TNR9_HUMAN
ID TNR9_HUMAN Reviewed; 255 AA.
AC Q07011;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Tumor necrosis factor receptor superfamily member 9;
DE AltName: Full=4-1BB ligand receptor;
DE AltName: Full=CDw137;
DE AltName: Full=T-cell antigen 4-1BB homolog;
DE AltName: Full=T-cell antigen ILA;
DE AltName: CD_antigen=CD137;
DE Flags: Precursor;
GN Name=TNFRSF9; Synonyms=CD137, ILA;
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].
RC TISSUE=Blood;
RX PubMed=8088337; DOI=10.1002/eji.1830240943;
RA Alderson M.R., Smith C.A., Tough T.W., Davis-Smith T., Armitage R.J.,
RA Falk B., Roux E., Baker E., Sutherland G.R., Din W.S., Goodwin R.G.;
RT "Molecular and biological characterization of human 4-1BB and its ligand.";
RL Eur. J. Immunol. 24:2219-2227(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Blood;
RX PubMed=8262389; DOI=10.1016/0378-1119(93)90110-o;
RA Schwarz H., Tuckwell J., Lotz M.;
RT "A receptor induced by lymphocyte activation (ILA): a new member of the
RT human nerve-growth-factor/tumor-necrosis-factor receptor family.";
RL Gene 134:295-298(1993).
RN [3]
RP SEQUENCE REVISION TO 107.
RA Schwarz H.;
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Blood;
RX PubMed=7622190; DOI=10.1016/0165-2478(94)00227-i;
RA Zhou Z., Kim S., Hurtado J., Lee Z.H., Kim K.K., Pollok K.E., Kwon B.S.;
RT "Characterization of human homologue of 4-1BB and its ligand.";
RL Immunol. Lett. 45:67-73(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-56; ASN-115 AND
RP ASP-176.
RG NIEHS SNPs program;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [8]
RP PROTEIN SEQUENCE OF 24-38.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [9]
RP INTERACTION WITH TRAF1; TRAF2 AND TRAF3.
RX PubMed=9418902; DOI=10.1128/mcb.18.1.558;
RA Arch R.H., Thompson C.B.;
RT "4-1BB and Ox40 are members of a tumor necrosis factor (TNF)-nerve growth
RT factor receptor subfamily that bind TNF receptor-associated factors and
RT activate nuclear factor kappaB.";
RL Mol. Cell. Biol. 18:558-565(1998).
RN [10]
RP INTERACTION WITH TRAF1 AND TRAF2.
RX PubMed=9607925; DOI=10.1084/jem.187.11.1849;
RA Saoulli K., Lee S.Y., Cannons J.L., Yeh W.C., Santana A., Goldstein M.D.,
RA Bangia N., DeBenedette M.A., Mak T.W., Choi Y., Watts T.H.;
RT "CD28-independent, TRAF2-dependent costimulation of resting T cells by 4-
RT 1BB ligand.";
RL J. Exp. Med. 187:1849-1862(1998).
RN [11]
RP INTERACTION WITH LRR-REPEAT PROTEIN 1/LRR-1.
RX PubMed=11804328;
RA Jang I.-K., Lee Z.-H., Kim H.-H., Hill J.M., Kim J.-D., Kwon B.S.;
RT "A novel leucine-rich repeat protein (LRR-1): potential involvement in 4-
RT 1BB-mediated signal transduction.";
RL Mol. Cells 12:304-312(2001).
RN [12]
RP VARIANT [LARGE SCALE ANALYSIS] GLY-250.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Receptor for TNFSF9/4-1BBL. Possibly active during T cell
CC activation.
CC -!- SUBUNIT: Interacts with TRAF1, TRAF2 and TRAF3. Interacts with LRR-
CC repeat protein 1/LRR-1. {ECO:0000269|PubMed:11804328,
CC ECO:0000269|PubMed:9418902, ECO:0000269|PubMed:9607925}.
CC -!- INTERACTION:
CC Q07011; Q9Y6X1: SERP1; NbExp=3; IntAct=EBI-12945620, EBI-10329948;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed on the surface of activated T-cells.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/tnfrsf9/";
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DR EMBL; U03397; AAA53133.1; -; mRNA.
DR EMBL; L12964; AAA62478.2; -; mRNA.
DR EMBL; AY438976; AAR05440.1; -; Genomic_DNA.
DR EMBL; AL009183; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006196; AAH06196.1; -; mRNA.
DR CCDS; CCDS92.1; -.
DR PIR; I38426; I38426.
DR RefSeq; NP_001552.2; NM_001561.5.
DR RefSeq; XP_011539688.1; XM_011541386.2.
DR PDB; 6A3V; X-ray; 3.39 A; B/D/F/H/J/L/N/P/R/T/V/X=24-180.
DR PDB; 6A3W; X-ray; 2.00 A; C/F/I/L=24-180.
DR PDB; 6BWV; X-ray; 2.40 A; D/E=24-160.
DR PDB; 6CPR; X-ray; 2.70 A; D/E/F=23-160.
DR PDB; 6CU0; X-ray; 3.20 A; G/H/I/J/K/L=23-160.
DR PDB; 6MGP; X-ray; 2.13 A; X/Y/Z=25-162.
DR PDB; 6MHR; X-ray; 2.80 A; C/F=25-162.
DR PDB; 6MI2; X-ray; 2.72 A; C/F=25-162.
DR PDB; 6Y8K; X-ray; 2.01 A; AAA=24-160.
DR PDB; 7D4B; X-ray; 3.14 A; A=25-162.
DR PDBsum; 6A3V; -.
DR PDBsum; 6A3W; -.
DR PDBsum; 6BWV; -.
DR PDBsum; 6CPR; -.
DR PDBsum; 6CU0; -.
DR PDBsum; 6MGP; -.
DR PDBsum; 6MHR; -.
DR PDBsum; 6MI2; -.
DR PDBsum; 6Y8K; -.
DR PDBsum; 7D4B; -.
DR AlphaFoldDB; Q07011; -.
DR SMR; Q07011; -.
DR BioGRID; 109817; 36.
DR DIP; DIP-3021N; -.
DR ELM; Q07011; -.
DR IntAct; Q07011; 5.
DR STRING; 9606.ENSP00000478699; -.
DR ChEMBL; CHEMBL3712857; -.
DR DrugBank; DB12077; Urelumab.
DR GuidetoPHARMACOLOGY; 1878; -.
DR TCDB; 9.B.87.4.2; the selenoprotein p receptor (selp-receptor) family.
DR GlyGen; Q07011; 2 sites.
DR iPTMnet; Q07011; -.
DR PhosphoSitePlus; Q07011; -.
DR BioMuta; TNFRSF9; -.
DR DMDM; 728738; -.
DR MassIVE; Q07011; -.
DR PaxDb; Q07011; -.
DR PeptideAtlas; Q07011; -.
DR PRIDE; Q07011; -.
DR ProteomicsDB; 58498; -.
DR ABCD; Q07011; 3 sequenced antibodies.
DR Antibodypedia; 3718; 1365 antibodies from 47 providers.
DR CPTC; Q07011; 6 antibodies.
DR DNASU; 3604; -.
DR Ensembl; ENST00000377507.8; ENSP00000366729.3; ENSG00000049249.9.
DR Ensembl; ENST00000615230.4; ENSP00000478699.1; ENSG00000049249.9.
DR GeneID; 3604; -.
DR KEGG; hsa:3604; -.
DR MANE-Select; ENST00000377507.8; ENSP00000366729.3; NM_001561.6; NP_001552.2.
DR UCSC; uc001aot.4; human.
DR CTD; 3604; -.
DR DisGeNET; 3604; -.
DR GeneCards; TNFRSF9; -.
DR HGNC; HGNC:11924; TNFRSF9.
DR HPA; ENSG00000049249; Tissue enriched (lymphoid).
DR MIM; 602250; gene.
DR neXtProt; NX_Q07011; -.
DR OpenTargets; ENSG00000049249; -.
DR PharmGKB; PA36617; -.
DR VEuPathDB; HostDB:ENSG00000049249; -.
DR eggNOG; ENOG502S017; Eukaryota.
DR GeneTree; ENSGT00730000111279; -.
DR HOGENOM; CLU_076906_0_0_1; -.
DR InParanoid; Q07011; -.
DR OMA; CISGFHC; -.
DR OrthoDB; 1102119at2759; -.
DR PhylomeDB; Q07011; -.
DR TreeFam; TF336151; -.
DR PathwayCommons; Q07011; -.
DR Reactome; R-HSA-5669034; TNFs bind their physiological receptors.
DR SignaLink; Q07011; -.
DR BioGRID-ORCS; 3604; 11 hits in 1071 CRISPR screens.
DR GeneWiki; CD137; -.
DR GenomeRNAi; 3604; -.
DR Pharos; Q07011; Tbio.
DR PRO; PR:Q07011; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q07011; protein.
DR Bgee; ENSG00000049249; Expressed in buccal mucosa cell and 109 other tissues.
DR ExpressionAtlas; Q07011; baseline and differential.
DR Genevisible; Q07011; HS.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0019955; F:cytokine binding; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0033084; P:regulation of immature T cell proliferation in thymus; IEA:Ensembl.
DR CDD; cd13410; TNFRSF9; 1.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR InterPro; IPR020413; TNFR_9.
DR InterPro; IPR034020; TNFRSF9_N.
DR PANTHER; PTHR47139:SF1; PTHR47139:SF1; 1.
DR Pfam; PF00020; TNFR_c6; 1.
DR PRINTS; PR01924; TNFACTORR9.
DR SMART; SM00208; TNFR; 2.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS00652; TNFR_NGFR_1; 1.
DR PROSITE; PS50050; TNFR_NGFR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 24..255
FT /note="Tumor necrosis factor receptor superfamily member 9"
FT /id="PRO_0000034577"
FT TOPO_DOM 24..186
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..255
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 24..45
FT /note="TNFR-Cys 1"
FT REPEAT 47..86
FT /note="TNFR-Cys 2"
FT REPEAT 87..118
FT /note="TNFR-Cys 3"
FT REPEAT 119..159
FT /note="TNFR-Cys 4"
FT REGION 161..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..255
FT /note="Interaction with LRR-1"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..37
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 31..45
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 48..62
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 65..78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 68..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 88..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 99..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 102..117
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 121..133
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 139..158
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT VARIANT 56
FT /note="A -> T (in dbSNP:rs9657963)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_018920"
FT VARIANT 115
FT /note="K -> N (in dbSNP:rs9657965)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_018921"
FT VARIANT 176
FT /note="A -> D (in dbSNP:rs9657979)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_018922"
FT VARIANT 250
FT /note="E -> G (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs776878260)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035478"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:6A3W"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:6A3W"
FT TURN 39..42
FT /evidence="ECO:0007829|PDB:6A3W"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:6A3W"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:6BWV"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:6MGP"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:6A3W"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:6MGP"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:6A3W"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:6A3W"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:6MGP"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:6A3W"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:6A3W"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:6A3W"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:6A3W"
FT HELIX 139..142
FT /evidence="ECO:0007829|PDB:6A3W"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:6A3W"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:6A3W"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:6A3W"
SQ SEQUENCE 255 AA; 27899 MW; F3A563FE5EF00460 CRC64;
MGNSCYNIVA TLLLVLNFER TRSLQDPCSN CPAGTFCDNN RNQICSPCPP NSFSSAGGQR
TCDICRQCKG VFRTRKECSS TSNAECDCTP GFHCLGAGCS MCEQDCKQGQ ELTKKGCKDC
CFGTFNDQKR GICRPWTNCS LDGKSVLVNG TKERDVVCGP SPADLSPGAS SVTPPAPARE
PGHSPQIISF FLALTSTALL FLLFFLTLRF SVVKRGRKKL LYIFKQPFMR PVQTTQEEDG
CSCRFPEEEE GGCEL
