Tumor necrosis factor

mammalian protein found in the house mouse (Mus musculus)

Protein protein Q21992447

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Tumor necrosis factor

Summary

Tumor necrosis factor is a protein^[1].

Key Facts

Tumor necrosis factor's instance of is recorded as protein^[2].
Tumor necrosis factor's UniProt protein ID is recorded as P06804^[3].
Tumor necrosis factor's part of is recorded as Tumour necrosis factor-like domain superfamily^[4].
Tumor necrosis factor's part of is recorded as Tumour necrosis factor alpha^[5].
Tumor necrosis factor's part of is recorded as membrane protein^[6].
Tumor necrosis factor's part of is recorded as Tumour necrosis factor domain, protein family^[7].
Tumor necrosis factor's part of is recorded as Tumour necrosis factor, conserved site, protein family^[8].
Tumor necrosis factor's has part is recorded as Tumour necrosis factor domain^[9].
Tumor necrosis factor's has part is recorded as Tumour necrosis factor, conserved site^[10].
Tumor necrosis factor's RefSeq protein ID is recorded as NP_001265530^[11].
Tumor necrosis factor's RefSeq protein ID is recorded as NP_038721^[12].
Tumor necrosis factor's PDB structure ID is recorded as 2TNF^[13].
Tumor necrosis factor's molecular function is recorded as cytokine activity^[14].
Tumor necrosis factor's molecular function is recorded as tumor necrosis factor receptor binding^[15].
Tumor necrosis factor's molecular function is recorded as protease binding^[16].
Tumor necrosis factor's molecular function is recorded as protein binding^[17].
Tumor necrosis factor's molecular function is recorded as identical protein binding^[18].
Tumor necrosis factor's molecular function is recorded as RNA polymerase II transcription regulatory region sequence-specific DNA binding^[19].
Tumor necrosis factor's molecular function is recorded as cytokine activity^[20].
Tumor necrosis factor's molecular function is recorded as tumor necrosis factor receptor binding^[21].
Tumor necrosis factor's cell component is recorded as membrane^[22].
Tumor necrosis factor's cell component is recorded as extracellular region^[23].
Tumor necrosis factor's cell component is recorded as cell surface^[24].
Tumor necrosis factor's cell component is recorded as membrane raft^[25].
Tumor necrosis factor's cell component is recorded as recycling endosome^[26].

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Quick Facts

Instance of protein

Part of Tumour necrosis factor-like domain superfamily, Tumour necrosis factor alpha, membrane protein, Tumour necrosis factor domain, protein family, Tumour necrosis factor, conserved site, protein family

