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Protein

Bardet-Biedl syndrome 10 protein

Gene

BBS10

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • RNA polymerase II repressing transcription factor binding Source: MGI

GO - Biological processi

  • chaperone-mediated protein complex assembly Source: MGI
  • non-motile cilium assembly Source: BHF-UCL
  • photoreceptor cell maintenance Source: BHF-UCL
  • regulation of protein complex assembly Source: MGI
  • response to stimulus Source: UniProtKB-KW
  • retina homeostasis Source: BHF-UCL
  • visual perception Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Sensory transduction, Vision

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000179941-MONOMER.
ReactomeiR-HSA-5620922. BBSome-mediated cargo-targeting to cilium.

Names & Taxonomyi

Protein namesi
Recommended name:
Bardet-Biedl syndrome 10 protein
Gene namesi
Name:BBS10
Synonyms:C12orf58
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:26291. BBS10.

Subcellular locationi

GO - Cellular componenti

  • cilium Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell projection

Pathology & Biotechi

Involvement in diseasei

Bardet-Biedl syndrome 10 (BBS10)5 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:615987
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07572211V → G in BBS10. 1 PublicationCorresponds to variant rs137852838dbSNPEnsembl.1
Natural variantiVAR_02639134R → P in BBS10; has moderately reduced ability to interact with BBS7 and BBS9. 2 PublicationsCorresponds to variant rs137852836dbSNPEnsembl.1
Natural variantiVAR_02639249R → W in BBS10; has moderately reduced ability to interact with BBS7 and BBS9. 4 PublicationsCorresponds to variant rs768933093dbSNPEnsembl.1
Natural variantiVAR_06625255L → P in BBS10. 1 Publication1
Natural variantiVAR_02639391C → W in BBS10; has moderately reduced ability to interact with BBS7 and BBS9. 3 PublicationsCorresponds to variant rs148374859dbSNPEnsembl.1
Natural variantiVAR_026394170L → S in BBS10. 1 PublicationCorresponds to variant rs780916348dbSNPEnsembl.1
Natural variantiVAR_066254188K → T in BBS10; associated with V-636. 1 Publication1
Natural variantiVAR_026395195C → W in BBS10. 1 Publication1
Natural variantiVAR_026396197Y → C in BBS10. 1 PublicationCorresponds to variant rs756632517dbSNPEnsembl.1
Natural variantiVAR_026397240V → G in BBS10; has moderately reduced ability to interact with BBS7 and BBS9; severely reduces the interaction with BBS12; 8% of wild-type. 2 Publications1
Natural variantiVAR_026398308L → F in BBS10; has moderately reduced ability to interact with BBS7 and BBS9. 2 Publications1
Natural variantiVAR_026399311S → A in BBS10; has moderately reduced ability to interact with BBS7 and BBS9; severely reduces the interaction with BBS12; 19% of wild-type. 3 PublicationsCorresponds to variant rs137852837dbSNPEnsembl.1
Natural variantiVAR_026400329S → L in BBS10; has moderately reduced ability to interact with BBS7 and BBS9; severely reduces the interaction with BBS12; 15% of wild-type. 2 Publications1
Natural variantiVAR_026401363P → L in BBS10; has moderately reduced ability to interact with BBS7 and BBS9. 2 Publications1
Natural variantiVAR_066257410H → Q in BBS10. 1 Publication1
Natural variantiVAR_026403414L → S in BBS10. 2 PublicationsCorresponds to variant rs786204575dbSNPEnsembl.1
Natural variantiVAR_026404579K → R in BBS10. 1 PublicationCorresponds to variant rs141521925dbSNPEnsembl.1
Natural variantiVAR_066258600L → S in BBS10. 1 Publication1
Natural variantiVAR_026405613Y → C in BBS10. 1 PublicationCorresponds to variant rs575957641dbSNPEnsembl.1
Natural variantiVAR_026406613Y → H in BBS10; has moderately reduced ability to interact with BBS7 and BBS9. 2 PublicationsCorresponds to variant rs141647931dbSNPEnsembl.1
Natural variantiVAR_066259636A → V in BBS10; associated with T-188. 1 PublicationCorresponds to variant rs113224628dbSNPEnsembl.1
Natural variantiVAR_026407677G → V in BBS10; has moderately reduced ability to interact with BBS7 and BBS9. 2 Publications1
Natural variantiVAR_066260687L → P in BBS10. 1 Publication1
Natural variantiVAR_026408689T → P in BBS10; has moderately reduced ability to interact with BBS7 and BBS9. 2 PublicationsCorresponds to variant rs759387000dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi81D → 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. 1 Publication1

Keywords - Diseasei

Bardet-Biedl syndrome, Ciliopathy, Disease mutation, Mental retardation, Obesity

Organism-specific databases

DisGeNETi79738.
MalaCardsiBBS10.
MIMi615987. phenotype.
OpenTargetsiENSG00000179941.
Orphaneti110. Bardet-Biedl syndrome.
PharmGKBiPA143485387.

