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P06804

- TNFA_MOUSE

UniProt

P06804 - TNFA_MOUSE

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Protein

Tumor necrosis factor

Gene

Tnf

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei34 – 352Cleavage; by SPPL2A or SPPL2BBy similarity
Sitei39 – 402Cleavage; by SPPL2A or SPPL2BBy similarity
Sitei49 – 502Cleavage; by SPPL2A or SPPL2BBy similarity
Sitei51 – 522Cleavage; by SPPL2A or SPPL2BBy similarity
Sitei79 – 802Cleavage; by ADAM17By similarity

GO - Molecular functioni

  1. cytokine activity Source: MGI
  2. protease binding Source: BHF-UCL
  3. transcription regulatory region DNA binding Source: Ensembl
  4. tumor necrosis factor receptor binding Source: MGI

GO - Biological processi

  1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: MGI
  2. activation of MAPK activity Source: Ensembl
  3. activation of MAPKKK activity Source: Ensembl
  4. apoptotic signaling pathway Source: MGI
  5. calcium-mediated signaling Source: Ensembl
  6. cell activation Source: Ensembl
  7. cell proliferation Source: MGI
  8. cellular extravasation Source: MGI
  9. cellular response to amino acid stimulus Source: MGI
  10. cellular response to lipopolysaccharide Source: MGI
  11. cellular response to nicotine Source: Ensembl
  12. chronic inflammatory response to antigenic stimulus Source: Ensembl
  13. defense response Source: MGI
  14. defense response to bacterium Source: MGI
  15. defense response to Gram-positive bacterium Source: MGI
  16. embryonic digestive tract development Source: Ensembl
  17. epithelial cell proliferation involved in salivary gland morphogenesis Source: MGI
  18. extracellular matrix organization Source: MGI
  19. extrinsic apoptotic signaling pathway Source: MGI
  20. extrinsic apoptotic signaling pathway via death domain receptors Source: MGI
  21. glucose metabolic process Source: MGI
  22. humoral immune response Source: MGI
  23. inflammatory response Source: MGI
  24. intrinsic apoptotic signaling pathway in response to DNA damage Source: MGI
  25. JNK cascade Source: MGI
  26. leukocyte migration Source: MGI
  27. leukocyte tethering or rolling Source: Ensembl
  28. lipopolysaccharide-mediated signaling pathway Source: Ensembl
  29. multicellular organismal development Source: MGI
  30. necroptotic signaling pathway Source: UniProtKB
  31. negative regulation of alkaline phosphatase activity Source: BHF-UCL
  32. negative regulation of branching involved in lung morphogenesis Source: Ensembl
  33. negative regulation of cell proliferation Source: Ensembl
  34. negative regulation of cytokine secretion involved in immune response Source: Ensembl
  35. negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
  36. negative regulation of glucose import Source: MGI
  37. negative regulation of growth of symbiont in host Source: MGI
  38. negative regulation of interleukin-6 production Source: Ensembl
  39. negative regulation of L-glutamate transport Source: Ensembl
  40. negative regulation of lipid catabolic process Source: Ensembl
  41. negative regulation of osteoblast differentiation Source: BHF-UCL
  42. negative regulation of protein complex disassembly Source: UniProtKB
  43. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  44. negative regulation of viral genome replication Source: Ensembl
  45. organ morphogenesis Source: MGI
  46. osteoclast differentiation Source: MGI
  47. positive regulation of apoptotic process Source: UniProtKB
  48. positive regulation of calcidiol 1-monooxygenase activity Source: Ensembl
  49. positive regulation of cell proliferation Source: MGI
  50. positive regulation of chemokine (C-X-C motif) ligand 2 production Source: Ensembl
  51. positive regulation of chemokine biosynthetic process Source: Ensembl
  52. positive regulation of chronic inflammatory response to antigenic stimulus Source: MGI
  53. positive regulation of cytokine secretion Source: Ensembl
  54. positive regulation of fever generation Source: BHF-UCL
  55. positive regulation of hair follicle development Source: UniProtKB
  56. positive regulation of heterotypic cell-cell adhesion Source: Ensembl
  57. positive regulation of humoral immune response mediated by circulating immunoglobulin Source: MGI
  58. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: MGI
  59. positive regulation of interferon-gamma production Source: MGI
  60. positive regulation of interleukin-18 production Source: Ensembl
  61. positive regulation of interleukin-6 production Source: MGI
  62. positive regulation of interleukin-8 biosynthetic process Source: Ensembl
  63. positive regulation of JNK cascade Source: MGI
  64. positive regulation of JUN kinase activity Source: UniProtKB
  65. positive regulation of MAP kinase activity Source: UniProtKB
  66. positive regulation of membrane protein ectodomain proteolysis Source: Ensembl
  67. positive regulation of mitosis Source: Ensembl
  68. positive regulation of neuron apoptotic process Source: Ensembl
  69. positive regulation of NFAT protein import into nucleus Source: Ensembl
  70. positive regulation of NF-kappaB import into nucleus Source: BHF-UCL
  71. positive regulation of NF-kappaB transcription factor activity Source: MGI
  72. positive regulation of nitric oxide biosynthetic process Source: Ensembl
  73. positive regulation of osteoclast differentiation Source: Ensembl
  74. positive regulation of peptidyl-serine phosphorylation Source: Ensembl
  75. positive regulation of podosome assembly Source: Ensembl
  76. positive regulation of protein complex disassembly Source: UniProtKB
  77. positive regulation of protein kinase B signaling Source: MGI
  78. positive regulation of protein localization to cell surface Source: Ensembl
  79. positive regulation of protein phosphorylation Source: UniProtKB
  80. positive regulation of smooth muscle cell proliferation Source: Ensembl
  81. positive regulation of synaptic transmission Source: Ensembl
  82. positive regulation of transcription, DNA-templated Source: MGI
  83. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  84. positive regulation of translational initiation by iron Source: MGI
  85. positive regulation of vitamin D biosynthetic process Source: Ensembl
  86. protein import into nucleus, translocation Source: Ensembl
  87. protein kinase B signaling Source: Ensembl
  88. receptor biosynthetic process Source: Ensembl
  89. regulation of branching involved in salivary gland morphogenesis Source: MGI
  90. regulation of cell proliferation Source: MGI
  91. regulation of immunoglobulin secretion Source: MGI
  92. regulation of insulin secretion Source: Ensembl
  93. regulation of osteoclast differentiation Source: MGI
  94. regulation of protein phosphorylation Source: MGI
  95. regulation of protein secretion Source: MGI
  96. regulation of reactive oxygen species metabolic process Source: MGI
  97. response to activity Source: Ensembl
  98. response to drug Source: Ensembl
  99. response to glucocorticoid Source: Ensembl
  100. response to hypoxia Source: Ensembl
  101. response to mechanical stimulus Source: Ensembl
  102. response to virus Source: Ensembl
  103. sequestering of triglyceride Source: Ensembl
  104. skeletal muscle contraction Source: Ensembl
  105. transformed cell apoptotic process Source: MGI
  106. tumor necrosis factor-mediated signaling pathway Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Cytokine

