UniProtKB - P16599 (TNFA_RAT)
Protein
Tumor necrosis factor
Gene
Tnf
Organism
Rattus norvegicus (Rat)
Status
Functioni
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 (By similarity). Induces insulin resistance in adipocytes via inhibition of insulin-induced IRS1 tyrosine phosphorylation and insulin-induced glucose uptake. Induces GKAP42 protein degradation in adipocytes which is partially responsible for TNF-induced insulin resistance (By similarity). Plays a role in angiogenesis by inducing VEGF production synergistically with IL1B and IL6 (By similarity).By similarity
The TNF intracellular domain (ICD) form induces IL12 production in dendritic cells.By similarity
GO - Molecular functioni
- cytokine activity Source: RGD
- identical protein binding Source: RGD
- protease binding Source: RGD
- transcription regulatory region sequence-specific DNA binding Source: RGD
- tumor necrosis factor receptor binding Source: RGD
GO - Biological processi
- activation of cysteine-type endopeptidase activity involved in apoptotic process Source: RGD
- activation of MAPK activity Source: RGD
- activation of MAPKKK activity Source: RGD
- acute inflammatory response Source: RGD
- animal organ morphogenesis Source: RGD
- apoptotic process Source: RGD
- apoptotic signaling pathway Source: RGD
- calcium-mediated signaling Source: RGD
- cell activation Source: RGD
- cellular extravasation Source: RGD
- cellular response to amino acid stimulus Source: RGD
- cellular response to amyloid-beta Source: RGD
- cellular response to interferon-gamma Source: RGD
- cellular response to lipopolysaccharide Source: RGD
- cellular response to molecule of bacterial origin Source: RGD
- cellular response to nicotine Source: RGD
- cellular response to organic cyclic compound Source: RGD
- cellular response to retinoic acid Source: RGD
- cellular response to toxic substance Source: RGD
- chronic inflammatory response to antigenic stimulus Source: RGD
- circadian rhythm Source: RGD
- cortical actin cytoskeleton organization Source: RGD
- defense response Source: RGD
- defense response to bacterium Source: RGD
- defense response to Gram-positive bacterium Source: RGD
- detection of mechanical stimulus involved in sensory perception of pain Source: RGD
- embryonic digestive tract development Source: RGD
- endothelial cell apoptotic process Source: RGD
- epithelial cell proliferation involved in salivary gland morphogenesis Source: RGD
- extracellular matrix organization Source: RGD
- extrinsic apoptotic signaling pathway Source: RGD
- extrinsic apoptotic signaling pathway via death domain receptors Source: RGD
- glucose metabolic process Source: RGD
- humoral immune response Source: RGD
- inflammatory response Source: RGD
- intrinsic apoptotic signaling pathway in response to DNA damage Source: RGD
- JNK cascade Source: RGD
- leukocyte migration Source: RGD
- leukocyte migration involved in inflammatory response Source: RGD
- leukocyte tethering or rolling Source: RGD
- lipopolysaccharide-mediated signaling pathway Source: RGD
- liver regeneration Source: RGD
- MAPK cascade Source: RGD
- microglial cell activation Source: RGD
- multicellular organism development Source: RGD
- necroptotic signaling pathway Source: UniProtKB
- negative regulation of alkaline phosphatase activity Source: RGD
- negative regulation of amyloid-beta clearance Source: RGD
- negative regulation of apoptotic process Source: RGD
- negative regulation of apoptotic signaling pathway Source: RGD
- negative regulation of bicellular tight junction assembly Source: RGD
- negative regulation of bile acid secretion Source: RGD
- negative regulation of blood vessel endothelial cell migration Source: RGD
- negative regulation of branching involved in lung morphogenesis Source: RGD
- negative regulation of cell population proliferation Source: RGD
- negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: RGD
- negative regulation of cytokine production involved in immune response Source: RGD
- negative regulation of endothelial cell proliferation Source: RGD
- negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: RGD
- negative regulation of fat cell differentiation Source: RGD
- negative regulation of gene expression Source: RGD
- negative regulation of glucose import Source: RGD
- negative regulation of heart rate Source: RGD
- negative regulation of interleukin-6 production Source: RGD
- negative regulation of L-glutamate import across plasma membrane Source: RGD
- negative regulation of lipid catabolic process Source: RGD
- negative regulation of mitotic cell cycle Source: RGD
- negative regulation of myelination Source: RGD
- negative regulation of myoblast differentiation Source: RGD
- negative regulation of myosin-light-chain-phosphatase activity Source: RGD
- negative regulation of osteoblast differentiation Source: RGD
- negative regulation of oxidative phosphorylation Source: RGD
- negative regulation of production of miRNAs involved in gene silencing by miRNA Source: RGD
- negative regulation of protein-containing complex disassembly Source: RGD
- negative regulation of signaling receptor activity Source: RGD
- negative regulation of systemic arterial blood pressure Source: RGD
- negative regulation of transcription, DNA-templated Source: RGD
- negative regulation of transcription by RNA polymerase II Source: RGD
- negative regulation of vascular wound healing Source: RGD
- negative regulation of viral genome replication Source: RGD
- osteoclast differentiation Source: RGD
- positive regulation of action potential Source: RGD
- positive regulation of amyloid-beta formation Source: RGD
- positive regulation of apoptotic process Source: RGD
- positive regulation of blood microparticle formation Source: RGD
- positive regulation of calcidiol 1-monooxygenase activity Source: RGD
- positive regulation of calcineurin-NFAT signaling cascade Source: RGD
- positive regulation of cell adhesion Source: RGD
- positive regulation of chemokine (C-X-C motif) ligand 2 production Source: RGD
- positive regulation of chemokine production Source: RGD
- positive regulation of chronic inflammatory response to antigenic stimulus Source: RGD
- positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: RGD
- positive regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis Source: RGD
- positive regulation of cytokine production Source: RGD
- positive regulation of cytokine production involved in inflammatory response Source: RGD
- positive regulation of DNA-binding transcription factor activity Source: RGD
- positive regulation of DNA biosynthetic process Source: RGD
- positive regulation of extrinsic apoptotic signaling pathway Source: GO_Central
- positive regulation of fever generation Source: RGD
- positive regulation of fractalkine production Source: ARUK-UCL
- positive regulation of gene expression Source: UniProtKB
- positive regulation of glial cell proliferation Source: RGD
- positive regulation of hair follicle development Source: RGD
- positive regulation of hepatocyte proliferation Source: RGD
- positive regulation of heterotypic cell-cell adhesion Source: RGD
- positive regulation of humoral immune response mediated by circulating immunoglobulin Source: RGD
- positive regulation of I-kappaB kinase/NF-kappaB signaling Source: ARUK-UCL
- positive regulation of I-kappaB phosphorylation Source: RGD
- positive regulation of inflammatory response Source: RGD
- positive regulation of interferon-gamma production Source: RGD
- positive regulation of interleukin-18 production Source: RGD
- positive regulation of interleukin-1 beta production Source: RGD
- positive regulation of interleukin-33 production Source: RGD
- positive regulation of interleukin-6 production Source: ARUK-UCL
- positive regulation of interleukin-8 production Source: RGD
- positive regulation of JNK cascade Source: RGD
- positive regulation of JUN kinase activity Source: RGD
- positive regulation of leukocyte adhesion to arterial endothelial cell Source: RGD
- positive regulation of leukocyte adhesion to vascular endothelial cell Source: RGD
- positive regulation of MAP kinase activity Source: RGD
- positive regulation of membrane protein ectodomain proteolysis Source: RGD
- positive regulation of mitotic nuclear division Source: RGD
- positive regulation of neuron apoptotic process Source: RGD
- positive regulation of neutrophil activation Source: RGD
- positive regulation of NF-kappaB transcription factor activity Source: ARUK-UCL
- positive regulation of NIK/NF-kappaB signaling Source: RGD
- positive regulation of nitric oxide biosynthetic process Source: RGD
- positive regulation of nitric-oxide synthase activity Source: RGD
- positive regulation of nitrogen compound metabolic process Source: RGD
- positive regulation of osteoclast differentiation Source: RGD
- positive regulation of oxidative stress-induced neuron death Source: RGD
- positive regulation of peptidyl-serine phosphorylation Source: ARUK-UCL
- positive regulation of phagocytosis Source: RGD
- positive regulation of phosphatidylinositol 3-kinase signaling Source: ARUK-UCL
- positive regulation of podosome assembly Source: RGD
- positive regulation of pri-miRNA transcription by RNA polymerase II Source: RGD
- positive regulation of programmed cell death Source: RGD
- positive regulation of protein catabolic process Source: RGD
- positive regulation of protein-containing complex assembly Source: RGD
- positive regulation of protein-containing complex disassembly Source: RGD
- positive regulation of protein kinase activity Source: RGD
- positive regulation of protein kinase B signaling Source: ARUK-UCL
- positive regulation of protein localization to cell surface Source: RGD
- positive regulation of protein localization to plasma membrane Source: ARUK-UCL
- positive regulation of protein phosphorylation Source: RGD
- positive regulation of protein transport Source: RGD
- positive regulation of receptor signaling pathway via JAK-STAT Source: ARUK-UCL
- positive regulation of smooth muscle cell proliferation Source: RGD
- positive regulation of superoxide dismutase activity Source: RGD
- positive regulation of synaptic transmission Source: RGD
- positive regulation of synoviocyte proliferation Source: RGD
- positive regulation of transcription, DNA-templated Source: RGD
- positive regulation of transcription by RNA polymerase II Source: ARUK-UCL
- positive regulation of translational initiation by iron Source: RGD
- positive regulation of tyrosine phosphorylation of STAT protein Source: ARUK-UCL
- positive regulation of vascular associated smooth muscle cell proliferation Source: RGD
- positive regulation of vitamin D biosynthetic process Source: RGD
- protein kinase B signaling Source: RGD
- protein localization to plasma membrane Source: RGD
- regulation of branching involved in salivary gland morphogenesis Source: RGD
- regulation of cell population proliferation Source: RGD
- regulation of endothelial cell apoptotic process Source: RGD
- regulation of establishment of endothelial barrier Source: RGD
- regulation of I-kappaB kinase/NF-kappaB signaling Source: RGD
- regulation of immunoglobulin production Source: RGD
- regulation of inflammatory response Source: RGD
- regulation of insulin secretion Source: RGD
- regulation of osteoclast differentiation Source: RGD
- regulation of protein phosphorylation Source: RGD
- regulation of protein secretion Source: RGD
- regulation of reactive oxygen species metabolic process Source: RGD
- regulation of synapse organization Source: RGD
- regulation of transcription by RNA polymerase II Source: ARUK-UCL
- response to 3,3',5-triiodo-L-thyronine Source: RGD
- response to activity Source: RGD
- response to bacterium Source: RGD
- response to drug Source: RGD
- response to ethanol Source: RGD
- response to glucocorticoid Source: RGD
- response to gold nanoparticle Source: RGD
- response to Gram-negative bacterium Source: RGD
- response to hypoxia Source: RGD
- response to lipopolysaccharide Source: UniProtKB
- response to mechanical stimulus Source: RGD
- response to nutrient levels Source: RGD
- response to organic cyclic compound Source: RGD
- response to organic substance Source: RGD
- response to paracetamol Source: RGD
- response to radiation Source: RGD
- response to virus Source: RGD
- sequestering of triglyceride Source: RGD
- signal transduction Source: RGD
- skeletal muscle contraction Source: RGD
- toll-like receptor 3 signaling pathway Source: UniProtKB
- tumor necrosis factor-mediated signaling pathway Source: RGD
- vascular endothelial growth factor production Source: UniProtKB
- vasodilation Source: RGD
Keywordsi
Molecular function | Cytokine |
Enzyme and pathway databases
Reactomei | R-RNO-5357786, TNFR1-induced proapoptotic signaling R-RNO-5357905, Regulation of TNFR1 signaling R-RNO-5357956, TNFR1-induced NFkappaB signaling pathway R-RNO-5626978, TNFR1-mediated ceramide production R-RNO-5668541, TNFR2 non-canonical NF-kB pathway R-RNO-75893, TNF signaling |
Names & Taxonomyi
Protein namesi | Recommended name: Tumor necrosis factorAlternative name(s): Cachectin TNF-alpha Tumor necrosis factor ligand superfamily member 2 Short name: TNF-a Cleaved into the following 6 chains: Alternative name(s): N-terminal fragment Short name: NTF |
Gene namesi | Name:Tnf Synonyms:Tnfa, Tnfsf2 |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 3876, Tnf |
Subcellular locationi
Plasma membrane
- Cell membrane By similarity; Single-pass type II membrane protein By similarity
Other locations
- Membrane By similarity; Single-pass type II membrane protein By similarity
Extracellular region or secreted
- Secreted By similarity
Extracellular region or secreted
- Secreted By similarity
Extracellular region or secreted
- Secreted By similarity
Endosome
- recycling endosome Source: RGD
Extracellular region or secreted
- extracellular space Source: RGD
Plasma Membrane
- external side of plasma membrane Source: RGD
- integral component of plasma membrane Source: RGD
- phagocytic cup Source: RGD
- plasma membrane Source: RGD
Other locations
- cell surface Source: RGD
- cytoplasm Source: RGD
- membrane raft Source: RGD
- neuronal cell body Source: RGD
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 35 | CytoplasmicSequence analysisAdd BLAST | 35 | |
Transmembranei | 36 – 56 | Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST | 21 | |
Topological domaini | 57 – 235 | ExtracellularSequence analysisAdd BLAST | 179 |
Keywords - Cellular componenti
Cell membrane, Membrane, SecretedPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000034451 | 1 – 235 | Tumor necrosis factor, membrane formAdd BLAST | 235 | |
ChainiPRO_0000417287 | 1 – 39 | Intracellular domain 1By similarityAdd BLAST | 39 | |
ChainiPRO_0000417288 | 1 – 35 | Intracellular domain 2By similarityAdd BLAST | 35 | |
ChainiPRO_0000417289 | 50 – ? | C-domain 1By similarity | ||
ChainiPRO_0000417290 | 52 – ? | C-domain 2By similarity | ||
ChainiPRO_0000034452 | 80 – 235 | Tumor necrosis factor, soluble formAdd BLAST | 156 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | Phosphoserine; by CK1By similarity | 1 | |
Lipidationi | 19 | N6-myristoyl lysineBy similarity | 1 | |
Lipidationi | 20 | N6-myristoyl lysineBy similarity | 1 | |
Glycosylationi | 83 | O-linked (GalNAc...) serine; in soluble formBy similarity | 1 | |
Glycosylationi | 86 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 148 ↔ 179 | By similarity |
Post-translational modificationi
The soluble form derives from the membrane form by proteolytic processing. 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).By similarity
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).By similarity
O-glycosylated; glycans contain galactose, N-acetylgalactosamine and N-acetylneuraminic acid.By similarity
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 34 – 35 | Cleavage; by SPPL2A or SPPL2BBy similarity | 2 | |
Sitei | 39 – 40 | Cleavage; by SPPL2A or SPPL2BBy similarity | 2 | |
Sitei | 49 – 50 | Cleavage; by SPPL2A or SPPL2BBy similarity | 2 | |
Sitei | 51 – 52 | Cleavage; by SPPL2A or SPPL2BBy similarity | 2 | |
Sitei | 79 – 80 | Cleavage; by ADAM17By similarity | 2 |
Keywords - PTMi
Disulfide bond, Glycoprotein, Lipoprotein, Myristate, PhosphoproteinProteomic databases
PaxDbi | P16599 |
PRIDEi | P16599 |
PTM databases
GlyGeni | P16599, 2 sites |
PhosphoSitePlusi | P16599 |
Expressioni
Gene expression databases
Bgeei | ENSRNOG00000000837, Expressed in brain and 8 other tissues |
Genevisiblei | P16599, RN |
Interactioni
Subunit structurei
Homotrimer.
Interacts with SPPL2B (By similarity).
By similarityGO - Molecular functioni
- cytokine activity Source: RGD
- identical protein binding Source: RGD
- protease binding Source: RGD
- tumor necrosis factor receptor binding Source: RGD
Protein-protein interaction databases
DIPi | DIP-39461N |
IntActi | P16599, 74 interactors |
STRINGi | 10116.ENSRNOP00000001110 |
Chemistry databases
BindingDBi | P16599 |
Family & Domainsi
Sequence similaritiesi
Belongs to the tumor necrosis factor family.Curated
Keywords - Domaini
Signal-anchor, Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | ENOG502S4K8, Eukaryota |
GeneTreei | ENSGT01010000222306 |
HOGENOMi | CLU_070352_3_1_1 |
InParanoidi | P16599 |
OMAi | GATMLFC |
OrthoDBi | 1124938at2759 |
PhylomeDBi | P16599 |
TreeFami | TF332169 |
Family and domain databases
CDDi | cd00184, TNF, 1 hit |
Gene3Di | 2.60.120.40, 1 hit |
InterProi | View protein in InterPro IPR006053, TNF IPR002959, TNF_alpha IPR021184, TNF_CS IPR006052, TNF_dom IPR008983, Tumour_necrosis_fac-like_dom |
PANTHERi | PTHR11471:SF23, PTHR11471:SF23, 1 hit |
Pfami | View protein in Pfam PF00229, TNF, 1 hit |
PRINTSi | PR01234, TNECROSISFCT PR01235, TNFALPHA |
SMARTi | View protein in SMART SM00207, TNF, 1 hit |
SUPFAMi | SSF49842, SSF49842, 1 hit |
PROSITEi | View protein in PROSITE PS00251, TNF_1, 1 hit PS50049, TNF_2, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P16599-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSTESMIRDV ELAEEALPKK MGGLQNSRRC LCLSLFSFLL VAGATTLFCL
60 70 80 90 100
LNFGVIGPNK EEKFPNGLPL ISSMAQTLTL RSSSQNSSDK PVAHVVANHQ
110 120 130 140 150
AEEQLEWLSQ RANALLANGM DLKDNQLVVP ADGLYLIYSQ VLFKGQGCPD
160 170 180 190 200
YVLLTHTVSR FAISYQEKVS LLSAIKSPCP KDTPEGAELK PWYEPMYLGG
210 220 230
VFQLEKGDLL SAEVNLPKYL DITESGQVYF GVIAL
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 39 | L → P in CAA05290 (PubMed:1627266).Curated | 1 | |
Sequence conflicti | 39 | L → P in CAA47146 (PubMed:1627266).Curated | 1 | |
Sequence conflicti | 163 | I → T in CAA05290 (PubMed:1627266).Curated | 1 | |
Sequence conflicti | 163 | I → T in CAA47146 (PubMed:1627266).Curated | 1 | |
Sequence conflicti | 202 | F → S in CAA05290 (PubMed:1627266).Curated | 1 | |
Sequence conflicti | 202 | F → S in CAA47146 (PubMed:1627266).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural varianti | 122 | L → P1 Publication | 1 | |
Natural varianti | 190 | K → E1 Publication | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D00475 Genomic DNA Translation: BAA00367.1 X66539 mRNA Translation: CAA47146.1 AJ002278 mRNA Translation: CAA05290.1 L00981 Genomic DNA Translation: AAA16275.1 AF329982 Genomic DNA Translation: AAK53568.1 AF329983 Genomic DNA Translation: AAK53569.1 AF329984 Genomic DNA Translation: AAK53570.1 AF329985 Genomic DNA Translation: AAK53571.1 AF329986 Genomic DNA Translation: AAK53572.1 AF329987 Genomic DNA Translation: AAK53573.1 AF269159 mRNA Translation: AAF82567.1 AF269160 mRNA Translation: AAF82568.1 AY427673 Genomic DNA Translation: AAR91624.1 AY427674 Genomic DNA Translation: AAR91625.1 AY427675 Genomic DNA Translation: AAR91626.1 BX883046 Genomic DNA Translation: CAE84003.1 BC107671 mRNA Translation: AAI07672.1 L19123 Genomic DNA Translation: AAA42255.1 |
PIRi | JU0029 |
RefSeqi | NP_036807.1, NM_012675.3 XP_008770997.1, XM_008772775.2 |
Genome annotation databases
Ensembli | ENSRNOT00000001110; ENSRNOP00000001110; ENSRNOG00000000837 ENSRNOT00000079677; ENSRNOP00000074520; ENSRNOG00000055156 |
