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Q07011

- TNR9_HUMAN

UniProt

Q07011 - TNR9_HUMAN

Protein

Tumor necrosis factor receptor superfamily member 9

Gene

TNFRSF9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    Receptor for TNFSF9/4-1BBL. Possibly active during T cell activation.

    GO - Molecular functioni

    1. receptor activity Source: ProtInc

    GO - Biological processi

    1. apoptotic process Source: ProtInc
    2. negative regulation of cell proliferation Source: ProtInc
    3. negative regulation of interleukin-10 secretion Source: Ensembl
    4. negative regulation of interleukin-12 secretion Source: Ensembl
    5. protein homotrimerization Source: Ensembl

    Keywords - Molecular functioni

    Receptor

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tumor necrosis factor receptor superfamily member 9
    Alternative name(s):
    4-1BB ligand receptor
    CDw137
    T-cell antigen 4-1BB homolog
    T-cell antigen ILA
    CD_antigen: CD137
    Gene namesi
    Name:TNFRSF9
    Synonyms:CD137, ILA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:11924. TNFRSF9.

    Subcellular locationi

    GO - Cellular componenti

    1. external side of plasma membrane Source: Ensembl
    2. extracellular space Source: Ensembl
    3. integral component of plasma membrane Source: ProtInc

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36617.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 23231 PublicationAdd
    BLAST
    Chaini24 – 255232Tumor necrosis factor receptor superfamily member 9PRO_0000034577Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi28 ↔ 37PROSITE-ProRule annotation
    Disulfide bondi31 ↔ 45PROSITE-ProRule annotation
    Disulfide bondi48 ↔ 62PROSITE-ProRule annotation
    Disulfide bondi65 ↔ 78PROSITE-ProRule annotation
    Disulfide bondi68 ↔ 86PROSITE-ProRule annotation
    Disulfide bondi88 ↔ 94PROSITE-ProRule annotation
    Disulfide bondi99 ↔ 106PROSITE-ProRule annotation
    Disulfide bondi102 ↔ 117PROSITE-ProRule annotation
    Disulfide bondi121 ↔ 133PROSITE-ProRule annotation
    Glycosylationi138 – 1381N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi139 ↔ 158PROSITE-ProRule annotation
    Glycosylationi149 – 1491N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ07011.
    PRIDEiQ07011.

    PTM databases

    PhosphoSiteiQ07011.

    Expressioni

    Tissue specificityi

    Expressed on the surface of activated T-cells.

    Gene expression databases

    ArrayExpressiQ07011.
    BgeeiQ07011.
    CleanExiHS_TNFRSF9.
    GenevestigatoriQ07011.

    Organism-specific databases

    HPAiCAB002423.

    Interactioni

    Subunit structurei

    Interacts with TRAF1, TRAF2 and TRAF3. Interacts with LRR-repeat protein 1/LRR-1.3 Publications

    Protein-protein interaction databases

    BioGridi109817. 9 interactions.
    DIPiDIP-3021N.
    STRINGi9606.ENSP00000366729.

    Structurei

    3D structure databases

    ProteinModelPortaliQ07011.
    SMRiQ07011. Positions 28-159.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini24 – 186163ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini214 – 25542CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei187 – 21327HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati24 – 4522TNFR-Cys 1Add
    BLAST
    Repeati47 – 8640TNFR-Cys 2Add
    BLAST
    Repeati87 – 11832TNFR-Cys 3Add
    BLAST
    Repeati119 – 15941TNFR-Cys 4Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni214 – 25542Interaction with LRR-1Add
    BLAST

    Sequence similaritiesi

    Contains 4 TNFR-Cys repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG44848.
    HOGENOMiHOG000033708.
    HOVERGENiHBG000021.
    InParanoidiQ07011.
    KOiK05146.
    OMAiTNCSLDG.
    OrthoDBiEOG786H2Q.
    PhylomeDBiQ07011.
    TreeFamiTF336151.

    Family and domain databases

    InterProiIPR009030. Growth_fac_rcpt_N_dom.
    IPR001368. TNFR/NGFR_Cys_rich_reg.
    IPR020413. TNFR_9.
    [Graphical view]
    PfamiPF00020. TNFR_c6. 1 hit.
    [Graphical view]
    PRINTSiPR01924. TNFACTORR9.
    SMARTiSM00208. TNFR. 2 hits.
    [Graphical view]
    SUPFAMiSSF57184. SSF57184. 1 hit.
    PROSITEiPS00652. TNFR_NGFR_1. 1 hit.
    PS50050. TNFR_NGFR_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q07011-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGNSCYNIVA TLLLVLNFER TRSLQDPCSN CPAGTFCDNN RNQICSPCPP    50
    NSFSSAGGQR TCDICRQCKG VFRTRKECSS TSNAECDCTP GFHCLGAGCS 100
    MCEQDCKQGQ ELTKKGCKDC CFGTFNDQKR GICRPWTNCS LDGKSVLVNG 150
    TKERDVVCGP SPADLSPGAS SVTPPAPARE PGHSPQIISF FLALTSTALL 200
    FLLFFLTLRF SVVKRGRKKL LYIFKQPFMR PVQTTQEEDG CSCRFPEEEE 250
    GGCEL 255
    Length:255
    Mass (Da):27,899
    Last modified:February 1, 1995 - v1
    Checksum:iF3A563FE5EF00460
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti56 – 561A → T.1 Publication
    Corresponds to variant rs9657963 [ dbSNP | Ensembl ].
    VAR_018920
    Natural varianti115 – 1151K → N.1 Publication
    Corresponds to variant rs9657965 [ dbSNP | Ensembl ].
    VAR_018921
    Natural varianti176 – 1761A → D.1 Publication
    Corresponds to variant rs9657979 [ dbSNP | Ensembl ].
    VAR_018922
    Natural varianti250 – 2501E → G in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035478

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U03397 mRNA. Translation: AAA53133.1.
    L12964 mRNA. Translation: AAA62478.2.
    AY438976 Genomic DNA. Translation: AAR05440.1.
    AL009183 Genomic DNA. Translation: CAB57398.1.
    BC006196 mRNA. Translation: AAH06196.1.
    CCDSiCCDS92.1.
    PIRiI38426.
    RefSeqiNP_001552.2. NM_001561.5.
    UniGeneiHs.738942.
    Hs.86447.

    Genome annotation databases

    EnsembliENST00000377507; ENSP00000366729; ENSG00000049249.
    GeneIDi3604.
    KEGGihsa:3604.
    UCSCiuc001aot.3. human.

    Polymorphism databases

    DMDMi728738.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U03397 mRNA. Translation: AAA53133.1 .
    L12964 mRNA. Translation: AAA62478.2 .
    AY438976 Genomic DNA. Translation: AAR05440.1 .
    AL009183 Genomic DNA. Translation: CAB57398.1 .
    BC006196 mRNA. Translation: AAH06196.1 .
    CCDSi CCDS92.1.
    PIRi I38426.
    RefSeqi NP_001552.2. NM_001561.5.
    UniGenei Hs.738942.
    Hs.86447.

    3D structure databases

    ProteinModelPortali Q07011.
    SMRi Q07011. Positions 28-159.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109817. 9 interactions.
    DIPi DIP-3021N.
    STRINGi 9606.ENSP00000366729.

    Chemistry

    GuidetoPHARMACOLOGYi 1878.

    PTM databases

    PhosphoSitei Q07011.

    Polymorphism databases

    DMDMi 728738.

    Proteomic databases

    PaxDbi Q07011.
    PRIDEi Q07011.

    Protocols and materials databases

    DNASUi 3604.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000377507 ; ENSP00000366729 ; ENSG00000049249 .
    GeneIDi 3604.
    KEGGi hsa:3604.
    UCSCi uc001aot.3. human.

    Organism-specific databases

    CTDi 3604.
    GeneCardsi GC01M007980.
    HGNCi HGNC:11924. TNFRSF9.
    HPAi CAB002423.
    MIMi 602250. gene.
    neXtProti NX_Q07011.
    PharmGKBi PA36617.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG44848.
    HOGENOMi HOG000033708.
    HOVERGENi HBG000021.
    InParanoidi Q07011.
    KOi K05146.
    OMAi TNCSLDG.
    OrthoDBi EOG786H2Q.
    PhylomeDBi Q07011.
    TreeFami TF336151.

    Miscellaneous databases

    GeneWikii CD137.
    GenomeRNAii 3604.
    NextBioi 14085.
    PROi Q07011.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q07011.
    Bgeei Q07011.
    CleanExi HS_TNFRSF9.
    Genevestigatori Q07011.

    Family and domain databases

    InterProi IPR009030. Growth_fac_rcpt_N_dom.
    IPR001368. TNFR/NGFR_Cys_rich_reg.
    IPR020413. TNFR_9.
    [Graphical view ]
    Pfami PF00020. TNFR_c6. 1 hit.
    [Graphical view ]
    PRINTSi PR01924. TNFACTORR9.
    SMARTi SM00208. TNFR. 2 hits.
    [Graphical view ]
    SUPFAMi SSF57184. SSF57184. 1 hit.
    PROSITEi PS00652. TNFR_NGFR_1. 1 hit.
    PS50050. TNFR_NGFR_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Blood.
    2. "A receptor induced by lymphocyte activation (ILA): a new member of the human nerve-growth-factor/tumor-necrosis-factor receptor family."
      Schwarz H., Tuckwell J., Lotz M.
      Gene 134:295-298(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Blood.
    3. Schwarz H.
      Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 107.
    4. "Characterization of human homologue of 4-1BB and its ligand."
      Zhou Z., Kim S., Hurtado J., Lee Z.H., Kim K.K., Pollok K.E., Kwon B.S.
      Immunol. Lett. 45:67-73(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Blood.
    5. NIEHS SNPs program
      Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-56; ASN-115 AND ASP-176.
    6. "The DNA sequence and biological annotation of human chromosome 1."
      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.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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.
    8. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
      Zhang Z., Henzel W.J.
      Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 24-38.
    9. "4-1BB and Ox40 are members of a tumor necrosis factor (TNF)-nerve growth factor receptor subfamily that bind TNF receptor-associated factors and activate nuclear factor kappaB."
      Arch R.H., Thompson C.B.
      Mol. Cell. Biol. 18:558-565(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRAF1; TRAF2 AND TRAF3.
    10. "CD28-independent, TRAF2-dependent costimulation of resting T cells by 4-1BB ligand."
      Saoulli K., Lee S.Y., Cannons J.L., Yeh W.C., Santana A., Goldstein M.D., Bangia N., DeBenedette M.A., Mak T.W., Choi Y., Watts T.H.
      J. Exp. Med. 187:1849-1862(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRAF1 AND TRAF2.
    11. "A novel leucine-rich repeat protein (LRR-1): potential involvement in 4-1BB-mediated signal transduction."
      Jang I.-K., Lee Z.-H., Kim H.-H., Hill J.M., Kim J.-D., Kwon B.S.
      Mol. Cells 12:304-312(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LRR-REPEAT PROTEIN 1/LRR-1.
    12. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLY-250.

    Entry informationi

    Entry nameiTNR9_HUMAN
    AccessioniPrimary (citable) accession number: Q07011
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 132 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3