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Q9BXC9

- BBS2_HUMAN

UniProt

Q9BXC9 - BBS2_HUMAN

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Protein

Bardet-Biedl syndrome 2 protein

Gene

BBS2

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

Functioni

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.2 Publications

GO - Molecular functioni

  1. RNA polymerase II repressing transcription factor binding Source: MGI

GO - Biological processi

  1. adult behavior Source: BHF-UCL
  2. artery smooth muscle contraction Source: Ensembl
  3. brain morphogenesis Source: BHF-UCL
  4. cartilage development Source: Ensembl
  5. cerebral cortex development Source: BHF-UCL
  6. cilium morphogenesis Source: BHF-UCL
  7. fat cell differentiation Source: BHF-UCL
  8. Golgi to plasma membrane protein transport Source: MGI
  9. hippocampus development Source: BHF-UCL
  10. melanosome transport Source: BHF-UCL
  11. negative regulation of appetite by leptin-mediated signaling pathway Source: BHF-UCL
  12. negative regulation of gene expression Source: Ensembl
  13. negative regulation of multicellular organism growth Source: BHF-UCL
  14. nonmotile primary cilium assembly Source: InterPro
  15. photoreceptor cell maintenance Source: BHF-UCL
  16. positive regulation of multicellular organism growth Source: Ensembl
  17. protein localization Source: BHF-UCL
  18. protein localization to organelle Source: BHF-UCL
  19. regulation of cilium beat frequency involved in ciliary motility Source: BHF-UCL
  20. sperm axoneme assembly Source: BHF-UCL
  21. striatum development Source: BHF-UCL
  22. vasodilation Source: Ensembl
  23. visual perception Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cilium biogenesis/degradation, Protein transport, Sensory transduction, Transport, Vision

Names & Taxonomyi

Protein namesi
Recommended name:
Bardet-Biedl syndrome 2 protein
Gene namesi
Name:BBS2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:967. BBS2.

Subcellular locationi

GO - Cellular componenti

  1. BBSome Source: UniProtKB
  2. ciliary basal body Source: BHF-UCL
  3. cytoplasm Source: UniProtKB-KW
  4. motile cilium Source: BHF-UCL
  5. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cilium, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Involvement in diseasei

Bardet-Biedl syndrome 2 (BBS2) [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.7 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti23 – 231R → P in BBS2. 1 Publication
VAR_038889
Natural varianti70 – 701N → S in BBS2. 1 Publication
Corresponds to variant rs4784677 [ dbSNP | Ensembl ].
VAR_013162
Natural varianti75 – 751V → G in BBS2; in linkage disequilibrium with V-123 in a Bedouin kindred. 1 Publication
VAR_013163
Natural varianti81 – 811G → C in BBS2. 1 Publication
VAR_066280
Natural varianti104 – 1041D → A in BBS2. 2 Publications
VAR_013164
Natural varianti125 – 1251L → R in BBS2. 1 Publication
VAR_066281
Natural varianti136 – 1361A → P in BBS2. 1 Publication
VAR_066282
Natural varianti174 – 1741D → E in BBS2. 1 Publication
VAR_038890
Natural varianti307 – 3071C → W in BBS2. 1 Publication
VAR_066283
Natural varianti315 – 3151R → Q in BBS2. 2 Publications
VAR_013166
Natural varianti315 – 3151R → W in BBS2. 1 Publication
VAR_013167
Natural varianti317 – 3171Y → C in BBS2. 1 Publication
VAR_066284
Natural varianti349 – 3491L → W in BBS2; has a modifier effect on BBS. 1 Publication
VAR_038891
Natural varianti558 – 5581T → I in BBS2. 1 Publication
VAR_013168
Natural varianti632 – 6321R → P in BBS2. 2 Publications
VAR_013169
Natural varianti643 – 6431R → H in BBS2. 1 Publication
VAR_038892

Keywords - Diseasei

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

Organism-specific databases

MIMi209900. phenotype.
Orphaneti110. Bardet-Biedl syndrome.
PharmGKBiPA25276.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 721721Bardet-Biedl syndrome 2 proteinPRO_0000064843Add
BLAST

Proteomic databases

MaxQBiQ9BXC9.
PaxDbiQ9BXC9.
PRIDEiQ9BXC9.

