BBS4_HUMAN - dbPTM
BBS4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BBS4_HUMAN
UniProt AC Q96RK4
Protein Name Bardet-Biedl syndrome 4 protein
Gene Name BBS4
Organism Homo sapiens (Human).
Sequence Length 519
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cell projection, cilium membrane. Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite. Cell projection, cilium, flagellum . Cell projection
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. Required for microtubule anchoring at the centrosome but not for microtubule nucleation. May be required for the dynein-mediated transport of pericentriolar proteins to the centrosome..
Protein Sequence MAEERVATRTQFPVSTESQKPRQKKAPEFPILEKQNWLIHLHYIRKDYEACKAVIKEQLQETQGLCEYAIYVQALIFRLEGNIQESLELFQTCAVLSPQSADNLKQVARSLFLLGKHKAAIEVYNEAAKLNQKDWEISHNLGVCYIYLKQFNKAQDQLHNALNLNRHDLTYIMLGKIHLLEGDLDKAIEVYKKAVEFSPENTELLTTLGLLYLQLGIYQKAFEHLGNALTYDPTNYKAILAAGSMMQTHGDFDVALTKYRVVACAVPESPPLWNNIGMCFFGKKKYVAAISCLKRANYLAPFDWKILYNLGLVHLTMQQYASAFHFLSAAINFQPKMGELYMLLAVALTNLEDIENAKRAYAEAVHLDKCNPLVNLNYAVLLYNQGEKKNALAQYQEMEKKVSLLKDNSSLEFDSEMVEMAQKLGAALQVGEALVWTKPVKDPKSKHQTTSTSKPASFQQPLGSNQALGQAMSSAAAYRTLPSGAGGTSQFTKPPSLPLEPEPAVESSPTETSEQIREK
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
15PhosphorylationTRTQFPVSTESQKPR
CCCCCCCCCCCCCCH		27.0529083192
16PhosphorylationRTQFPVSTESQKPRQ
CCCCCCCCCCCCCHH		39.6329083192
18PhosphorylationQFPVSTESQKPRQKK
CCCCCCCCCCCHHCC		43.5229083192
20AcetylationPVSTESQKPRQKKAP
CCCCCCCCCHHCCCC		51.9923749302
20 (in isoform 1)Ubiquitination-51.9921906983
20UbiquitinationPVSTESQKPRQKKAP
CCCCCCCCCHHCCCC		51.9921906983
28 (in isoform 2)Ubiquitination-69.7621906983
43PhosphorylationNWLIHLHYIRKDYEA
CEEEEEEHHHHCHHH		14.58-
48PhosphorylationLHYIRKDYEACKAVI
EEHHHHCHHHHHHHH		14.41-
52UbiquitinationRKDYEACKAVIKEQL
HHCHHHHHHHHHHHH		53.38-
118 (in isoform 1)Ubiquitination-42.8921906983
118UbiquitinationLFLLGKHKAAIEVYN
HHHHHHHHHHHHHHH		42.8921906983
124 (in isoform 2)Ubiquitination-8.42-
126 (in isoform 2)Ubiquitination-32.1121906983
129 (in isoform 1)Ubiquitination-55.8321906983
129UbiquitinationEVYNEAAKLNQKDWE
HHHHHHHHHCHHHHH		55.832190698
137 (in isoform 2)Ubiquitination-4.4121906983
153UbiquitinationIYLKQFNKAQDQLHN
HHHHHHHHHHHHHHH		49.03-
170PhosphorylationNLNRHDLTYIMLGKI
CCCHHHHHHHEECCE		19.63-
171PhosphorylationLNRHDLTYIMLGKIH
CCHHHHHHHEECCEE		7.51-
186UbiquitinationLLEGDLDKAIEVYKK
HHCCCHHHHHHHHHH		59.57-
191PhosphorylationLDKAIEVYKKAVEFS
HHHHHHHHHHHHHCC		8.25-
201 (in isoform 2)Ubiquitination-42.09-
202PhosphorylationVEFSPENTELLTTLG
HHCCHHHHHHHHHHH		26.7524719451
206PhosphorylationPENTELLTTLGLLYL
HHHHHHHHHHHHHHH		32.3824719451
218PhosphorylationLYLQLGIYQKAFEHL
HHHHHCHHHHHHHHH		11.3624719451
244PhosphorylationKAILAAGSMMQTHGD
HHHHHHHHHHHHCCC		13.3222210691
248PhosphorylationAAGSMMQTHGDFDVA
HHHHHHHHCCCCCCE		15.2122210691
257PhosphorylationGDFDVALTKYRVVAC
CCCCCEECEEEEEEE		19.1122210691
259PhosphorylationFDVALTKYRVVACAV
CCCEECEEEEEEEEC		11.9122210691
285MalonylationMCFFGKKKYVAAISC
EECCCCHHHHHHHHH		48.7426320211
294UbiquitinationVAAISCLKRANYLAP
HHHHHHHHHCCCCCC		54.51-
302 (in isoform 2)Ubiquitination-16.98-
389UbiquitinationLYNQGEKKNALAQYQ
HHCCCCHHHHHHHHH		43.05-
395PhosphorylationKKNALAQYQEMEKKV
HHHHHHHHHHHHHHH		10.79-
397 (in isoform 2)Ubiquitination-44.36-
403PhosphorylationQEMEKKVSLLKDNSS
HHHHHHHHHHCCCCC		36.5424719451
406UbiquitinationEKKVSLLKDNSSLEF
HHHHHHHCCCCCCCC		61.22-
409 (in isoform 2)Ubiquitination-46.57-
414 (in isoform 2)Ubiquitination-34.02-
454UbiquitinationHQTTSTSKPASFQQP
CCCCCCCCCCCCCCC		44.70-
478PhosphorylationAMSSAAAYRTLPSGA
HHHHHHHHHCCCCCC		10.21-
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 BBS4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BBS4_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 BBS4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PCM1_HUMANPCM1physical
15107855
DCTN1_HUMANDCTN1physical
15107855
ACTB_HUMANACTBphysical
18000879
ALDOB_HUMANALDOBphysical
18000879
BHMT1_HUMANBHMTphysical
18000879
CALC_HUMANCALCAphysical
18000879
CALCA_HUMANCALCAphysical
18000879
DCTN1_HUMANDCTN1physical
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
PCM1_HUMANPCM1physical
18000879
MYOG_HUMANMYOGphysical
25416956
BBS5_HUMANBBS5physical
27173435
BBS1_HUMANBBS1physical
27173435
PTHB1_HUMANBBS9physical
27173435
BBS7_HUMANBBS7physical
27173435
Drug and Disease Associations
Kegg Disease
H00418 Bardet-Biedl syndrome (BBS)
OMIM Disease
615982Bardet-Biedl syndrome 4 (BBS4)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BBS4_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory