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P19438

- TNR1A_HUMAN

UniProt

P19438 - TNR1A_HUMAN

Protein

Tumor necrosis factor receptor superfamily member 1A

Gene

TNFRSF1A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 189 (01 Oct 2014)
      Sequence version 1 (01 Feb 1991)
      Previous versions | rss
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    Functioni

    Receptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. Contributes to the induction of non-cytocidal TNF effects including anti-viral state and activation of the acid sphingomyelinase.

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. tumor necrosis factor-activated receptor activity Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: Reactome
    2. apoptotic signaling pathway Source: Reactome
    3. cellular response to estradiol stimulus Source: Ensembl
    4. cellular response to mechanical stimulus Source: UniProtKB
    5. cytokine-mediated signaling pathway Source: UniProtKB
    6. defense response to bacterium Source: Ensembl
    7. extrinsic apoptotic signaling pathway via death domain receptors Source: BHF-UCL
    8. inflammatory response Source: UniProtKB
    9. intrinsic apoptotic signaling pathway in response to DNA damage Source: Ensembl
    10. negative regulation of apoptotic process Source: Ensembl
    11. negative regulation of gene expression Source: Ensembl
    12. negative regulation of inflammatory response Source: BHF-UCL
    13. negative regulation of interleukin-6 production Source: Ensembl
    14. positive regulation of angiogenesis Source: Ensembl
    15. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    16. positive regulation of inflammatory response Source: UniProtKB
    17. positive regulation of protein import into nucleus, translocation Source: Ensembl
    18. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    19. positive regulation of tumor necrosis factor production Source: Ensembl
    20. positive regulation of tyrosine phosphorylation of Stat1 protein Source: BHF-UCL
    21. prostaglandin metabolic process Source: InterPro
    22. protein heterooligomerization Source: Ensembl
    23. response to alkaloid Source: Ensembl
    24. response to amino acid Source: Ensembl
    25. response to ethanol Source: Ensembl
    26. response to hypoxia Source: Ensembl
    27. response to lipopolysaccharide Source: Ensembl
    28. tetrapyrrole metabolic process Source: Ensembl
    29. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Apoptosis, Host-virus interaction

    Enzyme and pathway databases

    ReactomeiREACT_1432. TNF signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tumor necrosis factor receptor superfamily member 1A
    Alternative name(s):
    Tumor necrosis factor receptor 1
    Short name:
    TNF-R1
    Tumor necrosis factor receptor type I
    Short name:
    TNF-RI
    Short name:
    TNFR-I
    p55
    p60
    CD_antigen: CD120a
    Cleaved into the following 2 chains:
    Gene namesi
    Name:TNFRSF1A
    Synonyms:TNFAR, TNFR1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:11916. TNFRSF1A.

    Subcellular locationi

    Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication. Golgi apparatus membrane 1 Publication; Single-pass type I membrane protein 1 Publication. Secreted 1 Publication
    Note: A secreted form is produced through proteolytic processing.
    Isoform 4 : Secreted
    Note: Lacks a Golgi-retention motif, is not membrane bound and therefore is secreted.

