TNR1B_HUMAN
ID TNR1B_HUMAN Reviewed; 461 AA.
AC P20333; B1AJZ3; Q16042; Q6YI29; Q9UIH1;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 3.
DT 03-AUG-2022, entry version 229.
DE RecName: Full=Tumor necrosis factor receptor superfamily member 1B;
DE AltName: Full=Tumor necrosis factor receptor 2;
DE Short=TNF-R2;
DE AltName: Full=Tumor necrosis factor receptor type II;
DE Short=TNF-RII;
DE Short=TNFR-II;
DE AltName: Full=p75;
DE AltName: Full=p80 TNF-alpha receptor;
DE AltName: CD_antigen=CD120b;
DE AltName: INN=Etanercept;
DE Contains:
DE RecName: Full=Tumor necrosis factor receptor superfamily member 1b, membrane form;
DE Contains:
DE RecName: Full=Tumor necrosis factor-binding protein 2;
DE AltName: Full=TBP-2;
DE AltName: Full=TBPII;
DE Flags: Precursor;
GN Name=TNFRSF1B; Synonyms=TNFBR, TNFR2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ARG-196.
RX PubMed=2172983; DOI=10.1073/pnas.87.21.8331;
RA Kohno T., Brewer M.T., Baker S.L., Schwartz P.E., King M.W., Hale K.K.,
RA Squires C.H., Thompson R.C., Vannice J.L.;
RT "A second tumor necrosis factor receptor gene product can shed a naturally
RT occurring tumor necrosis factor inhibitor.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:8331-8335(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2160731; DOI=10.1126/science.2160731;
RA Smith C.A., Davis T., Anderson D., Solam L., Beckmann M.P., Jerzy R.,
RA Dower S.K., Cosman D., Goodwin R.G.;
RT "A receptor for tumor necrosis factor defines an unusual family of cellular
RT and viral proteins.";
RL Science 248:1019-1023(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=8661109; DOI=10.1006/geno.1996.0327;
RA Beltinger C.P., White P.S., Maris J.M., Sulman E.P., Jensen S.J.,
RA Lepaslier D., Stallard B.J., Goeddel D.V., Desauvage F.J., Brodeur G.M.;
RT "Physical mapping and genomic structure of the human TNFR2 gene.";
RL Genomics 35:94-100(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, AND FUNCTION
RP (ISOFORM 2).
RX PubMed=14688072; DOI=10.1093/intimm/dxh014;
RA Lainez B., Fernandez-Real J.M., Romero X., Esplugues E., Canete J.D.,
RA Ricart W., Engel P.;
RT "Identification and characterization of a novel spliced variant that
RT encodes human soluble tumor necrosis factor receptor 2.";
RL Int. Immunol. 16:169-177(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS MET-187; ARG-196; LYS-232;
RP THR-236; PRO-264 AND ARG-295.
RG NIEHS SNPs program;
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-196; LYS-232; PRO-269
RP AND ARG-301.
RG SeattleSNPs variation discovery resource;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=PNS;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP PROTEIN SEQUENCE OF 23-40; 65-69; 136-141; 300-306 AND 346-362.
RX PubMed=2173696; DOI=10.1016/s0021-9258(17)30479-9;
RA Loetscher H., Schlaeger E.J., Lahm H.-W., Pan Y.-C.E., Lesslauer W.,
RA Brockhaus M.;
RT "Purification and partial amino acid sequence analysis of two distinct
RT tumor necrosis factor receptors from HL60 cells.";
RL J. Biol. Chem. 265:20131-20138(1990).
RN [12]
RP PROTEIN SEQUENCE OF 27-37.
RC TISSUE=Urine;
RX PubMed=8015639; DOI=10.1159/000187851;
RA Suzuki J., Tomizawa S., Arai H., Seki Y., Maruyama K., Kuroume T.;
RT "Purification of two types of TNF inhibitors in the urine of the patient
RT with chronic glomerulonephritis.";
RL Nephron 66:386-390(1994).
RN [13]
RP PROTEIN SEQUENCE OF 27-31.
RC TISSUE=Urine;
RX PubMed=2153136; DOI=10.1016/s0021-9258(19)40049-5;
RA Engelmann H., Novick D., Wallach D.;
RT "Two tumor necrosis factor-binding proteins purified from human urine.
RT Evidence for immunological cross-reactivity with cell surface tumor
RT necrosis factor receptors.";
RL J. Biol. Chem. 265:1531-1536(1990).
RN [14]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 37-461 (ISOFORM 1).
RX PubMed=1966549; DOI=10.1016/1043-4666(90)90022-l;
RA Dembic Z., Loetscher H., Gubler U., Pan Y.C., Lahm H.-W., Gentz R.,
RA Brockhaus M., Lesslauer W.;
RT "Two human TNF receptors have similar extracellular, but distinct
RT intracellular, domain sequences.";
RL Cytokine 2:231-237(1990).
RN [15]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 116-461 (ISOFORM 1), PARTIAL PROTEIN
RP SEQUENCE, AND VARIANT ARG-196.
RX PubMed=2166946; DOI=10.1073/pnas.87.16.6151;
RA Heller R.A., Song K., Onasch M.A., Fischer W.H., Chang D., Ringold G.M.;
RT "Complementary DNA cloning of a receptor for tumor necrosis factor and
RT demonstration of a shed form of the receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:6151-6155(1990).
RN [16]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 154-183, AND VARIANTS ARG-196 AND
RP LYS-232.
RX PubMed=11197692; DOI=10.1038/sj.gene.6363700;
RA Tsuchiya N., Komata T., Matsushita M., Ohashi J., Tokunaga K.;
RT "New single nucleotide polymorphisms in the coding region of human TNFR2:
RT association with systemic lupus erythematosus.";
RL Genes Immun. 1:501-503(2000).
RN [17]
RP CHARACTERIZATION.
RX PubMed=1328224; DOI=10.1016/s0021-9258(19)36813-9;
RA Pennica D., Lam V.T., Mize N.K., Weber R.F., Lewis M., Fendly B.M.,
RA Lipari M.T., Goeddel D.V.;
RT "Biochemical properties of the 75-kDa tumor necrosis factor receptor.
RT Characterization of ligand binding, internalization, and receptor
RT phosphorylation.";
RL J. Biol. Chem. 267:21172-21178(1992).
RN [18]
RP INTERACTION WITH TRAF2.
RX PubMed=8069916; DOI=10.1016/0092-8674(94)90532-0;
RA Rothe M., Wong S.C., Henzel W.J., Goeddel D.V.;
RT "A novel family of putative signal transducers associated with the
RT cytoplasmic domain of the 75 kDa tumor necrosis factor receptor.";
RL Cell 78:681-692(1994).
RN [19]
RP FUNCTION, AND INTERACTION WITH BMX.
RX PubMed=12370298; DOI=10.1128/mcb.22.21.7512-7523.2002;
RA Pan S., An P., Zhang R., He X., Yin G., Min W.;
RT "Etk/Bmx as a tumor necrosis factor receptor type 2-specific kinase: role
RT in endothelial cell migration and angiogenesis.";
RL Mol. Cell. Biol. 22:7512-7523(2002).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [21]
RP GLYCOSYLATION AT THR-30; THR-206; SER-221 AND THR-222, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=25456591; DOI=10.1016/j.chroma.2014.10.046;
RA Huang L.J., Lin J.H., Tsai J.H., Chu Y.Y., Chen Y.W., Chen S.L., Chen S.H.;
RT "Identification of protein O-glycosylation site and corresponding glycans
RT using liquid chromatography-tandem mass spectrometry via mapping accurate
RT mass and retention time shift.";
RL J. Chromatogr. A 1371:136-145(2014).
RN [22]
RP INTERACTION WITH XPNPEP3.
RX PubMed=25609706; DOI=10.1242/jcs.149385;
RA Inoue M., Kamada H., Abe Y., Higashisaka K., Nagano K., Mukai Y.,
RA Yoshioka Y., Tsutsumi Y., Tsunoda S.;
RT "Aminopeptidase P3, a new member of the TNF-TNFR2 signaling complex,
RT induces phosphorylation of JNK1 and JNK2.";
RL J. Cell Sci. 128:656-669(2015).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 419-428 IN COMPLEX WITH TRAF2.
