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Bardet-Biedl syndrome 2 protein

 BBS2_HUMAN              Reviewed;         721 AA.
Q9BXC9; Q96CM0; Q96SN9;
02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
12-SEP-2018, entry version 153.
RecName: Full=Bardet-Biedl syndrome 2 protein;
Name=BBS2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], VARIANT BBS2 GLY-75, AND VARIANT VAL-123.
PubMed=11285252; DOI=10.1093/hmg/10.8.865;
Nishimura D.Y., Searby C.C., Carmi R., Elbedour K., Van Maldergem L.,
Fulton A.B., Lam B.L., Powell B.R., Swiderski R.E., Bugge K.E.,
Haider N.B., Kwitek-Black A.E., Ying L., Duhl D.M., Gorman S.M.,
Heon E., Iannaccone A., Bonneau D., Biesecker L.G., Jacobson S.G.,
Stone E.M., Sheffield V.C.;
"Positional cloning of a novel gene on chromosome 16q causing Bardet-
Biedl syndrome (BBS2).";
Hum. Mol. Genet. 10:865-874(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-122.
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INVOLVEMENT IN BBS2, AND VARIANT BBS2 VAL-139.
PubMed=16823392; DOI=10.1038/sj.ejhg.5201688;
Laurier V., Stoetzel C., Muller J., Thibault C., Corbani S., Jalkh N.,
Salem N., Chouery E., Poch O., Licaire S., Danse J.M.,
Amati-Bonneau P., Bonneau D., Megarbane A., Mandel J.L., Dollfus H.;
"Pitfalls of homozygosity mapping: an extended consanguineous Bardet-
Biedl syndrome family with two mutant genes (BBS2, BBS10), three
mutations, but no triallelism.";
Eur. J. Hum. Genet. 14:1195-1203(2006).
[5]
INTERACTION WITH CCDC28B.
PubMed=16327777; DOI=10.1038/nature04370;
Badano J.L., Leitch C.C., Ansley S.J., May-Simera H., Lawson S.,
Lewis R.A., Beales P.L., Dietz H.C., Fisher S., Katsanis N.;
"Dissection of epistasis in oligogenic Bardet-Biedl syndrome.";
Nature 439:326-330(2006).
[6]
IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, FUNCTION, AND
SUBCELLULAR LOCATION.
PubMed=17574030; DOI=10.1016/j.cell.2007.03.053;
Nachury M.V., Loktev A.V., Zhang Q., Westlake C.J., Peraenen J.,
Merdes A., Slusarski D.C., Scheller R.H., Bazan J.F., Sheffield V.C.,
Jackson P.K.;
"A core complex of BBS proteins cooperates with the GTPase Rab8 to
promote ciliary membrane biogenesis.";
Cell 129:1201-1213(2007).
[7]
INTERACTION WITH ALDOB.
PubMed=18000879; DOI=10.1002/cm.20250;
Oeffner F., Moch C., Neundorf A., Hofmann J., Koch M., Grzeschik K.H.;
"Novel interaction partners of Bardet-Biedl syndrome proteins.";
Cell Motil. Cytoskeleton 65:143-155(2008).
[8]
INTERACTION WITH BBS7 AND MKKS.
PubMed=20080638; DOI=10.1073/pnas.0910268107;
Seo S., Baye L.M., Schulz N.P., Beck J.S., Zhang Q., Slusarski D.C.,
Sheffield V.C.;
"BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family
chaperonins and mediate BBSome assembly.";
Proc. Natl. Acad. Sci. U.S.A. 107:1488-1493(2010).
[9]
FUNCTION, FUNCTION OF THE BBSOME COMPLEX, IDENTIFICATION IN THE BBSOME
COMPLEX, AND SUBCELLULAR LOCATION.
PubMed=22072986; DOI=10.1371/journal.pgen.1002358;
Seo S., Zhang Q., Bugge K., Breslow D.K., Searby C.C., Nachury M.V.,
Sheffield V.C.;
"A novel protein LZTFL1 regulates ciliary trafficking of the BBSome
and Smoothened.";
PLoS Genet. 7:E1002358-E1002358(2011).