    GO - Cellular componenti

    1. axon Source: Ensembl
    2. cell surface Source: Ensembl
    3. extracellular region Source: UniProtKB
    4. extracellular space Source: BHF-UCL
    5. Golgi membrane Source: UniProtKB
    6. integral component of plasma membrane Source: ProtInc
    7. membrane raft Source: BHF-UCL
    8. nucleus Source: Ensembl
    9. plasma membrane Source: Reactome
    10. receptor complex Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Golgi apparatus, Membrane, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Familial hibernian fever (FHF) [MIM:142680]: A hereditary periodic fever syndrome characterized by recurrent fever, abdominal pain, localized tender skin lesions and myalgia. Reactive amyloidosis is the main complication and occurs in 25% of cases.5 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti51 – 511H → Q in FHF. 1 Publication
    VAR_019329
    Natural varianti59 – 591C → R in FHF. 1 Publication
    VAR_013410
    Natural varianti59 – 591C → S in FHF. 2 Publications
    VAR_019302
    Natural varianti62 – 621C → G in FHF. 1 Publication
    VAR_019303
    Natural varianti62 – 621C → Y in FHF. 1 Publication
    VAR_013411
    Natural varianti75 – 751P → L in FHF; may be a polymorphism. 2 Publications
    Corresponds to variant rs4149637 [ dbSNP | Ensembl ].
    VAR_019330
    Natural varianti79 – 791T → M in FHF. 1 Publication
    VAR_013412
    Natural varianti81 – 811C → F in FHF. 1 Publication
    VAR_013413
    Natural varianti99 – 991C → S in FHF. 2 Publications
    VAR_019304
    Natural varianti115 – 1151S → G in FHF. 1 Publication
    VAR_019331
    Natural varianti117 – 1171C → R in FHF. 1 Publication
    VAR_013414
    Natural varianti117 – 1171C → Y in FHF. 1 Publication
    VAR_013415
    Natural varianti121 – 1211R → P in FHF. 1 Publication
    Corresponds to variant rs4149584 [ dbSNP | Ensembl ].
    VAR_019305
    Natural varianti121 – 1211R → Q in FHF; may be a polymorphism. 2 Publications
    Corresponds to variant rs4149584 [ dbSNP | Ensembl ].
    VAR_019332
    Multiple sclerosis 5 (MS5) [MIM:614810]: A multifactorial, inflammatory, demyelinating disease of the central nervous system. Sclerotic lesions are characterized by perivascular infiltration of monocytes and lymphocytes and appear as indurated areas in pathologic specimens (sclerosis in plaques). The pathological mechanism is regarded as an autoimmune attack of the myelin sheath, mediated by both cellular and humoral immunity. Clinical manifestations include visual loss, extra-ocular movement disorders, paresthesias, loss of sensation, weakness, dysarthria, spasticity, ataxia and bladder dysfunction. Genetic and environmental factors influence susceptibility to the disease.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. An intronic mutation affecting alternative splicing and skipping of exon 6 directs increased expression of isoform 4 a transcript encoding a C-terminally truncated protein which is secreted and may function as a TNF antagonist.

    Keywords - Diseasei

    Amyloidosis, Disease mutation

    Organism-specific databases

    MIMi142680. phenotype.
    614810. phenotype.
    Orphaneti329967. Intermittent hydrarthrosis.
    802. Multiple sclerosis.
    32960. TRAPS syndrome.
    PharmGKBiPA36609.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Add
    BLAST
    Chaini22 – 455434Tumor necrosis factor receptor superfamily member 1A, membrane formPRO_0000034543Add
    BLAST
    Chaini41 – 201161Tumor necrosis factor-binding protein 1PRO_0000034544Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi44 ↔ 58
    Glycosylationi54 – 541N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi59 ↔ 72
    Disulfide bondi62 ↔ 81
    Disulfide bondi84 ↔ 99
    Disulfide bondi102 ↔ 117
    Disulfide bondi105 ↔ 125
    Disulfide bondi127 ↔ 143
    Glycosylationi145 – 1451N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi146 ↔ 158
    Disulfide bondi149 ↔ 166
    Glycosylationi151 – 1511N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi168 ↔ 179
    Disulfide bondi182 ↔ 195
    Disulfide bondi185 ↔ 191

    Post-translational modificationi

    The soluble form is produced from the membrane form by proteolytic processing.

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP19438.
    PaxDbiP19438.
    PRIDEiP19438.

    PTM databases

    PhosphoSiteiP19438.

    Miscellaneous databases

    PMAP-CutDBP19438.

    Expressioni

    Gene expression databases

    ArrayExpressiP19438.
    BgeeiP19438.
    CleanExiHS_TNFRSF1A.
    GenevestigatoriP19438.

    Organism-specific databases

    HPAiCAB010309.
    HPA004102.

