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Protein

Tumor necrosis factor receptor superfamily member 6

Gene

Fas

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

Functioni

Receptor for TNFSF6/FASLG. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. FAS-mediated apoptosis may have a role in the induction of peripheral tolerance, in the antigen-stimulated suicide of mature T-cells, or both (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

  • activation-induced cell death of T cells Source: MGI
  • apoptotic process Source: MGI
  • apoptotic signaling pathway Source: MGI
  • B cell mediated immunity Source: MGI
  • cellular response to hyperoxia Source: MGI
  • cellular response to lithium ion Source: MGI
  • cellular response to mechanical stimulus Source: Ensembl
  • circadian rhythm Source: UniProtKB
  • extrinsic apoptotic signaling pathway Source: MGI
  • extrinsic apoptotic signaling pathway in absence of ligand Source: MGI
  • extrinsic apoptotic signaling pathway via death domain receptors Source: BHF-UCL
  • gene expression Source: MGI
  • hepatocyte apoptotic process Source: MGI
  • immunoglobulin production Source: MGI
  • inflammatory cell apoptotic process Source: MGI
  • motor neuron apoptotic process Source: MGI
  • necroptotic signaling pathway Source: MGI
  • negative regulation of apoptotic process Source: MGI
  • negative regulation of B cell activation Source: MGI
  • negative thymic T cell selection Source: MGI
  • neuron apoptotic process Source: MGI
  • positive regulation of apoptotic process Source: MGI
  • positive regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: MGI
  • positive regulation of protein homooligomerization Source: BHF-UCL
  • positive regulation of release of cytochrome c from mitochondria Source: BHF-UCL
  • protein homooligomerization Source: MGI
  • regulation of lymphocyte differentiation Source: MGI
  • regulation of myeloid cell differentiation Source: MGI
  • renal system process Source: MGI
  • response to glucocorticoid Source: MGI
  • response to toxic substance Source: MGI
  • spleen development Source: MGI
  • T cell homeostasis Source: MGI
  • transformed cell apoptotic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

ReactomeiREACT_284952. FasL/ CD95L signaling.
REACT_301406. Dimerization of procaspase-8.
REACT_310781. Regulation by c-FLIP.
REACT_354529. Ligand-dependent caspase activation.
REACT_362347. CASP8 activity is inhibited.
REACT_362359. RIPK1-mediated regulated necrosis.

Names & Taxonomyi

Protein namesi
Recommended name:
Tumor necrosis factor receptor superfamily member 6
Alternative name(s):
Apo-1 antigen
Apoptosis-mediating surface antigen FAS
FASLG receptor
CD_antigen: CD95
Gene namesi
Name:Fas
Synonyms:Apt1, Tnfrsf6
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:95484. Fas.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini22 – 169148ExtracellularSequence AnalysisAdd
BLAST
Transmembranei170 – 18617HelicalSequence AnalysisAdd
BLAST
Topological domaini187 – 327141CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • CD95 death-inducing signaling complex Source: UniProtKB
  • cell surface Source: MGI
  • cytoplasm Source: MGI
  • death-inducing signaling complex Source: MGI
  • external side of plasma membrane Source: MGI
  • extracellular exosome Source: MGI
  • extracellular region Source: MGI
  • integral component of membrane Source: UniProtKB-KW
  • membrane raft Source: MGI
  • nucleus Source: MGI
  • plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Defects in Fas are the cause of the lymphoproliferation phenotype (lpr). Lpr mice show lymphadenopathy and autoantibody production.

