BBS2_HUMAN - dbPTM
BBS2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BBS2_HUMAN
UniProt AC Q9BXC9
Protein Name Bardet-Biedl syndrome 2 protein
Gene Name BBS2
Organism Homo sapiens (Human).
Sequence Length 721
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..
Protein Sequence MLLPVFTLKLRHKISPRMVAIGRYDGTHPCLAAATQTGKVFIHNPHTRNQHVSASRVFQSPLESDVSLLNINQAVSCLTAGVLNPELGYDALLVGTQTNLLAYDVYNNSDLFYREVADGANAIVLGTLGDISSPLAIIGGNCALQGFNHEGSDLFWTVTGDNVNSLALCDFDGDGKKELLVGSEDFDIRVFKEDEIVAEMTETEIVTSLCPMYGSRFGYALSNGTVGVYDKTSRYWRIKSKNHAMSIHAFDLNSDGVNELITGWSNGKVDARSDRTGEVIFKDNFSSAIAGVVEGDYRMDGHIQLICCSVDGEIRGYLPGTAEMRGNLMDTSAEQDLIRELSQKKQNLLLELRNYEENAKAELASPLNEADGHRGIIPANTRLHTTLSVSLGNETQTAHTELRISTSNDTIIRAVLIFAEGIFTGESHVVHPSIHNLSSSICIPIVPPKDVPVDLHLKAFVGYRSSTQFHVFESTRQLPRFSMYALTSLDPASEPISYVNFTIAERAQRVVVWLGQNFLLPEDTHIQNAPFQVCFTSLRNGGHLHIKIKLSGEITINTDDIDLAGDIIQSMASFFAIEDLQVEADFPVYFEELRKVLVKVDEYHSVHQKLSADMADHSNLIRSLLVGAEDARLMRDMKTMKSRYMELYDLNRDLLNGYKIRCNNHTELLGNLKAVNQAIQRAGRLRVGKPKNQVITACRDAIRSNNINTLFKIMRVGTASS
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
7Phosphorylation-MLLPVFTLKLRHKI
-CCCCEEEEEEECCC		24.1829396449
9UbiquitinationLLPVFTLKLRHKISP
CCCEEEEEEECCCCC		40.1833845483
13UbiquitinationFTLKLRHKISPRMVA
EEEEEECCCCCCEEE		38.1429967540
39UbiquitinationAAATQTGKVFIHNPH
EEEECCCCEEEECCC		37.0421963094
201PhosphorylationDEIVAEMTETEIVTS
CCEEEECCCHHHHHH		31.1232142685
203PhosphorylationIVAEMTETEIVTSLC
EEEECCCHHHHHHHC		23.1132142685
208PhosphorylationTETEIVTSLCPMYGS
CCHHHHHHHCCCCCC		19.65-
213PhosphorylationVTSLCPMYGSRFGYA
HHHHCCCCCCCCEEE		9.33-
231UbiquitinationGTVGVYDKTSRYWRI
CEEEEEECCCCEEEE		30.6121906983
239MethylationTSRYWRIKSKNHAMS
CCCEEEEEECCCCEE		46.97-
268UbiquitinationITGWSNGKVDARSDR
HHCCCCCCEECCCCC		40.99-
329SulfoxidationAEMRGNLMDTSAEQD
HHHCCCCCCCCHHHH		6.4830846556
345UbiquitinationIRELSQKKQNLLLEL
HHHHHHHHHHHHHHH		36.4633845483
360UbiquitinationRNYEENAKAELASPL
HCHHHHHHHHHCCCC		54.7121906983
365PhosphorylationNAKAELASPLNEADG
HHHHHHCCCCCCCCC		42.4127050516
405O-linked_GlycosylationAHTELRISTSNDTII
EEEEEEEECCCHHHH		21.2528657654
573PhosphorylationDIIQSMASFFAIEDL
HHHHHHHHHHCCCCC		16.5626074081
599UbiquitinationELRKVLVKVDEYHSV
HHHHHHEEHHHHHCH		39.5529967540
603PhosphorylationVLVKVDEYHSVHQKL
HHEEHHHHHCHHHHH		8.5727642862
609UbiquitinationEYHSVHQKLSADMAD
HHHCHHHHHCHHHCC		29.5421906983
623PhosphorylationDHSNLIRSLLVGAED
CCHHHHHHHHHCHHH		21.04-
638AcetylationARLMRDMKTMKSRYM
HHHHHHHHHHHHHHH		50.167395433
658PhosphorylationNRDLLNGYKIRCNNH
CHHHHCCCEEECCCC		11.36-
659UbiquitinationRDLLNGYKIRCNNHT
HHHHCCCEEECCCCH		25.6921906983
673UbiquitinationTELLGNLKAVNQAIQ
HHHHHHHHHHHHHHH		55.0521963094
689UbiquitinationAGRLRVGKPKNQVIT
HCCCCCCCCHHHHHH		50.3829967540
691UbiquitinationRLRVGKPKNQVITAC
CCCCCCCHHHHHHHH		64.5929967540
712UbiquitinationNNINTLFKIMRVGTA
CCHHHHHHHEECCCC		38.4123000965
718PhosphorylationFKIMRVGTASS----
HHHEECCCCCC----		22.1021712546
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
-KUbiquitinationE3 ubiquitin ligaseTRIM32Q13049
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BBS2_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 BBS2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PSME3_HUMANPSME3physical
16189514
ALDOB_HUMANALDOBphysical
18000879
BHMT1_HUMANBHMTphysical
18000879
EF1A1_HUMANEEF1A1physical
18000879
EPAS1_HUMANEPAS1physical
18000879
EXOC7_HUMANEXOC7physical
18000879
FHOD1_HUMANFHOD1physical
18000879
HSC20_HUMANHSCBphysical
18000879
K1C18_HUMANKRT18physical
18000879
PAX2_HUMANPAX2physical
18000879
GLIS2_HUMANGLIS2physical
24500717
MDFI_HUMANMDFIphysical
25416956
PSME3_HUMANPSME3physical
25416956
RBPMS_HUMANRBPMSphysical
25416956
PTHB1_HUMANBBS9physical
27173435
BBS7_HUMANBBS7physical
27173435
BBS5_HUMANBBS5physical
27173435
BBS1_HUMANBBS1physical
27173435
BBS4_HUMANBBS4physical
27173435
Drug and Disease Associations
Kegg Disease
H00418 Bardet-Biedl syndrome (BBS)
OMIM Disease
615981Bardet-Biedl syndrome 2 (BBS2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BBS2_HUMAN

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Related Literatures of Post-Translational Modification

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