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Tumor necrosis factor receptor superfamily member 1B (Tumor necrosis factor receptor 2) (TNF-R2) (Tumor necrosis factor receptor type II) (TNF-RII) (TNFR-II) (p75) (p80 TNF-alpha receptor) (CD antigen CD120b) (Etanercept) [Cleaved into: Tumor necrosis factor receptor superfamily member 1b, membrane form; Tumor necrosis factor-binding protein 2 (TBP-2) (TBPII)]

 TNR1B_HUMAN             Reviewed;         461 AA.
P20333; B1AJZ3; Q16042; Q6YI29; Q9UIH1;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
27-MAY-2002, sequence version 3.
25-OCT-2017, entry version 200.
RecName: Full=Tumor necrosis factor receptor superfamily member 1B;
AltName: Full=Tumor necrosis factor receptor 2;
Short=TNF-R2;
AltName: Full=Tumor necrosis factor receptor type II;
Short=TNF-RII;
Short=TNFR-II;
AltName: Full=p75;
AltName: Full=p80 TNF-alpha receptor;
AltName: CD_antigen=CD120b;
AltName: INN=Etanercept;
Contains:
RecName: Full=Tumor necrosis factor receptor superfamily member 1b, membrane form;
Contains:
RecName: Full=Tumor necrosis factor-binding protein 2;
AltName: Full=TBP-2;
AltName: Full=TBPII;
Flags: Precursor;
Name=TNFRSF1B; Synonyms=TNFBR, TNFR2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ARG-196.
PubMed=2172983; DOI=10.1073/pnas.87.21.8331;
Kohno T., Brewer M.T., Baker S.L., Schwartz P.E., King M.W.,
Hale K.K., Squires C.H., Thompson R.C., Vannice J.L.;
"A second tumor necrosis factor receptor gene product can shed a
naturally occurring tumor necrosis factor inhibitor.";
Proc. Natl. Acad. Sci. U.S.A. 87:8331-8335(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2160731; DOI=10.1126/science.2160731;
Smith C.A., Davis T., Anderson D., Solam L., Beckmann M.P., Jerzy R.,
Dower S.K., Cosman D., Goodwin R.G.;
"A receptor for tumor necrosis factor defines an unusual family of
cellular and viral proteins.";
Science 248:1019-1023(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=8661109; DOI=10.1006/geno.1996.0327;
Beltinger C.P., White P.S., Maris J.M., Sulman E.P., Jensen S.J.,
Lepaslier D., Stallard B.J., Goeddel D.V., Desauvage F.J.,
Brodeur G.M.;
"Physical mapping and genomic structure of the human TNFR2 gene.";
Genomics 35:94-100(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, AND
FUNCTION (ISOFORM 2).
PubMed=14688072; DOI=10.1093/intimm/dxh014;
Lainez B., Fernandez-Real J.M., Romero X., Esplugues E., Canete J.D.,
Ricart W., Engel P.;
"Identification and characterization of a novel spliced variant that
encodes human soluble tumor necrosis factor receptor 2.";
Int. Immunol. 16:169-177(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS MET-187; ARG-196;
LYS-232; THR-236; PRO-264 AND ARG-295.
NIEHS SNPs program;
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-196; LYS-232;
PRO-269 AND ARG-301.
SeattleSNPs variation discovery resource;
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=PNS;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
PROTEIN SEQUENCE OF 23-40; 65-69; 136-141; 300-306 AND 346-362.
PubMed=2173696;
Loetscher H., Schlaeger E.J., Lahm H.-W., Pan Y.-C.E., Lesslauer W.,
Brockhaus M.;
"Purification and partial amino acid sequence analysis of two distinct
tumor necrosis factor receptors from HL60 cells.";
J. Biol. Chem. 265:20131-20138(1990).
[12]
PROTEIN SEQUENCE OF 27-37.
TISSUE=Urine;
PubMed=8015639;
Suzuki J., Tomizawa S., Arai H., Seki Y., Maruyama K., Kuroume T.;
"Purification of two types of TNF inhibitors in the urine of the
patient with chronic glomerulonephritis.";
Nephron 66:386-390(1994).
[13]
PROTEIN SEQUENCE OF 27-31.
TISSUE=Urine;
PubMed=2153136;
Engelmann H., Novick D., Wallach D.;
"Two tumor necrosis factor-binding proteins purified from human urine.
Evidence for immunological cross-reactivity with cell surface tumor
necrosis factor receptors.";
J. Biol. Chem. 265:1531-1536(1990).
[14]
NUCLEOTIDE SEQUENCE [MRNA] OF 37-461 (ISOFORM 1).
PubMed=1966549; DOI=10.1016/1043-4666(90)90022-L;
Dembic Z., Loetscher H., Gubler U., Pan Y.C., Lahm H.-W., Gentz R.,
Brockhaus M., Lesslauer W.;
"Two human TNF receptors have similar extracellular, but distinct
intracellular, domain sequences.";
Cytokine 2:231-237(1990).
[15]
NUCLEOTIDE SEQUENCE [MRNA] OF 116-461 (ISOFORM 1), PARTIAL PROTEIN
SEQUENCE, AND VARIANT ARG-196.
PubMed=2166946; DOI=10.1073/pnas.87.16.6151;
Heller R.A., Song K., Onasch M.A., Fischer W.H., Chang D.,
Ringold G.M.;
"Complementary DNA cloning of a receptor for tumor necrosis factor and
demonstration of a shed form of the receptor.";
Proc. Natl. Acad. Sci. U.S.A. 87:6151-6155(1990).
[16]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 154-183, AND VARIANTS ARG-196 AND
LYS-232.
PubMed=11197692; DOI=10.1038/sj.gene.6363700;
Tsuchiya N., Komata T., Matsushita M., Ohashi J., Tokunaga K.;
"New single nucleotide polymorphisms in the coding region of human
TNFR2: association with systemic lupus erythematosus.";
Genes Immun. 1:501-503(2000).
[17]
CHARACTERIZATION.
PubMed=1328224;
Pennica D., Lam V.T., Mize N.K., Weber R.F., Lewis M., Fendly B.M.,
Lipari M.T., Goeddel D.V.;
"Biochemical properties of the 75-kDa tumor necrosis factor receptor.
Characterization of ligand binding, internalization, and receptor
phosphorylation.";
J. Biol. Chem. 267:21172-21178(1992).
[18]
INTERACTION WITH TRAF2.
PubMed=8069916; DOI=10.1016/0092-8674(94)90532-0;
Rothe M., Wong S.C., Henzel W.J., Goeddel D.V.;
"A novel family of putative signal transducers associated with the
cytoplasmic domain of the 75 kDa tumor necrosis factor receptor.";
Cell 78:681-692(1994).
[19]
FUNCTION, AND INTERACTION WITH BMX.
PubMed=12370298; DOI=10.1128/MCB.22.21.7512-7523.2002;
Pan S., An P., Zhang R., He X., Yin G., Min W.;
"Etk/Bmx as a tumor necrosis factor receptor type 2-specific kinase:
role in endothelial cell migration and angiogenesis.";
Mol. Cell. Biol. 22:7512-7523(2002).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[21]
GLYCOSYLATION AT THR-30; THR-206; SER-221 AND THR-222, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=25456591; DOI=10.1016/j.chroma.2014.10.046;
Huang L.J., Lin J.H., Tsai J.H., Chu Y.Y., Chen Y.W., Chen S.L.,
Chen S.H.;
"Identification of protein O-glycosylation site and corresponding
glycans using liquid chromatography-tandem mass spectrometry via
mapping accurate mass and retention time shift.";
J. Chromatogr. A 1371:136-145(2014).
[22]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 419-428 IN COMPLEX WITH
TRAF2.
PubMed=10206649; DOI=10.1038/19110;
Park Y.C., Burkitt V., Villa A.R., Tong L., Wu H.;
"Structural basis for self-association and receptor recognition of
human TRAF2.";
Nature 398:533-538(1999).
[23]
VARIANTS ARG-196 AND LYS-232.
PubMed=11762942;
DOI=10.1002/1529-0131(200112)44:12<2819::AID-ART469>3.0.CO;2-2;
Morita C., Horiuchi T., Tsukamoto H., Hatta N., Kikuchi Y.,
Arinobu Y., Otsuka T., Sawabe T., Harashima S., Nagasawa K., Niho Y.;
"Association of tumor necrosis factor receptor type II polymorphism
196R with systemic lupus erythematosus in the Japanese: molecular and
functional analysis.";
Arthritis Rheum. 44:2819-2827(2001).
[24]
VARIANT ARG-196.
PubMed=12161545; DOI=10.1210/jcem.87.8.8715;
Peral B., San Millan J.L., Castello R., Moghetti P.,
Escobar-Morreale H.F.;
"Comment: the methionine 196 arginine polymorphism in exon 6 of the
TNF receptor 2 gene (TNFRSF1B) is associated with the polycystic ovary
syndrome and hyperandrogenism.";
J. Clin. Endocrinol. Metab. 87:3977-3983(2002).
-!- FUNCTION: Receptor with high affinity for TNFSF2/TNF-alpha and
approximately 5-fold lower affinity for homotrimeric
TNFSF1/lymphotoxin-alpha. The TRAF1/TRAF2 complex recruits the
apoptotic suppressors BIRC2 and BIRC3 to TNFRSF1B/TNFR2. This
receptor mediates most of the metabolic effects of TNF-alpha.
Isoform 2 blocks TNF-alpha-induced apoptosis, which suggests that
it regulates TNF-alpha function by antagonizing its biological
activity. {ECO:0000269|PubMed:12370298}.
-!- SUBUNIT: Binds to TRAF2. Interacts with BMX.
{ECO:0000269|PubMed:10206649, ECO:0000269|PubMed:12370298,
ECO:0000269|PubMed:8069916}.
-!- INTERACTION:
P28799:GRN; NbExp=5; IntAct=EBI-358983, EBI-747754;
P01375:TNF; NbExp=2; IntAct=EBI-358983, EBI-359977;
Q12933:TRAF2; NbExp=3; IntAct=EBI-358983, EBI-355744;
-!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I
membrane protein.
-!- SUBCELLULAR LOCATION: Isoform 2: Secreted.
-!- SUBCELLULAR LOCATION: Tumor necrosis factor-binding protein 2:
Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P20333-1; Sequence=Displayed;
Name=2; Synonyms=DS-TNFR2(Delta7,8), sTNFR2;
IsoId=P20333-2; Sequence=VSP_011826, VSP_011827;
-!- PTM: Phosphorylated; mainly on serine residues and with a very low
level on threonine residues.
-!- PTM: A soluble form (tumor necrosis factor binding protein 2) is
produced from the membrane form by proteolytic processing.
-!- PHARMACEUTICAL: Available under the name Enbrel (Immunex and
Wyeth-Ayerst). Used to treat moderate to severe rheumatoid
arthritis (RA). Enbrel consist of the extracellular ligand-binding
portion of TNFRSF1B linked to an immunoglobulin Fc chain. It binds
to TNF-alpha and blocks its interactions with receptors.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/tnfrsf1b/";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/tnfrsf1b/";
-!- WEB RESOURCE: Name=Enbrel; Note=Clinical information on Enbrel;
URL="https://www.enbrel.com";
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EMBL; M55994; AAA36755.1; -; mRNA.
EMBL; M32315; AAA59929.1; -; mRNA.
EMBL; U52165; AAC50622.1; -; Genomic_DNA.
EMBL; U52156; AAC50622.1; JOINED; Genomic_DNA.
EMBL; U52157; AAC50622.1; JOINED; Genomic_DNA.
EMBL; U52158; AAC50622.1; JOINED; Genomic_DNA.
EMBL; U52159; AAC50622.1; JOINED; Genomic_DNA.
EMBL; U52160; AAC50622.1; JOINED; Genomic_DNA.
EMBL; U52161; AAC50622.1; JOINED; Genomic_DNA.
EMBL; U52162; AAC50622.1; JOINED; Genomic_DNA.
EMBL; U52163; AAC50622.1; JOINED; Genomic_DNA.
EMBL; U52164; AAC50622.1; JOINED; Genomic_DNA.
EMBL; AY148473; AAN72434.1; -; mRNA.
EMBL; BT019927; AAV38730.1; -; mRNA.
EMBL; AY264804; AAO89076.1; -; Genomic_DNA.
EMBL; AY342040; AAP88939.1; -; Genomic_DNA.
EMBL; AL031276; CAI19225.1; -; Genomic_DNA.
EMBL; AL357835; CAI19225.1; JOINED; Genomic_DNA.
EMBL; AL357835; CAH73721.1; -; Genomic_DNA.
EMBL; AL031276; CAH73721.1; JOINED; Genomic_DNA.
EMBL; CH471130; EAW71733.1; -; Genomic_DNA.
EMBL; BC052977; AAH52977.1; -; mRNA.
EMBL; S63368; AAB19824.2; -; mRNA.
EMBL; M35857; AAA63262.1; -; mRNA.
EMBL; AB030950; BAA89053.1; -; Genomic_DNA.
CCDS; CCDS145.1; -. [P20333-1]
PIR; A35356; A35356.
RefSeq; NP_001057.1; NM_001066.2. [P20333-1]
UniGene; Hs.256278; -.
PDB; 1CA9; X-ray; 2.30 A; G/H=420-428.
PDB; 3ALQ; X-ray; 3.00 A; R/S/T/U/V/W=33-205.
PDBsum; 1CA9; -.
PDBsum; 3ALQ; -.
ProteinModelPortal; P20333; -.
SMR; P20333; -.
BioGrid; 112987; 26.
CORUM; P20333; -.
DIP; DIP-78N; -.
ELM; P20333; -.
IntAct; P20333; 12.
MINT; MINT-134958; -.
STRING; 9606.ENSP00000365435; -.
ChEMBL; CHEMBL1250356; -.
DrugBank; DB00005; Etanercept.
iPTMnet; P20333; -.
PhosphoSitePlus; P20333; -.
BioMuta; TNFRSF1B; -.
DMDM; 21264534; -.
PaxDb; P20333; -.
PeptideAtlas; P20333; -.
PRIDE; P20333; -.
DNASU; 7133; -.
Ensembl; ENST00000376259; ENSP00000365435; ENSG00000028137. [P20333-1]
GeneID; 7133; -.
KEGG; hsa:7133; -.
UCSC; uc001att.4; human. [P20333-1]
CTD; 7133; -.
DisGeNET; 7133; -.
EuPathDB; HostDB:ENSG00000028137.16; -.
GeneCards; TNFRSF1B; -.
HGNC; HGNC:11917; TNFRSF1B.
HPA; HPA004796; -.
MalaCards; TNFRSF1B; -.
MIM; 191191; gene.
neXtProt; NX_P20333; -.
OpenTargets; ENSG00000028137; -.
PharmGKB; PA36610; -.
eggNOG; ENOG410IJ06; Eukaryota.
eggNOG; ENOG410YPQW; LUCA.
GeneTree; ENSGT00760000119204; -.
HOGENOM; HOG000132845; -.
HOVERGEN; HBG054237; -.
InParanoid; P20333; -.
KO; K05141; -.
OMA; NCVIMTQ; -.
OrthoDB; EOG091G03XW; -.
PhylomeDB; P20333; -.
TreeFam; TF331157; -.
Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
Reactome; R-HSA-5669034; TNFs bind their physiological receptors.
Reactome; R-HSA-6783783; Interleukin-10 signaling.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
Reactome; R-HSA-6798695; Neutrophil degranulation.
SIGNOR; P20333; -.
ChiTaRS; TNFRSF1B; human.
EvolutionaryTrace; P20333; -.
GeneWiki; TNFRSF1B; -.
GenomeRNAi; 7133; -.
PMAP-CutDB; P20333; -.
PRO; PR:P20333; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000028137; -.
CleanEx; HS_TNFRSF1B; -.
ExpressionAtlas; P20333; baseline and differential.
Genevisible; P20333; HS.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0045121; C:membrane raft; IDA:BHF-UCL.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
GO; GO:0043196; C:varicosity; IEA:Ensembl.
GO; GO:0005031; F:tumor necrosis factor-activated receptor activity; IBA:GO_Central.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0097190; P:apoptotic signaling pathway; IBA:GO_Central.
GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:Ensembl.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:BHF-UCL.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0006955; P:immune response; IBA:GO_Central.
GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
GO; GO:0007275; P:multicellular organism development; IBA:GO_Central.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IMP:BHF-UCL.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0050779; P:RNA destabilization; IEA:Ensembl.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
CDD; cd10577; TNFRSF1B; 1.
InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
InterPro; IPR020411; TNFR_1B.
InterPro; IPR033996; TNFRSF1B_N.
Pfam; PF00020; TNFR_c6; 3.
PRINTS; PR01919; TNFACTORR1B.
SMART; SM00208; TNFR; 4.
PROSITE; PS00652; TNFR_NGFR_1; 2.
PROSITE; PS50050; TNFR_NGFR_2; 3.
1: Evidence at protein level;
3D-structure; Alternative splicing; Apoptosis; Cell membrane;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Membrane; Pharmaceutical; Phosphoprotein; Polymorphism;
Receptor; Reference proteome; Repeat; Secreted; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 22 {ECO:0000269|PubMed:2173696}.
CHAIN 23 461 Tumor necrosis factor receptor
superfamily member 1b, membrane form.
/FTId=PRO_0000034548.
CHAIN 27 ? Tumor necrosis factor-binding protein 2.
/FTId=PRO_0000034549.
TOPO_DOM 23 257 Extracellular. {ECO:0000255}.
TRANSMEM 258 287 Helical. {ECO:0000255}.
TOPO_DOM 288 461 Cytoplasmic. {ECO:0000255}.
REPEAT 39 76 TNFR-Cys 1.
REPEAT 77 118 TNFR-Cys 2.
REPEAT 119 162 TNFR-Cys 3.
REPEAT 163 201 TNFR-Cys 4.
MOD_RES 330 330 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CARBOHYD 30 30 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:25456591}.
CARBOHYD 171 171 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 193 193 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 206 206 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:25456591}.
CARBOHYD 221 221 O-linked (GalNAc...) serine.
{ECO:0000269|PubMed:25456591}.
CARBOHYD 222 222 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:25456591}.
DISULFID 40 53 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 54 67 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 57 75 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 78 93 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 96 110 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 100 118 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 120 126 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 134 143 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 137 161 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 164 179 {ECO:0000255|PROSITE-ProRule:PRU00206}.
VAR_SEQ 263 268 GLIVGV -> ASLACR (in isoform 2).
{ECO:0000303|PubMed:14688072}.
/FTId=VSP_011826.
VAR_SEQ 269 461 Missing (in isoform 2).
{ECO:0000303|PubMed:14688072}.
/FTId=VSP_011827.
VARIANT 187 187 V -> M (in dbSNP:rs2228494).
{ECO:0000269|Ref.6}.
/FTId=VAR_017176.
VARIANT 196 196 M -> R (frequent polymorphism; seems to
be associated with hyperandrogenism,
polycystic ovary syndrome (PCOS) and
systemic lupus erythematosus;
dbSNP:rs1061622).
{ECO:0000269|PubMed:11197692,
ECO:0000269|PubMed:11762942,
ECO:0000269|PubMed:12161545,
ECO:0000269|PubMed:2166946,
ECO:0000269|PubMed:2172983,
ECO:0000269|Ref.6, ECO:0000269|Ref.7}.
/FTId=VAR_015434.
VARIANT 232 232 E -> K (in dbSNP:rs5746026).
{ECO:0000269|PubMed:11197692,
ECO:0000269|PubMed:11762942,
ECO:0000269|Ref.6, ECO:0000269|Ref.7}.
/FTId=VAR_015435.
VARIANT 236 236 A -> T (in dbSNP:rs5746027).
{ECO:0000269|Ref.6}.
/FTId=VAR_017177.
VARIANT 264 264 L -> P (in dbSNP:rs2229700).
{ECO:0000269|Ref.6}.
/FTId=VAR_017178.
VARIANT 269 269 T -> P (in dbSNP:rs17879042).
{ECO:0000269|Ref.7}.
/FTId=VAR_017179.
VARIANT 295 295 Q -> R (in dbSNP:rs5746032).
{ECO:0000269|Ref.6}.
/FTId=VAR_017180.
VARIANT 301 301 P -> R (in dbSNP:rs17883432).
{ECO:0000269|Ref.7}.
/FTId=VAR_017181.
CONFLICT 35 37 EPG -> APT (in Ref. 12; AA sequence).
{ECO:0000305}.
CONFLICT 98 98 S -> P (in Ref. 4; AAN72434).
{ECO:0000305}.
CONFLICT 102 102 S -> P (in Ref. 4; AAN72434).
{ECO:0000305}.
CONFLICT 141 141 R -> P (in Ref. 15; AAA63262).
{ECO:0000305}.
CONFLICT 363 363 A -> T (in Ref. 15; AAA63262).
{ECO:0000305}.
STRAND 44 47 {ECO:0000244|PDB:3ALQ}.
TURN 48 51 {ECO:0000244|PDB:3ALQ}.
STRAND 52 55 {ECO:0000244|PDB:3ALQ}.
STRAND 61 65 {ECO:0000244|PDB:3ALQ}.
STRAND 74 77 {ECO:0000244|PDB:3ALQ}.
STRAND 86 88 {ECO:0000244|PDB:3ALQ}.
STRAND 104 108 {ECO:0000244|PDB:3ALQ}.
STRAND 112 114 {ECO:0000244|PDB:3ALQ}.
STRAND 117 120 {ECO:0000244|PDB:3ALQ}.
STRAND 124 129 {ECO:0000244|PDB:3ALQ}.
STRAND 131 139 {ECO:0000244|PDB:3ALQ}.
STRAND 147 151 {ECO:0000244|PDB:3ALQ}.
TURN 154 156 {ECO:0000244|PDB:3ALQ}.
STRAND 160 163 {ECO:0000244|PDB:3ALQ}.
STRAND 174 176 {ECO:0000244|PDB:3ALQ}.
STRAND 194 196 {ECO:0000244|PDB:3ALQ}.
SEQUENCE 461 AA; 48291 MW; 603D0AE1CD69ACBF CRC64;
MAPVAVWAAL AVGLELWAAA HALPAQVAFT PYAPEPGSTC RLREYYDQTA QMCCSKCSPG
QHAKVFCTKT SDTVCDSCED STYTQLWNWV PECLSCGSRC SSDQVETQAC TREQNRICTC
RPGWYCALSK QEGCRLCAPL RKCRPGFGVA RPGTETSDVV CKPCAPGTFS NTTSSTDICR
PHQICNVVAI PGNASMDAVC TSTSPTRSMA PGAVHLPQPV STRSQHTQPT PEPSTAPSTS
FLLPMGPSPP AEGSTGDFAL PVGLIVGVTA LGLLIIGVVN CVIMTQVKKK PLCLQREAKV
PHLPADKARG TQGPEQQHLL ITAPSSSSSS LESSASALDR RAPTRNQPQA PGVEASGAGE
ARASTGSSDS SPGGHGTQVN VTCIVNVCSS SDHSSQCSSQ ASSTMGDTDS SPSESPKDEQ
VPFSKEECAF RSQLETPETL LGSTEEKPLP LGVPDAGMKP S


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