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Q8N3I7 (BBS5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bardet-Biedl syndrome 5 protein
Gene names
Name:BBS5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length341 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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 BBSome complex ciliary localization but not for the proper complex assembly. Ref.7 Ref.8

Subunit structure

Part of BBSome complex, that contains BBS1, BBS2, BBS4, BBS5, BBS7, BBS8/TTC8, BBS9 and BBIP10. Binds to phosphoinositides. Interacts with CCDC28B. Interacts with SMO; the interaction is indicative for the association of SMO with the BBsome complex to facilitate ciliary localization of SMO. Ref.6 Ref.7 Ref.8

Subcellular location

Cell projectioncilium membrane. Cytoplasm. Cytoplasmcytoskeletoncilium basal body By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriolar satellite. Note: Localizes to basal bodies By similarity. Ref.7 Ref.8

Involvement in disease

Bardet-Biedl syndrome 5 (BBS5) [MIM:209900]: 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.9

Miscellaneous

BBS5 may interact genetically with BBS1.

Sequence similarities

Belongs to the BBS5 family.

Ontologies

Keywords
   Biological processCilium biogenesis/degradation
Protein transport
Sensory transduction
Transport
Vision
   Cellular componentCell membrane
Cell projection
Cilium
Cytoplasm
Cytoskeleton
Membrane
   Coding sequence diversityAlternative splicing
   DiseaseBardet-Biedl syndrome
Ciliopathy
Disease mutation
Mental retardation
Obesity
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcilium assembly

Inferred from mutant phenotype Ref.7. Source: BHF-UCL

heart looping

Inferred from sequence or structural similarity. Source: BHF-UCL

melanosome transport

Inferred from sequence or structural similarity. Source: BHF-UCL

motile cilium assembly

Inferred from sequence or structural similarity. Source: BHF-UCL

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

response to stimulus

Inferred from electronic annotation. Source: UniProtKB-KW

visual perception

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentBBSome

Inferred from direct assay PubMed 24550735. Source: UniProtKB

ciliary basal body

Inferred from sequence or structural similarity. Source: BHF-UCL

ciliary membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

intracellular

Inferred from direct assay. Source: LIFEdb

   Molecular_functionRNA polymerase II repressing transcription factor binding

Inferred from physical interaction PubMed 22302990. Source: MGI

phosphatidylinositol-3-phosphate binding

Inferred from direct assay Ref.7. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.6PubMed 24550735. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

BBS9Q3SYG43EBI-2892592,EBI-2826852

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8N3I7-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8N3I7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     207-227: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 341341Bardet-Biedl syndrome 5 protein
PRO_0000223254

Natural variations

Alternative sequence207 – 22721Missing in isoform 2.
VSP_017240
Natural variant721G → S in BBS5. Ref.9
VAR_066290
Natural variant1841N → S Found in patients with Bardet-Biedl syndrome carrying homozygous mutations in other BBS genes; might have a modifying effect on disease phenotype. Ref.1 Ref.9
Corresponds to variant rs150063999 [ dbSNP | Ensembl ].
VAR_025316
Natural variant2071R → H Found as heterozygous variant in patients with Bardet-Biedl syndrome; might have a modifying effect on disease phenotype. Ref.1
Corresponds to variant rs35487251 [ dbSNP | Ensembl ].
VAR_025317
Natural variant2511N → D. Ref.9
Corresponds to variant rs143113298 [ dbSNP | Ensembl ].
VAR_066291

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 63D67D877FDFD25B

FASTA34138,755
        10         20         30         40         50         60 
MSVLDALWED RDVRFDLSAQ QMKTRPGEVL IDCLDSIEDT KGNNGDRGRL LVTNLRILWH 

        70         80         90        100        110        120 
SLALSRVNVS VGYNCILNIT TRTANSKLRG QTEALYILTK CNSTRFEFIF TNLVPGSPRL 

       130        140        150        160        170        180 
FTSVMAVHRA YETSKMYRDF KLRSALIQNK QLRLLPQEHV YDKINGVWNL SSDQGNLGTF 

       190        200        210        220        230        240 
FITNVRIVWH ANMNDSFNVS IPYLQIRSIK IRDSKFGLAL VIESSQQSGG YVLGFKIDPV 

       250        260        270        280        290        300 
EKLQESVKEI NSLHKVYSAS PIFGVDYEME EKPQPLEALT VEQIQDDVEI DSDGHTDAFV 

       310        320        330        340 
AYFADGNKQQ DREPVFSEEL GLAIEKLKDG FTLQGLWEVM S 

« Hide

Isoform 2 [UniParc].

