BBS1_HUMAN
ID BBS1_HUMAN Reviewed; 593 AA.
AC Q8NFJ9; Q32MM9; Q32MN0; Q96SN4;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Bardet-Biedl syndrome 1 protein;
DE AltName: Full=BBS2-like protein 2;
GN Name=BBS1; Synonyms=BBS2L2;
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] (ISOFORM 1), AND VARIANT BBS1 ARG-390.
RX PubMed=12118255; DOI=10.1038/ng935;
RA Mykytyn K., Nishimura D.Y., Searby C.C., Shastri M., Yen H., Beck J.S.,
RA Braun T., Streb L.M., Cornier A.S., Cox G.F., Fulton A.B., Carmi R.,
RA Lueleci G., Chandrasekharappa S.C., Collins F.S., Jacobson S.G.,
RA Heckenlively J.R., Weleber R.G., Stone E.M., Sheffield V.C.;
RT "Identification of the gene (BBS1) most commonly involved in Bardet-Biedl
RT syndrome, a complex human obesity syndrome.";
RL Nat. Genet. 31:435-438(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
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 [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, SUBCELLULAR
RP LOCATION, AND INTERACTION WITH RAB3IP.
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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
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 PKD1.
RX PubMed=24939912; DOI=10.1093/hmg/ddu267;
RA Su X., Driscoll K., Yao G., Raed A., Wu M., Beales P.L., Zhou J.;
RT "Bardet-Biedl syndrome proteins 1 and 3 regulate the ciliary trafficking of
RT polycystic kidney disease 1 protein.";
RL Hum. Mol. Genet. 23:5441-5451(2014).
RN [11]
RP VARIANTS BBS1 200-ILE-THR-201 DEL; ARG-390 AND PRO-518.
RX PubMed=12524598; DOI=10.1086/346172;
RA Mykytyn K., Nishimura D.Y., Searby C.C., Beck G., Bugge K., Haines H.L.,
RA Cornier A.S., Cox G.F., Fulton A.B., Carmi R., Iannaccone A.,
RA Jacobson S.G., Weleber R.G., Wright A.F., Riise R., Hennekam R.C.M.,
RA Lueleci G., Berker-Karauzum S., Biesecker L.G., Stone E.M., Sheffield V.C.;
RT "Evaluation of complex inheritance involving the most common Bardet-Biedl
RT syndrome locus (BBS1).";
RL Am. J. Hum. Genet. 72:429-437(2003).
RN [12]
RP VARIANT BBS1 LYS-234.
RX PubMed=12567324; DOI=10.1086/368204;
RA Badano J.L., Ansley S.J., Leitch C.C., Lewis R.A., Lupski J.R.,
RA Katsanis N.;
RT "Identification of a novel Bardet-Biedl syndrome protein, BBS7, that shares
RT structural features with BBS1 and BBS2.";
RL Am. J. Hum. Genet. 72:650-658(2003).
RN [13]
RP VARIANTS BBS1 ARG-35; GLU-53; ASN-148; LYS-234; SER-305; ILE-389 DEL;
RP ARG-390; SER-434 HIS-503 AND GLN-518.
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 VARIANTS BBS1 ARG-390 AND PRO-518.
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 [15]
RP VARIANTS BBS1 GLN-160 AND ARG-390.
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 [16]
RP VARIANTS VAL-206 AND LEU-245, AND VARIANT BBS1 ARG-390.
RX PubMed=21052717; DOI=10.1007/s00439-010-0902-8;
RA Janssen S., Ramaswami G., Davis E.E., Hurd T., Airik R., Kasanuki J.M.,
RA Van Der Kraak L., Allen S.J., Beales P.L., Katsanis N., Otto E.A.,
RA Hildebrandt F.;
RT "Mutation analysis in Bardet-Biedl syndrome by DNA pooling and massively
RT parallel resequencing in 105 individuals.";
RL Hum. Genet. 129:79-90(2011).
RN [17]
RP VARIANT ASP-559, AND INVOLVEMENT IN CILIOPATHIES.
RX PubMed=21258341; DOI=10.1038/ng.756;
RA Davis E.E., Zhang Q., Liu Q., Diplas B.H., Davey L.M., Hartley J.,
RA Stoetzel C., Szymanska K., Ramaswami G., Logan C.V., Muzny D.M.,
RA Young A.C., Wheeler D.A., Cruz P., Morgan M., Lewis L.R., Cherukuri P.,
RA Maskeri B., Hansen N.F., Mullikin J.C., Blakesley R.W., Bouffard G.G.,
RA Gyapay G., Rieger S., Tonshoff B., Kern I., Soliman N.A., Neuhaus T.J.,
RA Swoboda K.J., Kayserili H., Gallagher T.E., Lewis R.A., Bergmann C.,
RA Otto E.A., Saunier S., Scambler P.J., Beales P.L., Gleeson J.G.,
RA Maher E.R., Attie-Bitach T., Dollfus H., Johnson C.A., Green E.D.,
RA Gibbs R.A., Hildebrandt F., Pierce E.A., Katsanis N.;
RT "TTC21B contributes both causal and modifying alleles across the ciliopathy
RT spectrum.";
RL Nat. Genet. 43:189-196(2011).
RN [18]
RP VARIANTS BBS1 GLN-160; THR-330; ARG-390 AND ASN-524 DEL.
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 (PubMed:17574030, PubMed:22072986). Plays a role in olfactory cilium
CC biogenesis/maintenance and trafficking (By similarity).
CC {ECO:0000250|UniProtKB:Q3V3N7, ECO:0000269|PubMed:17574030,
CC ECO:0000269|PubMed:22072986}.
CC -!- SUBUNIT: Part of BBSome complex, that contains BBS1, BBS2, BBS4, BBS5,
CC BBS7, BBS8/TTC8, BBS9 and BBIP10. Interacts with the C-terminus of
CC RAB3IP. Interacts with CCDC28B and ALDOB. Interacts with PKD1
CC (PubMed:24939912). {ECO:0000269|PubMed:16327777,
CC ECO:0000269|PubMed:17574030, ECO:0000269|PubMed:18000879,
CC ECO:0000269|PubMed:22072986, ECO:0000269|PubMed:24939912}.
CC -!- INTERACTION:
CC Q8NFJ9; P05062: ALDOB; NbExp=4; IntAct=EBI-1805484, EBI-1045507;
CC Q8NFJ9; Q9H0F7: ARL6; NbExp=4; IntAct=EBI-1805484, EBI-2891949;
CC Q8NFJ9; Q9H0F7-1: ARL6; NbExp=3; IntAct=EBI-1805484, EBI-16127759;
CC Q8NFJ9; Q9BXC9: BBS2; NbExp=8; IntAct=EBI-1805484, EBI-748297;
CC Q8NFJ9; Q96RK4: BBS4; NbExp=8; IntAct=EBI-1805484, EBI-1805814;
CC Q8NFJ9; Q8IWZ6: BBS7; NbExp=7; IntAct=EBI-1805484, EBI-1806001;
CC Q8NFJ9; Q3SYG4: BBS9; NbExp=12; IntAct=EBI-1805484, EBI-2826852;
CC Q8NFJ9; Q14203-5: DCTN1; NbExp=3; IntAct=EBI-1805484, EBI-25840379;
CC Q8NFJ9; P68104: EEF1A1; NbExp=3; IntAct=EBI-1805484, EBI-352162;
CC Q8NFJ9; Q15051: IQCB1; NbExp=4; IntAct=EBI-1805484, EBI-2805823;
CC Q8NFJ9; Q99497: PARK7; NbExp=4; IntAct=EBI-1805484, EBI-1164361;
CC Q8NFJ9; Q15154: PCM1; NbExp=2; IntAct=EBI-1805484, EBI-741421;
CC Q8NFJ9; Q96QF0-1: RAB3IP; NbExp=2; IntAct=EBI-1805484, EBI-747860;
CC Q8NFJ9; P48356-1: Lepr; Xeno; NbExp=3; IntAct=EBI-1805484, EBI-6143588;
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium membrane. Cytoplasm.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome,
CC centriolar satellite.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8NFJ9-1; Sequence=Displayed;
CC Name=3; Synonyms=DPP3-BBS1;
CC IsoId=Q8NFJ9-2; Sequence=VSP_008854;
CC Name=2;
CC IsoId=Q8NFJ9-3; Sequence=VSP_054152, VSP_054153;
CC -!- TISSUE SPECIFICITY: Highly expressed in the kidney. Also found in fetal
CC tissue, testis, retina, adipose tissue, heart, skeletal muscle and
CC pancreas.
CC -!- DISEASE: Note=Ciliary dysfunction leads to a broad spectrum of
CC disorders, collectively termed ciliopathies. Overlapping clinical
CC features include retinal degeneration, renal cystic disease, skeletal
CC abnormalities, fibrosis of various organ, and a complex range of
CC anatomical and functional defects of the central and peripheral nervous
CC system. The ciliopathy range of diseases includes Meckel-Gruber
CC syndrome, Bardet-Biedl syndrome, Joubert syndrome, nephronophtisis,
CC Senior-Loken syndrome, and Jeune asphyxiating thoracic dystrophy among
CC others. Single-locus allelism is insufficient to explain the variable
CC penetrance and expressivity of such disorders, leading to the
CC suggestion that variations across multiple sites of the ciliary
CC proteome, including BBS1, influence the clinical outcome.
CC -!- DISEASE: Bardet-Biedl syndrome 1 (BBS1) [MIM:209900]: 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:12118255, ECO:0000269|PubMed:12524598,
CC ECO:0000269|PubMed:12567324, ECO:0000269|PubMed:12677556,
CC ECO:0000269|PubMed:12920096, ECO:0000269|PubMed:15770229,
CC ECO:0000269|PubMed:21052717, ECO:0000269|PubMed:21344540}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: [Isoform 3]: Based on a readthrough transcript which may
CC produce a DPP3-BBS1 fusion protein. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Mutations of the BBS1 gene; Note=Retina
CC International's Scientific Newsletter;
CC URL="https://www.retina-international.org/files/sci-news/bbs1mut.htm";
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DR EMBL; AF503941; AAM92770.1; -; mRNA.
DR EMBL; AK027645; BAB55261.1; -; mRNA.
DR EMBL; AP002748; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC109064; AAI09065.1; -; mRNA.
DR EMBL; BC109065; AAI09066.1; -; mRNA.
DR CCDS; CCDS8142.1; -. [Q8NFJ9-1]
DR RefSeq; NP_078925.3; NM_024649.4. [Q8NFJ9-1]
DR PDB; 6XT9; EM; 3.80 A; A=1-593.
DR PDBsum; 6XT9; -.
DR AlphaFoldDB; Q8NFJ9; -.
DR SMR; Q8NFJ9; -.
DR BioGRID; 107058; 125.
DR ComplexPortal; CPX-1908; BBSome complex.
DR CORUM; Q8NFJ9; -.
DR DIP; DIP-46564N; -.
DR IntAct; Q8NFJ9; 50.
DR STRING; 9606.ENSP00000317469; -.
DR iPTMnet; Q8NFJ9; -.
DR PhosphoSitePlus; Q8NFJ9; -.
DR BioMuta; BBS1; -.
DR DMDM; 38257662; -.
DR EPD; Q8NFJ9; -.
DR jPOST; Q8NFJ9; -.
DR MassIVE; Q8NFJ9; -.
DR MaxQB; Q8NFJ9; -.
DR PaxDb; Q8NFJ9; -.
DR PeptideAtlas; Q8NFJ9; -.
