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P19438

- TNR1A_HUMAN

UniProt

P19438 - TNR1A_HUMAN

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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

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. 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. response to wounding Source: Ensembl
  29. tetrapyrrole metabolic process Source: Ensembl
  30. viral process Source: UniProtKB-KW
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiP19438.
CleanExiHS_TNFRSF1A.
ExpressionAtlasiP19438. baseline and differential.
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. 95 interactions.
DIPiDIP-407N.
IntActiP19438. 27 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.
GeneTreeiENSGT00530000064001.
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

        10         20         30         40         50
MGLSTVPDLL LPLVLLELLV GIYPSGVIGL VPHLGDREKR DSVCPQGKYI
60 70 80 90 100
HPQNNSICCT KCHKGTYLYN DCPGPGQDTD CRECESGSFT ASENHLRHCL
110 120 130 140 150
SCSKCRKEMG QVEISSCTVD RDTVCGCRKN QYRHYWSENL FQCFNCSLCL
160 170 180 190 200
NGTVHLSCQE KQNTVCTCHA GFFLRENECV SCSNCKKSLE CTKLCLPQIE
210 220 230 240 250
NVKGTEDSGT TVLLPLVIFF GLCLLSLLFI GLMYRYQRWK SKLYSIVCGK
260 270 280 290 300
STPEKEGELE GTTTKPLAPN PSFSPTPGFT PTLGFSPVPS STFTSSSTYT
310 320 330 340 350
PGDCPNFAAP RREVAPPYQG ADPILATALA SDPIPNPLQK WEDSAHKPQS
360 370 380 390 400
LDTDDPATLY AVVENVPPLR WKEFVRRLGL SDHEIDRLEL QNGRCLREAQ
410 420 430 440 450
YSMLATWRRR TPRREATLEL LGRVLRDMDL LGCLEDIEEA LCGPAALPPA

PSLLR
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]
uc010sfa.2. human.

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. 95 interactions.
DIPi DIP-407N.
IntActi P19438. 27 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 ]
uc010sfa.2. human.

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.
GeneTreei ENSGT00530000064001.
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

Bgeei P19438.
CleanExi HS_TNFRSF1A.
ExpressionAtlasi P19438. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 190 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

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