[10]
INVOLVEMENT IN RP74, AND VARIANTS RP74 ASP-33; ALA-104; ARG-134 AND
PRO-632.
PubMed=25541840; DOI=10.1001/jamaophthalmol.2014.5251;
Shevach E., Ali M., Mizrahi-Meissonnier L., McKibbin M., El-Asrag M.,
Watson C.M., Inglehearn C.F., Ben-Yosef T., Blumenfeld A., Jalas C.,
Banin E., Sharon D.;
"Association between missense mutations in the BBS2 gene and
nonsyndromic retinitis pigmentosa.";
JAMA Ophthalmol. 133:312-318(2015).
[11]
VARIANTS BBS2 SER-70; ALA-104; GLN-315; TRP-315; ILE-558 AND PRO-632.
PubMed=11567139; DOI=10.1126/science.1063525;
Katsanis N., Ansley S.J., Badano J.L., Eichers E.R., Lewis R.A.,
Hoskins B.E., Scambler P.J., Davidson W.S., Beales P.L., Lupski J.R.;
"Triallelic inheritance in Bardet-Biedl syndrome, a Mendelian
recessive disorder.";
Science 293:2256-2259(2001).
[12]
VARIANTS BBS2 GLN-315 AND TRP-349.
PubMed=12677556; DOI=10.1086/375178;
Beales P.L., Badano J.L., Ross A.J., Ansley S.J., Hoskins B.E.,
Kirsten B., Mein C.A., Froguel P., Scambler P.J., Lewis R.A.,
Lupski J.R., Katsanis N.;
"Genetic interaction of BBS1 mutations with alleles at other BBS loci
can result in non-Mendelian Bardet-Biedl syndrome.";
Am. J. Hum. Genet. 72:1187-1199(2003).
[13]
VARIANT BBS2 GLU-174.
PubMed=12872256; DOI=10.1002/humu.10241;
Hoskins B.E., Thorn A., Scambler P.J., Beales P.L.;
"Evaluation of multiplex capillary heteroduplex analysis: a rapid and
sensitive mutation screening technique.";
Hum. Mutat. 22:151-157(2003).
[14]
VARIANT BBS2 HIS-643.
PubMed=12920096; DOI=10.1136/jmg.40.8.e104;
Fauser S., Munz M., Besch D.;
"Further support for digenic inheritance in Bardet-Biedl syndrome.";
J. Med. Genet. 40:E104-E104(2003).
[15]
VARIANT BBS2 PRO-23, AND VARIANT VAL-123.
PubMed=15666242; DOI=10.1086/428679;
Karmous-Benailly H., Martinovic J., Gubler M.-C., Sirot Y., Clech L.,
Ozilou C., Auge J., Brahimi N., Etchevers H., Detrait E.,
Esculpavit C., Audollent S., Goudefroye G., Gonzales M., Tantau J.,
Loget P., Joubert M., Gaillard D., Jeanne-Pasquier C.,
Delezoide A.-L., Peter M.-O., Plessis G., Simon-Bouy B., Dollfus H.,
Le Merrer M., Munnich A., Encha-Razavi F., Vekemans M.,
Attie-Bitach T.;
"Antenatal presentation of Bardet-Biedl syndrome may mimic Meckel
syndrome.";
Am. J. Hum. Genet. 76:493-504(2005).
[16]
VARIANT VAL-123.
PubMed=15770229; DOI=10.1038/sj.ejhg.5201372;
Hichri H., Stoetzel C., Laurier V., Caron S., Sigaudy S., Sarda P.,
Hamel C., Martin-Coignard D., Gilles M., Leheup B., Holder M.,
Kaplan J., Bitoun P., Lacombe D., Verloes A., Bonneau D.,
Perrin-Schmitt F., Brandt C., Besancon A.-F., Mandel J.-L., Cossee M.,
Dollfus H.;
"Testing for triallelism: analysis of six BBS genes in a Bardet-Biedl
syndrome family cohort.";
Eur. J. Hum. Genet. 13:607-616(2005).
[17]
VARIANT LYS-629.