Properties

Biological process regulation of protein phosphorylation, positive regulation of protein phosphorylation, positive regulation of MAP kinase activity, positive regulation of calcidiol 1-monooxygenase activity, positive regulation of programmed cell death, tumor necrosis factor-mediated signaling pathway, positive regulation of JNK cascade, response to organic substance, negative regulation of osteoblast differentiation, positive regulation of cysteine-type endopeptidase activity involved in apoptotic process, negative regulation of viral genome replication, humoral immune response, positive regulation of interleukin-8 production, intrinsic apoptotic signaling pathway in response to DNA damage, positive regulation of protein localization to cell surface, glucose metabolic process, animal organ morphogenesis, apoptotic signaling pathway, negative regulation of alkaline phosphatase activity, cell population proliferation, activation of cysteine-type endopeptidase activity involved in apoptotic process, regulation of I-kappaB kinase/NF-kappaB signaling, defense response to Gram-positive bacterium, regulation of branching involved in salivary gland morphogenesis, positive regulation of phagocytosis, negative regulation of myoblast differentiation, positive regulation of protein kinase B signaling, extrinsic apoptotic signaling pathway, regulation of insulin secretion, osteoclast differentiation, response to virus, positive regulation of osteoclast differentiation, negative regulation of cytokine production involved in immune response, positive regulation of peptidyl-serine phosphorylation, negative regulation of branching involved in lung morphogenesis, positive regulation of transcription, DNA-templated, JNK cascade, regulation of osteoclast differentiation, defense response to bacterium, necroptotic signaling pathway, positive regulation of interleukin-6 production, inflammatory response, positive regulation of translational initiation by iron, sequestering of triglyceride, positive regulation of chronic inflammatory response to antigenic stimulus, positive regulation of chemokine (C-X-C motif) ligand 2 production, positive regulation of JUN kinase activity, positive regulation of hair follicle development, chronic inflammatory response to antigenic stimulus, cellular response to organic cyclic compound, positive regulation of fever generation, extracellular matrix organization, positive regulation of DNA-binding transcription factor activity, cellular response to nicotine, positive regulation of podosome assembly, negative regulation of transcription by RNA polymerase II, regulation of reactive oxygen species metabolic process, positive regulation of protein transport, immune response, leukocyte tethering or rolling, positive regulation of chemokine production, cellular extravasation, negative regulation of myosin-light-chain-phosphatase activity, negative regulation of transcription, DNA-templated, cortical actin cytoskeleton organization, embryonic digestive tract development, leukocyte migration, lipopolysaccharide-mediated signaling pathway, positive regulation of smooth muscle cell proliferation, positive regulation of protein kinase activity, positive regulation of superoxide dismutase activity, defense response, positive regulation of protein-containing complex assembly, protein kinase B signaling, positive regulation of cytokine production, epithelial cell proliferation involved in salivary gland morphogenesis, positive regulation of nitric oxide biosynthetic process, negative regulation of interleukin-6 production, positive regulation of membrane protein ectodomain proteolysis, positive regulation of humoral immune response mediated by circulating immunoglobulin, positive regulation of interferon-gamma production, response to glucocorticoid, positive regulation of vitamin D biosynthetic process, MAPK cascade, multicellular organism development, negative regulation of protein-containing complex disassembly, negative regulation of bicellular tight junction assembly, positive regulation of protein-containing complex disassembly, positive regulation of gene expression, regulation of cell population proliferation, positive regulation of cell population proliferation, positive regulation of apoptotic process, cellular response to amino acid stimulus, positive regulation of I-kappaB kinase/NF-kappaB signaling, negative regulation of extrinsic apoptotic signaling pathway in absence of ligand, cellular response to lipopolysaccharide, negative regulation of lipid catabolic process, regulation of establishment of endothelial barrier, extrinsic apoptotic signaling pathway via death domain receptors, positive regulation of cell adhesion, positive regulation of transcription by RNA polymerase II, regulation of protein secretion, positive regulation of blood microparticle formation, positive regulation of leukocyte adhesion to arterial endothelial cell, negative regulation of endothelial cell proliferation, positive regulation of heterotypic cell-cell adhesion, negative regulation of mitotic cell cycle, positive regulation of NF-kappaB transcription factor activity, endothelial cell apoptotic process, positive regulation of vascular associated smooth muscle cell proliferation, positive regulation of leukocyte adhesion to vascular endothelial cell, negative regulation of gene expression, protein localization to plasma membrane, regulation of signaling receptor activity, positive regulation of protein catabolic process, regulation of inflammatory response, positive regulation of calcineurin-NFAT signaling cascade, positive regulation of NIK/NF-kappaB signaling, cell activation, negative regulation of L-glutamate import across plasma membrane, apoptotic process, signal transduction, negative regulation of cell population proliferation, calcium-mediated signaling, negative regulation of myelination, response to lipopolysaccharide, positive regulation of interleukin-18 production, toll-like receptor 3 signaling pathway, positive regulation of neuron apoptotic process, positive regulation of action potential, positive regulation of mitotic nuclear division, negative regulation of glucose import, positive regulation of inflammatory response, positive regulation of synaptic transmission, detection of mechanical stimulus involved in sensory perception of pain, regulation of transcription by RNA polymerase II, positive regulation of gene expression, positive regulation of phosphatidylinositol 3-kinase signaling, vasodilation, positive regulation of tyrosine phosphorylation of STAT protein, positive regulation of receptor signaling pathway via JAK-STAT, positive regulation of synaptic transmission, regulation of synapse organization, positive regulation of protein kinase B signaling, positive regulation of glial cell proliferation, positive regulation of protein localization to plasma membrane, regulation of endothelial cell apoptotic process, microglial cell activation, regulation of cell population proliferation, positive regulation of neuron apoptotic process, negative regulation of fat cell differentiation, positive regulation of interleukin-6 production, extrinsic apoptotic signaling pathway via death domain receptors, positive regulation of interleukin-6 production, tumor necrosis factor-mediated signaling pathway, positive regulation of I-kappaB kinase/NF-kappaB signaling, positive regulation of transcription by RNA polymerase II, positive regulation of NF-kappaB transcription factor activity, positive regulation of nitrogen compound metabolic process, negative regulation of amyloid-beta clearance, positive regulation of amyloid-beta formation