Keywords - Diseasei

Disease mutation

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 327306Tumor necrosis factor receptor superfamily member 6PRO_0000034567Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi43 – 431N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi44 ↔ 55PROSITE-ProRule annotation
Disulfide bondi56 ↔ 69PROSITE-ProRule annotation
Disulfide bondi59 ↔ 78PROSITE-ProRule annotation
Disulfide bondi81 ↔ 97PROSITE-ProRule annotation
Disulfide bondi100 ↔ 115PROSITE-ProRule annotation
Disulfide bondi103 ↔ 123PROSITE-ProRule annotation
Glycosylationi114 – 1141N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi125 ↔ 139PROSITE-ProRule annotation
Disulfide bondi142 ↔ 153PROSITE-ProRule annotation
Disulfide bondi145 ↔ 161PROSITE-ProRule annotation
Modified residuei217 – 2171PhosphoserineBy similarity
Modified residuei220 – 2201Phosphoserine1 Publication
Modified residuei314 – 3141Phosphothreonine1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP25446.
PaxDbiP25446.
PRIDEiP25446.

PTM databases

PhosphoSiteiP25446.

Expressioni

Tissue specificityi

Detected in various tissues including thymus, liver, lung, heart, and adult ovary.

Inductioni

Expression oscillates in a circadian manner in the liver with peak levels seen at CT12.1 Publication

Gene expression databases

BgeeiP25446.
CleanExiMM_FAS.
ExpressionAtlasiP25446. baseline and differential.
GenevisibleiP25446. MM.

Interactioni

Subunit structurei

Binds DAXX and RIPK1. Interacts with BRE and FEM1B (By similarity). Interacts with HIPK3. Part of a complex containing HIPK3 and FADD. Interacts with FADD (By similarity). Interacts directly (via DED domain) with NOL3 (via CARD domain); inhibits death-inducing signaling complex (DISC) assembly by inhibiting the increase in FAS-FADD binding induced by FAS activation.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Casp8O891103EBI-296206,EBI-851690
DAXXQ9UER74EBI-296206,EBI-77321From a different organism.
DaxxO356132EBI-296206,EBI-77304
FADDQ131585EBI-296206,EBI-494804From a different organism.
FaddQ611603EBI-296206,EBI-524415
Hipk3Q9ERH73EBI-296206,EBI-524356
PmlQ609536EBI-296206,EBI-3895605

Protein-protein interaction databases

BioGridi199594. 6 interactions.
DIPiDIP-31093N.
IntActiP25446. 11 interactions.
MINTiMINT-144559.
STRINGi10090.ENSMUSP00000025691.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3OQ9X-ray6.80A/B/C/D/E223-308[»]
ProteinModelPortaliP25446.
SMRiP25446. Positions 48-159, 223-308.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25446.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati43 – 7937TNFR-Cys 1Add
BLAST
Repeati80 – 12344TNFR-Cys 2Add
BLAST
Repeati124 – 16239TNFR-Cys 3Add
BLAST
Domaini222 – 30685DeathPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni204 – 309106Interaction with HIPK3Add
BLAST

Domaini

Contains a death domain involved in the binding of FADD, and maybe to other cytosolic adapter proteins.

Sequence similaritiesi

Contains 1 death domain.PROSITE-ProRule annotation
Contains 3 TNFR-Cys repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG45364.
GeneTreeiENSGT00730000111280.
HOGENOMiHOG000139681.
HOVERGENiHBG004091.
InParanoidiP25446.
OMAiCTTCEHG.
OrthoDBiEOG7DVDC8.
TreeFamiTF333916.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
InterProiIPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR008063. Fas_rcpt.
IPR001368. TNFR/NGFR_Cys_rich_reg.
[Graphical view]
PfamiPF00531. Death. 1 hit.
PF00020. TNFR_c6. 3 hits.
[Graphical view]
PRINTSiPR01680. TNFACTORR6.
SMARTiSM00005. DEATH. 1 hit.
SM00208. TNFR. 3 hits.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
PROSITEiPS50017. DEATH_DOMAIN. 1 hit.
PS00652. TNFR_NGFR_1. 2 hits.
PS50050. TNFR_NGFR_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P25446-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLWIWAVLPL VLAGSQLRVH TQGTNSISES LKLRRRVRET DKNCSEGLYQ
60 70 80 90 100
GGPFCCQPCQ PGKKKVEDCK MNGGTPTCAP CTEGKEYMDK NHYADKCRRC
110 120 130 140 150
TLCDEEHGLE VETNCTLTQN TKCKCKPDFY CDSPGCEHCV RCASCEHGTL
160 170 180 190 200
EPCTATSNTN CRKQSPRNRL WLLTILVLLI PLVFIYRKYR KRKCWKRRQD
210 220 230 240 250
DPESRTSSRE TIPMNASNLS LSKYIPRIAE DMTIQEAKKF ARENNIKEGK
260 270 280 290 300
IDEIMHDSIQ DTAEQKVQLL LCWYQSHGKS DAYQDLIKGL KKAECRRTLD
310 320
KFQDMVQKDL GKSTPDTGNE NEGQCLE
Length:327
Mass (Da):37,437
Last modified:July 27, 2011 - v2
Checksum:iD8DA95CA525CED56
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti38 – 381R → H in AAA37593 (PubMed:1371136).Curated
Sequence conflicti38 – 381R → H in CAC00638 (Ref. 2) Curated
Sequence conflicti38 – 381R → H in AAB25700 (PubMed:7680478).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti246 – 2461I → N in lpr. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M83649 mRNA. Translation: AAA37593.1.
AK002590 mRNA. Translation: BAB22211.1.
AJ295702, AJ295703, AJ295704 Genomic DNA. Translation: CAC00638.1.
DQ846748 mRNA. Translation: ABI24112.1.
CH466534 Genomic DNA. Translation: EDL41748.1.
BC061160 mRNA. Translation: AAH61160.1.
S56490, S56485, S56486 Genomic DNA. Translation: AAB25700.1.
CCDSiCCDS29758.1.
PIRiA46484.
RefSeqiNP_032013.2. NM_007987.2.
UniGeneiMm.1626.

Genome annotation databases

EnsembliENSMUST00000025691; ENSMUSP00000025691; ENSMUSG00000024778.
GeneIDi14102.
UCSCiuc008hgi.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M83649 mRNA. Translation: AAA37593.1.
AK002590 mRNA. Translation: BAB22211.1.
AJ295702, AJ295703, AJ295704 Genomic DNA. Translation: CAC00638.1.
DQ846748 mRNA. Translation: ABI24112.1.
CH466534 Genomic DNA. Translation: EDL41748.1.
BC061160 mRNA. Translation: AAH61160.1.
S56490, S56485, S56486 Genomic DNA. Translation: AAB25700.1.
CCDSiCCDS29758.1.
PIRiA46484.
RefSeqiNP_032013.2. NM_007987.2.
UniGeneiMm.1626.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3OQ9X-ray6.80A/B/C/D/E223-308[»]
ProteinModelPortaliP25446.
SMRiP25446. Positions 48-159, 223-308.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199594. 6 interactions.
DIPiDIP-31093N.
IntActiP25446. 11 interactions.
MINTiMINT-144559.
STRINGi10090.ENSMUSP00000025691.

PTM databases

PhosphoSiteiP25446.

Proteomic databases

MaxQBiP25446.
PaxDbiP25446.
PRIDEiP25446.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025691; ENSMUSP00000025691; ENSMUSG00000024778.
GeneIDi14102.
UCSCiuc008hgi.2. mouse.

Organism-specific databases

CTDi355.
MGIiMGI:95484. Fas.

Phylogenomic databases

eggNOGiNOG45364.
GeneTreeiENSGT00730000111280.
HOGENOMiHOG000139681.
HOVERGENiHBG004091.
InParanoidiP25446.
OMAiCTTCEHG.
OrthoDBiEOG7DVDC8.
TreeFamiTF333916.

Enzyme and pathway databases

ReactomeiREACT_284952. FasL/ CD95L signaling.
REACT_301406. Dimerization of procaspase-8.
REACT_310781. Regulation by c-FLIP.
REACT_354529. Ligand-dependent caspase activation.
REACT_362347. CASP8 activity is inhibited.
REACT_362359. RIPK1-mediated regulated necrosis.

