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P06804 (TNFA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 157. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tumor necrosis factor
Alternative name(s):
Cachectin
TNF-alpha
Tumor necrosis factor ligand superfamily member 2
Short name=TNF-a

Cleaved into the following 6 chains:

  1. Tumor necrosis factor, membrane form
    Alternative name(s):
    N-terminal fragment
    Short name=NTF
  2. Intracellular domain 1
    Short name=ICD1
  3. Intracellular domain 2
    Short name=ICD2
  4. C-domain 1
  5. C-domain 2
  6. Tumor necrosis factor, soluble form
Gene names
Name:Tnf
Synonyms:Tnfa, Tnfsf2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length235 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. It is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It is potent pyrogen causing fever by direct action or by stimulation of interleukin-1 secretion and is implicated in the induction of cachexia, Under certain conditions it can stimulate cell proliferation and induce cell differentiation.

The TNF intracellular domain (ICD) form induces IL12 production in dendritic cells By similarity.

Subunit structure

Interacts with SPPL2B By similarity. Homotrimer.

Subcellular location

Cell membrane; Single-pass type II membrane protein.

Tumor necrosis factor, membrane form: Membrane; Single-pass type II membrane protein By similarity.

Tumor necrosis factor, soluble form: Secreted.

C-domain 1: Secreted By similarity.

C-domain 2: Secreted By similarity.

Post-translational modification

The membrane-bound form is further proteolytically processed by SPPL2A or SPPL2B through regulated intramembrane proteolysis producing TNF intracellular domains (ICD1 and ICD2) released in the cytosol and TNF C-domain 1 and C-domain 2 secreted into the extracellular space By similarity. The soluble form derives from the membrane form by proteolytic processing.

The membrane form, but not the soluble form, is phosphorylated on serine residues. Dephosphorylation of the membrane form occurs by binding to soluble TNFRSF1A/TNFR1 By similarity.

O-glycosylated; glycans contain galactose, N-acetylgalactosamine and N-acetylneuraminic acid By similarity.

Sequence similarities

Belongs to the tumor necrosis factor family.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
Secreted
   Coding sequence diversityPolymorphism
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   Molecular functionCytokine
   PTMDisulfide bond
Glycoprotein
Lipoprotein
Myristate
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processJNK cascade

Inferred from genetic interaction PubMed 17015619. Source: MGI

activation of MAPK activity

Inferred from electronic annotation. Source: Ensembl

activation of MAPKKK activity

Inferred from electronic annotation. Source: Ensembl

activation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from direct assay PubMed 16183742. Source: MGI

apoptotic signaling pathway

Inferred from direct assay PubMed 15629131PubMed 8208546. Source: MGI

calcium-mediated signaling

Inferred from electronic annotation. Source: Ensembl

cell activation

Inferred from electronic annotation. Source: Ensembl

cell proliferation

Traceable author statement PubMed 7636227. Source: MGI

cellular amino acid biosynthetic process

Inferred from direct assay PubMed 10588860. Source: MGI

cellular extravasation

Inferred from direct assay PubMed 10528208. Source: MGI

cellular response to amino acid stimulus

Inferred from direct assay PubMed 20548288. Source: MGI

cellular response to nicotine

Inferred from electronic annotation. Source: Ensembl

chronic inflammatory response to antigenic stimulus

Inferred from electronic annotation. Source: Ensembl

defense response

Inferred from mutant phenotype PubMed 8395024PubMed 9223320. Source: MGI

defense response to Gram-positive bacterium

Inferred from genetic interaction PubMed 9834074. Source: MGI

defense response to bacterium

Inferred from direct assay PubMed 10899905. Source: MGI

embryonic digestive tract development

Inferred from electronic annotation. Source: Ensembl

epithelial cell proliferation involved in salivary gland morphogenesis

Inferred from direct assay PubMed 11241200. Source: MGI

extracellular matrix organization

Inferred from direct assay PubMed 15381731. Source: MGI

extrinsic apoptotic signaling pathway

Inferred from genetic interaction PubMed 19498109PubMed 22089168. Source: MGI

extrinsic apoptotic signaling pathway via death domain receptors

Inferred from genetic interaction PubMed 12431371PubMed 20080598. Source: MGI

glucose metabolic process

Inferred from direct assay PubMed 12068289. Source: MGI

humoral immune response

Inferred from mutant phenotype PubMed 8879212. Source: MGI

inflammatory response

Inferred from genetic interaction PubMed 21148126. Source: MGI

intrinsic apoptotic signaling pathway in response to DNA damage

Inferred from direct assay PubMed 17242187. Source: MGI

leukocyte migration

Inferred from direct assay PubMed 15034066. Source: MGI

leukocyte tethering or rolling

Inferred from electronic annotation. Source: Ensembl

lipopolysaccharide-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

multicellular organismal development

Inferred from mutant phenotype PubMed 9368616. Source: MGI

necroptotic signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of L-glutamate transport