Cell component membrane, extracellular region, cell surface, membrane raft, recycling endosome, plasma membrane, secretory granule, integral component of plasma membrane, phagocytic cup, external side of plasma membrane, intracellular anatomical structure, extracellular space, integral component of membrane, external side of plasma membrane, integral component of membrane, cytoplasm, soma, extracellular space, cell surface

Encoded by Tnf

Found in taxon house mouse

Has part(s) Tumour necrosis factor domain, Tumour necrosis factor, conserved site

Imported from wholeness_audit_2026-05-02

Molecular function cytokine activity, tumor necrosis factor receptor binding, protease binding, protein binding, identical protein binding, RNA polymerase II transcription regulatory region sequence-specific DNA binding, cytokine activity, tumor necrosis factor receptor binding

External References (4)

Ensembl protein id ENSMUSP00000025263, ENSMUSP00000126122

Pdb structure id 2TNF

Refseq protein id NP_001265530, NP_038721

Uniprot protein id P06804

References

Programmatic citations — every numbered marker resolves to a verifiable graph row below.

Direct Wikidata claims

[2] ↑ Tumor necrosis factor — instance of (P31): protein. Q905695. Retrieved 2022-05-25. wikidata.org.
[3] ↑ Tumor necrosis factor — UniProt protein ID (P352): P06804. Q905695. Retrieved 2022-05-25. wikidata.org.
[4] ↑ Tumor necrosis factor — part of (P361): Tumour necrosis factor-like domain superfamily. InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
[5] ↑ Tumor necrosis factor — part of (P361): Tumour necrosis factor alpha. InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
[6] ↑ Tumor necrosis factor — part of (P361): membrane protein. wikidata.org.
[7] ↑ Tumor necrosis factor — part of (P361): Tumour necrosis factor domain, protein family. wikidata.org.
[8] ↑ Tumor necrosis factor — part of (P361): Tumour necrosis factor, conserved site, protein family. wikidata.org.
[9] ↑ Tumor necrosis factor — has part(s) (P527): Tumour necrosis factor domain. InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
[10] ↑ Tumor necrosis factor — has part(s) (P527): Tumour necrosis factor, conserved site. InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
[11] ↑ Tumor necrosis factor — RefSeq protein ID (P637): NP_001265530. Q20641742. Retrieved 2022-03-20. wikidata.org.
[12] ↑ Tumor necrosis factor — RefSeq protein ID (P637): NP_038721. Q20641742. Retrieved 2022-03-20. wikidata.org.
[13] ↑ Tumor necrosis factor — PDB structure ID (P638): 2TNF. Q905695. Retrieved 2016-08-09. wikidata.org.
[14] ↑ Tumor necrosis factor — molecular function (P680): cytokine activity. GOA. Retrieved 2019-04-08. ebi.ac.uk. Provenance: wikidata.org.
[15] ↑ Tumor necrosis factor — molecular function (P680): tumor necrosis factor receptor binding. Mice deficient for the 55 kd tumor necrosis factor receptor are resistant to endotoxic shock, yet succumb to L. monocytogenes infection. Retrieved 2019-04-08. ebi.ac.uk. Provenance: wikidata.org.