PubMed=20120035; DOI=10.1002/humu.21204;
Hjortshoj T.D., Gronskov K., Philp A.R., Nishimura D.Y., Riise R.,
Sheffield V.C., Rosenberg T., Brondum-Nielsen K.;
"Bardet-Biedl syndrome in Denmark -- report of 13 novel sequence
variations in six genes.";
Hum. Mutat. 31:429-436(2010).
[18]
VARIANTS BBS2 CYS-81; ALA-104; ARG-125; PRO-136; TRP-307; CYS-317 AND
PRO-632.
PubMed=21344540; DOI=10.1002/humu.21480;
Deveault C., Billingsley G., Duncan J.L., Bin J., Theal R.,
Vincent A., Fieggen K.J., Gerth C., Noordeh N., Traboulsi E.I.,
Fishman G.A., Chitayat D., Knueppel T., Millan J.M., Munier F.L.,
Kennedy D., Jacobson S.G., Innes A.M., Mitchell G.A., Boycott K.,
Heon E.;
"BBS genotype-phenotype assessment of a multiethnic patient cohort
calls for a revision of the disease definition.";
Hum. Mutat. 32:610-619(2011).
-!- FUNCTION: The BBSome complex is thought to function as a coat
complex required for sorting of specific membrane proteins to the
primary cilia. The BBSome complex is required for ciliogenesis but
is dispensable for centriolar satellite function. This ciliogenic
function is mediated in part by the Rab8 GDP/GTP exchange factor,
which localizes to the basal body and contacts the BBSome.
Rab8(GTP) enters the primary cilium and promotes extension of the
ciliary membrane. Firstly the BBSome associates with the ciliary
membrane and binds to RAB3IP/Rabin8, the guanosyl exchange factor
(GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and
promotes docking and fusion of carrier vesicles to the base of the
ciliary membrane. The BBSome complex, together with the LTZL1,
controls SMO ciliary trafficking and contributes to the sonic
hedgehog (SHH) pathway regulation. Required for proper BBSome
complex assembly and its ciliary localization.
{ECO:0000269|PubMed:17574030, ECO:0000269|PubMed:22072986}.
-!- SUBUNIT: Part of BBSome complex, that contains BBS1, BBS2, BBS4,
BBS5, BBS7, BBS8/TTC8, BBS9 and BBIP10. Interacts (via C-terminus)
with BBS7. Interacts (via coiled coil domain) with MKKS. Interacts
with CCDC28B and ALDOB. {ECO:0000269|PubMed:16327777,
ECO:0000269|PubMed:17574030, ECO:0000269|PubMed:18000879,
ECO:0000269|PubMed:20080638, ECO:0000269|PubMed:22072986}.
-!- INTERACTION:
P05062:ALDOB; NbExp=4; IntAct=EBI-748297, EBI-1045507;
Q8NFJ9:BBS1; NbExp=8; IntAct=EBI-748297, EBI-1805484;
Q8IWZ6:BBS7; NbExp=13; IntAct=EBI-748297, EBI-1806001;
Q3SYG4:BBS9; NbExp=10; IntAct=EBI-748297, EBI-2826852;
O15078:CEP290; NbExp=3; IntAct=EBI-748297, EBI-1811944;
Q15051:IQCB1; NbExp=8; IntAct=EBI-748297, EBI-2805823;
Q99750:MDFI; NbExp=5; IntAct=EBI-748297, EBI-724076;
Q9NPJ1:MKKS; NbExp=4; IntAct=EBI-748297, EBI-721319;
P61289:PSME3; NbExp=6; IntAct=EBI-748297, EBI-355546;
Q93062:RBPMS; NbExp=3; IntAct=EBI-748297, EBI-740322;
-!- SUBCELLULAR LOCATION: Cell projection, cilium membrane. Cytoplasm.
Cytoplasm, cytoskeleton, microtubule organizing center,
centrosome, centriolar satellite.
-!- TISSUE SPECIFICITY: Widely expressed.
-!- DISEASE: Bardet-Biedl syndrome 2 (BBS2) [MIM:615981]: A syndrome
characterized by usually severe pigmentary retinopathy, early-
onset obesity, polydactyly, hypogenitalism, renal malformation and
mental retardation. Secondary features include diabetes mellitus,
hypertension and congenital heart disease. Bardet-Biedl syndrome
inheritance is autosomal recessive, but three mutated alleles (two
at one locus, and a third at a second locus) may be required for
clinical manifestation of some forms of the disease.
{ECO:0000269|PubMed:11285252, ECO:0000269|PubMed:11567139,
ECO:0000269|PubMed:12677556, ECO:0000269|PubMed:12872256,
ECO:0000269|PubMed:12920096, ECO:0000269|PubMed:15666242,
ECO:0000269|PubMed:16823392, ECO:0000269|PubMed:21344540}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Retinitis pigmentosa 74 (RP74) [MIM:616562]: A retinal
dystrophy belonging to the group of pigmentary retinopathies.
Retinitis pigmentosa is characterized by retinal pigment deposits
visible on fundus examination and primary loss of rod
photoreceptor cells followed by secondary loss of cone
photoreceptors. Patients typically have night vision blindness and
loss of midperipheral visual field. As their condition progresses,
they lose their far peripheral visual field and eventually central
vision as well. {ECO:0000269|PubMed:25541840}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- WEB RESOURCE: Name=Mutations of the BBS2 gene; Note=Retina
International's Scientific Newsletter;
URL="http://www.retina-international.org/files/sci-news/bbs2mut.htm";
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EMBL; AF342736; AAK28552.1; -; mRNA.
EMBL; AK027635; BAB55252.1; -; mRNA.
EMBL; BC014140; AAH14140.1; -; mRNA.
CCDS; CCDS32451.1; -.
RefSeq; NP_114091.3; NM_031885.3.
UniGene; Hs.333738; -.
ProteinModelPortal; Q9BXC9; -.
BioGrid; 107059; 30.
ComplexPortal; CPX-1908; BBSome complex.
CORUM; Q9BXC9; -.
DIP; DIP-46563N; -.
IntAct; Q9BXC9; 43.
STRING; 9606.ENSP00000245157; -.
iPTMnet; Q9BXC9; -.
PhosphoSitePlus; Q9BXC9; -.
BioMuta; BBS2; -.
DMDM; 20454827; -.
EPD; Q9BXC9; -.
MaxQB; Q9BXC9; -.
PaxDb; Q9BXC9; -.
PeptideAtlas; Q9BXC9; -.
PRIDE; Q9BXC9; -.
ProteomicsDB; 79404; -.
DNASU; 583; -.
Ensembl; ENST00000245157; ENSP00000245157; ENSG00000125124.
GeneID; 583; -.
KEGG; hsa:583; -.
UCSC; uc002ejd.3; human.
CTD; 583; -.
DisGeNET; 583; -.
EuPathDB; HostDB:ENSG00000125124.11; -.
GeneCards; BBS2; -.
GeneReviews; BBS2; -.
HGNC; HGNC:967; BBS2.
HPA; HPA041315; -.
MalaCards; BBS2; -.
MIM; 606151; gene.
MIM; 615981; phenotype.
MIM; 616562; phenotype.
neXtProt; NX_Q9BXC9; -.
Orphanet; 110; Bardet-Biedl syndrome.
PharmGKB; PA25276; -.
eggNOG; ENOG410IF6W; Eukaryota.
eggNOG; ENOG410XPDF; LUCA.
HOGENOM; HOG000007549; -.
HOVERGEN; HBG031114; -.
InParanoid; Q9BXC9; -.
KO; K16747; -.
OrthoDB; EOG091G03EK; -.
PhylomeDB; Q9BXC9; -.
TreeFam; TF313236; -.
Reactome; R-HSA-5620922; BBSome-mediated cargo-targeting to cilium.
ChiTaRS; BBS2; human.
GeneWiki; BBS2; -.
GenomeRNAi; 583; -.
PRO; PR:Q9BXC9; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000125124; Expressed in 199 organ(s), highest expression level in adrenal tissue.
CleanEx; HS_BBS2; -.
