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Q96RK4 (BBS4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 132. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bardet-Biedl syndrome 4 protein
Gene names
Name:BBS4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length519 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 proper BBSome complex assembly and its ciliary localization. Required for microtubule anchoring at the centrosome but not for microtubule nucleation. May be required for the dynein-mediated transport of pericentriolar proteins to the centrosome. Ref.7 Ref.10 Ref.11

Subunit structure

Part of BBSome complex, that contains BBS1, BBS2, BBS4, BBS5, BBS7, BBS8/TTC8, BBS9 and BBIP10. Interacts with PCM1 and DCTN1. Interacts with DC28B. Interacts with ALDOB. Ref.6 Ref.7 Ref.8 Ref.10 Ref.11

Subcellular location

Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytoskeleton. Cell projectioncilium membrane. Cytoplasm. Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriolar satellite. Cell projectionciliumflagellum By similarity. Note: Localizes to the pericentriolar region throughout the cell cycle. Centrosomal localization requires dynein. Ref.7 Ref.10

Tissue specificity

Ubiquitously expressed. The highest level of expression is found in the kidney.

Involvement in disease

Bardet-Biedl syndrome 4 (BBS4) [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 Ref.12 Ref.13 Ref.14 Ref.15

Sequence similarities

Belongs to the BBS4 family.

Contains 10 TPR repeats.

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
Polymorphism
   DiseaseBardet-Biedl syndrome
Ciliopathy
Disease mutation
Mental retardation
Obesity
   DomainRepeat
TPR repeat
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadult behavior

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

brain morphogenesis

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

centrosome organization

Inferred from mutant phenotype Ref.10. Source: UniProtKB

cerebral cortex development

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

cilium assembly

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

cilium morphogenesis

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

convergent extension involved in gastrulation

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

dendrite development

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

fat cell differentiation

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

heart looping

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

hippocampus development

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

intracellular transport

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

maintenance of protein location in nucleus

Inferred from genetic interaction Ref.10. Source: BHF-UCL

melanosome transport

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

metabolic process

Inferred from mutant phenotype Ref.10. Source: GOC

microtubule anchoring at centrosome

Inferred from mutant phenotype Ref.10. Source: BHF-UCL

microtubule cytoskeleton organization

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

mitotic cytokinesis

Inferred from mutant phenotype Ref.10. Source: BHF-UCL

negative regulation of appetite by leptin-mediated signaling pathway

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

negative regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

negative regulation of systemic arterial blood pressure

Inferred from electronic annotation. Source: Ensembl

neural tube closure

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

nonmotile primary cilium assembly

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

photoreceptor cell maintenance

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

pigment granule aggregation in cell center

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

positive regulation of cilium assembly

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

positive regulation of multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

protein localization to centrosome

Inferred from mutant phenotype Ref.10. Source: BHF-UCL

protein localization to organelle

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

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of cilium beat frequency involved in ciliary motility

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

regulation of cytokinesis

Inferred from mutant phenotype Ref.10. Source: BHF-UCL

regulation of lipid metabolic process

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

retina homeostasis

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

retinal rod cell development

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

sensory perception of smell

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

sensory processing

Traceable author statement PubMed 14520415. Source: BHF-UCL

spermatid development

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

striatum development

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

visual perception

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentBBSome

Inferred from direct assay PubMed 24550735. Source: UniProtKB

centriolar satellite

Inferred from direct assay PubMed 24550735. Source: UniProtKB

centriole

Inferred from direct assay Ref.10. Source: BHF-UCL

centrosome

Inferred from direct assay PubMed 24550735. Source: UniProtKB

ciliary basal body

Inferred from direct assay Ref.10PubMed 18299575. Source: BHF-UCL

ciliary membrane

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

cilium

Inferred from direct assay PubMed 24550735. Source: UniProtKB

motile cilium

Inferred from direct assay PubMed 18299575. Source: BHF-UCL

nonmotile primary cilium

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

pericentriolar material

Inferred from direct assay Ref.10. Source: UniProtKB

   Molecular_functionRNA polymerase II repressing transcription factor binding

Inferred from physical interaction PubMed 22302990. Source: MGI

alpha-tubulin binding

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

beta-tubulin binding

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

dynactin binding

Inferred from direct assay Ref.10. Source: BHF-UCL

microtubule motor activity

Inferred from mutant phenotype Ref.10. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.10Ref.6PubMed 24550735. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96RK4-1)