Polymorphism and mutation databases

BioMutaiBBS10.
DMDMi97043964.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002352721 – 723Bardet-Biedl syndrome 10 proteinAdd BLAST723

Proteomic databases

MaxQBiQ8TAM1.
PaxDbiQ8TAM1.
PeptideAtlasiQ8TAM1.
PRIDEiQ8TAM1.

PTM databases

iPTMnetiQ8TAM1.
PhosphoSitePlusiQ8TAM1.

Expressioni

Gene expression databases

BgeeiENSG00000179941.
CleanExiHS_BBS10.
GenevisibleiQ8TAM1. HS.

Organism-specific databases

HPAiHPA047954.
HPA058743.

Interactioni

Subunit structurei

Component of the BBS/CCT complex composed at least of MKKS, BBS10, BBS12, TCP1, CCT2, CCT3, CCT4, CCT5 AND CCT8.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
BBS12Q6ZW615EBI-6128013,EBI-6128352
BBS7Q8IWZ64EBI-6128013,EBI-1806001
BBS9Q3SYG42EBI-6128013,EBI-2826852

GO - Molecular functioni

  • RNA polymerase II repressing transcription factor binding Source: MGI

Protein-protein interaction databases

BioGridi122851. 16 interactors.
DIPiDIP-60347N.
IntActiQ8TAM1. 22 interactors.
MINTiMINT-8247383.
STRINGi9606.ENSP00000376946.

Structurei

3D structure databases

ProteinModelPortaliQ8TAM1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TCP-1 chaperonin family.Curated

Phylogenomic databases

eggNOGiKOG0360. Eukaryota.
COG0459. LUCA.
GeneTreeiENSGT00390000002417.
HOGENOMiHOG000050242.
HOVERGENiHBG055802.
InParanoidiQ8TAM1.
KOiK19401.
OMAiCVLPVGG.
OrthoDBiEOG091G0H6P.
PhylomeDBiQ8TAM1.
TreeFamiTF335867.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027413. GROEL-like_equatorial.
[Graphical view]
PfamiPF00118. Cpn60_TCP1. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8TAM1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSSMAAAGS VKAALQVAEV LEAIVSCCVG PEGRQVLCTK PTGEVLLSRN
60 70 80 90 100
GGRLLEALHL EHPIARMIVD CVSSHLKKTG DGAKTFIIFL CHLLRGLHAI
110 120 130 140 150
TDREKDPLMC ENIQTHGRHW KNCSRWKFIS QALLTFQTQI LDGIMDQYLS
160 170 180 190 200
RHFLSIFSSA KERTLCRSSL ELLLEAYFCG RVGRNNHKFI SQLMCDYFFK
210 220 230 240 250
CMTCKSGIGV FELVDDHFVE LNVGVTGLPV SDSRIIAGLV LQKDFSVYRP
260 270 280 290 300
ADGDMRMVIV TETIQPLFST SGSEFILNSE AQFQTSQFWI MEKTKAIMKH
310 320 330 340 350
LHSQNVKLLI SSVKQPDLVS YYAGVNGISV VECLSSEEVS LIRRIIGLSP
360 370 380 390 400
FVPPQAFSQC EIPNTALVKF CKPLILRSKR YVHLGLISTC AFIPHSIVLC
410 420 430 440 450
GPVHGLIEQH EDALHGALKM LRQLFKDLDL NYMTQTNDQN GTSSLFIYKN
460 470 480 490 500
SGESYQAPDP GNGSIQRPYQ DTVAENKDAL EKTQTYLKVH SNLVIPDVEL
510 520 530 540 550
ETYIPYSTPT LTPTDTFQTV ETLTCLSLER NRLTDYYEPL LKNNSTAYST
560 570 580 590 600
RGNRIEISYE NLQVTNITRK GSMLPVSCKL PNMGTSQSYL SSSMPAGCVL
610 620 630 640 650
PVGGNFEILL HYYLLNYAKK CHQSEETMVS MIIANALLGI PKVLYKSKTG
660 670 680 690 700
KYSFPHTYIR AVHALQTNQP LVSSQTGLES VMGKYQLLTS VLQCLTKILT
710 720
IDMVITVKRH PQKVHNQDSE DEL
Length:723
Mass (Da):80,838
Last modified:May 16, 2006 - v2
Checksum:i558143FFA5F191DD
GO

Sequence cautioni

The sequence AAH13795 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB15695 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti514T → S in BAB15695 (PubMed:14702039).Curated1
Sequence conflicti586S → Y in BAB15695 (PubMed:14702039).Curated1
Sequence conflicti607E → D in AAH26355 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07572211V → G in BBS10. 1 PublicationCorresponds to variant rs137852838dbSNPEnsembl.1
Natural variantiVAR_02639134R → P in BBS10; has moderately reduced ability to interact with BBS7 and BBS9. 2 PublicationsCorresponds to variant rs137852836dbSNPEnsembl.1
Natural variantiVAR_02639249R → W in BBS10; has moderately reduced ability to interact with BBS7 and BBS9. 4 PublicationsCorresponds to variant rs768933093dbSNPEnsembl.1
Natural variantiVAR_06625255L → P in BBS10. 1 Publication1
Natural variantiVAR_02639391C → W in BBS10; has moderately reduced ability to interact with BBS7 and BBS9. 3 PublicationsCorresponds to variant rs148374859dbSNPEnsembl.1
Natural variantiVAR_066253142D → N.1 PublicationCorresponds to variant rs142863601dbSNPEnsembl.1
Natural variantiVAR_026394170L → S in BBS10. 1 PublicationCorresponds to variant rs780916348dbSNPEnsembl.1
Natural variantiVAR_066254188K → T in BBS10; associated with V-636. 1 Publication1
Natural variantiVAR_026395195C → W in BBS10. 1 Publication1
Natural variantiVAR_026396197Y → C in BBS10. 1 PublicationCorresponds to variant rs756632517dbSNPEnsembl.1
Natural variantiVAR_026397240V → G in BBS10; has moderately reduced ability to interact with BBS7 and BBS9; severely reduces the interaction with BBS12; 8% of wild-type. 2 Publications1
Natural variantiVAR_066255255M → I Found in a patient with Bardet-Biedl syndrome homozygous for a mutation in BBS2; unknown pathological significance. 1 PublicationCorresponds to variant rs139658279dbSNPEnsembl.1
Natural variantiVAR_066256296A → T Found in a patient with Bardet-Biedl syndrome compound heterozygote for mutations in BBS1; rare variant; unknown pathological significance. 1 PublicationCorresponds to variant rs150587582dbSNPEnsembl.1
Natural variantiVAR_026398308L → F in BBS10; has moderately reduced ability to interact with BBS7 and BBS9. 2 Publications1
Natural variantiVAR_026399311S → A in BBS10; has moderately reduced ability to interact with BBS7 and BBS9; severely reduces the interaction with BBS12; 19% of wild-type. 3 PublicationsCorresponds to variant rs137852837dbSNPEnsembl.1
Natural variantiVAR_026400329S → L in BBS10; has moderately reduced ability to interact with BBS7 and BBS9; severely reduces the interaction with BBS12; 15% of wild-type. 2 Publications1
Natural variantiVAR_026401363P → L in BBS10; has moderately reduced ability to interact with BBS7 and BBS9. 2 Publications1
Natural variantiVAR_026402376L → F.Corresponds to variant rs11109474dbSNPEnsembl.1
Natural variantiVAR_066257410H → Q in BBS10. 1 Publication1
Natural variantiVAR_026403414L → S in BBS10. 2 PublicationsCorresponds to variant rs786204575dbSNPEnsembl.1
Natural variantiVAR_052272539P → L.1 PublicationCorresponds to variant rs35676114dbSNPEnsembl.1
Natural variantiVAR_026404579K → R in BBS10. 1 PublicationCorresponds to variant rs141521925dbSNPEnsembl.1
Natural variantiVAR_066258600L → S in BBS10. 1 Publication1
Natural variantiVAR_026405613Y → C in BBS10. 1 PublicationCorresponds to variant rs575957641dbSNPEnsembl.1
Natural variantiVAR_026406613Y → H in BBS10; has moderately reduced ability to interact with BBS7 and BBS9. 2 PublicationsCorresponds to variant rs141647931dbSNPEnsembl.1
Natural variantiVAR_066259636A → V in BBS10; associated with T-188. 1 PublicationCorresponds to variant rs113224628dbSNPEnsembl.1
Natural variantiVAR_026407677G → V in BBS10; has moderately reduced ability to interact with BBS7 and BBS9. 2 Publications1
Natural variantiVAR_066260687L → P in BBS10. 1 Publication1
Natural variantiVAR_026408689T → P in BBS10; has moderately reduced ability to interact with BBS7 and BBS9. 2 PublicationsCorresponds to variant rs759387000dbSNPEnsembl.1
Natural variantiVAR_066261715H → R.1 PublicationCorresponds to variant rs769179905dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC013795 mRNA. Translation: AAH13795.1. Different initiation.
BC026355 mRNA. Translation: AAH26355.2.
AK027213 mRNA. Translation: BAB15695.1. Different initiation.
CCDSiCCDS9014.2.
RefSeqiNP_078961.3. NM_024685.3.
UniGeneiHs.96322.

