Tag | Content |
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CPLM ID | CPLM-017705 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Bardet-Biedl syndrome 1 protein |
Protein Synonyms/Alias | BBS2-like protein 2 |
Gene Name | BBS1 |
Gene Synonyms/Alias | BBS2L2 |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
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190 | RIDPLTLKEMLESIR | ubiquitination | [1] | 245 | TTMTTLKKNLADEDA | ubiquitination | [1] | 356 | HGFTHKGKKLWTVQM | ubiquitination | [1] | 398 | EVRIYRDKALLNVIH | ubiquitination | [1] | 602 | KGISDIIKVLVLREG | ubiquitination | [1] |
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Reference | [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments. Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA. Mol Cell Proteomics. 2013 Mar;12(3):825-31. [ PMID: 23266961] |
Functional Description | 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. |
Sequence Annotation | MOD_RES 2 2 N-acetylalanine. |
Keyword | Acetylation; Alternative splicing; Bardet-Biedl syndrome; Cell membrane; Cell projection; Ciliopathy; Cilium; Complete proteome; Cytoplasm; Disease mutation; Membrane; Mental retardation; Obesity; Polymorphism; Reference proteome; Sensory transduction; Vision. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 593 AA |
Protein Sequence | MDPSWRRSSH SWPQPMPDSG RAPVRPHLAK LEEDVWPCPQ FHQTKAASGP PFVNEANSKW 60 LDAHYDPMAN IHTFSACLAL ADLHGDGEYK LVVGDLGPGG QQPRLKVLKG PLVMTESPLP 120 ALPAAAATFL MEQHEPRTPA LALASGPCVY VYKNLRPYFK FSLPQLPPNP LEQDLWNQAK 180 EDRIDPLTLK EMLESIRETA EEPLSIQSLR FLQLELSEME AFVNQHKSNS IKRQTVITTM 240 TTLKKNLADE DAVSCLVLGT ENKELLVLDP EAFTILAKMS LPSVPVFLEV SGQFDVEFRL 300 AAACRNGNIY ILRRDSKHPK YCIELSAQPV GLIRVHKVLV VGSTQDSLHG FTHKGKKLWT 360 VQMPAAILTM NLLEQHSRGL QAVMAGLANG EVRIYRDKAL LNVIHTPDAV TSLCFGRYGR 420 EDNTLIMTTR GGGLIIKILK RTAVFVEGGS EVGPPPAQAM KLNVPRKTRL YVDQTLRERE 480 AGTAMHRAFQ TDLYLLRLRA ARAYLQALES SLSPLSTTAR EPLKLHAVVQ GLGPTFKLTL 540 HLQNTSTTRP VLGLLVCFLY NEALYSLPRA FFKVPLLVPG LNYPLETFVE SLSNKGISDI 600 IKVLVLREGQ SAPLLSAHVN MPGSEGLAAA 630 |
Gene Ontology | GO:0034464; C:BBSome; IDA:BHF-UCL. GO:0060170; C:cilium membrane; IEA:UniProtKB-SubCell. GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0043001; P:Golgi to plasma membrane protein transport; IMP:MGI. GO:0035058; P:nonmotile primary cilium assembly; IMP:BHF-UCL. GO:0045494; P:photoreceptor cell maintenance; IMP:BHF-UCL. GO:0050896; P:response to stimulus; IEA:UniProtKB-KW. GO:0001895; P:retina homeostasis; IMP:BHF-UCL. |
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