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Q9DBI2

- BBS10_MOUSE

UniProt

Q9DBI2 - BBS10_MOUSE

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Protein
Bardet-Biedl syndrome 10 protein homolog
Gene
Bbs10
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript 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 By similarity.

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW

GO - Biological processi

  1. cellular protein metabolic process Source: InterPro
  2. chaperone-mediated protein complex assembly Source: Ensembl
  3. nonmotile primary cilium assembly Source: Ensembl
  4. photoreceptor cell maintenance Source: Ensembl
  5. regulation of protein complex assembly Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Bardet-Biedl syndrome 10 protein homolog
Gene namesi
Name:Bbs10
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 10

Organism-specific databases

MGIiMGI:1919019. Bbs10.

Subcellular locationi

Cell projectioncilium By similarity
Note: Located within the basal body of the primary cilium of differentiating preadipocytes By similarity.

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell projection

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 713713Bardet-Biedl syndrome 10 protein homolog
PRO_0000235273Add
BLAST

Proteomic databases

PRIDEiQ9DBI2.

PTM databases

PhosphoSiteiQ9DBI2.

Expressioni

Gene expression databases

BgeeiQ9DBI2.
CleanExiMM_BBS10.
GenevestigatoriQ9DBI2.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-60356N.
IntActiQ9DBI2. 4 interactions.
STRINGi10090.ENSMUSP00000049387.

Structurei

3D structure databases

ProteinModelPortaliQ9DBI2.
SMRiQ9DBI2. Positions 9-100.

Family & Domainsi

Sequence similaritiesi

Belongs to the TCP-1 chaperonin family.

Phylogenomic databases

eggNOGiKOG0360.
GeneTreeiENSGT00390000002417.
HOGENOMiHOG000050242.
HOVERGENiHBG055802.
InParanoidiQ9DBI2.
OMAiCVLPVGG.
OrthoDBiEOG7SXW5J.
PhylomeDBiQ9DBI2.
TreeFamiTF335867.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
InterProiIPR002423. Cpn60/TCP-1.
IPR027413. GROEL-like_equatorial.
[Graphical view]
PfamiPF00118. Cpn60_TCP1. 2 hits.
[Graphical view]
SUPFAMiSSF48592. SSF48592. 2 hits.

Sequencei

Sequence statusi: Complete.

Q9DBI2-1 [UniParc]FASTAAdd to Basket

« Hide

MASQGSVTAA LRVAEVLESI ANRCVGPEGG QVLCTKPTGE VLLSRDGGCL    50
LEALHLEHPL ARMIVACVSS HLKKTGDGAK TFIIFLCHLL RGLHAIGEKG 100
KDSFTSENIQ SHERHWKNCC QWKSISQALQ TFQTQTLGCI VDRSLSRHYL 150
SVFSSSTEGR KLCRHSLELL LEAYFCGRVG RNNHRFISQL MCDYVFKCMA 200
CESGVEVFEL LDHCFAELNV GVTGLPVSDS RIIDGLVLPR DFSMYCPADG 250
DIRMVIVTEI LQPQFSSAGS EFVLNSETQF QASQCWITDR TKTVMNHLRG 300
QNVKLLLTSV KQPDLVIYCA RLNSISVVEC LSAEEVSLVQ RITGLSPCVL 350
PEVASQCEIS DSTLVKFCKP LILRSKRYVH LGLISTCAFI PHSMVLCGPV 400
LGLVEQHERA FHGAFKMLRQ LFTDLDLNYI IQTKQQCNPS PLAYDNSRER 450
NHSPETDKYQ DIVAKSKNKL ETQTHLEVYS GLGASDTELR AGKPWSAHKK 500
TPIAPSQTDE MLKCLPPERS GIIDNCDLSI ENHSTGNPTA EDTGTEISFE 550
HLQVSDNAGK GYTLPVMRKS LDTCTCQGYC SSTVPAGCVL PVGGSFEILM 600
SYYLLSYAKQ CRQSDETVIS MLIADALLGI PKILYKPKKG KDSFPHIYMR 650
SLHALQASQP MVSGQSGFES VAGKYQLLTS VLQCLMKILT IDLIINIKRQ 700
PQKTADQESE DEF 713
Length:713
Mass (Da):78,924
Last modified:May 16, 2006 - v2
Checksum:iAEEBC611994FDB84
GO

Sequence cautioni

The sequence BAB23682.1 differs from that shown. Reason: Intron retention. Several introns.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK004937 mRNA. Translation: BAB23682.1. Sequence problems.
CCDSiCCDS48689.1.
RefSeqiNP_082190.1. NM_027914.1.
UniGeneiMm.45256.

Genome annotation databases

EnsembliENSMUST00000040454; ENSMUSP00000049387; ENSMUSG00000035759.
GeneIDi71769.
KEGGimmu:71769.
UCSCiuc011xnf.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK004937 mRNA. Translation: BAB23682.1 . Sequence problems.
CCDSi CCDS48689.1.
RefSeqi NP_082190.1. NM_027914.1.
UniGenei Mm.45256.

3D structure databases

ProteinModelPortali Q9DBI2.
SMRi Q9DBI2. Positions 9-100.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-60356N.
IntActi Q9DBI2. 4 interactions.
STRINGi 10090.ENSMUSP00000049387.

PTM databases

PhosphoSitei Q9DBI2.

Proteomic databases

PRIDEi Q9DBI2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000040454 ; ENSMUSP00000049387 ; ENSMUSG00000035759 .
GeneIDi 71769.
KEGGi mmu:71769.
UCSCi uc011xnf.1. mouse.

Organism-specific databases

CTDi 79738.
MGIi MGI:1919019. Bbs10.

Phylogenomic databases

eggNOGi KOG0360.
GeneTreei ENSGT00390000002417.
HOGENOMi HOG000050242.
HOVERGENi HBG055802.
InParanoidi Q9DBI2.
OMAi CVLPVGG.
OrthoDBi EOG7SXW5J.
PhylomeDBi Q9DBI2.
TreeFami TF335867.

Miscellaneous databases

NextBioi 334461.
PROi Q9DBI2.
SOURCEi Search...

Gene expression databases

Bgeei Q9DBI2.
CleanExi MM_BBS10.
Genevestigatori Q9DBI2.

Family and domain databases

Gene3Di 1.10.560.10. 2 hits.
InterProi IPR002423. Cpn60/TCP-1.
IPR027413. GROEL-like_equatorial.
[Graphical view ]
Pfami PF00118. Cpn60_TCP1. 2 hits.
[Graphical view ]
SUPFAMi SSF48592. SSF48592. 2 hits.
ProtoNeti Search...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Liver.

Entry informationi

Entry nameiBBS10_MOUSE
AccessioniPrimary (citable) accession number: Q9DBI2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: May 16, 2006
Last modified: July 9, 2014
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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