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: Q96RK4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-8: MAEERVAT → MALTVVPSFSVSGVWK
Note: No experimental confirmation available.
Isoform 3 (identifier: Q96RK4-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-172: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 519519Bardet-Biedl syndrome 4 protein
PRO_0000106263

Regions

Repeat67 – 10034TPR 1
Repeat101 – 13434TPR 2
Repeat135 – 16834TPR 3
Repeat169 – 20133TPR 4
Repeat203 – 23533TPR 5
Repeat237 – 26933TPR 6
Repeat270 – 30334TPR 7
Repeat304 – 33734TPR 8
Repeat339 – 37133TPR 9
Repeat373 – 40836TPR 10
Region1 – 6666Required for localization to centrosomes
Region101 – 337237Interaction with PCM1
Region338 – 519182Required for localization to centrosomes

Natural variations

Alternative sequence1 – 172172Missing in isoform 3.
VSP_047507
Alternative sequence1 – 88MAEERVAT → MALTVVPSFSVSGVWK in isoform 2.
VSP_024410
Natural variant461K → R. Ref.14 Ref.16
Corresponds to variant rs75295839 [ dbSNP | Ensembl ].
VAR_038894
Natural variant611E → K Found in patients with Bardet-Biedl syndrome carrying mutations in other BBS genes; uncertain pathological role. Ref.16
VAR_066287
Natural variant1651N → H in BBS4. Ref.9
VAR_017049
Natural variant2681E → K.
Corresponds to variant rs11638283 [ dbSNP | Ensembl ].
VAR_028722
Natural variant2951R → P in BBS4. Ref.1
VAR_013170
Natural variant3271L → P in BBS4. Ref.9
VAR_017050
Natural variant3511L → R in BBS4. Ref.15
VAR_038895
Natural variant3541I → T. Ref.3 Ref.14 Ref.15
Corresponds to variant rs2277598 [ dbSNP | Ensembl ].
VAR_017054
Natural variant3641A → E in BBS4. Ref.9
VAR_017051
Natural variant3681D → G in BBS4. Ref.14
VAR_038896
Natural variant3931A → V. Ref.5
Corresponds to variant rs17852452 [ dbSNP | Ensembl ].
VAR_028723
Natural variant4121E → D in a patient with Bardet-Biedl syndrome compound heterozygote for mutations in BBS1; uncertain pathological role. Ref.16
Corresponds to variant rs147202164 [ dbSNP | Ensembl ].
VAR_066288
Natural variant4571S → I in BBS4. Ref.9
VAR_017052
Natural variant4721M → V in BBS4. Ref.12 Ref.13
Corresponds to variant rs2277596 [ dbSNP | Ensembl ].
VAR_017053
Natural variant4881T → K in a patient with Bardet-Biedl syndrome homozygous for a mutation in BBS12; uncertain pathological role. Ref.16
VAR_066289
Natural variant5031P → L in BBS4.
VAR_038897

Sequences

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

Last modified October 23, 2007. Version 2.
Checksum: 59BC9B29355C8E3C

FASTA51958,282
        10         20         30         40         50         60 
MAEERVATRT QFPVSTESQK PRQKKAPEFP ILEKQNWLIH LHYIRKDYEA CKAVIKEQLQ 

        70         80         90        100        110        120 
ETQGLCEYAI YVQALIFRLE GNIQESLELF QTCAVLSPQS ADNLKQVARS LFLLGKHKAA 

       130        140        150        160        170        180 
IEVYNEAAKL NQKDWEISHN LGVCYIYLKQ FNKAQDQLHN ALNLNRHDLT YIMLGKIHLL 

       190        200        210        220        230        240 
EGDLDKAIEV YKKAVEFSPE NTELLTTLGL LYLQLGIYQK AFEHLGNALT YDPTNYKAIL 

       250        260        270        280        290        300 
AAGSMMQTHG DFDVALTKYR VVACAVPESP PLWNNIGMCF FGKKKYVAAI SCLKRANYLA 

       310        320        330        340        350        360 
PFDWKILYNL GLVHLTMQQY ASAFHFLSAA INFQPKMGEL YMLLAVALTN LEDIENAKRA 

       370        380        390        400        410        420 
YAEAVHLDKC NPLVNLNYAV LLYNQGEKKN ALAQYQEMEK KVSLLKDNSS LEFDSEMVEM 

       430        440        450        460        470        480 
AQKLGAALQV GEALVWTKPV KDPKSKHQTT STSKPASFQQ PLGSNQALGQ AMSSAAAYRT 

       490        500        510 
LPSGAGGTSQ FTKPPSLPLE PEPAVESSPT ETSEQIREK 

« Hide

Isoform 2 [UniParc].

Checksum: 09A45FF715582D14
Show »

FASTA52759,084
Isoform 3 [UniParc].

Checksum: 22AAB3D93C36F0E9
Show »

FASTA34738,282

References

« Hide 'large scale' references
[1]"Identification of the gene that, when mutated, causes the human obesity syndrome BBS4."
Mykytyn K., Braun T., Carmi R., Haider N.B., Searby C.C., Shastri M., Beck G., Wright A.F., Iannaccone A., Elbedour K., Riise R., Baldi A., Raas-Rothschild A., Gorman S.W., Duhl D.M., Jacobson S.G., Casavant T., Stone E.M., Sheffield V.C.
Nat. Genet. 28:188-191(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT BBS4 PRO-295.
[2]"Cloning and characterization of a splice variant of human Bardet-Biedl syndrome 4 gene (BBS4)."
Ye X., Dai J., Fang W., Jin W., Guo Y., Song J., Ji C., Gu S., Xie Y., Mao Y.
DNA Seq. 15:213-218(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), VARIANT THR-354.
Tissue: Kidney.
[4]"Analysis of the DNA sequence and duplication history of human chromosome 15."
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. expand/collapse author list , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
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), VARIANT VAL-393.
Tissue: Testis and Uterus.
[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.
[8]"Novel interaction partners of Bardet-Biedl syndrome proteins."
Oeffner F., Moch C., Neundorf A., Hofmann J., Koch M., Grzeschik K.H.
Cell Motil. Cytoskeleton 65:143-155(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ALDOB.
[9]"BBS4 is a minor contributor to Bardet-Biedl syndrome and may also participate in triallelic inheritance."
Katsanis N., Eichers E.R., Ansley S.J., Lewis R.A., Kayserili H., Hoskins B.E., Scambler P.J., Beales P.L., Lupski J.R.
Am. J. Hum. Genet. 71:22-29(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS BBS4 HIS-165; PRO-327; GLU-364 AND ILE-457.
[10]"The Bardet-Biedl protein BBS4 targets cargo to the pericentriolar region and is required for microtubule anchoring and cell cycle progression."
Kim J.C., Badano J.L., Sibold S., Esmail M.A., Hill J., Hoskins B.E., Leitch C.C., Venner K., Ansley S.J., Ross A.J., Leroux M.R., Katsanis N., Beales P.L.
Nat. Genet. 36:462-470(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH DCTN1 AND PCM1, SUBCELLULAR LOCATION.
[11]"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 LZTL1.
[12]"Genetic interaction of BBS1 mutations with alleles at other BBS loci can result in non-Mendelian Bardet-Biedl syndrome."
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.
Am. J. Hum. Genet. 72:1187-1199(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BBS4 VAL-472.
[13]"Evaluation of multiplex capillary heteroduplex analysis: a rapid and sensitive mutation screening technique."
Hoskins B.E., Thorn A., Scambler P.J., Beales P.L.
Hum. Mutat. 22:151-157(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BBS4 VAL-472.
[14]"Antenatal presentation of Bardet-Biedl syndrome may mimic Meckel syndrome."
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. expand/collapse author list , 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.
Am. J. Hum. Genet. 76:493-504(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BBS4 GLY-368, VARIANTS ARG-46 AND THR-354.
[15]"Testing for triallelism: analysis of six BBS genes in a Bardet-Biedl syndrome family cohort."
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. expand/collapse author list , Besancon A.-F., Mandel J.-L., Cossee M., Dollfus H.
Eur. J. Hum. Genet. 13:607-616(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BBS4 ARG-351, VARIANT THR-354.
[16]"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: VARIANTS ARG-46; LYS-61; ASP-412 AND LYS-488.
+Additional computationally mapped references.