ExpressionAtlas; Q9BXC9; baseline and differential.
Genevisible; Q9BXC9; HS.
GO; GO:0034464; C:BBSome; IDA:UniProtKB.
GO; GO:0036064; C:ciliary basal body; IDA:BHF-UCL.
GO; GO:0060170; C:ciliary membrane; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016020; C:membrane; IBA:GO_Central.
GO; GO:0005902; C:microvillus; IEA:Ensembl.
GO; GO:0031514; C:motile cilium; IDA:BHF-UCL.
GO; GO:0032420; C:stereocilium; IEA:Ensembl.
GO; GO:0001103; F:RNA polymerase II repressing transcription factor binding; IPI:MGI.
GO; GO:0030534; P:adult behavior; ISS:BHF-UCL.
GO; GO:0014824; P:artery smooth muscle contraction; IEA:Ensembl.
GO; GO:0048854; P:brain morphogenesis; ISS:BHF-UCL.
GO; GO:0051216; P:cartilage development; IEA:Ensembl.
GO; GO:0021987; P:cerebral cortex development; ISS:BHF-UCL.
GO; GO:0060271; P:cilium assembly; ISS:BHF-UCL.
GO; GO:0045444; P:fat cell differentiation; ISS:BHF-UCL.
GO; GO:0043001; P:Golgi to plasma membrane protein transport; IMP:MGI.
GO; GO:0021766; P:hippocampus development; ISS:BHF-UCL.
GO; GO:0032402; P:melanosome transport; ISS:BHF-UCL.
GO; GO:0038108; P:negative regulation of appetite by leptin-mediated signaling pathway; ISS:BHF-UCL.
GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
GO; GO:0040015; P:negative regulation of multicellular organism growth; ISS:BHF-UCL.
GO; GO:1905515; P:non-motile cilium assembly; IEA:Ensembl.
GO; GO:0045494; P:photoreceptor cell maintenance; ISS:BHF-UCL.
GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:Ensembl.
GO; GO:0008104; P:protein localization; ISS:BHF-UCL.
GO; GO:1903441; P:protein localization to ciliary membrane; IBA:GO_Central.
GO; GO:0033365; P:protein localization to organelle; ISS:BHF-UCL.
GO; GO:0060296; P:regulation of cilium beat frequency involved in ciliary motility; ISS:BHF-UCL.
GO; GO:0007288; P:sperm axoneme assembly; ISS:BHF-UCL.
GO; GO:0021756; P:striatum development; ISS:BHF-UCL.
GO; GO:0042311; P:vasodilation; IEA:Ensembl.
GO; GO:0007601; P:visual perception; IMP:UniProtKB.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR016616; Bardet-Biedl_syndrome_2_prot.
InterPro; IPR029333; BBS2_C.
InterPro; IPR029429; BBS2_Mid.
InterPro; IPR029430; BBS2_N.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF14782; BBS2_C; 1.
Pfam; PF14783; BBS2_Mid; 1.
Pfam; PF14781; BBS2_N; 1.
PIRSF; PIRSF013684; BBS2; 1.
SUPFAM; SSF50978; SSF50978; 2.
1: Evidence at protein level;
Bardet-Biedl syndrome; Cell membrane; Cell projection; Ciliopathy;
Cilium; Cilium biogenesis/degradation; Coiled coil; Complete proteome;
Cytoplasm; Cytoskeleton; Disease mutation; Membrane;
Mental retardation; Obesity; Polymorphism; Protein transport;
Reference proteome; Retinitis pigmentosa; Sensory transduction;
Transport; Vision.
CHAIN 1 721 Bardet-Biedl syndrome 2 protein.
/FTId=PRO_0000064843.
COILED 325 369 {ECO:0000255}.
VARIANT 23 23 R -> P (in BBS2).
{ECO:0000269|PubMed:15666242}.
/FTId=VAR_038889.
VARIANT 33 33 A -> D (in RP74).
{ECO:0000269|PubMed:25541840}.
/FTId=VAR_075726.
VARIANT 70 70 N -> S (in BBS2; dbSNP:rs4784677).
{ECO:0000269|PubMed:11567139}.