DR PRIDE; Q8NFJ9; -.
DR ProteomicsDB; 61606; -.
DR ProteomicsDB; 73319; -. [Q8NFJ9-1]
DR ProteomicsDB; 73320; -. [Q8NFJ9-2]
DR Antibodypedia; 30172; 99 antibodies from 25 providers.
DR DNASU; 582; -.
DR Ensembl; ENST00000318312.12; ENSP00000317469.7; ENSG00000174483.20. [Q8NFJ9-1]
DR Ensembl; ENST00000393994.4; ENSP00000377563.2; ENSG00000174483.20. [Q8NFJ9-3]
DR GeneID; 582; -.
DR KEGG; hsa:582; -.
DR MANE-Select; ENST00000318312.12; ENSP00000317469.7; NM_024649.5; NP_078925.3.
DR UCSC; uc001oij.2; human. [Q8NFJ9-1]
DR CTD; 582; -.
DR DisGeNET; 582; -.
DR GeneCards; BBS1; -.
DR GeneReviews; BBS1; -.
DR HGNC; HGNC:966; BBS1.
DR HPA; ENSG00000174483; Low tissue specificity.
DR MalaCards; BBS1; -.
DR MIM; 209900; phenotype.
DR MIM; 209901; gene.
DR neXtProt; NX_Q8NFJ9; -.
DR OpenTargets; ENSG00000174483; -.
DR OpenTargets; ENSG00000256349; -.
DR Orphanet; 110; Bardet-Biedl syndrome.
DR PharmGKB; PA25275; -.
DR VEuPathDB; HostDB:ENSG00000174483; -.
DR eggNOG; ENOG502QS2X; Eukaryota.
DR GeneTree; ENSGT00390000005232; -.
DR HOGENOM; CLU_032988_1_0_1; -.
DR InParanoid; Q8NFJ9; -.
DR OMA; FGTERGM; -.
DR OrthoDB; 783386at2759; -.
DR PhylomeDB; Q8NFJ9; -.
DR TreeFam; TF312892; -.
DR PathwayCommons; Q8NFJ9; -.
DR Reactome; R-HSA-5620922; BBSome-mediated cargo-targeting to cilium.
DR SignaLink; Q8NFJ9; -.
DR SIGNOR; Q8NFJ9; -.
DR BioGRID-ORCS; 582; 19 hits in 1073 CRISPR screens.
DR ChiTaRS; BBS1; human.
DR GeneWiki; BBS1; -.
DR GenomeRNAi; 582; -.
DR Pharos; Q8NFJ9; Tbio.
DR PRO; PR:Q8NFJ9; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q8NFJ9; protein.
DR Bgee; ENSG00000174483; Expressed in right uterine tube and 97 other tissues.
DR ExpressionAtlas; Q8NFJ9; baseline and differential.
DR Genevisible; Q8NFJ9; HS.
DR GO; GO:0005930; C:axoneme; IBA:GO_Central.
DR GO; GO:0034464; C:BBSome; IDA:UniProtKB.
DR GO; GO:0034451; C:centriolar satellite; IEA:Ensembl.
DR GO; GO:0005813; C:centrosome; IDA:SYSCILIA_CCNET.
DR GO; GO:0060170; C:ciliary membrane; IDA:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0031514; C:motile cilium; IEA:Ensembl.
DR GO; GO:0005113; F:patched binding; IPI:MGI.
DR GO; GO:0051219; F:phosphoprotein binding; IEA:Ensembl.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:MGI.
DR GO; GO:0005119; F:smoothened binding; IPI:MGI.
DR GO; GO:0030534; P:adult behavior; IEA:Ensembl.
DR GO; GO:0048854; P:brain morphogenesis; IEA:Ensembl.
DR GO; GO:0051216; P:cartilage development; IEA:Ensembl.
DR GO; GO:0044255; P:cellular lipid metabolic process; IEA:Ensembl.
DR GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR GO; GO:0060271; P:cilium assembly; IMP:BHF-UCL.
DR GO; GO:0016358; P:dendrite development; IEA:Ensembl.
DR GO; GO:0045444; P:fat cell differentiation; IEA:Ensembl.
DR GO; GO:0009566; P:fertilization; IEA:Ensembl.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IMP:MGI.
DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR GO; GO:0042445; P:hormone metabolic process; IEA:Ensembl.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0061351; P:neural precursor cell proliferation; IEA:Ensembl.
DR GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR GO; GO:1905515; P:non-motile cilium assembly; IMP:BHF-UCL.
DR GO; GO:0042048; P:olfactory behavior; IEA:Ensembl.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IMP:BHF-UCL.
DR GO; GO:0008594; P:photoreceptor cell morphogenesis; IEA:Ensembl.
DR GO; GO:0061512; P:protein localization to cilium; IMP:GO_Central.
DR GO; GO:0060296; P:regulation of cilium beat frequency involved in ciliary motility; IEA:Ensembl.
DR GO; GO:0007608; P:sensory perception of smell; IEA:UniProtKB-KW.
DR GO; GO:0021756; P:striatum development; IEA:Ensembl.
DR GO; GO:0021591; P:ventricular system development; IEA:Ensembl.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR InterPro; IPR028784; BBS1.
DR InterPro; IPR032728; BBS1_N.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR PANTHER; PTHR20870; PTHR20870; 1.
DR Pfam; PF14779; BBS1; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Bardet-Biedl syndrome;
KW Cell membrane; Cell projection; Ciliopathy; Cilium;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; Disease variant;
KW Intellectual disability; Membrane; Obesity; Olfaction; Protein transport;
KW Reference proteome; Sensory transduction; Transport; Vision.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..593
FT /note="Bardet-Biedl syndrome 1 protein"
FT /id="PRO_0000064841"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT VAR_SEQ 1..16
FT /note="MAAASSSDSDACGAES -> MDPSWRRSSHSWPQPMPDSGRAPVRPHLAKLE
FT EDVWPCPQFHQTKAASGPPFV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_008854"
FT VAR_SEQ 242..370
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_054152"
FT VAR_SEQ 567..593
FT /note="LVLREGQSAPLLSAHVNMPGSEGLAAA -> GPALVPRGR (in isoform
FT 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_054153"
FT VARIANT 35
FT /note="H -> R (in BBS1; dbSNP:rs775990952)"
FT /evidence="ECO:0000269|PubMed:12677556"
FT /id="VAR_038880"
FT VARIANT 53
FT /note="K -> E (in BBS1; dbSNP:rs766602837)"
FT /evidence="ECO:0000269|PubMed:12677556"
FT /id="VAR_038881"
FT VARIANT 148
FT /note="D -> N (in BBS1; dbSNP:rs200688985)"
FT /evidence="ECO:0000269|PubMed:12677556"
FT /id="VAR_038882"
FT VARIANT 160
FT /note="R -> Q (in BBS1; dbSNP:rs376894444)"
FT /evidence="ECO:0000269|PubMed:15770229,
FT ECO:0000269|PubMed:21344540"
FT /id="VAR_038883"
FT VARIANT 200..201
FT /note="Missing (in BBS1)"
FT /evidence="ECO:0000269|PubMed:12524598"
FT /id="VAR_017214"
FT VARIANT 206
FT /note="L -> V (in a patient with Bardet-Biedl syndrome;
FT dbSNP:rs146052054)"
FT /evidence="ECO:0000269|PubMed:21052717"
FT /id="VAR_066485"
FT VARIANT 234
FT /note="E -> K (in BBS1; dbSNP:rs35520756)"
FT /evidence="ECO:0000269|PubMed:12567324,
FT ECO:0000269|PubMed:12677556"
FT /id="VAR_017215"
FT VARIANT 245
FT /note="P -> L (in a patient with Bardet-Biedl syndrome;
FT dbSNP:rs151203205)"
FT /evidence="ECO:0000269|PubMed:21052717"
FT /id="VAR_066486"
FT VARIANT 305
FT /note="G -> S (in BBS1; dbSNP:rs942862410)"
FT /evidence="ECO:0000269|PubMed:12677556"
FT /id="VAR_038884"
FT VARIANT 330
FT /note="I -> T (in BBS1)"
FT /evidence="ECO:0000269|PubMed:21344540"
FT /id="VAR_066278"
FT VARIANT 389
FT /note="Missing (in BBS1)"
FT /evidence="ECO:0000269|PubMed:12677556"
FT /id="VAR_038885"
FT VARIANT 390
FT /note="M -> R (in BBS1; dbSNP:rs113624356)"
FT /evidence="ECO:0000269|PubMed:12118255,
FT ECO:0000269|PubMed:12524598, ECO:0000269|PubMed:12677556,
FT ECO:0000269|PubMed:12920096, ECO:0000269|PubMed:15770229,
FT ECO:0000269|PubMed:21052717, ECO:0000269|PubMed:21344540"
FT /id="VAR_017216"
FT VARIANT 434
FT /note="Y -> S (in BBS1)"
FT /id="VAR_038886"
FT VARIANT 503
FT /note="L -> H (in BBS1; dbSNP:rs778225393)"
FT /evidence="ECO:0000269|PubMed:12677556"
FT /id="VAR_038887"
FT VARIANT 518
FT /note="L -> P (in BBS1; dbSNP:rs121917778)"
FT /evidence="ECO:0000269|PubMed:12524598,
FT ECO:0000269|PubMed:12920096"
FT /id="VAR_017217"
FT VARIANT 518
FT /note="L -> Q (in BBS1)"
FT /evidence="ECO:0000269|PubMed:12677556"
FT /id="VAR_038888"
FT VARIANT 524
FT /note="Missing (in BBS1; dbSNP:rs863224782)"
FT /evidence="ECO:0000269|PubMed:21344540"
FT /id="VAR_066279"
FT VARIANT 559
FT /note="G -> D (in a patient with Meckel-Gruber like
FT syndrome also carrying L-753 in TTC21B and a variant in
FT CC2D2A; dbSNP:rs544767888)"
FT /evidence="ECO:0000269|PubMed:21258341"
FT /id="VAR_065554"
SQ SEQUENCE 593 AA; 65083 MW; 94C0C05667FE582D CRC64;
MAAASSSDSD ACGAESNEAN SKWLDAHYDP MANIHTFSAC LALADLHGDG EYKLVVGDLG
PGGQQPRLKV LKGPLVMTES PLPALPAAAA TFLMEQHEPR TPALALASGP CVYVYKNLRP
YFKFSLPQLP PNPLEQDLWN QAKEDRIDPL TLKEMLESIR ETAEEPLSIQ SLRFLQLELS
EMEAFVNQHK SNSIKRQTVI TTMTTLKKNL ADEDAVSCLV LGTENKELLV LDPEAFTILA
KMSLPSVPVF LEVSGQFDVE FRLAAACRNG NIYILRRDSK HPKYCIELSA QPVGLIRVHK
VLVVGSTQDS LHGFTHKGKK LWTVQMPAAI LTMNLLEQHS RGLQAVMAGL ANGEVRIYRD
KALLNVIHTP DAVTSLCFGR YGREDNTLIM TTRGGGLIIK ILKRTAVFVE GGSEVGPPPA
QAMKLNVPRK TRLYVDQTLR EREAGTAMHR AFQTDLYLLR LRAARAYLQA LESSLSPLST
TAREPLKLHA VVQGLGPTFK LTLHLQNTST TRPVLGLLVC FLYNEALYSL PRAFFKVPLL
VPGLNYPLET FVESLSNKGI SDIIKVLVLR EGQSAPLLSA HVNMPGSEGL AAA
