TNF11_HUMAN - dbPTM
TNF11_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TNF11_HUMAN
UniProt AC O14788
Protein Name Tumor necrosis factor ligand superfamily member 11
Gene Name TNFSF11
Organism Homo sapiens (Human).
Sequence Length 317
Subcellular Localization Isoform 1: Cell membrane
Single-pass type II membrane protein.
Isoform 3: Cell membrane
Single-pass type II membrane protein.
Isoform 2: Cytoplasm.
Tumor necrosis factor ligand superfamily member 11, soluble form: Secreted.
Protein Description Cytokine that binds to TNFRSF11B/OPG and to TNFRSF11A/RANK. Osteoclast differentiation and activation factor. Augments the ability of dendritic cells to stimulate naive T-cell proliferation. May be an important regulator of interactions between T-cells and dendritic cells and may play a role in the regulation of the T-cell-dependent immune response. May also play an important role in enhanced bone-resorption in humoral hypercalcemia of malignancy. [PubMed: 22664871 Induces osteoclastogenesis by activating multiple signaling pathways in osteoclast precursor cells, chief among which is induction of long lasting oscillations in the intracellular concentration of Ca (2+) resulting in the activation of NFATC1, which translocates to the nucleus and induces osteoclast-specific gene transcription to allow differentiation of osteoclasts. During osteoclast differentiation, in a TMEM64 and ATP2A2-dependent manner induces activation of CREB1 and mitochondrial ROS generation necessary for proper osteoclast generation (By similarity]
Protein Sequence MRRASRDYTKYLRGSEEMGGGPGAPHEGPLHAPPPPAPHQPPAASRSMFVALLGLGLGQVVCSVALFFYFRAQMDPNRISEDGTHCIYRILRLHENADFQDTTLESQDTKLIPDSCRRIKQAFQGAVQKELQHIVGSQHIRAEKAMVDGSWLDLAKRSKLEAQPFAHLTINATDIPSGSHKVSLSSWYHDRGWAKISNMTFSNGKLIVNQDGFYYLYANICFRHHETSGDLATEYLQLMVYVTKTSIKIPSSHTLMKGGSTKYWSGNSEFHFYSINVGGFFKLRSGEEISIEVSNPSLLDPDQDATYFGAFKVRDID
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
137PhosphorylationELQHIVGSQHIRAEK
HHHHHHCCHHHEEEE
14.00-
171N-linked_GlycosylationPFAHLTINATDIPSG
CCCEEEEECCCCCCC
31.39UniProtKB CARBOHYD
198N-linked_GlycosylationRGWAKISNMTFSNGK
CCEEEEEEEEEECCE
36.67UniProtKB CARBOHYD

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 TNF11_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TNF11_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 TNF11_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SRC_HUMANSRCphysical
10635328
ZN675_HUMANZNF675genetic
11751921
PLK1_HUMANPLK1physical
21900206
DDAH2_HUMANDDAH2physical
21900206
PGFS_HUMANFAM213Bphysical
21900206
TMOD3_HUMANTMOD3physical
21900206
LMO4_HUMANLMO4physical
21900206
TRM2A_HUMANTRMT2Aphysical
21900206
MED24_HUMANMED24physical
21900206
BBS10_HUMANBBS10physical
21900206
U1SBP_HUMANSNRNP35physical
21900206
CE126_HUMANKIAA1377physical
21900206
MTMR5_HUMANSBF1physical
21900206
PHAX_HUMANPHAXphysical
21900206
MBTP1_HUMANMBTPS1physical
21900206
EF1A1_HUMANEEF1A1physical
21900206
NIPA_HUMANZC3HC1physical
21900206
EZH2_HUMANEZH2physical
21900206
GALT7_HUMANGALNT7physical
26186194
GOSR1_HUMANGOSR1physical
26186194
AT5G1_HUMANATP5G1physical
26186194
NU1M_HUMANND1physical
26186194
DNJB9_HUMANDNAJB9physical
26186194
B4GT7_HUMANB4GALT7physical
26186194
GOSR1_HUMANGOSR1physical
28514442
AT5G1_HUMANATP5G1physical
28514442
DNJB9_HUMANDNAJB9physical
28514442
NU1M_HUMANND1physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TNF11_HUMAN

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Related Literatures of Post-Translational Modification

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