Genome annotation databases

EnsembliENST00000393262; ENSP00000376946; ENSG00000179941.
GeneIDi79738.
KEGGihsa:79738.
UCSCiuc001syd.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC013795 mRNA. Translation: AAH13795.1. Different initiation.
BC026355 mRNA. Translation: AAH26355.2.
AK027213 mRNA. Translation: BAB15695.1. Different initiation.
CCDSiCCDS9014.2.
RefSeqiNP_078961.3. NM_024685.3.
UniGeneiHs.96322.

3D structure databases

ProteinModelPortaliQ8TAM1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122851. 16 interactors.
DIPiDIP-60347N.
IntActiQ8TAM1. 22 interactors.
MINTiMINT-8247383.
STRINGi9606.ENSP00000376946.

PTM databases

iPTMnetiQ8TAM1.
PhosphoSitePlusiQ8TAM1.

Polymorphism and mutation databases

BioMutaiBBS10.
DMDMi97043964.

Proteomic databases

MaxQBiQ8TAM1.
PaxDbiQ8TAM1.
PeptideAtlasiQ8TAM1.
PRIDEiQ8TAM1.

Protocols and materials databases

DNASUi79738.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000393262; ENSP00000376946; ENSG00000179941.
GeneIDi79738.
KEGGihsa:79738.
UCSCiuc001syd.2. human.

Organism-specific databases

CTDi79738.
DisGeNETi79738.
GeneCardsiBBS10.
GeneReviewsiBBS10.
H-InvDBHIX0010839.
HGNCiHGNC:26291. BBS10.
HPAiHPA047954.
HPA058743.
MalaCardsiBBS10.
MIMi610148. gene.
615987. phenotype.
neXtProtiNX_Q8TAM1.
OpenTargetsiENSG00000179941.
Orphaneti110. Bardet-Biedl syndrome.
PharmGKBiPA143485387.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0360. Eukaryota.
COG0459. LUCA.
GeneTreeiENSGT00390000002417.
HOGENOMiHOG000050242.
HOVERGENiHBG055802.
InParanoidiQ8TAM1.
KOiK19401.
OMAiCVLPVGG.
OrthoDBiEOG091G0H6P.
PhylomeDBiQ8TAM1.
TreeFamiTF335867.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000179941-MONOMER.
ReactomeiR-HSA-5620922. BBSome-mediated cargo-targeting to cilium.

Miscellaneous databases

ChiTaRSiBBS10. human.
GeneWikiiBBS10.
GenomeRNAii79738.
PROiQ8TAM1.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000179941.
CleanExiHS_BBS10.
GenevisibleiQ8TAM1. HS.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027413. GROEL-like_equatorial.
[Graphical view]
PfamiPF00118. Cpn60_TCP1. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBBS10_HUMAN
AccessioniPrimary (citable) accession number: Q8TAM1
Secondary accession number(s): Q96CW2, Q9H5D2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: May 16, 2006
Last modified: November 30, 2016
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

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 in the pathogenesis of obesity in BBS.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.