GeneIDi | 103694380 24835 |
KEGGi | rno:103694380 rno:24835 |
UCSCi | RGD:3876, rat |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D00475 Genomic DNA Translation: BAA00367.1 X66539 mRNA Translation: CAA47146.1 AJ002278 mRNA Translation: CAA05290.1 L00981 Genomic DNA Translation: AAA16275.1 AF329982 Genomic DNA Translation: AAK53568.1 AF329983 Genomic DNA Translation: AAK53569.1 AF329984 Genomic DNA Translation: AAK53570.1 AF329985 Genomic DNA Translation: AAK53571.1 AF329986 Genomic DNA Translation: AAK53572.1 AF329987 Genomic DNA Translation: AAK53573.1 AF269159 mRNA Translation: AAF82567.1 AF269160 mRNA Translation: AAF82568.1 AY427673 Genomic DNA Translation: AAR91624.1 AY427674 Genomic DNA Translation: AAR91625.1 AY427675 Genomic DNA Translation: AAR91626.1 BX883046 Genomic DNA Translation: CAE84003.1 BC107671 mRNA Translation: AAI07672.1 L19123 Genomic DNA Translation: AAA42255.1 |
PIRi | JU0029 |
RefSeqi | NP_036807.1, NM_012675.3 XP_008770997.1, XM_008772775.2 |
3D structure databases
SMRi | P16599 |
ModBasei | Search... |
Protein-protein interaction databases
DIPi | DIP-39461N |
IntActi | P16599, 74 interactors |
STRINGi | 10116.ENSRNOP00000001110 |
Chemistry databases
BindingDBi | P16599 |
PTM databases
GlyGeni | P16599, 2 sites |
PhosphoSitePlusi | P16599 |
Proteomic databases
PaxDbi | P16599 |
PRIDEi | P16599 |
Genome annotation databases
Ensembli | ENSRNOT00000001110; ENSRNOP00000001110; ENSRNOG00000000837 ENSRNOT00000079677; ENSRNOP00000074520; ENSRNOG00000055156 |
GeneIDi | 103694380 24835 |
KEGGi | rno:103694380 rno:24835 |
UCSCi | RGD:3876, rat |
Organism-specific databases
CTDi | 7124 |
RGDi | 3876, Tnf |
Phylogenomic databases
eggNOGi | ENOG502S4K8, Eukaryota |
GeneTreei | ENSGT01010000222306 |
HOGENOMi | CLU_070352_3_1_1 |
InParanoidi | P16599 |
OMAi | GATMLFC |
OrthoDBi | 1124938at2759 |
PhylomeDBi | P16599 |
TreeFami | TF332169 |
Enzyme and pathway databases
Reactomei | R-RNO-5357786, TNFR1-induced proapoptotic signaling R-RNO-5357905, Regulation of TNFR1 signaling R-RNO-5357956, TNFR1-induced NFkappaB signaling pathway R-RNO-5626978, TNFR1-mediated ceramide production R-RNO-5668541, TNFR2 non-canonical NF-kB pathway R-RNO-75893, TNF signaling |
Miscellaneous databases
PROi | PR:P16599 |
Gene expression databases
Bgeei | ENSRNOG00000000837, Expressed in brain and 8 other tissues |
Genevisiblei | P16599, RN |
Family and domain databases
CDDi | cd00184, TNF, 1 hit |
Gene3Di | 2.60.120.40, 1 hit |
InterProi | View protein in InterPro IPR006053, TNF IPR002959, TNF_alpha IPR021184, TNF_CS IPR006052, TNF_dom IPR008983, Tumour_necrosis_fac-like_dom |
PANTHERi | PTHR11471:SF23, PTHR11471:SF23, 1 hit |
Pfami | View protein in Pfam PF00229, TNF, 1 hit |
PRINTSi | PR01234, TNECROSISFCT PR01235, TNFALPHA |
SMARTi | View protein in SMART SM00207, TNF, 1 hit |
SUPFAMi | SSF49842, SSF49842, 1 hit |
PROSITEi | View protein in PROSITE PS00251, TNF_1, 1 hit PS50049, TNF_2, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | TNFA_RAT | |
Accessioni | P16599Primary (citable) accession number: P16599 Secondary accession number(s): Q6EE11, Q9JI26, Q9JI27 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 1, 1990 |
Last sequence update: | August 1, 1990 | |
Last modified: | April 7, 2021 | |
This is version 187 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families