    Interactioni

    Subunit structurei

    Binding of TNF to the extracellular domain leads to homotrimerization. The aggregated death domains provide a novel molecular interface that interacts specifically with the death domain of TRADD. Various TRADD-interacting proteins such as TRAFS, RIPK1 and possibly FADD, are recruited to the complex by their association with TRADD. This complex activates at least two distinct signaling cascades, apoptosis and NF-kappa-B signaling. Interacts with BAG4, BRE, FEM1B, GRB2, SQSTM1 and TRPC4AP. Interacts with HCV core protein. Interacts with human cytomegalovirus/HHV-5 protein UL138.8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GRNP287994EBI-299451,EBI-747754
    RIPK1Q135466EBI-299451,EBI-358507
    TNFP013759EBI-299451,EBI-359977
    TRADDQ1562811EBI-299451,EBI-359215
    TRAF2Q129334EBI-299451,EBI-355744

    Protein-protein interaction databases

    BioGridi112986. 92 interactions.
    DIPiDIP-407N.
    IntActiP19438. 26 interactions.
    MINTiMINT-135026.
    STRINGi9606.ENSP00000162749.

    Structurei

    Secondary structure

    1
    455
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi48 – 503
    Beta strandi52 – 543
    Beta strandi58 – 603
    Beta strandi66 – 705
    Beta strandi80 – 834
    Beta strandi92 – 943
    Helixi107 – 1093
    Beta strandi112 – 1154
    Beta strandi124 – 1263
    Beta strandi131 – 1377
    Beta strandi140 – 1456
    Beta strandi152 – 1565
    Beta strandi160 – 1623
    Beta strandi165 – 1684
    Beta strandi172 – 1754
    Beta strandi178 – 1814
    Helixi182 – 1843
    Helixi192 – 1954
    Helixi357 – 3659
    Helixi371 – 3788
    Helixi382 – 39110
    Helixi396 – 41015
    Helixi417 – 42711
    Helixi431 – 44111

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EXTX-ray1.85A/B41-201[»]
    1FT4X-ray2.90A/B41-201[»]
    1ICHNMR-A345-455[»]
    1NCFX-ray2.25A/B41-201[»]
    1TNRX-ray2.85R44-182[»]
    ProteinModelPortaliP19438.
    SMRiP19438. Positions 42-201, 356-442.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP19438.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini22 – 211190ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini235 – 455221CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei212 – 23423HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati43 – 8240TNFR-Cys 1Add
    BLAST
    Repeati83 – 12543TNFR-Cys 2Add
    BLAST
    Repeati126 – 16641TNFR-Cys 3Add
    BLAST
    Repeati167 – 19630TNFR-Cys 4Add
    BLAST
    Domaini356 – 44186DeathPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni338 – 34811N-SMase activation domain (NSD)Add
    BLAST

    Domaini

    The domain that induces A-SMASE is probably identical to the death domain. The N-SMASE activation domain (NSD) is both necessary and sufficient for activation of N-SMASE.
    Both the cytoplasmic membrane-proximal region and the C-terminal region containing the death domain are involved in the interaction with TRPC4AP.By similarity

    Sequence similaritiesi

    Contains 1 death domain.PROSITE-ProRule annotation
    Contains 4 TNFR-Cys repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG39168.
    HOVERGENiHBG058842.
    InParanoidiP19438.
    KOiK03158.
    OMAiCLREAHY.
    PhylomeDBiP19438.
    TreeFamiTF333916.

    Family and domain databases

    Gene3Di1.10.533.10. 1 hit.
    InterProiIPR011029. DEATH-like_dom.
    IPR000488. Death_domain.
    IPR001368. TNFR/NGFR_Cys_rich_reg.
    IPR020419. TNFR_1A.
    [Graphical view]
    PfamiPF00531. Death. 1 hit.
    PF00020. TNFR_c6. 3 hits.
    [Graphical view]
    PRINTSiPR01918. TNFACTORR1A.
    SMARTiSM00005. DEATH. 1 hit.
    SM00208. TNFR. 4 hits.
    [Graphical view]
    SUPFAMiSSF47986. SSF47986. 1 hit.
    PROSITEiPS50017. DEATH_DOMAIN. 1 hit.
    PS00652. TNFR_NGFR_1. 3 hits.
    PS50050. TNFR_NGFR_2. 3 hits.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

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

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P19438-1) [UniParc]FASTAAdd to Basket

    Also known as: FL-TNFR1

    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

    MGLSTVPDLL LPLVLLELLV GIYPSGVIGL VPHLGDREKR DSVCPQGKYI    50
    HPQNNSICCT KCHKGTYLYN DCPGPGQDTD CRECESGSFT ASENHLRHCL 100
    SCSKCRKEMG QVEISSCTVD RDTVCGCRKN QYRHYWSENL FQCFNCSLCL 150
    NGTVHLSCQE KQNTVCTCHA GFFLRENECV SCSNCKKSLE CTKLCLPQIE 200
    NVKGTEDSGT TVLLPLVIFF GLCLLSLLFI GLMYRYQRWK SKLYSIVCGK 250
    STPEKEGELE GTTTKPLAPN PSFSPTPGFT PTLGFSPVPS STFTSSSTYT 300
    PGDCPNFAAP RREVAPPYQG ADPILATALA SDPIPNPLQK WEDSAHKPQS 350
    LDTDDPATLY AVVENVPPLR WKEFVRRLGL SDHEIDRLEL QNGRCLREAQ 400
    YSMLATWRRR TPRREATLEL LGRVLRDMDL LGCLEDIEEA LCGPAALPPA 450
    PSLLR 455
    Length:455
    Mass (Da):50,495
    Last modified:February 1, 1991 - v1
    Checksum:i4CEFBA96D03B8225
    GO
    Isoform 2 (identifier: P19438-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-108: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:347
    Mass (Da):38,651
    Checksum:i8C629DAF8D7BA515
    GO
    Isoform 4 (identifier: P19438-4) [UniParc]FASTAAdd to Basket

    Also known as: Delta6-TNFR1

    The sequence of this isoform differs from the canonical sequence as follows:
         184-455: NCKKSLECTK...ALPPAPSLLR → KHHSAVAPGH...LLHCLWEIDT

    Note: Disease-associated isoform. Isoform 4 splicing pattern is driven by a variation in the exon 6/intron 6 boundary region that alters exon 6 splicing. Exon 6 skipping introduces a frameshift and the translation of a protein lacking the intracellular, the transmembrane and part of the extracellular domain.

    Show »
    Length:228
    Mass (Da):25,577
    Checksum:iA67C489AF6DDBFEC
    GO
    Isoform 3 (identifier: P19438-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-232: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:223
    Mass (Da):24,794
    Checksum:i31BDA9ACAEF12FC3
    GO
    Isoform 5 (identifier: P19438-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         184-218: NCKKSLECTKLCLPQIENVKGTEDSGTTVLLPLVI → KVLLCRPGWNAVARSRLTATSASQIQAILLLQPPK
         219-455: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:218
    Mass (Da):24,194
    Checksum:iFBDD906CEF26F405
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti13 – 131L → LILPQ in BAG51763. (PubMed:14702039)Curated
    Sequence conflicti255 – 2551K → E in BAG37891. (PubMed:14702039)Curated
    Sequence conflicti286 – 2861S → G in BAG51763. (PubMed:14702039)Curated
    Sequence conflicti394 – 3941R → L in BAF83777. (PubMed:14702039)Curated
    Sequence conflicti412 – 4121Missing in AAA36756. (PubMed:2170974)Curated
    Sequence conflicti443 – 4464GPAA → APP in AAA36756. (PubMed:2170974)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti51 – 511H → Q in FHF. 1 Publication
    VAR_019329
    Natural varianti59 – 591C → R in FHF. 1 Publication
    VAR_013410
    Natural varianti59 – 591C → S in FHF. 2 Publications
    VAR_019302
    Natural varianti62 – 621C → G in FHF. 1 Publication
    VAR_019303
    Natural varianti62 – 621C → Y in FHF. 1 Publication
    VAR_013411
    Natural varianti75 – 751P → L in FHF; may be a polymorphism. 2 Publications
    Corresponds to variant rs4149637 [ dbSNP | Ensembl ].
    VAR_019330
    Natural varianti79 – 791T → M in FHF. 1 Publication
    VAR_013412
    Natural varianti81 – 811C → F in FHF. 1 Publication
    VAR_013413
    Natural varianti99 – 991C → S in FHF. 2 Publications
    VAR_019304
    Natural varianti115 – 1151S → G in FHF. 1 Publication
    VAR_019331
    Natural varianti117 – 1171C → R in FHF. 1 Publication
    VAR_013414
    Natural varianti117 – 1171C → Y in FHF. 1 Publication
    VAR_013415
    Natural varianti121 – 1211R → P in FHF. 1 Publication
    Corresponds to variant rs4149584 [ dbSNP | Ensembl ].
    VAR_019305
    Natural varianti121 – 1211R → Q in FHF; may be a polymorphism. 2 Publications
    Corresponds to variant rs4149584 [ dbSNP | Ensembl ].
    VAR_019332
    Natural varianti305 – 3051P → T.
    Corresponds to variant rs1804532 [ dbSNP | Ensembl ].
    VAR_011813

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 232232Missing in isoform 3. 1 PublicationVSP_037154Add
    BLAST
    Alternative sequencei1 – 108108Missing in isoform 2. 1 PublicationVSP_037153Add
    BLAST
    Alternative sequencei184 – 455272NCKKS…PSLLR → KHHSAVAPGHFLWSLPFIPP LHWFNVSLPTVEVQALLHCL WEIDT in isoform 4. CuratedVSP_044949Add
    BLAST
    Alternative sequencei184 – 21835NCKKS…LPLVI → KVLLCRPGWNAVARSRLTAT SASQIQAILLLQPPK in isoform 5. 1 PublicationVSP_047613Add
    BLAST
    Alternative sequencei219 – 455237Missing in isoform 5. 1 PublicationVSP_047614Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M58286 mRNA. Translation: AAA36753.1.
    M33294 mRNA. Translation: AAA03210.1.
    M63121 mRNA. Translation: AAA36754.1.
    X55313 mRNA. Translation: CAA39021.1.
    M60275 mRNA. Translation: AAA36756.1.
    M75866, M75864, M75865 Genomic DNA. Translation: AAA61201.1.
    AY131997 Genomic DNA. Translation: AAM77802.1.
    AK056611 mRNA. Translation: BAG51763.1.
    AK291088 mRNA. Translation: BAF83777.1.
    AK298729 mRNA. Translation: BAG60879.1.
    AK304517 mRNA. Translation: BAG65321.1.
    AK315509 mRNA. Translation: BAG37891.1.
    EU927389 mRNA. Translation: ACH57451.1.
    AC006057 Genomic DNA. No translation available.
    CH471116 Genomic DNA. Translation: EAW88805.1.
    CH471116 Genomic DNA. Translation: EAW88806.1.
    BC010140 mRNA. Translation: AAH10140.1.
    CCDSiCCDS8542.1. [P19438-1]
    PIRiA38208. GQHUT1.
    RefSeqiNP_001056.1. NM_001065.3. [P19438-1]
    UniGeneiHs.279594.

    Genome annotation databases

    EnsembliENST00000162749; ENSP00000162749; ENSG00000067182. [P19438-1]
    ENST00000366159; ENSP00000380389; ENSG00000067182. [P19438-5]
    GeneIDi7132.
    KEGGihsa:7132.
    UCSCiuc001qnt.3. human. [P19438-1]
    uc010sey.2. human. [P19438-3]

    Polymorphism databases

    DMDMi135959.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    INFEVERS

    Repertory of FMF and hereditary autoinflammatory disorders mutations

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M58286 mRNA. Translation: AAA36753.1 .
    M33294 mRNA. Translation: AAA03210.1 .
    M63121 mRNA. Translation: AAA36754.1 .
    X55313 mRNA. Translation: CAA39021.1 .
    M60275 mRNA. Translation: AAA36756.1 .
    M75866 , M75864 , M75865 Genomic DNA. Translation: AAA61201.1 .
    AY131997 Genomic DNA. Translation: AAM77802.1 .
    AK056611 mRNA. Translation: BAG51763.1 .
    AK291088 mRNA. Translation: BAF83777.1 .
    AK298729 mRNA. Translation: BAG60879.1 .
    AK304517 mRNA. Translation: BAG65321.1 .
    AK315509 mRNA. Translation: BAG37891.1 .
    EU927389 mRNA. Translation: ACH57451.1 .
    AC006057 Genomic DNA. No translation available.
    CH471116 Genomic DNA. Translation: EAW88805.1 .
    CH471116 Genomic DNA. Translation: EAW88806.1 .
    BC010140 mRNA. Translation: AAH10140.1 .
    CCDSi CCDS8542.1. [P19438-1 ]
    PIRi A38208. GQHUT1.
    RefSeqi NP_001056.1. NM_001065.3. [P19438-1 ]
    UniGenei Hs.279594.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EXT X-ray 1.85 A/B 41-201 [» ]
    1FT4 X-ray 2.90 A/B 41-201 [» ]
    1ICH NMR - A 345-455 [» ]
    1NCF X-ray 2.25 A/B 41-201 [» ]
    1TNR X-ray 2.85 R 44-182 [» ]
    ProteinModelPortali P19438.
    SMRi P19438. Positions 42-201, 356-442.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112986. 92 interactions.
    DIPi DIP-407N.
    IntActi P19438. 26 interactions.
    MINTi MINT-135026.
    STRINGi 9606.ENSP00000162749.

    Chemistry

    BindingDBi P19438.
    ChEMBLi CHEMBL3378.
    GuidetoPHARMACOLOGYi 1870.

    PTM databases

    PhosphoSitei P19438.

    Polymorphism databases

    DMDMi 135959.

    Proteomic databases

    MaxQBi P19438.
    PaxDbi P19438.
    PRIDEi P19438.

    Protocols and materials databases

    DNASUi 7132.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000162749 ; ENSP00000162749 ; ENSG00000067182 . [P19438-1 ]
    ENST00000366159 ; ENSP00000380389 ; ENSG00000067182 . [P19438-5 ]
    GeneIDi 7132.
    KEGGi hsa:7132.
    UCSCi uc001qnt.3. human. [P19438-1 ]
    uc010sey.2. human. [P19438-3 ]

    Organism-specific databases

    CTDi 7132.
    GeneCardsi GC12M006412.
    HGNCi HGNC:11916. TNFRSF1A.
    HPAi CAB010309.
    HPA004102.
    MIMi 142680. phenotype.
    191190. gene.
    614810. phenotype.
    neXtProti NX_P19438.
    Orphaneti 329967. Intermittent hydrarthrosis.
    802. Multiple sclerosis.
    32960. TRAPS syndrome.
    PharmGKBi PA36609.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG39168.
    HOVERGENi HBG058842.
    InParanoidi P19438.
    KOi K03158.
    OMAi CLREAHY.
    PhylomeDBi P19438.
    TreeFami TF333916.

    Enzyme and pathway databases

    Reactomei REACT_1432. TNF signaling.

    Miscellaneous databases

    ChiTaRSi TNFRSF1A. human.
    EvolutionaryTracei P19438.
    GeneWikii TNFRSF1A.
    GenomeRNAii 7132.
    NextBioi 27905.
    PMAP-CutDB P19438.
    PROi P19438.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P19438.
    Bgeei P19438.
    CleanExi HS_TNFRSF1A.
    Genevestigatori P19438.

    Family and domain databases

    Gene3Di 1.10.533.10. 1 hit.
    InterProi IPR011029. DEATH-like_dom.
    IPR000488. Death_domain.
    IPR001368. TNFR/NGFR_Cys_rich_reg.
    IPR020419. TNFR_1A.
    [Graphical view ]
    Pfami PF00531. Death. 1 hit.
    PF00020. TNFR_c6. 3 hits.
    [Graphical view ]
    PRINTSi PR01918. TNFACTORR1A.
    SMARTi SM00005. DEATH. 1 hit.
    SM00208. TNFR. 4 hits.
    [Graphical view ]
    SUPFAMi SSF47986. SSF47986. 1 hit.
    PROSITEi PS50017. DEATH_DOMAIN. 1 hit.
    PS00652. TNFR_NGFR_1. 3 hits.
    PS50050. TNFR_NGFR_2. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and expression of the human 55 kd tumor necrosis factor receptor."
      Loetscher H., Pan Y.-C.E., Lahm H.-W., Gentz R., Brockhaus M., Tabuchi H., Lesslauer W.
      Cell 61:351-359(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Molecular cloning and expression of a receptor for human tumor necrosis factor."
      Schall T.J., Lewis M., Koller K.J., Lee A., Rice G.C., Wong G.H.W., Getanaga T., Granger G.A., Lentz R., Raab H., Kohr W.J., Goeddel D.V.
      Cell 61:361-370(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Placenta.
    3. "Molecular cloning and expression of human and rat tumor necrosis factor receptor chain (p60) and its soluble derivative, tumor necrosis factor-binding protein."
      Himmler A., Maurer-Fogy I., Kroenke M., Scheurich P., Pfizenmaier K., Lantz M., Olsson I., Hauptmann R., Stratowa C., Adolf G.R.
      DNA Cell Biol. 9:705-715(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "Soluble forms of tumor necrosis factor receptors (TNF-Rs). The cDNA for the type I TNF-R, cloned using amino acid sequence data of its soluble form, encodes both the cell surface and a soluble form of the receptor."
      Nophar Y., Kemper O., Brakebusch C., Engelmann H., Zwang R., Aderka D., Holtmann H., Wallach D.
      EMBO J. 9:3269-3278(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 41-53; 110-124 AND 199-201 (ISOFORM 1).
    5. "Cloning of human tumor necrosis factor (TNF) receptor cDNA and expression of recombinant soluble TNF-binding protein."
      Gray P.W., Barrett K., Chantry D., Turner M., Feldman M.
      Proc. Natl. Acad. Sci. U.S.A. 87:7380-7384(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Placenta.
    6. "Structure of the human TNF receptor 1 (p60) gene (TNFR1) and localization to chromosome 12p13."
      Fuchs P., Strehl S., Dworzak M., Himmler A., Ambros P.F.
      Genomics 13:219-224(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    7. SeattleSNPs variation discovery resource
      Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-75 AND GLN-121.
    8. "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] (ISOFORMS 1; 2 AND 3).
      Tissue: Neutrophil, Teratocarcinoma, Tongue and Uterus.
    9. "Discovery of novel human transcript variants by analysis of intronic single-block EST with polyadenylation site."
      Wang P., Yu P., Gao P., Shi T., Ma D.
      BMC Genomics 10:518-518(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
    10. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    12. "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] (ISOFORM 1).
      Tissue: Muscle.
    13. "Purification of two types of TNF inhibitors in the urine of the patient with chronic glomerulonephritis."
      Suzuki J., Tomizawa S., Arai H., Seki Y., Maruyama K., Kuroume T.
      Nephron 66:386-390(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 41-57 (ISOFORM 1).
      Tissue: Urine.
    14. "Two tumor necrosis factor-binding proteins purified from human urine. Evidence for immunological cross-reactivity with cell surface tumor necrosis factor receptors."
      Engelmann H., Novick D., Wallach D.
      J. Biol. Chem. 265:1531-1536(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 41-45 (ISOFORM 1).
    15. "Hepatitis C virus core protein binds to the cytoplasmic domain of tumor necrosis factor (TNF) receptor 1 and enhances TNF-induced apoptosis."
      Zhu N., Khoshnan A., Schneider R., Matsumoto M., Dennert G., Ware C.F., Lai M.M.C.
      J. Virol. 72:3691-3697(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HCV CORE PROTEIN.
    16. "The interaction of p62 with RIP links the atypical PKCs to NF-kappaB activation."
      Sanz L., Sanchez P., Lallena M.-J., Diaz-Meco M.T., Moscat J.
      EMBO J. 18:3044-3053(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RIPK1 AND SQSTM1.
    17. "F1Aalpha, a death receptor-binding protein homologous to the Caenorhabditis elegans sex-determining protein, FEM-1, is a caspase substrate that mediates apoptosis."
      Chan S.-L., Tan K.-O., Zhang L., Yee K.S.Y., Ronca F., Chan M.-Y., Yu V.C.
      J. Biol. Chem. 274:32461-32468(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FEM1B.
    18. "Identification of Grb2 as a novel binding partner of tumor necrosis factor (TNF) receptor I."
      Hildt E., Oess S.
      J. Exp. Med. 189:1707-1714(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GRB2.
    19. "Prevention of constitutive TNF receptor 1 signaling by silencer of death domains."
      Jiang Y., Woronicz J.D., Liu W., Goeddel D.V.
      Science 283:543-546(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BAG4.
    20. "A death receptor-associated anti-apoptotic protein, BRE, inhibits mitochondrial apoptotic pathway."
      Li Q., Ching A.K.-K., Chan B.C.-L., Chow S.K.-Y., Lim P.-L., Ho T.C.-Y., Ip W.-K., Wong C.-K., Lam C.W.-K., Lee K.K.-H., Chan J.Y.-H., Chui Y.-L.
      J. Biol. Chem. 279:52106-52116(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BRE.
    21. "The cytomegaloviral protein pUL138 acts as potentiator of tumor necrosis factor (TNF) receptor 1 surface density to enhance ULb'-encoded modulation of TNF-alpha signaling."
      Le V.T., Trilling M., Hengel H.
      J. Virol. 85:13260-13270(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HHV-5 PROTEIN UL138.
    22. Cited for: INVOLVEMENT IN MS5, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING (ISOFORM 4).
    23. "Crystal structure of the soluble human 55 kd TNF receptor-human TNF beta complex: implications for TNF receptor activation."
      Banner D.W., D'Arcy A., Janes W., Gentz R., Schoenfeld H.-J., Broger C., Loetscher H., Lesslauer W.
      Cell 73:431-445(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 30-211 IN COMPLEX WITH TNFB.
    24. "Structures of the extracellular domain of the type I tumor necrosis factor receptor."
      Naismith J.H., Devine T.Q., Khono H., Sprang S.R.
      Structure 4:1251-1262(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 41-202.
    25. Cited for: VARIANTS FHF ARG-59; TYR-62; MET-79; PHE-81; ARG-117 AND TYR-117.
    26. "A novel missense mutation (C30S) in the gene encoding tumor necrosis factor receptor 1 linked to autosomal-dominant recurrent fever with localized myositis in a French family."
      Dode C., Papo T., Fieschi C., Pecheux C., Dion E., Picard F., Godeau P., Bienvenu J., Piette J.-C., Delpech M., Grateau G.
      Arthritis Rheum. 43:1535-1542(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT FHF SER-59.
    27. "The tumor-necrosis-factor receptor-associated periodic syndrome: new mutations in TNFRSF1A, ancestral origins, genotype-phenotype studies, and evidence for further genetic heterogeneity of periodic fevers."
      Aksentijevich I., Galon J., Soares M., Mansfield E., Hull K., Oh H.-H., Goldbach-Mansky R., Dean J., Athreya B., Reginato A.J., Henrickson M., Pons-Estel B., O'Shea J.J., Kastner D.L.
      Am. J. Hum. Genet. 69:301-314(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS FHF GLN-51; SER-59; GLY-62; LEU-75; GLY-115 AND GLN-121.
    28. Cited for: VARIANTS FHF SER-99 AND PRO-121.
    29. "Tumour necrosis factor receptor-associated periodic syndrome with a novel mutation in the TNFRSF1A gene in a Japanese family."
      Kusuhara K., Nomura A., Nakao F., Hara T.
      Eur. J. Pediatr. 163:30-32(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT FHF SER-99.

    Entry informationi

    Entry nameiTNR1A_HUMAN
    AccessioniPrimary (citable) accession number: P19438
    Secondary accession number(s): A8K4X3
    , B2RDE4, B3KPQ1, B4DQB7, B4E309, B5M0B5, D3DUR1, Q9UCA4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: February 1, 1991
    Last modified: October 1, 2014
    This is version 189 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

    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 12
      Human chromosome 12: 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