/FTId=VAR_013162.
VARIANT 75 75 V -> G (in BBS2; in linkage
disequilibrium with V-123 in a Bedouin
kindred). {ECO:0000269|PubMed:11285252}.
/FTId=VAR_013163.
VARIANT 81 81 G -> C (in BBS2).
{ECO:0000269|PubMed:21344540}.
/FTId=VAR_066280.
VARIANT 104 104 D -> A (in BBS2 and RP74).
{ECO:0000269|PubMed:11567139,
ECO:0000269|PubMed:21344540,
ECO:0000269|PubMed:25541840}.
/FTId=VAR_013164.
VARIANT 122 122 A -> V (in dbSNP:rs17856449).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_029747.
VARIANT 123 123 I -> V (polymorphism in linkage
disequilibrium with G-75 in a Bedouin
kindred; dbSNP:rs11373).
{ECO:0000269|PubMed:11285252,
ECO:0000269|PubMed:15666242,
ECO:0000269|PubMed:15770229}.
/FTId=VAR_013165.
VARIANT 125 125 L -> R (in BBS2).
{ECO:0000269|PubMed:21344540}.
/FTId=VAR_066281.
VARIANT 134 134 P -> R (in RP74).
{ECO:0000269|PubMed:25541840}.
/FTId=VAR_075727.
VARIANT 136 136 A -> P (in BBS2).
{ECO:0000269|PubMed:21344540}.
/FTId=VAR_066282.
VARIANT 139 139 G -> V (in BBS2).
{ECO:0000269|PubMed:16823392}.
/FTId=VAR_075728.
VARIANT 174 174 D -> E (in BBS2).
{ECO:0000269|PubMed:12872256}.
/FTId=VAR_038890.
VARIANT 307 307 C -> W (in BBS2).
{ECO:0000269|PubMed:21344540}.
/FTId=VAR_066283.
VARIANT 315 315 R -> Q (in BBS2).
{ECO:0000269|PubMed:11567139,
ECO:0000269|PubMed:12677556}.
/FTId=VAR_013166.
VARIANT 315 315 R -> W (in BBS2).
{ECO:0000269|PubMed:11567139}.
/FTId=VAR_013167.
VARIANT 317 317 Y -> C (in BBS2).
{ECO:0000269|PubMed:21344540}.
/FTId=VAR_066284.
VARIANT 349 349 L -> W (in BBS2; has a modifier effect on
BBS). {ECO:0000269|PubMed:12677556}.
/FTId=VAR_038891.
VARIANT 504 504 A -> V (in dbSNP:rs16957538).
/FTId=VAR_029748.
VARIANT 558 558 T -> I (in BBS2).
{ECO:0000269|PubMed:11567139}.
/FTId=VAR_013168.
VARIANT 629 629 E -> K (in a patient with Bardet-Biedl
syndrome compound heterozygote for
mutations in BBS10; uncertain
pathological role).
{ECO:0000269|PubMed:20120035}.
/FTId=VAR_066285.
VARIANT 632 632 R -> P (in BBS2 and RP74).
{ECO:0000269|PubMed:11567139,
ECO:0000269|PubMed:21344540,
ECO:0000269|PubMed:25541840}.
/FTId=VAR_013169.
VARIANT 643 643 R -> H (in BBS2).
{ECO:0000269|PubMed:12920096}.
/FTId=VAR_038892.
CONFLICT 63 63 E -> G (in Ref. 2; BAB55252).
{ECO:0000305}.
CONFLICT 169 169 C -> R (in Ref. 2; BAB55252).
{ECO:0000305}.
CONFLICT 457 457 L -> S (in Ref. 2; BAB55252).
{ECO:0000305}.
CONFLICT 648 648 Y -> H (in Ref. 2; BAB55252).
{ECO:0000305}.
SEQUENCE 721 AA; 79871 MW; 8FA1CDAED725BEAF CRC64;
MLLPVFTLKL RHKISPRMVA IGRYDGTHPC LAAATQTGKV FIHNPHTRNQ HVSASRVFQS
PLESDVSLLN 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


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