PTHB1_HUMAN - dbPTM
PTHB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PTHB1_HUMAN
UniProt AC Q3SYG4
Protein Name Protein PTHB1
Gene Name BBS9
Organism Homo sapiens (Human).
Sequence Length 887
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. 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. Required for proper BBSome complex assembly and its ciliary localization..
Protein Sequence MSLFKARDWWSTILGDKEEFDQGCLCLANVDNSGNGQDKIIVGSFMGYLRIFSPHPAKTGDGAQAEDLLLEVDLRDPVLQVEVGKFVSGTEMLHLAVLHSRKLCVYSVSGTLGNVEHGNQCQMKLMYEHNLQRTACNMTYGSFGGVKGRDLICIQSMDGMLMVFEQESYAFGRFLPGFLLPGPLAYSSRTDSFLTVSSCQQVESYKYQVLAFATDADKRQETEQQKLGSGKRLVVDWTLNIGEQALDICIVSFNQSASSVFVLGERNFFCLKDNGQIRFMKKLDWSPSCFLPYCSVSEGTINTLIGNHNNMLHIYQDVTLKWATQLPHIPVAVRVGCLHDLKGVIVTLSDDGHLQCSYLGTDPSLFQAPNVQSRELNYDELDVEMKELQKIIKDVNKSQGVWPMTEREDDLNVSVVVSPNFDSVSQATDVEVGTDLVPSVTVKVTLQNRVILQKAKLSVYVQPPLELTCDQFTFEFMTPDLTRTVSFSVYLKRSYTPSELEGNAVVSYSRPTDRNPDGIPRVIQCKFRLPLKLICLPGQPSKTASHKITIDTNKSPVSLLSLFPGFASQSDDDQVNVMGFHFLGGARITVLASKTSQRYRIQSEQFEDLWLITNELILRLQEYFEKQGVKDFACSFSGSIPLQEYFELIDHHFELRINGEKLEELLSERAVQFRAIQRRLLARFKDKTPAPLQHLDTLLDGTYKQVIALADAVEENQGNLFQSFTRLKSATHLVILLIALWQKLSADQVAILEAAFLPLQEDTQELGWEETVDAAISHLLKTCLSKSSKEQALNLNSQLNIPKDTSQLKKHITLLCDRLSKGGRLCLSTDAAAPQTMVMPGGCTTIPESDLEERSVEQDSTELFTNHRHLTAETPRPEVSPLQGVSE
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
2Phosphorylation------MSLFKARDW
------CCCCHHHHH
42.3824719451
5Ubiquitination---MSLFKARDWWST
---CCCCHHHHHHHH
48.05-
127PhosphorylationQCQMKLMYEHNLQRT
CEEEEEHHHHCCCCH
25.1922210691
134PhosphorylationYEHNLQRTACNMTYG
HHHCCCCHHCCCCCC
23.7022210691
147UbiquitinationYGSFGGVKGRDLICI
CCCCCCCCCCEEEEE
52.05-
226UbiquitinationRQETEQQKLGSGKRL
HHHHHHHHCCCCCEE
55.28-
286PhosphorylationFMKKLDWSPSCFLPY
EEECCCCCCCCCCCE
13.4522210691
300PhosphorylationYCSVSEGTINTLIGN
EEECCCCCEEEECCC
13.6522210691
319PhosphorylationLHIYQDVTLKWATQL
EEEEEEEEHHHHHCC
30.8022210691
378PhosphorylationVQSRELNYDELDVEM
CCCCCCCHHHHHHHH
24.3428796482
386UbiquitinationDELDVEMKELQKIIK
HHHHHHHHHHHHHHH
41.59-
390MalonylationVEMKELQKIIKDVNK
HHHHHHHHHHHHHHH
60.0526320211
390AcetylationVEMKELQKIIKDVNK
HHHHHHHHHHHHHHH
60.0523749302
473 (in isoform 4)Phosphorylation-19.34-
494PhosphorylationFSVYLKRSYTPSELE
EEEEEECCCCHHHEE
31.6025262027
495PhosphorylationSVYLKRSYTPSELEG
EEEEECCCCHHHEEC
27.0625262027
496PhosphorylationVYLKRSYTPSELEGN
EEEECCCCHHHEECC
22.9125262027
498PhosphorylationLKRSYTPSELEGNAV
EECCCCHHHEECCEE
47.1925262027
507 (in isoform 7)Phosphorylation-15.7022210691
507PhosphorylationLEGNAVVSYSRPTDR
EECCEEEEECCCCCC
15.7025262027
508 (in isoform 7)Phosphorylation-9.3322210691
508PhosphorylationEGNAVVSYSRPTDRN
ECCEEEEECCCCCCC
9.3325262027
509 (in isoform 7)Phosphorylation-25.0322210691
509PhosphorylationGNAVVSYSRPTDRNP
CCEEEEECCCCCCCC
25.0325262027
512PhosphorylationVVSYSRPTDRNPDGI
EEEECCCCCCCCCCC
46.6230206219
542UbiquitinationCLPGQPSKTASHKIT
ECCCCCCCCCCEEEE
55.59-
549PhosphorylationKTASHKITIDTNKSP
CCCCEEEEEECCCCC
20.01-
552PhosphorylationSHKITIDTNKSPVSL
CEEEEEECCCCCCHH
40.47-
593O-linked_GlycosylationARITVLASKTSQRYR
CEEEEEEECCCCCCC
32.1030379171
595O-linked_GlycosylationITVLASKTSQRYRIQ
EEEEEECCCCCCCCC
27.8330379171
785PhosphorylationHLLKTCLSKSSKEQA
HHHHHHCCCCCHHHH
32.4123532336
788PhosphorylationKTCLSKSSKEQALNL
HHHCCCCCHHHHHCC
43.9023532336
789UbiquitinationTCLSKSSKEQALNLN
HHCCCCCHHHHHCCH
62.02-
810UbiquitinationKDTSQLKKHITLLCD
CCHHHHHHHHHHHHH
49.16-
828PhosphorylationKGGRLCLSTDAAAPQ
CCCCEEEECCCCCCC
24.2022210691
836PhosphorylationTDAAAPQTMVMPGGC
CCCCCCCEEEECCCC
15.6326074081
844PhosphorylationMVMPGGCTTIPESDL
EEECCCCCCCCHHHH
30.9122210691
845PhosphorylationVMPGGCTTIPESDLE
EECCCCCCCCHHHHH
38.3126074081
849PhosphorylationGCTTIPESDLEERSV
CCCCCCHHHHHCCCC
41.9826074081
880PhosphorylationETPRPEVSPLQGVSE
CCCCCCCCCCCCCCC
20.4525159151

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 PTHB1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PTHB1_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 PTHB1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BBS5_HUMANBBS5physical
27173435
BBS1_HUMANBBS1physical
27173435
BBS7_HUMANBBS7physical
27173435

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PTHB1_HUMAN

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Related Literatures of Post-Translational Modification

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