Inferred from electronic annotation. Source: Ensembl

negative regulation of alkaline phosphatase activity

Inferred from direct assay PubMed 21689636. Source: BHF-UCL

negative regulation of branching involved in lung morphogenesis

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of cytokine secretion involved in immune response

Inferred from electronic annotation. Source: Ensembl

negative regulation of extrinsic apoptotic signaling pathway in absence of ligand

Inferred from electronic annotation. Source: Ensembl

negative regulation of glucose import

Inferred from direct assay PubMed 12068289. Source: MGI

negative regulation of growth of symbiont in host

Inferred from genetic interaction PubMed 9834074. Source: MGI

negative regulation of interleukin-6 production

Inferred from electronic annotation. Source: Ensembl

negative regulation of lipid catabolic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of osteoblast differentiation

Inferred from direct assay PubMed 21689636. Source: BHF-UCL

negative regulation of protein complex disassembly

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 21689636. Source: BHF-UCL

negative regulation of viral genome replication

Inferred from electronic annotation. Source: Ensembl

organ morphogenesis

Inferred from mutant phenotype PubMed 8879212. Source: MGI

osteoclast differentiation

Inferred from genetic interaction PubMed 15485831. Source: MGI

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from direct assay PubMed 12867038PubMed 16260493PubMed 22089168. Source: MGI

positive regulation of JNK cascade

Inferred from direct assay PubMed 16260493PubMed 20080598. Source: MGI

positive regulation of JUN kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of MAP kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of NF-kappaB import into nucleus

Inferred from mutant phenotype PubMed 21689636. Source: BHF-UCL

positive regulation of NF-kappaB transcription factor activity

Inferred from sequence orthology PubMed 15790681. Source: MGI

positive regulation of NFAT protein import into nucleus

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of calcidiol 1-monooxygenase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Traceable author statement PubMed 8171322. Source: MGI

positive regulation of chemokine (C-X-C motif) ligand 2 production

Inferred from electronic annotation. Source: Ensembl

positive regulation of chemokine biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of chronic inflammatory response to antigenic stimulus

Inferred from genetic interaction PubMed 9834074. Source: MGI

positive regulation of cytokine secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of fever generation

Inferred from direct assay PubMed 19940926. Source: BHF-UCL

positive regulation of hair follicle development

Inferred from mutant phenotype PubMed 16702408. Source: UniProtKB

positive regulation of heterotypic cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

positive regulation of humoral immune response mediated by circulating immunoglobulin

Inferred from genetic interaction PubMed 9834074. Source: MGI

positive regulation of interferon-gamma production

Inferred from genetic interaction PubMed 9834074. Source: MGI

positive regulation of interleukin-18 production

Inferred from electronic annotation. Source: Ensembl

positive regulation of interleukin-6 production

Inferred from direct assay PubMed 11894098. Source: MGI

positive regulation of interleukin-8 biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of membrane protein ectodomain proteolysis

Inferred from electronic annotation. Source: Ensembl

positive regulation of mitosis

Inferred from electronic annotation. Source: Ensembl

positive regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of nitric oxide biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of osteoclast differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of peptidyl-serine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of podosome assembly

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein complex disassembly

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein kinase B signaling

Inferred from direct assay PubMed 20080598. Source: MGI

positive regulation of protein localization to cell surface

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of smooth muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of synaptic transmission

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 17670746PubMed 19404405PubMed 9305915. Source: MGI

