376306240)" FT /evidence="ECO:0000269|PubMed:25541840" FT /id="VAR_075727" FT VARIANT 136 FT /note="A -> P (in BBS2)" FT /evidence="ECO:0000269|PubMed:21344540" FT /id="VAR_066282" FT VARIANT 139 FT /note="G -> V (in BBS2; dbSNP:rs121908181)" FT /evidence="ECO:0000269|PubMed:16823392" FT /id="VAR_075728" FT VARIANT 174 FT /note="D -> E (in BBS2; dbSNP:rs767373822)" FT /evidence="ECO:0000269|PubMed:12872256" FT /id="VAR_038890" FT VARIANT 307 FT /note="C -> W (in BBS2)" FT /evidence="ECO:0000269|PubMed:21344540" FT /id="VAR_066283" FT VARIANT 315 FT /note="R -> Q (in BBS2; dbSNP:rs544773389)" FT /evidence="ECO:0000269|PubMed:11567139, FT ECO:0000269|PubMed:12677556" FT /id="VAR_013166" FT VARIANT 315 FT /note="R -> W (in BBS2; dbSNP:rs121908178)" FT /evidence="ECO:0000269|PubMed:11567139" FT /id="VAR_013167" FT VARIANT 317 FT /note="Y -> C (in BBS2; dbSNP:rs1597016660)" FT /evidence="ECO:0000269|PubMed:21344540" FT /id="VAR_066284" FT VARIANT 349 FT /note="L -> W (in BBS2; has a modifier effect on BBS; FT dbSNP:rs752280639)" FT /evidence="ECO:0000269|PubMed:12677556" FT /id="VAR_038891" FT VARIANT 504 FT /note="A -> V (in dbSNP:rs16957538)" FT /id="VAR_029748" FT VARIANT 558 FT /note="T -> I (in BBS2; dbSNP:rs370581600)" FT /evidence="ECO:0000269|PubMed:11567139" FT /id="VAR_013168" FT VARIANT 629 FT /note="E -> K (in a patient with Bardet-Biedl syndrome FT compound heterozygote for mutations in BBS10; uncertain FT significance; dbSNP:rs746505864)" FT /evidence="ECO:0000269|PubMed:20120035" FT /id="VAR_066285" FT VARIANT 632 FT /note="R -> P (in BBS2 and RP74; dbSNP:rs138043021)" FT /evidence="ECO:0000269|PubMed:11567139, FT ECO:0000269|PubMed:21344540, ECO:0000269|PubMed:25541840" FT /id="VAR_013169" FT VARIANT 643 FT /note="R -> H (in BBS2; dbSNP:rs532361142)" FT /evidence="ECO:0000269|PubMed:12920096" FT /id="VAR_038892" FT CONFLICT 63 FT /note="E -> G (in Ref. 2; BAB55252)" FT /evidence="ECO:0000305" FT CONFLICT 169 FT /note="C -> R (in Ref. 2; BAB55252)" FT /evidence="ECO:0000305" FT CONFLICT 457 FT /note="L -> S (in Ref. 2; BAB55252)" FT /evidence="ECO:0000305" FT CONFLICT 648 FT /note="Y -> H (in Ref. 2; BAB55252)" FT /evidence="ECO:0000305" SQ SEQUENCE 721 AA; 79844 MW; EF97CAA28709A089 CRC64; MLLPVFTLKL RHKISPRMVA IGRYDGTHPC LAAATQTGKV FIHNPHTRNQ HVSASRVFQS PLESDVSLLS INQAVSCLTA GVLNPELGYD ALLVGTQTNL LAYDVYNNSD LFYREVADGA NAIVLGTLGD ISSPLAIIGG NCALQGFNHE GSDLFWTVTG DNVNSLALCD FDGDGKKELL VGSEDFDIRV FKEDEIVAEM TETEIVTSLC PMYGSRFGYA LSNGTVGVYD KTSRYWRIKS KNHAMSIHAF DLNSDGVNEL ITGWSNGKVD ARSDRTGEVI FKDNFSSAIA GVVEGDYRMD GHIQLICCSV DGEIRGYLPG TAEMRGNLMD TSAEQDLIRE LSQKKQNLLL ELRNYEENAK AELASPLNEA DGHRGIIPAN TRLHTTLSVS LGNETQTAHT ELRISTSNDT IIRAVLIFAE GIFTGESHVV HPSIHNLSSS ICIPIVPPKD VPVDLHLKAF VGYRSSTQFH VFESTRQLPR FSMYALTSLD PASEPISYVN FTIAERAQRV VVWLGQNFLL PEDTHIQNAP FQVCFTSLRN GGHLHIKIKL SGEITINTDD IDLAGDIIQS MASFFAIEDL QVEADFPVYF EELRKVLVKV DEYHSVHQKL SADMADHSNL IRSLLVGAED ARLMRDMKTM KSRYMELYDL NRDLLNGYKI RCNNHTELLG NLKAVNQAIQ RAGRLRVGKP KNQVITACRD AIRSNNINTL FKIMRVGTAS S //