BBS1_HUMAN - dbPTM
BBS1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BBS1_HUMAN
UniProt AC Q8NFJ9
Protein Name Bardet-Biedl syndrome 1 protein
Gene Name BBS1
Organism Homo sapiens (Human).
Sequence Length 593
Subcellular Localization Cell projection, cilium membrane. Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite.
Protein Description 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. [PubMed: 17574030]
Protein Sequence MAAASSSDSDACGAESNEANSKWLDAHYDPMANIHTFSACLALADLHGDGEYKLVVGDLGPGGQQPRLKVLKGPLVMTESPLPALPAAAATFLMEQHEPRTPALALASGPCVYVYKNLRPYFKFSLPQLPPNPLEQDLWNQAKEDRIDPLTLKEMLESIRETAEEPLSIQSLRFLQLELSEMEAFVNQHKSNSIKRQTVITTMTTLKKNLADEDAVSCLVLGTENKELLVLDPEAFTILAKMSLPSVPVFLEVSGQFDVEFRLAAACRNGNIYILRRDSKHPKYCIELSAQPVGLIRVHKVLVVGSTQDSLHGFTHKGKKLWTVQMPAAILTMNLLEQHSRGLQAVMAGLANGEVRIYRDKALLNVIHTPDAVTSLCFGRYGREDNTLIMTTRGGGLIIKILKRTAVFVEGGSEVGPPPAQAMKLNVPRKTRLYVDQTLREREAGTAMHRAFQTDLYLLRLRAARAYLQALESSLSPLSTTAREPLKLHAVVQGLGPTFKLTLHLQNTSTTRPVLGLLVCFLYNEALYSLPRAFFKVPLLVPGLNYPLETFVESLSNKGISDIIKVLVLREGQSAPLLSAHVNMPGSEGLAAA
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MAAASSSDS
------CCCCCCCCC		16.2519413330
78PhosphorylationLKGPLVMTESPLPAL
EECCEEEECCCCCCH		26.3230624053
80PhosphorylationGPLVMTESPLPALPA
CCEEEECCCCCCHHH		23.6730624053
91PhosphorylationALPAAAATFLMEQHE
CHHHHHHHHHHHHCC		16.7530624053
143UbiquitinationQDLWNQAKEDRIDPL
HHHHHHHHHCCCCHH		50.8429967540
153UbiquitinationRIDPLTLKEMLESIR
CCCHHHHHHHHHHHH		35.522190698
153 (in isoform 1)Ubiquitination-35.5221906983
153UbiquitinationRIDPLTLKEMLESIR
CCCHHHHHHHHHHHH		35.5221906983
190 (in isoform 2)Ubiquitination-41.3821906983
190UbiquitinationEAFVNQHKSNSIKRQ
HHHHHHHHCCCHHHH		41.3822817900
195UbiquitinationQHKSNSIKRQTVITT
HHHCCCHHHHHHHEE		37.9722817900
198PhosphorylationSNSIKRQTVITTMTT
CCCHHHHHHHEEHHH		20.2228509920
201PhosphorylationIKRQTVITTMTTLKK
HHHHHHHEEHHHHHH		13.2328509920
204PhosphorylationQTVITTMTTLKKNLA
HHHHEEHHHHHHHCC		27.2128509920
205PhosphorylationTVITTMTTLKKNLAD
HHHEEHHHHHHHCCC		26.2628509920
208UbiquitinationTTMTTLKKNLADEDA
EEHHHHHHHCCCCCH		61.3729967540
245 (in isoform 2)Ubiquitination-26.44-
317MalonylationSLHGFTHKGKKLWTV
CCCCCCCCCCEEEEE		70.1726320211
317UbiquitinationSLHGFTHKGKKLWTV
CCCCCCCCCCEEEEE		70.1729967540
323PhosphorylationHKGKKLWTVQMPAAI
CCCCEEEEEECCHHH		15.9922210691
332PhosphorylationQMPAAILTMNLLEQH
ECCHHHHHHHHHHHH		9.63-
340PhosphorylationMNLLEQHSRGLQAVM
HHHHHHHHHHHHHHH		27.9522210691
356 (in isoform 2)Ubiquitination-18.87-
361UbiquitinationEVRIYRDKALLNVIH
EEEEECCHHHHEECC		31.75-
369PhosphorylationALLNVIHTPDAVTSL
HHHEECCCCHHHHHH		16.2522817900
374PhosphorylationIHTPDAVTSLCFGRY
CCCCHHHHHHHCCCC		20.0822817900
375PhosphorylationHTPDAVTSLCFGRYG
CCCHHHHHHHCCCCC		19.2822817900
381PhosphorylationTSLCFGRYGREDNTL
HHHHCCCCCCCCCEE		22.40-
387PhosphorylationRYGREDNTLIMTTRG
CCCCCCCEEEEEEEC		29.9522210691
391PhosphorylationEDNTLIMTTRGGGLI
CCCEEEEEEECCCHH		13.3222210691
392PhosphorylationDNTLIMTTRGGGLII
CCEEEEEEECCCHHH		15.2217924679
398 (in isoform 2)Ubiquitination-3.22-
424UbiquitinationPPPAQAMKLNVPRKT
CCHHHHHCCCCCCCE		39.67-
454PhosphorylationAMHRAFQTDLYLLRL
HHHHHHHHHHHHHHH		22.8624719451
457PhosphorylationRAFQTDLYLLRLRAA
HHHHHHHHHHHHHHH		13.3924719451
467PhosphorylationRLRAARAYLQALESS
HHHHHHHHHHHHHHC		8.1929978859
473PhosphorylationAYLQALESSLSPLST
HHHHHHHHCCCCCCC		37.1129978859
474PhosphorylationYLQALESSLSPLSTT
HHHHHHHCCCCCCCC		24.4029978859
476PhosphorylationQALESSLSPLSTTAR
HHHHHCCCCCCCCCC		26.2429978859
479PhosphorylationESSLSPLSTTAREPL
HHCCCCCCCCCCCCH		27.3929978859
480PhosphorylationSSLSPLSTTAREPLK
HCCCCCCCCCCCCHH		31.9629978859
481PhosphorylationSLSPLSTTAREPLKL
CCCCCCCCCCCCHHH		21.9729978859
498PhosphorylationVVQGLGPTFKLTLHL
HEECCCCEEEEEEEE		31.44-
565UbiquitinationKGISDIIKVLVLREG
CCHHHHHHHHHCCCC		29.83-
602 (in isoform 2)Ubiquitination--
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of BBS1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BBS1_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of BBS1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ALDOB_HUMANALDOBphysical
18000879
BHMT1_HUMANBHMTphysical
18000879
CALC_HUMANCALCAphysical
18000879
CALCA_HUMANCALCAphysical
18000879
DCTN1_HUMANDCTN1physical
18000879
PARK7_HUMANPARK7physical
18000879
EF1A1_HUMANEEF1A1physical
18000879
EIF3A_HUMANEIF3Aphysical
18000879
EPAS1_HUMANEPAS1physical
18000879
EXOC7_HUMANEXOC7physical
18000879
FHOD1_HUMANFHOD1physical
18000879
HSC20_HUMANHSCBphysical
18000879
K1C18_HUMANKRT18physical
18000879
PAX2_HUMANPAX2physical
18000879
TSN7_HUMANTSPAN7physical
18000879
GLIS2_HUMANGLIS2physical
24500717
PTHB1_HUMANBBS9physical
28514442
BBS4_HUMANBBS4physical
28514442
BBS7_HUMANBBS7physical
28514442
TTC8_HUMANTTC8physical
28514442
DPP3_HUMANDPP3physical
28514442
BBS2_HUMANBBS2physical
28514442
KBP_HUMANKIAA1279physical
28514442
HSP7C_HUMANHSPA8physical
28514442
BBS5_HUMANBBS5physical
27173435
BBS7_HUMANBBS7physical
27173435
Drug and Disease Associations
Kegg Disease
H00418 Bardet-Biedl syndrome (BBS)
OMIM Disease
Note=Ciliary dysfunction leads to a broad spectrum of disorders, collectively termed ciliopathies. Overlapping clinical features include retinal degeneration, renal cystic disease, skeletal abnormalities, fibrosis of various organ, and a complex range of anatomical and functional defects of the central and peripheral nervous system. The ciliopathy range of diseases includes Meckel-Gruber syndrome, Bardet-Biedl syndrome, Joubert syndrome, nephronophtisis, Senior-Loken syndrome, and Jeune asphyxiating thoracic dystrophy among others. Single-locus allelism is insufficient to explain the variable penetrance and expressivity of such disorders, leading to the suggestion that variations across multiple sites of the ciliary proteome, including BBS1, influence the clinical outcome.
209900
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BBS1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-369, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-392, AND MASSSPECTROMETRY.

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