[16] ↑ Tumor necrosis factor — molecular function (P680): protease binding. GOA. Retrieved 2019-05-09. ebi.ac.uk. Provenance: wikidata.org.
[17] ↑ Tumor necrosis factor — molecular function (P680): protein binding. Keratin 17 modulates hair follicle cycling in a TNFalpha-dependent fashion. Retrieved 2019-05-09. ebi.ac.uk. Provenance: wikidata.org.
[18] ↑ Tumor necrosis factor — molecular function (P680): identical protein binding. GOA. Retrieved 2019-05-09. ebi.ac.uk. Provenance: wikidata.org.
[19] ↑ Tumor necrosis factor — molecular function (P680): RNA polymerase II transcription regulatory region sequence-specific DNA binding. GOA. Retrieved 2019-04-08. ebi.ac.uk. Provenance: wikidata.org.
[20] ↑ Tumor necrosis factor — molecular function (P680): cytokine activity. GOA. Retrieved 2019-05-09. ebi.ac.uk. Provenance: wikidata.org.
[21] ↑ Tumor necrosis factor — molecular function (P680): tumor necrosis factor receptor binding. Mice lacking the tumour necrosis factor receptor 1 are resistant to TNF-mediated toxicity but highly susceptible to infection by Listeria monocytogenes. Retrieved 2019-05-09. ebi.ac.uk. Provenance: wikidata.org.
[22] ↑ Tumor necrosis factor — cell component (P681): membrane. GOA. Retrieved 2019-05-09. ebi.ac.uk. Provenance: wikidata.org.
[23] ↑ Tumor necrosis factor — cell component (P681): extracellular region. GOA. Retrieved 2019-05-09. ebi.ac.uk. Provenance: wikidata.org.
[24] ↑ Tumor necrosis factor — cell component (P681): cell surface. GOA. Retrieved 2019-04-08. ebi.ac.uk. Provenance: wikidata.org.
[25] ↑ Tumor necrosis factor — cell component (P681): membrane raft. GOA. Retrieved 2019-05-09. ebi.ac.uk. Provenance: wikidata.org.
[26] ↑ Tumor necrosis factor — cell component (P681): recycling endosome. A role for the phagosome in cytokine secretion. Retrieved 2019-05-09. ebi.ac.uk. Provenance: wikidata.org.

Class ancestry

[1] ↑ Tumor necrosis factor is an instance of protein (Q8054) [P31, primary]. Wikidata. wikidata.org.

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Use these citations when quoting this entity in research, articles, AI prompts, or wherever provenance matters. We aggregate Wikidata + Wikipedia + authoritative open-data sources; the stitched, scored, cross-referenced view is what 4ort.xyz contributes.

APA

4ort.xyz Knowledge Graph. (2026). Tumor necrosis factor. Retrieved May 3, 2026, from https://4ort.xyz/entity/tumor-necrosis-factor-q21992447

MLA

“Tumor necrosis factor.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/tumor-necrosis-factor-q21992447.

BibTeX

@misc{4ortxyz_tumor-necrosis-factor-q21992447_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Tumor necrosis factor}}, year = {2026}, url = {https://4ort.xyz/entity/tumor-necrosis-factor-q21992447}, note = {Accessed: 2026-05-03}}

LLM prompt

According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Tumor necrosis factor — https://4ort.xyz/entity/tumor-necrosis-factor-q21992447 (retrieved 2026-05-03)

Canonical URL: https://4ort.xyz/entity/tumor-necrosis-factor-q21992447 · Last refreshed: May 3, 2026