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 12761567. Source: MGI

positive regulation of translational initiation by iron

Inferred from direct assay PubMed 11588035. Source: MGI

positive regulation of vitamin D biosynthetic process

Inferred from electronic annotation. Source: Ensembl

protein import into nucleus, translocation

Inferred from electronic annotation. Source: Ensembl

protein kinase B signaling

Inferred from electronic annotation. Source: Ensembl

receptor biosynthetic process

Inferred from electronic annotation. Source: Ensembl

regulation of branching involved in salivary gland morphogenesis

Inferred from direct assay PubMed 11241200. Source: MGI

regulation of cell proliferation

Inferred from direct assay PubMed 11799106. Source: MGI

regulation of immunoglobulin secretion

Inferred from direct assay PubMed 12958312. Source: MGI

regulation of insulin secretion

Inferred from electronic annotation. Source: Ensembl

regulation of osteoclast differentiation

Inferred from direct assay PubMed 12490655. Source: MGI

regulation of protein phosphorylation

Inferred from direct assay PubMed 15169905. Source: MGI

regulation of protein secretion

Inferred from direct assay PubMed 19293336. Source: MGI

regulation of reactive oxygen species metabolic process

Inferred from direct assay PubMed 21052097. Source: MGI

response to activity

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to glucocorticoid

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

response to virus

Inferred from electronic annotation. Source: Ensembl

sequestering of triglyceride

Inferred from electronic annotation. Source: Ensembl

skeletal muscle contraction

Inferred from electronic annotation. Source: Ensembl

transformed cell apoptotic process

Traceable author statement PubMed 7636227PubMed 8171322PubMed 9368616. Source: MGI

tumor necrosis factor-mediated signaling pathway

Inferred from direct assay Ref.2. Source: MGI

   Cellular_componentexternal side of plasma membrane

Inferred from direct assay PubMed 16282525. Source: BHF-UCL

extracellular space

Inferred from direct assay PubMed 10545106PubMed 10549626PubMed 10899905PubMed 11168643PubMed 11728336PubMed 11894098PubMed 12855817PubMed 12872135PubMed 14764707PubMed 15220916PubMed 1577194PubMed 16236719PubMed 16239543PubMed 16275384PubMed 17693256PubMed 18261938PubMed 18997793. Source: MGI

integral component of plasma membrane

Traceable author statement PubMed 8879212. Source: MGI

intracellular

Inferred from direct assay PubMed 19723499. Source: MGI

membrane raft

Inferred from direct assay PubMed 17010968. Source: BHF-UCL

phagocytic cup

Inferred from direct assay PubMed 16282525. Source: BHF-UCL

plasma membrane

Inferred from direct assay PubMed 15155767. Source: MGI

recycling endosome

Inferred from direct assay PubMed 16282525. Source: BHF-UCL

secretory granule

Traceable author statement PubMed 8879212. Source: MGI

   Molecular_functioncytokine activity

Inferred from direct assay PubMed 11588035PubMed 11894098. Source: MGI

protease binding

Inferred from physical interaction PubMed 12135759. Source: BHF-UCL

transcription regulatory region DNA binding

Inferred from electronic annotation. Source: Ensembl

tumor necrosis factor receptor binding

Inferred from direct assay PubMed 11588035. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 235235Tumor necrosis factor, membrane form
PRO_0000034435
Chain1 – 3939Intracellular domain 1 By similarity
PRO_0000417255
Chain1 – 3535Intracellular domain 2 By similarity
PRO_0000417256
Chain50 – ?C-domain 1 By similarityPRO_0000417257
Chain52 – ?C-domain 2 By similarityPRO_0000417258
Chain80 – 235156Tumor necrosis factor, soluble form
PRO_0000034436

Regions

Topological domain1 – 3535Cytoplasmic Potential
Transmembrane36 – 5621Helical; Signal-anchor for type II membrane protein; Potential
Topological domain57 – 235179Extracellular Potential

Sites

Site34 – 352Cleavage; by SPPL2A or SPPL2B By similarity
Site39 – 402Cleavage; by SPPL2A or SPPL2B By similarity
Site49 – 502Cleavage; by SPPL2A or SPPL2B By similarity
Site51 – 522Cleavage; by SPPL2A or SPPL2B By similarity
Site79 – 802Cleavage; by ADAM17 By similarity

Amino acid modifications

Modified residue21Phosphoserine; by CK1 By similarity
Lipidation201N6-myristoyl lysine By similarity
Glycosylation831O-linked (GalNAc...); in soluble form By similarity
Glycosylation861N-linked (GlcNAc...)
Disulfide bond148 ↔ 179

Natural variations

Natural variant71I → T in strain: BALB/c and C57BL/6. Ref.8
Natural variant771T → A in strain: BALB/c and C57BL/6. Ref.8

Experimental info

Sequence conflict79 – 813Missing in AAB65593. Ref.8
Sequence conflict2311G → R Ref.3
Sequence conflict2311G → R Ref.4

Secondary structure

............................. 235
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06804 [UniParc].