RX PubMed=10206649; DOI=10.1038/19110;
RA Park Y.C., Burkitt V., Villa A.R., Tong L., Wu H.;
RT "Structural basis for self-association and receptor recognition of human
RT TRAF2.";
RL Nature 398:533-538(1999).
RN [24]
RP VARIANTS ARG-196 AND LYS-232.
RX PubMed=11762942;
RX DOI=10.1002/1529-0131(200112)44:12<2819::aid-art469>3.0.co;2-2;
RA Morita C., Horiuchi T., Tsukamoto H., Hatta N., Kikuchi Y., Arinobu Y.,
RA Otsuka T., Sawabe T., Harashima S., Nagasawa K., Niho Y.;
RT "Association of tumor necrosis factor receptor type II polymorphism 196R
RT with systemic lupus erythematosus in the Japanese: molecular and functional
RT analysis.";
RL Arthritis Rheum. 44:2819-2827(2001).
RN [25]
RP VARIANT ARG-196.
RX PubMed=12161545; DOI=10.1210/jcem.87.8.8715;
RA Peral B., San Millan J.L., Castello R., Moghetti P., Escobar-Morreale H.F.;
RT "Comment: the methionine 196 arginine polymorphism in exon 6 of the TNF
RT receptor 2 gene (TNFRSF1B) is associated with the polycystic ovary syndrome
RT and hyperandrogenism.";
RL J. Clin. Endocrinol. Metab. 87:3977-3983(2002).
CC -!- FUNCTION: Receptor with high affinity for TNFSF2/TNF-alpha and
CC approximately 5-fold lower affinity for homotrimeric
CC TNFSF1/lymphotoxin-alpha. The TRAF1/TRAF2 complex recruits the
CC apoptotic suppressors BIRC2 and BIRC3 to TNFRSF1B/TNFR2. This receptor
CC mediates most of the metabolic effects of TNF-alpha. Isoform 2 blocks
CC TNF-alpha-induced apoptosis, which suggests that it regulates TNF-alpha
CC function by antagonizing its biological activity.
CC {ECO:0000269|PubMed:12370298}.
CC -!- SUBUNIT: Binds to TRAF2 (PubMed:8069916, PubMed:10206649). Interacts
CC with BMX (PubMed:12370298). Interacts (activated form) with XPNPEP3
CC (PubMed:25609706). {ECO:0000269|PubMed:10206649,
CC ECO:0000269|PubMed:12370298, ECO:0000269|PubMed:25609706,
CC ECO:0000269|PubMed:8069916}.
CC -!- INTERACTION:
CC P20333; P28799: GRN; NbExp=5; IntAct=EBI-358983, EBI-747754;
CC P20333; P01375: TNF; NbExp=2; IntAct=EBI-358983, EBI-359977;
CC P20333; Q12933: TRAF2; NbExp=3; IntAct=EBI-358983, EBI-355744;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I
CC membrane protein.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted.
CC -!- SUBCELLULAR LOCATION: [Tumor necrosis factor-binding protein 2]:
CC Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P20333-1; Sequence=Displayed;
CC Name=2; Synonyms=DS-TNFR2(Delta7,8), sTNFR2;
CC IsoId=P20333-2; Sequence=VSP_011826, VSP_011827;
CC -!- PTM: Phosphorylated; mainly on serine residues and with a very low
CC level on threonine residues.
CC -!- PTM: A soluble form (tumor necrosis factor binding protein 2) is
CC produced from the membrane form by proteolytic processing.
CC -!- PHARMACEUTICAL: Available under the name Enbrel (Immunex and Wyeth-
CC Ayerst). Used to treat moderate to severe rheumatoid arthritis (RA).
CC Enbrel consist of the extracellular ligand-binding portion of TNFRSF1B
CC linked to an immunoglobulin Fc chain. It binds to TNF-alpha and blocks
CC its interactions with receptors.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/tnfrsf1b/";
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/tnfrsf1b/";
CC -!- WEB RESOURCE: Name=Enbrel; Note=Clinical information on Enbrel;
CC URL="https://www.enbrel.com";
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DR EMBL; M55994; AAA36755.1; -; mRNA.
DR EMBL; M32315; AAA59929.1; -; mRNA.
DR EMBL; U52165; AAC50622.1; -; Genomic_DNA.
DR EMBL; U52156; AAC50622.1; JOINED; Genomic_DNA.
DR EMBL; U52157; AAC50622.1; JOINED; Genomic_DNA.
DR EMBL; U52158; AAC50622.1; JOINED; Genomic_DNA.
DR EMBL; U52159; AAC50622.1; JOINED; Genomic_DNA.
DR EMBL; U52160; AAC50622.1; JOINED; Genomic_DNA.
DR EMBL; U52161; AAC50622.1; JOINED; Genomic_DNA.
DR EMBL; U52162; AAC50622.1; JOINED; Genomic_DNA.
DR EMBL; U52163; AAC50622.1; JOINED; Genomic_DNA.
DR EMBL; U52164; AAC50622.1; JOINED; Genomic_DNA.
DR EMBL; AY148473; AAN72434.1; -; mRNA.
DR EMBL; BT019927; AAV38730.1; -; mRNA.
DR EMBL; AY264804; AAO89076.1; -; Genomic_DNA.
DR EMBL; AY342040; AAP88939.1; -; Genomic_DNA.
DR EMBL; AL031276; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL357835; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471130; EAW71733.1; -; Genomic_DNA.
DR EMBL; BC052977; AAH52977.1; -; mRNA.
DR EMBL; S63368; AAB19824.2; -; mRNA.
DR EMBL; M35857; AAA63262.1; -; mRNA.
DR EMBL; AB030950; BAA89053.1; -; Genomic_DNA.
DR CCDS; CCDS145.1; -. [P20333-1]
DR PIR; A35356; A35356.
DR RefSeq; NP_001057.1; NM_001066.2. [P20333-1]
DR PDB; 1CA9; X-ray; 2.30 A; G/H=420-428.
DR PDB; 3ALQ; X-ray; 3.00 A; R/S/T/U/V/W=33-205.
DR PDBsum; 1CA9; -.
DR PDBsum; 3ALQ; -.
DR AlphaFoldDB; P20333; -.
DR SMR; P20333; -.
DR BioGRID; 112987; 159.
DR CORUM; P20333; -.
DR DIP; DIP-78N; -.
DR ELM; P20333; -.
DR IntAct; P20333; 12.
DR MINT; P20333; -.
DR STRING; 9606.ENSP00000365435; -.
DR ChEMBL; CHEMBL1250356; -.
DR DrugBank; DB11626; Tasonermin.
DR GlyConnect; 705; 2 O-Linked glycans (3 sites).
DR GlyGen; P20333; 7 sites, 4 O-linked glycans (4 sites).
DR iPTMnet; P20333; -.
DR PhosphoSitePlus; P20333; -.
DR BioMuta; TNFRSF1B; -.
DR DMDM; 21264534; -.
DR jPOST; P20333; -.
DR MassIVE; P20333; -.
DR PaxDb; P20333; -.
DR PeptideAtlas; P20333; -.
DR PRIDE; P20333; -.
DR ProteomicsDB; 53746; -. [P20333-1]
DR ProteomicsDB; 53747; -. [P20333-2]
DR Antibodypedia; 1344; 1073 antibodies from 47 providers.
DR DNASU; 7133; -.
DR Ensembl; ENST00000376259.7; ENSP00000365435.3; ENSG00000028137.19. [P20333-1]
DR GeneID; 7133; -.
DR KEGG; hsa:7133; -.
DR MANE-Select; ENST00000376259.7; ENSP00000365435.3; NM_001066.3; NP_001057.1.
DR UCSC; uc001att.4; human. [P20333-1]
DR CTD; 7133; -.
DR DisGeNET; 7133; -.
DR GeneCards; TNFRSF1B; -.
DR HGNC; HGNC:11917; TNFRSF1B.
DR HPA; ENSG00000028137; Tissue enhanced (lymphoid).
DR MalaCards; TNFRSF1B; -.
DR MIM; 191191; gene.
DR neXtProt; NX_P20333; -.
DR OpenTargets; ENSG00000028137; -.
DR Orphanet; 2584; Classic mycosis fungoides.
DR Orphanet; 3162; Sezary syndrome.
DR PharmGKB; PA36610; -.
DR VEuPathDB; HostDB:ENSG00000028137; -.
DR eggNOG; ENOG502RZ23; Eukaryota.
DR GeneTree; ENSGT00940000161800; -.
DR HOGENOM; CLU_047256_0_0_1; -.
DR InParanoid; P20333; -.
DR OMA; HKKCGKG; -.
DR OrthoDB; 559890at2759; -.
DR PhylomeDB; P20333; -.
DR TreeFam; TF331157; -.
DR PathwayCommons; P20333; -.
DR Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-HSA-5669034; TNFs bind their physiological receptors.
DR Reactome; R-HSA-6783783; Interleukin-10 signaling.
DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P20333; -.
DR SIGNOR; P20333; -.
DR BioGRID-ORCS; 7133; 13 hits in 1085 CRISPR screens.
DR ChiTaRS; TNFRSF1B; human.
DR EvolutionaryTrace; P20333; -.
DR GeneWiki; TNFRSF1B; -.
DR GenomeRNAi; 7133; -.
DR Pharos; P20333; Tbio.
DR PRO; PR:P20333; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P20333; protein.
DR Bgee; ENSG00000028137; Expressed in granulocyte and 180 other tissues.
DR ExpressionAtlas; P20333; baseline and differential.
DR Genevisible; P20333; HS.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; TAS:ARUK-UCL.
DR GO; GO:0045121; C:membrane raft; IDA:BHF-UCL.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR GO; GO:0002947; C:tumor necrosis factor receptor superfamily complex; TAS:ARUK-UCL.
DR GO; GO:0043196; C:varicosity; IEA:Ensembl.
DR GO; GO:0043120; F:tumor necrosis factor binding; IPI:ARUK-UCL.
DR GO; GO:0005031; F:tumor necrosis factor receptor activity; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0003176; P:aortic valve development; ISS:BHF-UCL.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:Ensembl.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:BHF-UCL.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IBA:GO_Central.
DR GO; GO:0150098; P:glial cell-neuron signaling; ISS:ARUK-UCL.
DR GO; GO:0006955; P:immune response; IEA:Ensembl.
DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IBA:GO_Central.
DR GO; GO:0010614; P:negative regulation of cardiac muscle hypertrophy; IEA:Ensembl.
DR GO; GO:0060548; P:negative regulation of cell death; ISS:ARUK-UCL.
DR GO; GO:0003332; P:negative regulation of extracellular matrix constituent secretion; ISS:BHF-UCL.
DR GO; GO:0150079; P:negative regulation of neuroinflammatory response; ISS:ARUK-UCL.
DR GO; GO:1901215; P:negative regulation of neuron death; ISS:ARUK-UCL.
DR GO; GO:1902339; P:positive regulation of apoptotic process involved in morphogenesis; ISS:BHF-UCL.
DR GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IMP:BHF-UCL.
DR GO; GO:0031643; P:positive regulation of myelination; ISS:ARUK-UCL.
DR GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; ISS:ARUK-UCL.
DR GO; GO:0003177; P:pulmonary valve development; ISS:BHF-UCL.
DR GO; GO:0002718; P:regulation of cytokine production involved in immune response; ISS:ARUK-UCL.
DR GO; GO:0031641; P:regulation of myelination; ISS:ARUK-UCL.
DR GO; GO:0150077; P:regulation of neuroinflammatory response; ISS:ARUK-UCL.
DR GO; GO:2001141; P:regulation of RNA biosynthetic process; ISS:ARUK-UCL.
DR GO; GO:0002724; P:regulation of T cell cytokine production; ISS:ARUK-UCL.
DR GO; GO:0042129; P:regulation of T cell proliferation; ISS:ARUK-UCL.
DR GO; GO:0050779; P:RNA destabilization; IEA:Ensembl.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:ARUK-UCL.
DR CDD; cd10577; TNFRSF1B; 1.
DR InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR InterPro; IPR020411; TNFR_1B.
DR InterPro; IPR033996; TNFRSF1B_N.
DR Pfam; PF00020; TNFR_c6; 3.
DR PRINTS; PR01919; TNFACTORR1B.
DR SMART; SM00208; TNFR; 4.
DR PROSITE; PS00652; TNFR_NGFR_1; 2.
DR PROSITE; PS50050; TNFR_NGFR_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Membrane;
KW Pharmaceutical; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:2173696"
FT CHAIN 23..461
FT /note="Tumor necrosis factor receptor superfamily member
FT 1b, membrane form"
FT /id="PRO_0000034548"
FT CHAIN 27..?
FT /note="Tumor necrosis factor-binding protein 2"
FT /id="PRO_0000034549"
FT TOPO_DOM 23..257
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..461
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 39..76
FT /note="TNFR-Cys 1"
FT REPEAT 77..118
FT /note="TNFR-Cys 2"
FT REPEAT 119..162
FT /note="TNFR-Cys 3"
FT REPEAT 163..201
FT /note="TNFR-Cys 4"
FT REGION 208..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CARBOHYD 30
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:25456591"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:25456591"
FT CARBOHYD 221
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:25456591"
FT CARBOHYD 222
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:25456591"
FT DISULFID 40..53
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 54..67
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 57..75
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 78..93
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 96..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 100..118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 120..126
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 134..143
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 137..161
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 164..179
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT VAR_SEQ 263..268
FT /note="GLIVGV -> ASLACR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14688072"
FT /id="VSP_011826"
FT VAR_SEQ 269..461
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14688072"
FT /id="VSP_011827"
FT VARIANT 187
FT /note="V -> M (in dbSNP:rs2228494)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_017176"
FT VARIANT 196
FT /note="M -> R (seems to be associated with
FT hyperandrogenism, polycystic ovary syndrome (PCOS) and
FT systemic lupus erythematosus; dbSNP:rs1061622)"
FT /evidence="ECO:0000269|PubMed:11197692,
FT ECO:0000269|PubMed:11762942, ECO:0000269|PubMed:12161545,
FT ECO:0000269|PubMed:2166946, ECO:0000269|PubMed:2172983,
FT ECO:0000269|Ref.6, ECO:0000269|Ref.7"
FT /id="VAR_015434"
FT VARIANT 232
FT /note="E -> K (in dbSNP:rs5746026)"
FT /evidence="ECO:0000269|PubMed:11197692,
FT ECO:0000269|PubMed:11762942, ECO:0000269|Ref.6,
FT ECO:0000269|Ref.7"
FT /id="VAR_015435"
FT VARIANT 236
FT /note="A -> T (in dbSNP:rs5746027)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_017177"
FT VARIANT 264
FT /note="L -> P (in dbSNP:rs2229700)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_017178"
FT VARIANT 269
FT /note="T -> P (in dbSNP:rs17879042)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_017179"
FT VARIANT 295
FT /note="Q -> R (in dbSNP:rs5746032)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_017180"
FT VARIANT 301
FT /note="P -> R (in dbSNP:rs17883432)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_017181"
FT CONFLICT 35..37
FT /note="EPG -> APT (in Ref. 12; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="S -> P (in Ref. 4; AAN72434)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="S -> P (in Ref. 4; AAN72434)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="R -> P (in Ref. 15; AAA63262)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="A -> T (in Ref. 15; AAA63262)"
FT /evidence="ECO:0000305"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:3ALQ"
FT TURN 48..51
FT /evidence="ECO:0007829|PDB:3ALQ"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:3ALQ"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:3ALQ"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:3ALQ"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:3ALQ"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:3ALQ"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:3ALQ"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:3ALQ"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:3ALQ"
FT STRAND 131..139
FT /evidence="ECO:0007829|PDB:3ALQ"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:3ALQ"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:3ALQ"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:3ALQ"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:3ALQ"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:3ALQ"
SQ 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