Enzyme and pathway databases

ReactomeiREACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

Names & Taxonomyi

Protein namesi
Recommended 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:
Gene namesi
Name:Tnf
Synonyms:Tnfa, Tnfsf2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 17

Organism-specific databases

MGIiMGI:104798. Tnf.

Subcellular locationi

Chain C-domain 1 : Secreted By similarity
Chain C-domain 2 : Secreted By similarity

GO - Cellular componenti

  1. external side of plasma membrane Source: BHF-UCL
  2. extracellular space Source: MGI
  3. integral component of plasma membrane Source: MGI
  4. intracellular Source: MGI
  5. membrane raft Source: BHF-UCL
  6. phagocytic cup Source: BHF-UCL
  7. plasma membrane Source: MGI
  8. recycling endosome Source: BHF-UCL
  9. secretory granule Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 235235Tumor necrosis factor, membrane formPRO_0000034435Add
BLAST
Chaini1 – 3939Intracellular domain 1By similarityPRO_0000417255Add
BLAST
Chaini1 – 3535Intracellular domain 2By similarityPRO_0000417256Add
BLAST
Chaini50 – ?C-domain 1By similarityPRO_0000417257
Chaini52 – ?C-domain 2By similarityPRO_0000417258
Chaini80 – 235156Tumor necrosis factor, soluble formPRO_0000034436Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21Phosphoserine; by CK1By similarity
Lipidationi20 – 201N6-myristoyl lysineBy similarity
Glycosylationi83 – 831O-linked (GalNAc...); in soluble formBy similarity
Glycosylationi86 – 861N-linked (GlcNAc...)
Disulfide bondi148 ↔ 179

Post-translational modificationi

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.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

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

PaxDbiP06804.
PRIDEiP06804.

PTM databases

PhosphoSiteiP06804.

Miscellaneous databases

PMAP-CutDBP06804.

Expressioni

Gene expression databases

BgeeiP06804.
CleanExiMM_TNF.
ExpressionAtlasiP06804. baseline and differential.
GenevestigatoriP06804.

Interactioni

Subunit structurei

Interacts with SPPL2B (By similarity). Homotrimer.By similarity

Protein-protein interaction databases

BioGridi204240. 12 interactions.
IntActiP06804. 1 interaction.

Structurei

Secondary structure

1
235
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi92 – 976
Beta strandi99 – 1013
Beta strandi107 – 1093
Beta strandi115 – 1173
Beta strandi121 – 1233
Beta strandi126 – 1283
Beta strandi130 – 14718
Beta strandi154 – 1618
Turni163 – 1653
Beta strandi168 – 1769
Beta strandi191 – 20414
Beta strandi209 – 2157
Helixi217 – 2193
Beta strandi227 – 2348

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2TNFX-ray1.40A/B/C80-234[»]
ProteinModelPortaliP06804.
SMRiP06804. Positions 88-235.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06804.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3535CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini57 – 235179ExtracellularSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei36 – 5621Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Sequence similaritiesi

Belongs to the tumor necrosis factor family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG40413.
GeneTreeiENSGT00530000062992.
HOGENOMiHOG000048729.
HOVERGENiHBG012516.
InParanoidiP06804.
KOiK03156.
OMAiPWYEPIY.
OrthoDBiEOG7V4B0Q.
PhylomeDBiP06804.
TreeFamiTF332169.

Family and domain databases

Gene3Di2.60.120.40. 1 hit.
InterProiIPR006053. TNF.
IPR002959. TNF_alpha.
IPR021184. TNF_CS.
IPR006052. TNF_dom.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view]
PfamiPF00229. TNF. 1 hit.
[Graphical view]
PRINTSiPR01234. TNECROSISFCT.
PR01235. TNFALPHA.
SMARTiSM00207. TNF. 1 hit.
[Graphical view]
SUPFAMiSSF49842. SSF49842. 1 hit.
PROSITEiPS00251. TNF_1. 1 hit.
PS50049. TNF_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P06804-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSTESMIRDV ELAEEALPQK MGGFQNSRRC LCLSLFSFLL VAGATTLFCL
60 70 80 90 100
LNFGVIGPQR DEKFPNGLPL ISSMAQTLTL RSSSQNSSDK PVAHVVANHQ
110 120 130 140 150
VEEQLEWLSQ RANALLANGM DLKDNQLVVP ADGLYLVYSQ VLFKGQGCPD
160 170 180 190 200
YVLLTHTVSR FAISYQEKVN LLSAVKSPCP KDTPEGAELK PWYEPIYLGG
210 220 230
VFQLEKGDQL SAEVNLPKYL DFAESGQVYF GVIAL
Length:235
Mass (Da):25,896
Last modified:July 1, 1989 - v2
Checksum:i16DD2A9676D68C5D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti79 – 813Missing in AAB65593. (PubMed:9089109)Curated
Sequence conflicti231 – 2311G → R(PubMed:2419912)Curated
Sequence conflicti231 – 2311G → R(PubMed:2989794)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti7 – 71I → T in strain: BALB/c and C57BL/6. 1 Publication
Natural varianti77 – 771T → A in strain: BALB/c and C57BL/6. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS28691.1.
PIRiA22908. QWMSN.
RefSeqiNP_001265530.1. NM_001278601.1.
NP_038721.1. NM_013693.3.
UniGeneiMm.1293.

Genome annotation databases

EnsembliENSMUST00000025263; ENSMUSP00000025263; ENSMUSG00000024401.
ENSMUST00000167924; ENSMUSP00000126122; ENSMUSG00000024401.
GeneIDi21926.
KEGGimmu:21926.
UCSCiuc008cgr.1. mouse.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS28691.1.
PIRi A22908. QWMSN.
RefSeqi NP_001265530.1. NM_001278601.1.
NP_038721.1. NM_013693.3.
UniGenei Mm.1293.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2TNF X-ray 1.40 A/B/C 80-234 [» ]
ProteinModelPortali P06804.
SMRi P06804. Positions 88-235.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204240. 12 interactions.
IntActi P06804. 1 interaction.

Chemistry

ChEMBLi CHEMBL4984.

PTM databases

PhosphoSitei P06804.

Proteomic databases

PaxDbi P06804.
PRIDEi P06804.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000025263 ; ENSMUSP00000025263 ; ENSMUSG00000024401 .
ENSMUST00000167924 ; ENSMUSP00000126122 ; ENSMUSG00000024401 .
GeneIDi 21926.
KEGGi mmu:21926.
UCSCi uc008cgr.1. mouse.

Organism-specific databases

CTDi 7124.
MGIi MGI:104798. Tnf.

Phylogenomic databases

eggNOGi NOG40413.
GeneTreei ENSGT00530000062992.
HOGENOMi HOG000048729.
HOVERGENi HBG012516.
InParanoidi P06804.
KOi K03156.
OMAi PWYEPIY.
OrthoDBi EOG7V4B0Q.
PhylomeDBi P06804.
TreeFami TF332169.

Enzyme and pathway databases

Reactomei REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

Miscellaneous databases

EvolutionaryTracei P06804.
NextBioi 301508.
PMAP-CutDB P06804.
PROi P06804.
SOURCEi Search...

Gene expression databases

Bgeei P06804.
CleanExi MM_TNF.
ExpressionAtlasi P06804. baseline and differential.
Genevestigatori P06804.

Family and domain databases

Gene3Di 2.60.120.40. 1 hit.
InterProi IPR006053. TNF.
IPR002959. TNF_alpha.
IPR021184. TNF_CS.
IPR006052. TNF_dom.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view ]
Pfami PF00229. TNF. 1 hit.
[Graphical view ]
PRINTSi PR01234. TNECROSISFCT.
PR01235. TNFALPHA.
SMARTi SM00207. TNF. 1 hit.
[Graphical view ]
SUPFAMi SSF49842. SSF49842. 1 hit.
PROSITEi PS00251. TNF_1. 1 hit.
PS50049. TNF_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiTNFA_MOUSE
AccessioniPrimary (citable) accession number: P06804
Secondary accession number(s): O35853, Q62326, Q91VF3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: July 1, 1989
Last modified: October 29, 2014
This is version 163 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

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