PTM databases

PhosphoSiteiQ9BXC9.

Expressioni

Tissue specificityi

Widely expressed.

Gene expression databases

BgeeiQ9BXC9.
CleanExiHS_BBS2.
ExpressionAtlasiQ9BXC9. baseline and differential.
GenevestigatoriQ9BXC9.

Organism-specific databases

HPAiHPA041315.

Interactioni

Subunit structurei

Part of BBSome complex, that contains BBS1, BBS2, BBS4, BBS5, BBS7, BBS8/TTC8, BBS9 and BBIP10. Interacts (via C-terminus) with BBS7. Interacts (via coiled coil domain) with MKKS. Interacts with CCDC28B and ALDOB.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ALDOBP050624EBI-748297,EBI-1045507
BBS1Q8NFJ95EBI-748297,EBI-1805484
BBS7Q8IWZ610EBI-748297,EBI-1806001
BBS9Q3SYG48EBI-748297,EBI-2826852
MKKSQ9NPJ14EBI-748297,EBI-721319

Protein-protein interaction databases

BioGridi107059. 18 interactions.
DIPiDIP-46563N.
IntActiQ9BXC9. 29 interactions.
MINTiMINT-1454659.
STRINGi9606.ENSP00000245157.

Structurei

3D structure databases

ProteinModelPortaliQ9BXC9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili325 – 36945Sequence AnalysisAdd
BLAST

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG87621.
HOGENOMiHOG000007549.
HOVERGENiHBG031114.
InParanoidiQ9BXC9.
KOiK16747.
PhylomeDBiQ9BXC9.
TreeFamiTF313236.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
InterProiIPR016616. Bardet-Biedl_syndrome_2_prot.
IPR029333. BBS2_C.
IPR029429. BBS2_Mid.
IPR029430. BBS2_N.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR017986. WD40_repeat_dom.
[Graphical view]
PANTHERiPTHR32465:SF0. PTHR32465:SF0. 1 hit.
PfamiPF14782. BBS2_C. 1 hit.
PF14783. BBS2_Mid. 1 hit.
PF14781. BBS2_N. 1 hit.
[Graphical view]
PIRSFiPIRSF013684. BBS2. 1 hit.
SUPFAMiSSF50978. SSF50978. 2 hits.

Sequencei

Sequence statusi: Complete.