Last modified July 1, 1989. Version 2.
Checksum: 16DD2A9676D68C5D

FASTA23525,896
        10         20         30         40         50         60 
MSTESMIRDV ELAEEALPQK MGGFQNSRRC LCLSLFSFLL VAGATTLFCL LNFGVIGPQR 

        70         80         90        100        110        120 
DEKFPNGLPL ISSMAQTLTL RSSSQNSSDK PVAHVVANHQ VEEQLEWLSQ RANALLANGM 

       130        140        150        160        170        180 
DLKDNQLVVP ADGLYLVYSQ VLFKGQGCPD YVLLTHTVSR FAISYQEKVN LLSAVKSPCP 

       190        200        210        220        230 
KDTPEGAELK PWYEPIYLGG VFQLEKGDQL SAEVNLPKYL DFAESGQVYF GVIAL 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression in Escherichia coli of the gene for mouse tumor necrosis factor."
Shirai T., Shimizu N., Shiojiri S., Horiguchi S., Ito H.
DNA 7:193-201(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Cloning and expression in Escherichia coli of the cDNA for murine tumor necrosis factor."
Pennica D., Hayflick J.S., Bringman T.S., Palladino M.A., Goeddel D.V.
Proc. Natl. Acad. Sci. U.S.A. 82:6060-6064(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Identification of a common nucleotide sequence in the 3'-untranslated region of mRNA molecules specifying inflammatory mediators."
Caput D., Beutler B., Hartog K., Thayer R., Brown-Shimer S., Cerami A.
Proc. Natl. Acad. Sci. U.S.A. 83:1670-1674(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Molecular cloning of mouse tumour necrosis factor cDNA and its eukaryotic expression."
Fransen L., Mueller R., Marmenout A., Tavernier J., van der Heyden J., Kawashima E., Chollet A., Tizard R., van Heuverswyn H., van Vliet A., Ruysschaert M.-R., Fiers W.
Nucleic Acids Res. 13:4417-4429(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]"Molecular cloning of genes coding for tumor necrosis factor. Complete nucleotide sequence of the genome copy of TNF-alpha in mice."
Shakhov A.N., Nedospasov S.A.
Bioorg. Khim. 13:701-705(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[6]"Nucleotide sequence of the murine TNF locus, including the TNF-alpha (tumor necrosis factor) and TNF-beta (lymphotoxin) genes."
Semon D., Kawashima E., Jongeneel C.V., Shakhov A.N., Nedospasov S.A.
Nucleic Acids Res. 15:9083-9084(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]"Identification of a new susceptibility locus for insulin-dependent diabetes mellitus by ancestral haplotype congenic mapping."
Ikegami H., Makino S., Yamato E., Kawaguchi Y., Ueda H., Sakamoto T., Takekawa K., Ogihara T.
J. Clin. Invest. 96:1936-1942(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: CTS and NOD.
[8]"Cloning and sequencing of the Tnfa genes of three inbred mouse strains."
Iraqi F., Teale A.
Immunogenetics 45:459-461(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-7 AND ALA-77.
Strain: A/J, BALB/c and C57BL/6.
[9]"Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse."
Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L.
Genome Res. 13:2621-2636(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 129.
[10]"Conspicuous differences among gene genealogies of 21 nuclear genes of five Mus musculus subspecies."
Liu Y., Kitano T., Koide T., Shiroishi T., Moriwaki K., Saitou N.
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE OF 1-96.
Strain: BFM/2Msf, BLG2/Msf, C57BL/10SnJ, CAST/Ei, HMI/Msf, MSM/Msf, NJL/Msf, pgn2 and SWN/Msf.
[11]"Alternative cleavage of the cachectin/tumor necrosis factor propeptide results in a larger, inactive form of secreted protein."
Cseh K., Beutler B.
J. Biol. Chem. 264:16256-16260(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 70-87.
[12]"Characterization of high molecular weight glycosylated forms of murine tumor necrosis factor."
Sherry B., Juc D.-M., Zentella A., Cerami A.
Biochem. Biophys. Res. Commun. 173:1072-1078(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 80-99.
[13]"A novel form of TNF/cachectin is a cell surface cytotoxic transmembrane protein: ramifications for the complex physiology of TNF."
Kriegler M., Perez X., Defay K., Albert I., Lu S.D.
Cell 53:45-53(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF MEMBRANE-BOUND FORM.
[14]"The structure of mouse tumour-necrosis factor at 1.4 A resolution: towards modulation of its selectivity and trimerization."
Baeyens K.J., De Bondt H.L., Raeymaekers A., Fiers W., De Ranter C.J.
Acta Crystallogr. D 55:772-778(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 80-235.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M20155 Genomic DNA. Translation: AAA40462.1. Sequence problems.
M11731 mRNA. Translation: AAA40458.1.
M13049 mRNA. Translation: AAA40457.1.
X02611 mRNA. Translation: CAA26457.1.
M38296 Genomic DNA. Translation: AAA40459.1.
Y00467 Genomic DNA. Translation: CAA68530.1.
U06950 Unassigned DNA. Translation: AAA18594.1.
D84196 Genomic DNA. Translation: BAA19512.1.
D84199 Genomic DNA. Translation: BAA19513.1.
U68414 Genomic DNA. Translation: AAB65593.1.
AF109719 Genomic DNA. Translation: AAC82484.1.
AB039224 Genomic DNA. Translation: BAB68748.1. Sequence problems.
AB039225 Genomic DNA. Translation: BAB68749.1. Sequence problems.
AB039226 Genomic DNA. Translation: BAB68750.1. Sequence problems.
AB039227 Genomic DNA. Translation: BAB68751.1. Sequence problems.
AB039228 Genomic DNA. Translation: BAB68752.1. Sequence problems.
AB039229 Genomic DNA. Translation: BAB68753.1. Sequence problems.
AB039230 Genomic DNA. Translation: BAB68754.1. Sequence problems.
AB039231 Genomic DNA. Translation: BAB68755.1. Sequence problems.
AB039232 Genomic DNA. Translation: BAB68756.1. Sequence problems.
PIRQWMSN. A22908.
RefSeqNP_001265530.1. NM_001278601.1.
NP_038721.1. NM_013693.3.
UniGeneMm.1293.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2TNFX-ray1.40A/B/C80-235[»]
ProteinModelPortalP06804.
SMRP06804. Positions 88-235.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204240. 9 interactions.
IntActP06804. 1 interaction.

Chemistry

ChEMBLCHEMBL4984.

PTM databases

PhosphoSiteP06804.

Proteomic databases

PaxDbP06804.
PRIDEP06804.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025263; ENSMUSP00000025263; ENSMUSG00000024401.
ENSMUST00000167924; ENSMUSP00000126122; ENSMUSG00000024401.
GeneID21926.
KEGGmmu:21926.
UCSCuc008cgr.1. mouse.

Organism-specific databases

CTD7124.
MGIMGI:104798. Tnf.

Phylogenomic databases

eggNOGNOG40413.
GeneTreeENSGT00530000062992.
HOGENOMHOG000048729.
HOVERGENHBG012516.
InParanoidP06804.
KOK03156.
OMAPWYEPIY.
OrthoDBEOG7V4B0Q.
PhylomeDBP06804.
TreeFamTF332169.

Gene expression databases

ArrayExpressP06804.
BgeeP06804.
CleanExMM_TNF.
GenevestigatorP06804.

Family and domain databases

Gene3D2.60.120.40. 1 hit.
InterProIPR006053. TNF.
IPR002959. TNF_alpha.
IPR021184. TNF_CS.
IPR006052. TNF_dom.
IPR008064. TNFalpha/TNFSF15.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view]
PANTHERPTHR11471:SF7. PTHR11471:SF7. 1 hit.
PfamPF00229. TNF. 1 hit.
[Graphical view]
PRINTSPR01234. TNECROSISFCT.
PR01235. TNFALPHA.
SMARTSM00207. TNF. 1 hit.
[Graphical view]
SUPFAMSSF49842. SSF49842. 1 hit.
PROSITEPS00251. TNF_1. 1 hit.
PS50049. TNF_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP06804.
NextBio301508.
PMAP-CutDBP06804.
PROP06804.
SOURCESearch...

Entry information

Entry nameTNFA_MOUSE
AccessionPrimary (citable) accession number: P06804
Secondary accession number(s): O35853, Q62326, Q91VF3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: July 1, 1989
Last modified: April 16, 2014
This is version 157 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot