Protein detail
TNR21
Tumor necrosis factor receptor superfamily member 21 (Death receptor 6) (CD antigen CD358)
Protein symbol TNR21 | UniProt ID | EVMP score 0.50 |
Frequency 4 | Transmembrane count 1 | Protein classification CD markersPlasma proteinsPredicted membrane proteins |
Basic Information
Protein Names
Tumor necrosis factor receptor superfamily member 21 (Death receptor 6) (CD antigen CD358)
Protein Class
CD markersPlasma proteinsPredicted membrane proteins
Protein Function
CD markers
Transmembrane
350..370; Helical
Transmembrane Count
1
Ensembl
Entrez Gene Symbol
Gene Synonym
CD358DR6
Gene Description
TNF receptor superfamily member 21
Chromosome
6
Position
47231532-47309905
Frequency
4
EVMP Score
0.50
Fluorescence & Localization
Cell SpecificColonocytesSingle-Nuclei Brain Specificendothelial cell
Function & Pathway
Protein Function
CD markers
Cellular Component
Molecular Function
Biological Process
Reactome
- R-hsa-3371568 attenuation phase
- R-hsa-8953897 cellular responses to stimuli
- R-hsa-3371556 cellular response to heat stress
- R-hsa-3371511 hsf1 activation
- R-hsa-3371571 hsf1 dependent transactivation
- R-hsa-556833 metabolism of lipids
- R-hsa-3371453 regulation of hsf1 mediated heat shock response
- R-hsa-400206 regulation of lipid metabolism by pparalpha
Mediation Categories
Adhesion and uptake mediationImmune mediationMetabolism mediation
Relations & Evidence
Enzyme-Mediated Modification
0 records.
Ligand-Receptor Signaling
58 records.
| Category | Parent | Database | Transmitter | Receiver | Secreted | Plasma Membrane (Transmembrane) | Plasma Membrane (Peripheral) |
|---|---|---|---|---|---|---|---|
| intracellular | intracellular | LOCATE | No | No | No | Yes | No |
| intracellular | intracellular | OmniPath | No | No | No | Yes | No |
| cell_adhesion | cell_adhesion | Cellinker | Yes | Yes | No | Yes | No |
| adhesion | adhesion | OmniPath | Yes | Yes | No | Yes | No |
| cell_adhesion | cell_adhesion | OmniPath | Yes | Yes | No | Yes | No |
| transmembrane | transmembrane | UniProt_location | No | No | No | Yes | No |
| transmembrane | transmembrane | UniProt_topology | No | No | No | Yes | No |
| transmembrane | transmembrane | UniProt_keyword | No | No | No | Yes | No |
| transmembrane_predicted | transmembrane | OmniPath | No | No | No | Yes | No |
| transmembrane | transmembrane | CellPhoneDB | No | No | No | Yes | No |
Regulatory Interaction Network
2 records.
| Source Protein Symbol | Source UniProt ID | Target Protein Symbol | Target UniProt ID | Is Directed | Is Stimulation | Is Inhibition | Database | References |
|---|---|---|---|---|---|---|---|---|
| TNR21 | O75509 | TRADD | Q15628 | Yes | Yes | No | HPRDSIGNOR | SIGNOR:14585074HPRD:9714541 |
| TNFA | P01375 | TNR21 | O75509 | Yes | Yes | No | HPMRFantom5_LRdbCellTalkDBHPMR_LRdbiTALKHPMR_CellinkertalklrRamilowski2015SIGNORconnectomeDB2020Baccin2019Ramilowski2015_Baccin2019CellinkerWangLRdbEMBRACEHPMR_talklr | HPMR:9714541LRdb:9714541Baccin2019:9714541CellTalkDB:9714541Cellinker:9714541SIGNOR:9714541connectomeDB2020:9714541 |
Protein Complex Composition
Sequence, Structure & Domains
Sequences
Length
655
Mass
71,845
Sequence
MGTSPSSSTALASCSRIARRATATMIAGSLLLLGFLSTTTAQPEQKASNLIGTYRHVDRATGQVLTCDKCPAGTYVSEHCTNTSLRVCSSCPVGTFTRHENGIEKCHDCSQPCPWPMIEKLPCAALTDRECTCPPGMFQSNATCAPHTVCPVGWGVRKKGTETEDVRCKQCARGTFSDVPSSVMKCKAYTDCLSQNLVVIKPGTKETDNVCGTLPSFSSSTSPSPGTAIFPRPEHMETHEVPSSTYVPKGMNSTESNSSASVRPKVLSSIQEGTVPDNTSSARGKEDVNKTLPNLQVVNHQQGPHHRHILKLLPSMEATGGEKSSTPIKGPKRGHPRQNLHKHFDINEHLPWMIVLFLLLVLVVIVVCSIRKSSRTLKKGPRQDPSAIVEKAGLKKSMTPTQNREKWIYYCNGHGIDILKLVAAQVGSQWKDIYQFLCNASEREVAAFSNGYTADHERAYAALQHWTIRGPEASLAQLISALRQHRRNDVVEKIRGLMEDTTQLETDKLALPMSPSPLSPSPIPSPNAKLENSALLTVEPSPQDKNKGFFVDESEPLLRCDSTSSGSSALSRNGSFITKEKKDTVLRQVRLDPCDLQPIFDDMLHFLNPEELRVIEEIPQAEDKLDRLFEIIGVKSQEASQTLLDSVYSHLPDLL
3D Structural Models
Turn
59..61
Helix
193..195; 579..591; 598..606; 609..616; 621..635; 637..650; 652..654
Beta Strand
53..57; 64..68; 74..78; 82..84; 87..90; 99..101; 118..121; 130..132; 137..140; 143..146; 154..158; 162..164; 167..170; 181..183; 198..201; 205..207; 210..212; 571..573
3D Structure
NMR spectroscopy (1); X-ray crystallography (6)
Domain & Motif Annotations
Compositional Bias
243..261; Polar residues; 268..282; Polar residues
Repeat
50..88; TNFR-Cys 1; 90..131; TNFR-Cys 2; 133..167; TNFR-Cys 3; 170..211; TNFR-Cys 4
Domain (FT)
415..498; Death
Region
243..286; Disordered; 318..337; Disordered