Checksum: 843BC731AE686410
Show »

FASTA32036,397

References

« Hide 'large scale' references
[1]"Comparative genomics identifies a flagellar and basal body proteome that includes the BBS5 human disease gene."
Li J.B., Gerdes J.M., Haycraft C.J., Fan Y., Teslovich T.M., May-Simera H., Li H., Blacque O.E., Li L., Leitch C.C., Lewis R.A., Green J.S., Parfrey P.S., Leroux M.R., Davidson W.S., Beales P.L., Guay-Woodford L.M., Yoder B.K. expand/collapse author list , Stormo G.D., Katsanis N., Dutcher S.K.
Cell 117:541-552(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INVOLVEMENT IN BBS5, VARIANTS SER-184 AND HIS-207.
[2]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Melanoma.
[3]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Testis.
[6]"Dissection of epistasis in oligogenic Bardet-Biedl syndrome."
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.
Nature 439:326-330(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CCDC28B.
[7]"A core complex of BBS proteins cooperates with the GTPase Rab8 to promote ciliary membrane biogenesis."
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.
Cell 129:1201-1213(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, FUNCTION, SUBCELLULAR LOCATION, BINDING TO PHOSPHOINOSITIDES.
[8]"A novel protein LZTFL1 regulates ciliary trafficking of the BBSome and Smoothened."
Seo S., Zhang Q., Bugge K., Breslow D.K., Searby C.C., Nachury M.V., Sheffield V.C.
PLoS Genet. 7:E1002358-E1002358(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, FUNCTION OF THE BBSOME COMPLEX, IDENTIFICATION IN THE BBSOME COMPLEX, INTERACTION WITH SMO, SUBCELLULAR LOCATION.
[9]"BBS genotype-phenotype assessment of a multiethnic patient cohort calls for a revision of the disease definition."
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. expand/collapse author list , Mitchell G.A., Boycott K., Heon E.
Hum. Mutat. 32:610-619(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BBS5 SER-72, VARIANTS SER-184 AND ASP-251.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY604003 mRNA. Translation: AAT08182.1.
AY604004 mRNA. Translation: AAT08183.1.
AL834305 mRNA. Translation: CAD38975.1.
AC093899 Genomic DNA. Translation: AAY24116.1.
CH471058 Genomic DNA. Translation: EAX11276.1.
CH471058 Genomic DNA. Translation: EAX11279.1.
BC044593 mRNA. Translation: AAH44593.1.
CCDSCCDS2233.1. [Q8N3I7-1]
RefSeqNP_689597.1. NM_152384.2. [Q8N3I7-1]
UniGeneHs.233398.

3D structure databases

ProteinModelPortalQ8N3I7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-60357N.
IntActQ8N3I7. 8 interactions.
MINTMINT-3039679.
STRING9606.ENSP00000295240.

PTM databases

PhosphoSiteQ8N3I7.

Polymorphism databases

DMDM74750959.

Proteomic databases

MaxQBQ8N3I7.
PaxDbQ8N3I7.
PRIDEQ8N3I7.

Protocols and materials databases

DNASU129880.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000295240; ENSP00000295240; ENSG00000163093. [Q8N3I7-1]
ENST00000392663; ENSP00000376431; ENSG00000163093. [Q8N3I7-2]
GeneID129880.
KEGGhsa:129880.
UCSCuc002uet.3. human. [Q8N3I7-1]
uc010fpw.3. human. [Q8N3I7-2]

Organism-specific databases

CTD129880.
GeneCardsGC02P170335.
GeneReviewsBBS5.
HGNCHGNC:970. BBS5.
HPAHPA036416.
MIM209900. phenotype.
603650. gene.
neXtProtNX_Q8N3I7.
Orphanet110. Bardet-Biedl syndrome.
PharmGKBPA25279.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG82102.
HOGENOMHOG000231964.
HOVERGENHBG053449.
InParanoidQ8N3I7.
KOK16748.
OMAELGFAME.
OrthoDBEOG7NCV3S.
PhylomeDBQ8N3I7.
TreeFamTF106129.

Gene expression databases

BgeeQ8N3I7.
CleanExHS_BBS5.
GenevestigatorQ8N3I7.

Family and domain databases

InterProIPR006606. BBL5.
[Graphical view]
PANTHERPTHR21351. PTHR21351. 1 hit.
PfamPF07289. DUF1448. 1 hit.
[Graphical view]
PIRSFPIRSF010072. DUF1448. 1 hit.
ProtoNetSearch...

Other

GeneWikiBBS5.
GenomeRNAi129880.
NextBio82665.
PROQ8N3I7.
SOURCESearch...

Entry information

Entry nameBBS5_HUMAN
AccessionPrimary (citable) accession number: Q8N3I7
Secondary accession number(s): D3DPC3, Q6PKN0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: October 1, 2002
Last modified: July 9, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM