TR11B_HUMAN - dbPTM
TR11B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TR11B_HUMAN
UniProt AC O00300
Protein Name Tumor necrosis factor receptor superfamily member 11B
Gene Name TNFRSF11B
Organism Homo sapiens (Human).
Sequence Length 401
Subcellular Localization Secreted.
Protein Description Acts as decoy receptor for TNFSF11/RANKL and thereby neutralizes its function in osteoclastogenesis. Inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local ratio between TNFSF11 and TNFRSF11B. May also play a role in preventing arterial calcification. May act as decoy receptor for TNFSF10/TRAIL and protect against apoptosis. TNFSF10/TRAIL binding blocks the inhibition of osteoclastogenesis..
Protein Sequence MNNLLCCALVFLDISIKWTTQETFPPKYLHYDEETSHQLLCDKCPPGTYLKQHCTAKWKTVCAPCPDHYYTDSWHTSDECLYCSPVCKELQYVKQECNRTHNRVCECKEGRYLEIEFCLKHRSCPPGFGVVQAGTPERNTVCKRCPDGFFSNETSSKAPCRKHTNCSVFGLLLTQKGNATHDNICSGNSESTQKCGIDVTLCEEAFFRFAVPTKFTPNWLSVLVDNLPGTKVNAESVERIKRQHSSQEQTFQLLKLWKHQNKDQDIVKKIIQDIDLCENSVQRHIGHANLTFEQLRSLMESLPGKKVGAEDIEKTIKACKPSDQILKLLSLWRIKNGDQDTLKGLMHALKHSKTYHFPKTVTQSLKKTIRFLHSFTMYKLYQKLFLEMIGNQVQSVKISCL
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
69PhosphorylationCAPCPDHYYTDSWHT
EEECCCCCCCCCCCC
18.5530576142
70PhosphorylationAPCPDHYYTDSWHTS
EECCCCCCCCCCCCC
10.7230576142
77PhosphorylationYTDSWHTSDECLYCS
CCCCCCCCCCCEECC
20.6530576142
98N-linked_GlycosylationQYVKQECNRTHNRVC
HHHHHHHHCCCCCEE
51.65UniProtKB CARBOHYD
152N-linked_GlycosylationCPDGFFSNETSSKAP
CCCCCCCCCCCCCCC
51.95UniProtKB CARBOHYD
154PhosphorylationDGFFSNETSSKAPCR
CCCCCCCCCCCCCCC
42.4230206219
155PhosphorylationGFFSNETSSKAPCRK
CCCCCCCCCCCCCCC
24.5430206219
156PhosphorylationFFSNETSSKAPCRKH
CCCCCCCCCCCCCCC
40.0130206219
165N-linked_GlycosylationAPCRKHTNCSVFGLL
CCCCCCCCCCHHEEE
18.78UniProtKB CARBOHYD
178N-linked_GlycosylationLLLTQKGNATHDNIC
EEEEECCCCCCCCCC
49.0222664871
236PhosphorylationGTKVNAESVERIKRQ
CCCCCHHHHHHHHHH
27.2022210691
245PhosphorylationERIKRQHSSQEQTFQ
HHHHHHCCCHHHHHH
25.9424043423
246PhosphorylationRIKRQHSSQEQTFQL
HHHHHCCCHHHHHHH
35.3024043423
250PhosphorylationQHSSQEQTFQLLKLW
HCCCHHHHHHHHHHH
16.7624043423
289N-linked_GlycosylationQRHIGHANLTFEQLR
HHHHCCCCCCHHHHH
33.66UniProtKB CARBOHYD
330PhosphorylationDQILKLLSLWRIKNG
HHHHHHHHHHHCCCC
36.0024719451
360PhosphorylationKTYHFPKTVTQSLKK
CCCCCCHHHHHHHHH
29.08-
362PhosphorylationYHFPKTVTQSLKKTI
CCCCHHHHHHHHHHH
20.06-
364PhosphorylationFPKTVTQSLKKTIRF
CCHHHHHHHHHHHHH
32.56-
368PhosphorylationVTQSLKKTIRFLHSF
HHHHHHHHHHHHHHH
18.7929396449
374PhosphorylationKTIRFLHSFTMYKLY
HHHHHHHHHHHHHHH
25.2629396449
376PhosphorylationIRFLHSFTMYKLYQK
HHHHHHHHHHHHHHH
23.7029396449
378PhosphorylationFLHSFTMYKLYQKLF
HHHHHHHHHHHHHHH
8.5229396449

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 TR11B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TR11B_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 TR11B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TNF11_HUMANTNFSF11physical
9520411

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TR11B_HUMAN

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Related Literatures of Post-Translational Modification

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