Miscellaneous databases

EvolutionaryTraceiP25446.
NextBioi285130.
PROiP25446.
SOURCEiSearch...

Gene expression databases

BgeeiP25446.
CleanExiMM_FAS.
ExpressionAtlasiP25446. baseline and differential.
GenevisibleiP25446. MM.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
InterProiIPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR008063. Fas_rcpt.
IPR001368. TNFR/NGFR_Cys_rich_reg.
[Graphical view]
PfamiPF00531. Death. 1 hit.
PF00020. TNFR_c6. 3 hits.
[Graphical view]
PRINTSiPR01680. TNFACTORR6.
SMARTiSM00005. DEATH. 1 hit.
SM00208. TNFR. 3 hits.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
PROSITEiPS50017. DEATH_DOMAIN. 1 hit.
PS00652. TNFR_NGFR_1. 2 hits.
PS50050. TNFR_NGFR_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The cDNA structure, expression, and chromosomal assignment of the mouse Fas antigen."
    Watanabe-Fukunaga R., Brannan C.I., Itoh N., Yonehara S., Copeland N.G., Jenkins N.A., Nagata S.
    J. Immunol. 148:1274-1279(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Role of a mutant fas receptor in a transgenic mouse."
    Koczan D., Ibrahim S.M., Thiesen H.J.
    Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/Sv.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Kidney.
  4. "A role for the Fas/FasL system in modulating genetic susceptibility to T-cell lymphoblastic lymphomas."
    Villa-Morales M., Santos J., Perez-Gomez E., Quintanilla M., Fernandez-Piqueras J.
    Cancer Res. 67:5107-5116(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
  5. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.
  7. "Aberrant transcription caused by the insertion of an early transposable element in an intron of the Fas antigen gene of lpr mice."
    Adachi M., Watanabe-Fukunaga R., Nagata S.
    Proc. Natl. Acad. Sci. U.S.A. 90:1756-1760(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-96.
  8. "Daxx, a novel Fas-binding protein that activates JNK and apoptosis."
    Yang X., Khosravi-Far R., Chang H.Y., Baltimore D.
    Cell 89:1067-1076(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DAXX.
  9. "FIST/HIPK3: a Fas/FADD-interacting serine/threonine kinase that induces FADD phosphorylation and inhibits Fas-mediated Jun NH2-terminal kinase activation."
    Rochat-Steiner V., Becker K., Micheau O., Schneider P., Burns K., Tschopp J.
    J. Exp. Med. 192:1165-1174(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIPK3.
  10. "Inhibition of both the extrinsic and intrinsic death pathways through nonhomotypic death-fold interactions."
    Nam Y.J., Mani K., Ashton A.W., Peng C.F., Krishnamurthy B., Hayakawa Y., Lee P., Korsmeyer S.J., Kitsis R.N.
    Mol. Cell 15:901-912(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NOL3.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220 AND THR-314, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "p75 neurotrophin receptor is a clock gene that regulates oscillatory components of circadian and metabolic networks."
    Baeza-Raja B., Eckel-Mahan K., Zhang L., Vagena E., Tsigelny I.F., Sassone-Corsi P., Ptacek L.J., Akassoglou K.
    J. Neurosci. 33:10221-10234(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  14. "Lymphoproliferation disorder in mice explained by defects in Fas antigen that mediates apoptosis."
    Watanabe-Fukunaga R., Brannan C.I., Copeland N.G., Jenkins N.A., Nagata S.
    Nature 356:314-317(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LPR ASN-246.

Entry informationi

Entry nameiTNR6_MOUSE
AccessioniPrimary (citable) accession number: P25446
Secondary accession number(s): Q6GT31, Q9DCQ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: July 27, 2011
Last modified: July 22, 2015
This is version 161 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, 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

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.