Q9BXC9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLLPVFTLKL RHKISPRMVA IGRYDGTHPC LAAATQTGKV FIHNPHTRNQ
60 70 80 90 100
HVSASRVFQS PLESDVSLLN INQAVSCLTA GVLNPELGYD ALLVGTQTNL
110 120 130 140 150
LAYDVYNNSD LFYREVADGA NAIVLGTLGD ISSPLAIIGG NCALQGFNHE
160 170 180 190 200
GSDLFWTVTG DNVNSLALCD FDGDGKKELL VGSEDFDIRV FKEDEIVAEM
210 220 230 240 250
TETEIVTSLC PMYGSRFGYA LSNGTVGVYD KTSRYWRIKS KNHAMSIHAF
260 270 280 290 300
DLNSDGVNEL ITGWSNGKVD ARSDRTGEVI FKDNFSSAIA GVVEGDYRMD
310 320 330 340 350
GHIQLICCSV DGEIRGYLPG TAEMRGNLMD TSAEQDLIRE LSQKKQNLLL
360 370 380 390 400
ELRNYEENAK AELASPLNEA DGHRGIIPAN TRLHTTLSVS LGNETQTAHT
410 420 430 440 450
ELRISTSNDT IIRAVLIFAE GIFTGESHVV HPSIHNLSSS ICIPIVPPKD
460 470 480 490 500
VPVDLHLKAF VGYRSSTQFH VFESTRQLPR FSMYALTSLD PASEPISYVN
510 520 530 540 550
FTIAERAQRV VVWLGQNFLL PEDTHIQNAP FQVCFTSLRN GGHLHIKIKL
560 570 580 590 600
SGEITINTDD IDLAGDIIQS MASFFAIEDL QVEADFPVYF EELRKVLVKV
610 620 630 640 650
DEYHSVHQKL SADMADHSNL IRSLLVGAED ARLMRDMKTM KSRYMELYDL
660 670 680 690 700
NRDLLNGYKI RCNNHTELLG NLKAVNQAIQ RAGRLRVGKP KNQVITACRD
710 720
AIRSNNINTL FKIMRVGTAS S
Length:721
Mass (Da):79,871
Last modified:June 1, 2001 - v1
Checksum:i8FA1CDAED725BEAF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti63 – 631E → G in BAB55252. (PubMed:14702039)Curated
Sequence conflicti169 – 1691C → R in BAB55252. (PubMed:14702039)Curated
Sequence conflicti457 – 4571L → S in BAB55252. (PubMed:14702039)Curated
Sequence conflicti648 – 6481Y → H in BAB55252. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti23 – 231R → P in BBS2. 1 Publication
VAR_038889
Natural varianti70 – 701N → S in BBS2. 1 Publication
Corresponds to variant rs4784677 [ dbSNP | Ensembl ].
VAR_013162
Natural varianti75 – 751V → G in BBS2; in linkage disequilibrium with V-123 in a Bedouin kindred. 1 Publication
VAR_013163
Natural varianti81 – 811G → C in BBS2. 1 Publication
VAR_066280
Natural varianti104 – 1041D → A in BBS2. 2 Publications
VAR_013164
Natural varianti122 – 1221A → V.1 Publication
Corresponds to variant rs17856449 [ dbSNP | Ensembl ].
VAR_029747
Natural varianti123 – 1231I → V Polymorphism in linkage disequilibrium with G-75 in a Bedouin kindred. 3 Publications
Corresponds to variant rs11373 [ dbSNP | Ensembl ].
VAR_013165
Natural varianti125 – 1251L → R in BBS2. 1 Publication
VAR_066281
Natural varianti136 – 1361A → P in BBS2. 1 Publication
VAR_066282
Natural varianti174 – 1741D → E in BBS2. 1 Publication
VAR_038890
Natural varianti307 – 3071C → W in BBS2. 1 Publication
VAR_066283
Natural varianti315 – 3151R → Q in BBS2. 2 Publications
VAR_013166
Natural varianti315 – 3151R → W in BBS2. 1 Publication
VAR_013167
Natural varianti317 – 3171Y → C in BBS2. 1 Publication
VAR_066284
Natural varianti349 – 3491L → W in BBS2; has a modifier effect on BBS. 1 Publication
VAR_038891
Natural varianti504 – 5041A → V.
Corresponds to variant rs16957538 [ dbSNP | Ensembl ].
VAR_029748
Natural varianti558 – 5581T → I in BBS2. 1 Publication
VAR_013168
Natural varianti629 – 6291E → K in a patient with Bardet-Biedl syndrome compound heterozygote for mutations in BBS10; uncertain pathological role. 1 Publication
VAR_066285
Natural varianti632 – 6321R → P in BBS2. 2 Publications
VAR_013169
Natural varianti643 – 6431R → H in BBS2. 1 Publication
VAR_038892

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF342736 mRNA. Translation: AAK28552.1.
AK027635 mRNA. Translation: BAB55252.1.
BC014140 mRNA. Translation: AAH14140.1.
CCDSiCCDS32451.1.
RefSeqiNP_114091.3. NM_031885.3.
UniGeneiHs.333738.

Genome annotation databases

EnsembliENST00000245157; ENSP00000245157; ENSG00000125124.
GeneIDi583.
KEGGihsa:583.
UCSCiuc002ejd.2. human.

Polymorphism databases

DMDMi20454827.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Mutations of the BBS2 gene

Retina International's Scientific Newsletter

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF342736 mRNA. Translation: AAK28552.1 .
AK027635 mRNA. Translation: BAB55252.1 .
BC014140 mRNA. Translation: AAH14140.1 .
CCDSi CCDS32451.1.
RefSeqi NP_114091.3. NM_031885.3.
UniGenei Hs.333738.

3D structure databases

ProteinModelPortali Q9BXC9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107059. 18 interactions.
DIPi DIP-46563N.
IntActi Q9BXC9. 29 interactions.
MINTi MINT-1454659.
STRINGi 9606.ENSP00000245157.

PTM databases

PhosphoSitei Q9BXC9.

Polymorphism databases

DMDMi 20454827.

Proteomic databases

MaxQBi Q9BXC9.
PaxDbi Q9BXC9.
PRIDEi Q9BXC9.

Protocols and materials databases

DNASUi 583.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000245157 ; ENSP00000245157 ; ENSG00000125124 .
GeneIDi 583.
KEGGi hsa:583.
UCSCi uc002ejd.2. human.

Organism-specific databases

CTDi 583.
GeneCardsi GC16M056500.
GeneReviewsi BBS2.
HGNCi HGNC:967. BBS2.
HPAi HPA041315.
MIMi 209900. phenotype.
606151. gene.
neXtProti NX_Q9BXC9.
Orphaneti 110. Bardet-Biedl syndrome.
PharmGKBi PA25276.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG87621.
HOGENOMi HOG000007549.
HOVERGENi HBG031114.
InParanoidi Q9BXC9.
KOi K16747.
PhylomeDBi Q9BXC9.
TreeFami TF313236.

Miscellaneous databases

ChiTaRSi BBS2. human.
GeneWikii BBS2.
GenomeRNAii 583.
NextBioi 2387.
PROi Q9BXC9.
SOURCEi Search...

Gene expression databases

Bgeei Q9BXC9.
CleanExi HS_BBS2.
ExpressionAtlasi Q9BXC9. baseline and differential.
Genevestigatori Q9BXC9.

Family and domain databases

Gene3Di 2.130.10.10. 2 hits.
InterProi IPR016616. Bardet-Biedl_syndrome_2_prot.
IPR029333. BBS2_C.
IPR029429. BBS2_Mid.
IPR029430. BBS2_N.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR017986. WD40_repeat_dom.
[Graphical view ]
PANTHERi PTHR32465:SF0. PTHR32465:SF0. 1 hit.
Pfami PF14782. BBS2_C. 1 hit.
PF14783. BBS2_Mid. 1 hit.
PF14781. BBS2_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF013684. BBS2. 1 hit.
SUPFAMi SSF50978. SSF50978. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT BBS2 GLY-75, VARIANT VAL-123.
  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].
  3. "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], VARIANT VAL-122.
    Tissue: Placenta.
  4. Cited for: INTERACTION WITH CCDC28B.
  5. "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.
  6. Cited for: INTERACTION WITH ALDOB.
  7. "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: INTERACTION WITH BBS7 AND MKKS.
  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, SUBCELLULAR LOCATION.
  9. Cited for: VARIANTS BBS2 SER-70; ALA-104; GLN-315; TRP-315; ILE-558 AND PRO-632.
  10. "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: VARIANTS BBS2 GLN-315 AND TRP-349.
  11. "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 BBS2 GLU-174.
  12. "Further support for digenic inheritance in Bardet-Biedl syndrome."
    Fauser S., Munz M., Besch D.
    J. Med. Genet. 40:E104-E104(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT BBS2 HIS-643.
  13. Cited for: VARIANT BBS2 PRO-23, VARIANT VAL-123.
  14. Cited for: VARIANT VAL-123.
  15. "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: VARIANT LYS-629.
  16. Cited for: VARIANTS BBS2 CYS-81; ALA-104; ARG-125; PRO-136; TRP-307; CYS-317 AND PRO-632.

Entry informationi

Entry nameiBBS2_HUMAN
AccessioniPrimary (citable) accession number: Q9BXC9
Secondary accession number(s): Q96CM0, Q96SN9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: June 1, 2001
Last modified: November 26, 2014
This is version 118 of the entry and version 1 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: 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

External Data

Dasty 3