Q8TAM1 (BBS10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bardet-Biedl syndrome 10 protein

Gene names

Name:	BBS10
Synonyms:	C12orf58

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	723 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Probable molecular chaperone. Assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Involved in adipogenic differentiation. Ref.3 Ref.4
Subunit structure	Component of the BBS/CCT complex composed at least of MKKS, BBS10, BBS12, TCP1, CCT2, CCT3, CCT4, CCT5 AND CCT8. Ref.4
Subcellular location	Cell projection › cilium. Note: Located within the basal body of the primary cilium of differentiating preadipocytes. Ref.3
Involvement in disease	Bardet-Biedl syndrome 10 (BBS10) [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.4 Ref.5 Ref.6 Ref.7
Miscellaneous	Adipocytes derived from BBS-patients' dermal fibroblasts in culture exhibit higher propensity for fat accumulation when compared to controls. This strongly suggests that a peripheral primary dysfunction of adipogenesis participates to the pathogenesis of obesity in BBS.
Sequence similarities	Belongs to the TCP-1 chaperonin family.
Sequence caution	The sequence AAH13795.1 differs from that shown. Reason: Erroneous initiation. The sequence BAB15695.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Sensory transduction Vision
Cellular component	Cell projection
Coding sequence diversity	Polymorphism
Disease	Bardet-Biedl syndrome Ciliopathy Disease mutation Mental retardation Obesity
Ligand	ATP-binding Nucleotide-binding
Molecular function	Chaperone
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular protein metabolic process Inferred from electronic annotation. Source: InterPro chaperone-mediated protein complex assembly Inferred from mutant phenotype Ref.4. Source: MGI nonmotile primary cilium assembly Inferred from mutant phenotype PubMed 17980398. Source: BHF-UCL photoreceptor cell maintenance Inferred from mutant phenotype PubMed 17980398. Source: BHF-UCL response to stimulus Inferred from electronic annotation. Source: UniProtKB-KW retina homeostasis Inferred from mutant phenotype PubMed 17980398. Source: BHF-UCL
Cellular_component	cilium Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BBS12	Q6ZW61	5	EBI-6128013,EBI-6128352
BBS7	Q8IWZ6	4	EBI-6128013,EBI-1806001
BBS9	Q3SYG4	2	EBI-6128013,EBI-2826852

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 723	723	Bardet-Biedl syndrome 10 protein		PRO_0000235272
Natural variations
	Natural variant	34	1	R → P in BBS10; has moderately reduced ability to interact with BBS7 and BBS9. Ref.4 Ref.5		VAR_026391
	Natural variant	49	1	R → W in BBS10; has moderately reduced ability to interact with BBS7 and BBS9. Ref.4 Ref.5 Ref.6 Ref.7		VAR_026392
	Natural variant	55	1	L → P in BBS10. Ref.7		VAR_066252
	Natural variant	91	1	C → W in BBS10; has moderately reduced ability to interact with BBS7 and BBS9. Ref.4 Ref.5 Ref.7		VAR_026393
	Natural variant	142	1	D → N. Ref.6 Corresponds to variant rs142863601 [ dbSNP | Ensembl ].		VAR_066253
	Natural variant	170	1	L → S in BBS10. Ref.5		VAR_026394
	Natural variant	188	1	K → T in BBS10; associated with V-636. Ref.7		VAR_066254
	Natural variant	195	1	C → W in BBS10. Ref.5		VAR_026395
	Natural variant	197	1	Y → C in BBS10. Ref.5		VAR_026396
	Natural variant	240	1	V → G in BBS10; has moderately reduced ability to interact with BBS7 and BBS9; severely reduces the interaction with BBS12 (8% of wild-type). Ref.4 Ref.5		VAR_026397
	Natural variant	255	1	M → I in a patient with Bardet-Biedl syndrome homozygous for a mutation in BBS2; uncertain pathological role. Ref.6 Corresponds to variant rs139658279 [ dbSNP | Ensembl ].		VAR_066255
	Natural variant	296	1	A → T Rare variant found in a patient with Bardet-Biedl syndrome compound heterozygote for mutations in BBS1. Ref.7 Corresponds to variant rs150587582 [ dbSNP | Ensembl ].		VAR_066256
	Natural variant	308	1	L → F in BBS10; has moderately reduced ability to interact with BBS7 and BBS9. Ref.4 Ref.5		VAR_026398
	Natural variant	311	1	S → A in BBS10; has moderately reduced ability to interact with BBS7 and BBS9; severely reduces the interaction with BBS12 (19% of wild-type). Ref.4 Ref.5		VAR_026399
	Natural variant	329	1	S → L in BBS10; has moderately reduced ability to interact with BBS7 and BBS9; severely reduces the interaction with BBS12 (15% of wild-type). Ref.4 Ref.5		VAR_026400
	Natural variant	363	1	P → L in BBS10; has moderately reduced ability to interact with BBS7 and BBS9. Ref.4 Ref.5		VAR_026401
	Natural variant	376	1	L → F. Corresponds to variant rs11109474 [ dbSNP | Ensembl ].		VAR_026402
	Natural variant	410	1	H → Q in BBS10. Ref.7		VAR_066257
	Natural variant	414	1	L → S in BBS10. Ref.5 Ref.7		VAR_026403
	Natural variant	539	1	P → L. Ref.6 Corresponds to variant rs35676114 [ dbSNP | Ensembl ].		VAR_052272
	Natural variant	579	1	K → R in BBS10. Ref.5		VAR_026404
	Natural variant	600	1	L → S in BBS10. Ref.7		VAR_066258
	Natural variant	613	1	Y → C in BBS10. Ref.5		VAR_026405
	Natural variant	613	1	Y → H in BBS10; has moderately reduced ability to interact with BBS7 and BBS9. Ref.4 Ref.5		VAR_026406
	Natural variant	636	1	A → V in BBS10; associated with T-188. Ref.7 Corresponds to variant rs113224628 [ dbSNP | Ensembl ].		VAR_066259
	Natural variant	677	1	G → V in BBS10; has moderately reduced ability to interact with BBS7 and BBS9. Ref.4 Ref.5		VAR_026407
	Natural variant	687	1	L → P in BBS10. Ref.6		VAR_066260
	Natural variant	689	1	T → P in BBS10; has moderately reduced ability to interact with BBS7 and BBS9. Ref.4 Ref.5		VAR_026408
	Natural variant	715	1	H → R. Ref.7		VAR_066261
Experimental info
	Mutagenesis	81	1	D → N: Greatly decreases all interactions with BBS7, BBS9 and BBS12 indicating that this residue may be required for overall protein conformation rather than required for ATP binding and substrate folding. Ref.4
	Sequence conflict	514	1	T → S in BAB15695. Ref.2
	Sequence conflict	586	1	S → Y in BAB15695. Ref.2
	Sequence conflict	607	1	E → D in AAH26355. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q8TAM1 [UniParc]. Last modified May 16, 2006. Version 2. Checksum: 558143FFA5F191DD	FASTA	723	80,838
	10 20 30 40 50 60 MLSSMAAAGS VKAALQVAEV LEAIVSCCVG PEGRQVLCTK PTGEVLLSRN GGRLLEALHL 70 80 90 100 110 120 EHPIARMIVD CVSSHLKKTG DGAKTFIIFL CHLLRGLHAI TDREKDPLMC ENIQTHGRHW 130 140 150 160 170 180 KNCSRWKFIS QALLTFQTQI LDGIMDQYLS RHFLSIFSSA KERTLCRSSL ELLLEAYFCG 190 200 210 220 230 240 RVGRNNHKFI SQLMCDYFFK CMTCKSGIGV FELVDDHFVE LNVGVTGLPV SDSRIIAGLV 250 260 270 280 290 300 LQKDFSVYRP ADGDMRMVIV TETIQPLFST SGSEFILNSE AQFQTSQFWI MEKTKAIMKH 310 320 330 340 350 360 LHSQNVKLLI SSVKQPDLVS YYAGVNGISV VECLSSEEVS LIRRIIGLSP FVPPQAFSQC 370 380 390 400 410 420 EIPNTALVKF CKPLILRSKR YVHLGLISTC AFIPHSIVLC GPVHGLIEQH EDALHGALKM 430 440 450 460 470 480 LRQLFKDLDL NYMTQTNDQN GTSSLFIYKN SGESYQAPDP GNGSIQRPYQ DTVAENKDAL 490 500 510 520 530 540 EKTQTYLKVH SNLVIPDVEL ETYIPYSTPT LTPTDTFQTV ETLTCLSLER NRLTDYYEPL 550 560 570 580 590 600 LKNNSTAYST RGNRIEISYE NLQVTNITRK GSMLPVSCKL PNMGTSQSYL SSSMPAGCVL 610 620 630 640 650 660 PVGGNFEILL HYYLLNYAKK CHQSEETMVS MIIANALLGI PKVLYKSKTG KYSFPHTYIR 670 680 690 700 710 720 AVHALQTNQP LVSSQTGLES VMGKYQLLTS VLQCLTKILT IDMVITVKRH PQKVHNQDSE DEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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]. Tissue: Hippocampus and Skin.
[2]	"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. , 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] OF 512-723. Tissue: Lung.
[3]	"Transient ciliogenesis involving Bardet-Biedl syndrome proteins is a fundamental characteristic of adipogenic differentiation." Marion V., Stoetzel C., Schlicht D., Messaddeq N., Koch M., Flori E., Danse J.M., Mandel J.-L., Dollfus H. Proc. Natl. Acad. Sci. U.S.A. 106:1820-1825(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[4]	"BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family chaperonins and mediate BBSome assembly." Seo S., Baye L.M., Schulz N.P., Beck J.S., Zhang Q., Slusarski D.C., Sheffield V.C. Proc. Natl. Acad. Sci. U.S.A. 107:1488-1493(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN BBS/CCT COMPLEX, CHARACTERIZATION OF VARIANTS BBS10 PRO-34; TRP-49; TRP-91; GLY-240; PHE-308; ALA-311; LEU-329; LEU-363; HIS-613; VAL-677 AND PRO-689, MUTAGENESIS OF ASP-81.
[5]	"BBS10 encodes a vertebrate-specific chaperonin-like protein and is a major BBS locus." Stoetzel C., Laurier V., Davis E.E., Muller J., Rix S., Badano J.L., Leitch C.C., Salem N., Chouery E., Corbani S., Jalk N., Vicaire S., Sarda P., Hamel C., Lacombe D., Holder M., Odent S., Holder S. , Brooks A.S., Elcioglu N.H., Da Silva E., Rossillion B., Sigaudy S., de Ravel T.J., Alan Lewis R., Leheup B., Verloes A., Amati-Bonneau P., Megarbane A., Poch O., Bonneau D., Beales P.L., Mandel J.-L., Katsanis N., Dollfus H. Nat. Genet. 38:521-524(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS BBS10 PRO-34; TRP-49; TRP-91; SER-170; TRP-195; CYS-197; GLY-240; PHE-308; ALA-311; LEU-329; LEU-363; SER-414; ARG-579; HIS-613; CYS-613; VAL-677 AND PRO-689.
[6]	"Bardet-Biedl syndrome in Denmark -- report of 13 novel sequence variations in six genes." Hjortshoj T.D., Gronskov K., Philp A.R., Nishimura D.Y., Riise R., Sheffield V.C., Rosenberg T., Brondum-Nielsen K. Hum. Mutat. 31:429-436(2010) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS BBS10 TRP-49 AND PRO-687, VARIANTS ASN-142; ILE-255 AND LEU-539.
[7]	"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. , Mitchell G.A., Boycott K., Heon E. Hum. Mutat. 32:610-619(2011) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS BBS10 TRP-49; PRO-55; TRP-91; THR-188; GLN-410; SER-414; SER-600 AND VAL-636, VARIANTS THR-296 AND ARG-715.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC013795 mRNA. Translation: AAH13795.1. Different initiation. BC026355 mRNA. Translation: AAH26355.2. AK027213 mRNA. Translation: BAB15695.1. Different initiation.
IPI	IPI00742775.
RefSeq	NP_078961.3. NM_024685.3.
UniGene	Hs.96322.
3D structure databases
ProteinModelPortal	Q8TAM1.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8TAM1. 7 interactions.
STRING	9606.ENSP00000376946.
PTM databases
PhosphoSite	Q8TAM1.
Polymorphism databases
DMDM	97043964.
Proteomic databases
PaxDb	Q8TAM1.
PRIDE	Q8TAM1.
Protocols and materials databases
DNASU	79738.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000393262; ENSP00000376946; ENSG00000179941.
GeneID	79738.
KEGG	hsa:79738.
UCSC	uc001syd.1. human.
Organism-specific databases
CTD	79738.
GeneCards	GC12M076738.
H-InvDB	HIX0010839.
HGNC	HGNC:26291. BBS10.
MIM	209900. phenotype. 610148. gene.
neXtProt	NX_Q8TAM1.
Orphanet	110. Bardet-Biedl syndrome.
PharmGKB	PA143485387.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0459.
HOGENOM	HOG000050242.
HOVERGEN	HBG055802.
InParanoid	Q8TAM1.
OMA	KYQLLTS.
OrthoDB	EOG43FGZ3.
Gene expression databases
ArrayExpress	Q8TAM1.
Bgee	Q8TAM1.
CleanEx	HS_BBS10.
Genevestigator	Q8TAM1.
GermOnline	ENSG00000179941. Homo sapiens.
Family and domain databases
InterPro	IPR002423. Cpn60/TCP-1. [Graphical view]
Pfam	PF00118. Cpn60_TCP1. 2 hits. [Graphical view]
SUPFAM	SSF48592. GroEL-ATPase. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	BBS10. human.
GenomeRNAi	79738.
NextBio	69134.
SOURCE	Search...

Entry information

Entry name

BBS10_HUMAN

Accession

Primary (citable) accession number: Q8TAM1
Secondary accession number(s): Q96CW2, Q9H5D2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2006
Last sequence update:	May 16, 2006
Last modified:	May 1, 2013
This is version 94 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.