Web resources

Mutations of the BBS4 gene

Retina International's Scientific Newsletter

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF359281 mRNA. Translation: AAK58868.1.
AY457143 mRNA. Translation: AAS13441.1.
AK075321 mRNA. Translation: BAC11547.1.
AK303706 mRNA. Translation: BAG64690.1.
AC009712 Genomic DNA. No translation available.
BC008923 mRNA. Translation: AAH08923.2.
BC027624 mRNA. Translation: AAH27624.1.
CCDSCCDS10246.1. [Q96RK4-1]
CCDS58377.1. [Q96RK4-3]
RefSeqNP_001239607.1. NM_001252678.1. [Q96RK4-3]
NP_149017.2. NM_033028.4. [Q96RK4-1]
UniGeneHs.208681.

3D structure databases

ProteinModelPortalQ96RK4.
SMRQ96RK4. Positions 76-429.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107060. 16 interactions.
DIPDIP-46540N.
IntActQ96RK4. 36 interactions.
STRING9606.ENSP00000268057.

PTM databases

PhosphoSiteQ96RK4.

Polymorphism databases

DMDM160359000.

Proteomic databases

MaxQBQ96RK4.
PaxDbQ96RK4.
PRIDEQ96RK4.

Protocols and materials databases

DNASU585.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000268057; ENSP00000268057; ENSG00000140463. [Q96RK4-1]
ENST00000395205; ENSP00000378631; ENSG00000140463. [Q96RK4-2]
ENST00000542334; ENSP00000445964; ENSG00000140463. [Q96RK4-3]
GeneID585.
KEGGhsa:585.
UCSCuc002avb.3. human. [Q96RK4-1]
uc002avd.3. human. [Q96RK4-2]

Organism-specific databases

CTD585.
GeneCardsGC15P072978.
GeneReviewsBBS4.
H-InvDBHIX0012411.
HGNCHGNC:969. BBS4.
HPAHPA039418.
MIM209900. phenotype.
600374. gene.
neXtProtNX_Q96RK4.
Orphanet110. Bardet-Biedl syndrome.
PharmGKBPA25278.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0457.
HOGENOMHOG000261391.
HOVERGENHBG024456.
InParanoidQ96RK4.
KOK16531.
OMALEFDAEM.
PhylomeDBQ96RK4.
TreeFamTF324966.

Gene expression databases

ArrayExpressQ96RK4.
BgeeQ96RK4.
CleanExHS_BBS4.
GenevestigatorQ96RK4.

Family and domain databases

Gene3D1.25.40.10. 3 hits.
InterProIPR028786. BBS4.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERPTHR23083:SF389. PTHR23083:SF389. 1 hit.
PfamPF13181. TPR_8. 1 hit.
[Graphical view]
SMARTSM00028. TPR. 8 hits.
[Graphical view]
PROSITEPS50005. TPR. 8 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiBBS4.
GenomeRNAi585.
NextBio2391.
PROQ96RK4.
SOURCESearch...

Entry information

Entry nameBBS4_HUMAN
AccessionPrimary (citable) accession number: Q96RK4
Secondary accession number(s): B4E178 expand/collapse secondary AC list , Q53DZ5, Q8NHU9, Q96H45
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: October 23, 2007
Last modified: July 9, 2014
This is version 132 of the entry and version 2 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 15

Human chromosome 15: entries, gene names and cross-references to MIM