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Q92956

- TNR14_HUMAN

UniProt

Q92956 - TNR14_HUMAN

Protein

Tumor necrosis factor receptor superfamily member 14

Gene

TNFRSF14

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 3 (27 Apr 2001)
      Previous versions | rss
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    Functioni

    Receptor for BTLA. Receptor for TNFSF14/LIGHT and homotrimeric TNFSF1/lymphotoxin-alpha. Involved in lymphocyte activation. Plays an important role in HSV pathogenesis because it enhanced the entry of several wild-type HSV strains of both serotypes into CHO cells, and mediated HSV entry into activated human T-cells.1 Publication

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. tumor necrosis factor-activated receptor activity Source: ProtInc
    3. ubiquitin protein ligase binding Source: UniProtKB
    4. virus receptor activity Source: UniProtKB-KW

    GO - Biological processi

    1. cell surface receptor signaling pathway Source: ProtInc
    2. defense response to Gram-negative bacterium Source: Ensembl
    3. defense response to Gram-positive bacterium Source: Ensembl
    4. immune response Source: ProtInc
    5. negative regulation of alpha-beta T cell proliferation Source: Ensembl
    6. positive regulation of cytokine secretion involved in immune response Source: Ensembl
    7. positive regulation of peptidyl-tyrosine phosphorylation Source: Ensembl
    8. positive regulation of T cell migration Source: Ensembl
    9. T cell costimulation Source: Reactome
    10. tumor necrosis factor-mediated signaling pathway Source: GOC
    11. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Host cell receptor for virus entry, Receptor

    Keywords - Biological processi

    Host-virus interaction

    Enzyme and pathway databases

    ReactomeiREACT_19344. Costimulation by the CD28 family.
    SignaLinkiQ92956.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tumor necrosis factor receptor superfamily member 14
    Alternative name(s):
    Herpes virus entry mediator A
    Short name:
    Herpesvirus entry mediator A
    Short name:
    HveA
    Tumor necrosis factor receptor-like 2
    Short name:
    TR2
    CD_antigen: CD270
    Gene namesi
    Name:TNFRSF14
    Synonyms:HVEA, HVEM
    ORF Names:UNQ329/PRO509
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:11912. TNFRSF14.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36605.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 38381 PublicationAdd
    BLAST
    Chaini39 – 283245Tumor necrosis factor receptor superfamily member 14PRO_0000034590Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi42 ↔ 53
    Disulfide bondi54 ↔ 67
    Disulfide bondi57 ↔ 75
    Disulfide bondi78 ↔ 93
    Disulfide bondi96 ↔ 111
    Disulfide bondi99 ↔ 119
    Glycosylationi110 – 1101N-linked (GlcNAc...)1 Publication
    Disulfide bondi121 ↔ 138
    Disulfide bondi127 ↔ 135
    Glycosylationi173 – 1731N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ92956.
    PRIDEiQ92956.

    Expressioni

    Tissue specificityi

    Widely expressed, with the highest expression in lung, spleen and thymus.

    Gene expression databases

    ArrayExpressiQ92956.
    BgeeiQ92956.
    CleanExiHS_TNFRSF14.
    GenevestigatoriQ92956.

    Organism-specific databases

    HPAiCAB026150.
    CAB030007.
    HPA006404.

    Interactioni

    Subunit structurei

    Interacts with TRAF2, TRAF3 and TRAF5. Interacts with herpes simplex virus 1 (HHV-1) and herpes simplex virus 1 (HHV-2) envelope glycoprotein D; functions as an entry receptor for these viruses.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TNFSF14O435572EBI-1056653,EBI-524131
    TRAF2Q12933-24EBI-1056653,EBI-355760
    TRAF5O004635EBI-1056653,EBI-523498

    Protein-protein interaction databases

    BioGridi114298. 30 interactions.
    DIPiDIP-34779N.
    DIP-6233N.
    IntActiQ92956. 29 interactions.
    MINTiMINT-208002.
    STRINGi9606.ENSP00000347948.

    Structurei

    Secondary structure

    1
    283
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi46 – 494
    Beta strandi52 – 554
    Beta strandi61 – 655
    Beta strandi69 – 713
    Beta strandi74 – 774
    Beta strandi86 – 883
    Helixi101 – 1033
    Beta strandi105 – 1095
    Beta strandi113 – 1153
    Beta strandi118 – 1214
    Beta strandi125 – 1317
    Beta strandi134 – 1407

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JMAX-ray2.65B39-199[»]
    2AW2X-ray2.80B/Y39-142[»]
    4FHQX-ray2.25A39-162[»]
    ProteinModelPortaliQ92956.
    SMRiQ92956. Positions 39-200.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ92956.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini39 – 202164ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini224 – 28360CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei203 – 22321HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati42 – 7534TNFR-Cys 1Add
    BLAST
    Repeati78 – 11942TNFR-Cys 2Add
    BLAST
    Repeati121 – 16242TNFR-Cys 3Add
    BLAST

    Sequence similaritiesi

    Contains 3 TNFR-Cys repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG40150.
    HOGENOMiHOG000065766.
    HOVERGENiHBG072084.
    InParanoidiQ92956.
    KOiK05152.
    OMAiSPGHFCI.
    PhylomeDBiQ92956.
    TreeFamiTF331157.

    Family and domain databases

    InterProiIPR001368. TNFR/NGFR_Cys_rich_reg.
    IPR022332. TNFR_14.
    [Graphical view]
    PfamiPF00020. TNFR_c6. 1 hit.
    [Graphical view]
    PRINTSiPR01965. TNFACTORR14.
    SMARTiSM00208. TNFR. 3 hits.
    [Graphical view]
    PROSITEiPS00652. TNFR_NGFR_1. 1 hit.
    PS50050. TNFR_NGFR_2. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q92956-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MEPPGDWGPP PWRSTPKTDV LRLVLYLTFL GAPCYAPALP SCKEDEYPVG    50
    SECCPKCSPG YRVKEACGEL TGTVCEPCPP GTYIAHLNGL SKCLQCQMCD 100
    PAMGLRASRN CSRTENAVCG CSPGHFCIVQ DGDHCAACRA YATSSPGQRV 150
    QKGGTESQDT LCQNCPPGTF SPNGTLEECQ HQTKCSWLVT KAGAGTSSSH 200
    WVWWFLSGSL VIVIVCSTVG LIICVKRRKP RGDVVKVIVS VQRKRQEAEG 250
    EATVIEALQA PPDVTTVAVE ETIPSFTGRS PNH 283
    Length:283
    Mass (Da):30,392
    Last modified:April 27, 2001 - v3
    Checksum:i46CE13C2C70242C1
    GO
    Isoform 2 (identifier: Q92956-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-100: MEPPGDWGPP...SKCLQCQMCD → MVSRPPRTPLSPSSWT

    Show »
    Length:199
    Mass (Da):21,351
    Checksum:iB14A3275B16BBD66
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti135 – 1351C → R in AAH29848. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti17 – 171K → R.3 Publications
    Corresponds to variant rs4870 [ dbSNP | Ensembl ].
    VAR_013007
    Natural varianti117 – 1171A → T.1 Publication
    Corresponds to variant rs2234163 [ dbSNP | Ensembl ].
    VAR_018955
    Natural varianti174 – 1741G → E.1 Publication
    Corresponds to variant rs11573986 [ dbSNP | Ensembl ].
    VAR_018956
    Natural varianti241 – 2411V → I.2 Publications
    Corresponds to variant rs2234167 [ dbSNP | Ensembl ].
    VAR_013440

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 100100MEPPG…CQMCD → MVSRPPRTPLSPSSWT in isoform 2. 2 PublicationsVSP_054186Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U70321 mRNA. Translation: AAB58354.1.
    U81232 mRNA. Translation: AAD00505.1.
    AF153978 mRNA. Translation: AAF75588.1.
    AF373877 mRNA. Translation: AAL47717.1.
    AF373878 mRNA. Translation: AAL47718.1.
    AY358879 mRNA. Translation: AAQ89238.1.
    AK124010 mRNA. Translation: BAG53992.1.
    CR456909 mRNA. Translation: CAG33190.1.
    AY466111 Genomic DNA. Translation: AAR23264.1.
    AL139246 Genomic DNA. Translation: CAX30824.1.
    CH471183 Genomic DNA. Translation: EAW56089.1.
    CH471183 Genomic DNA. Translation: EAW56090.1.
    BC002794 mRNA. Translation: AAH02794.1.
    BC029848 mRNA. Translation: AAH29848.1.
    CCDSiCCDS44046.1. [Q92956-1]
    RefSeqiNP_003811.2. NM_003820.2. [Q92956-1]
    UniGeneiHs.512898.

    Genome annotation databases

    EnsembliENST00000355716; ENSP00000347948; ENSG00000157873. [Q92956-1]
    GeneIDi8764.
    KEGGihsa:8764.
    UCSCiuc001ajr.3. human. [Q92956-1]

    Polymorphism databases

    DMDMi13878821.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U70321 mRNA. Translation: AAB58354.1 .
    U81232 mRNA. Translation: AAD00505.1 .
    AF153978 mRNA. Translation: AAF75588.1 .
    AF373877 mRNA. Translation: AAL47717.1 .
    AF373878 mRNA. Translation: AAL47718.1 .
    AY358879 mRNA. Translation: AAQ89238.1 .
    AK124010 mRNA. Translation: BAG53992.1 .
    CR456909 mRNA. Translation: CAG33190.1 .
    AY466111 Genomic DNA. Translation: AAR23264.1 .
    AL139246 Genomic DNA. Translation: CAX30824.1 .
    CH471183 Genomic DNA. Translation: EAW56089.1 .
    CH471183 Genomic DNA. Translation: EAW56090.1 .
    BC002794 mRNA. Translation: AAH02794.1 .
    BC029848 mRNA. Translation: AAH29848.1 .
    CCDSi CCDS44046.1. [Q92956-1 ]
    RefSeqi NP_003811.2. NM_003820.2. [Q92956-1 ]
    UniGenei Hs.512898.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JMA X-ray 2.65 B 39-199 [» ]
    2AW2 X-ray 2.80 B/Y 39-142 [» ]
    4FHQ X-ray 2.25 A 39-162 [» ]
    ProteinModelPortali Q92956.
    SMRi Q92956. Positions 39-200.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114298. 30 interactions.
    DIPi DIP-34779N.
    DIP-6233N.
    IntActi Q92956. 29 interactions.
    MINTi MINT-208002.
    STRINGi 9606.ENSP00000347948.

    Chemistry

    GuidetoPHARMACOLOGYi 1887.

    Polymorphism databases

    DMDMi 13878821.

    Proteomic databases

    PaxDbi Q92956.
    PRIDEi Q92956.

    Protocols and materials databases

    DNASUi 8764.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000355716 ; ENSP00000347948 ; ENSG00000157873 . [Q92956-1 ]
    GeneIDi 8764.
    KEGGi hsa:8764.
    UCSCi uc001ajr.3. human. [Q92956-1 ]

    Organism-specific databases

    CTDi 8764.
    GeneCardsi GC01P002487.
    HGNCi HGNC:11912. TNFRSF14.
    HPAi CAB026150.
    CAB030007.
    HPA006404.
    MIMi 602746. gene.
    neXtProti NX_Q92956.
    PharmGKBi PA36605.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG40150.
    HOGENOMi HOG000065766.
    HOVERGENi HBG072084.
    InParanoidi Q92956.
    KOi K05152.
    OMAi SPGHFCI.
    PhylomeDBi Q92956.
    TreeFami TF331157.

    Enzyme and pathway databases

    Reactomei REACT_19344. Costimulation by the CD28 family.
    SignaLinki Q92956.

    Miscellaneous databases

    ChiTaRSi TNFRSF14. human.
    EvolutionaryTracei Q92956.
    GeneWikii TNFRSF14.
    GenomeRNAii 8764.
    NextBioi 32872.
    PROi Q92956.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q92956.
    Bgeei Q92956.
    CleanExi HS_TNFRSF14.
    Genevestigatori Q92956.

    Family and domain databases

    InterProi IPR001368. TNFR/NGFR_Cys_rich_reg.
    IPR022332. TNFR_14.
    [Graphical view ]
    Pfami PF00020. TNFR_c6. 1 hit.
    [Graphical view ]
    PRINTSi PR01965. TNFACTORR14.
    SMARTi SM00208. TNFR. 3 hits.
    [Graphical view ]
    PROSITEi PS00652. TNFR_NGFR_1. 1 hit.
    PS50050. TNFR_NGFR_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Herpes simplex virus-1 entry into cells mediated by a novel member of the TNF/NGF receptor family."
      Montgomery R.I., Warner M.S., Lum B.J., Spear P.G.
      Cell 87:427-436(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION AS A RECEPTOR FOR HHV-1.
      Tissue: Cervix adenocarcinoma.
    2. "A newly identified member of the tumor necrosis factor receptor superfamily with a wide tissue distribution and involvement in lymphocyte activation."
      Kwon B.S., Tan K.B., Ni J., Oh K.-O., Lee Z.H., Kim K.K., Kim Y.-J., Wang S., Gentz R., Yu G.-L., Harrop J., Lyn S.D., Silverman C., Porter T.G., Truneh A., Young P.R.
      J. Biol. Chem. 272:14272-14276(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. Zhang W., Wan T., Cao X.
      Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "Search for polymorphisms in the genes for herpesvirus entry mediator, Nectin-1, and Nectin-2 in immune seronegative individuals."
      Struyf F., Posavad C.M., Keyaerts E., Van Ranst M., Corey L., Spear P.G.
      J. Infect. Dis. 185:36-44(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ARG-17 AND ILE-241.
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Spleen.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ARG-17.
    7. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    8. NIEHS SNPs program
      Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-17; THR-117; GLU-174 AND ILE-241.
    9. "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].
    10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. "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] (ISOFORMS 1 AND 2).
      Tissue: Skin.
    12. "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 39-53.
    13. "ATAR, a novel tumor necrosis factor receptor family member, signals through TRAF2 and TRAF5."
      Hsu H., Solovyev I., Colombero A., Elliott R., Kelley M., Boyle W.J.
      J. Biol. Chem. 272:13471-13474(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRAF2 AND TRAF5.
    14. "Herpesvirus entry mediator, a member of the tumor necrosis factor receptor (TNFR) family, interacts with members of the TNFR-associated factor family and activates the transcription factors NF-kappaB and AP-1."
      Marsters S.A., Ayres T.M., Skubatch M., Gray C.L., Rothe M., Ashkenazi A.
      J. Biol. Chem. 272:14029-14032(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRAF3 AND TRAF5.
    15. "Herpes simplex virus glycoprotein D can bind to poliovirus receptor-related protein 1 or herpesvirus entry mediator, two structurally unrelated mediators of virus entry."
      Krummenacher C., Nicola A.V., Whitbeck J.C., Lou H., Hou W., Lambris J.D., Geraghty R.J., Spear P.G., Cohen G.H., Eisenberg R.J.
      J. Virol. 72:7064-7074(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HHV-1 AND HHV-2 GLYCOPROTEIN D.
    16. "Herpes simplex virus glycoprotein D bound to the human receptor HveA."
      Carfi A., Willis S.H., Whitbeck J.C., Krummenacher C., Cohen G.H., Eisenberg R.J., Wiley D.C.
      Mol. Cell 8:169-179(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 39-200 IN COMPLEX WITH HUMAN HERPESVIRUS 1 GLYCOPROTEIN.
    17. "Attenuating lymphocyte activity: the crystal structure of the BTLA-HVEM complex."
      Compaan D.M., Gonzalez L.C., Tom I., Loyet K.M., Eaton D., Hymowitz S.G.
      J. Biol. Chem. 280:39553-39561(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 26-137 IN COMPLEX WITH BTLA, GLYCOSYLATION AT ASN-110.

    Entry informationi

    Entry nameiTNR14_HUMAN
    AccessioniPrimary (citable) accession number: Q92956
    Secondary accession number(s): B3KW30
    , B9DI89, Q6IB95, Q8N634, Q8WXR1, Q96J31, Q9UM65
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: April 27, 2001
    Last modified: October 1, 2014
    This is version 161 of the entry and version 3 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

    3D-structure, 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3