BBS2_HUMAN
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 03-AUG-2022, entry version 177.
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=8; IntAct=EBI-748297, EBI-1805484;
CC Q9BXC9; Q8IWZ6: BBS7; NbExp=14; IntAct=EBI-748297, EBI-1806001;
CC Q9BXC9; Q8IWZ6-2: BBS7; NbExp=6; IntAct=EBI-748297, EBI-20947190;
CC Q9BXC9; Q3SYG4: BBS9; NbExp=15; 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=4; 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";
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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 AlphaFoldDB; Q9BXC9; -.
DR SMR; Q9BXC9; -.
DR BioGRID; 107059; 74.
DR ComplexPortal; CPX-1908; BBSome complex.
DR CORUM; Q9BXC9; -.
DR DIP; DIP-46563N; -.
DR IntAct; Q9BXC9; 47.
DR STRING; 9606.ENSP00000245157; -.
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; Q9BXC9; -.
DR PeptideAtlas; Q9BXC9; -.
DR PRIDE; Q9BXC9; -.
DR ProteomicsDB; 79404; -.
DR Antibodypedia; 28577; 116 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 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 OrthoDB; 327831at2759; -.
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 1076 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 177 other tissues.
DR ExpressionAtlas; Q9BXC9; baseline and differential.
DR Genevisible; Q9BXC9; HS.
DR GO; GO:0034464; C:BBSome; IDA:UniProtKB.
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; -; 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; PTHR32465; 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; SSF50978; 1.
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 V-
FT 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 pathological role; 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
