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Protein

Tumor necrosis factor ligand superfamily member 18

Gene

TNFSF18

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cytokine that binds to TNFRSF18/AITR/GITR. Regulates T-cell responses. Can function as costimulator and lower the threshold for T-cell activation and T-cell proliferation. Important for interactions between activated T-lymphocytes and endothelial cells. Mediates activation of NF-kappa-B. Triggers increased phosphorylation of STAT1 and up-regulates expression of VCAM1 and ICAM1 (PubMed:23892569). Promotes leukocyte adhesion to endothelial cells (PubMed:23892569). Regulates migration of monocytes from the splenic reservoir to sites of inflammation (By similarity).By similarity3 Publications

GO - Molecular functioni

  • receptor binding Source: ProtInc
  • tumor necrosis factor receptor superfamily binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Cytokine

Keywords - Biological processi

Adaptive immunity, Immunity

Enzyme and pathway databases

BioCyciZFISH:ENSG00000120337-MONOMER.
ReactomeiR-HSA-5669034. TNFs bind their physiological receptors.

Names & Taxonomyi

Protein namesi
Recommended name:
Tumor necrosis factor ligand superfamily member 18
Alternative name(s):
Activation-inducible TNF-related ligand
Short name:
AITRL
Glucocorticoid-induced TNF-related ligand
Short name:
hGITRL
Gene namesi
Name:TNFSF18
Synonyms:AITRL, GITRL, TL6
ORF Names:UNQ149/PRO175
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:11932. TNFSF18.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini23 – 50CytoplasmicSequence analysisAdd BLAST28
Transmembranei51 – 71Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini72 – 199ExtracellularSequence analysisAdd BLAST128

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi8995.
OpenTargetsiENSG00000120337.
PharmGKBiPA36624.

Polymorphism and mutation databases

BioMutaiTNFSF18.
DMDMi325511353.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001855061 – 199Tumor necrosis factor ligand superfamily member 18Add BLAST199

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi80 ↔ 1001 Publication
Glycosylationi151N-linked (GlcNAc...)Sequence analysis1
Glycosylationi183N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9UNG2.
PeptideAtlasiQ9UNG2.
PRIDEiQ9UNG2.

Expressioni

Tissue specificityi

Expressed at high levels in the small intestine, ovary, testis, kidney and endothelial cells.

Inductioni

Up-regulated after stimulation by bacterial lipopolysaccharides (LPS).

Gene expression databases

BgeeiENSG00000120337.
CleanExiHS_TNFSF18.
ExpressionAtlasiQ9UNG2. baseline and differential.
GenevisibleiQ9UNG2. HS.

Organism-specific databases

HPAiHPA012699.

Interactioni

Subunit structurei

Homodimer (By similarity). Homotrimer.By similarity1 Publication

GO - Molecular functioni

  • receptor binding Source: ProtInc
  • tumor necrosis factor receptor superfamily binding Source: UniProtKB

Protein-protein interaction databases

DIPiDIP-29882N.
DIP-6243N.
STRINGi9606.ENSP00000385470.

Structurei

Secondary structure

1199
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi81 – 84Combined sources4
Beta strandi91 – 94Combined sources4
Beta strandi100 – 105Combined sources6
Beta strandi108 – 111Combined sources4
Beta strandi115 – 123Combined sources9
Beta strandi131 – 133Combined sources3
Beta strandi137 – 141Combined sources5
Beta strandi144 – 149Combined sources6
Beta strandi152 – 154Combined sources3
Beta strandi160 – 164Combined sources5
Beta strandi169 – 176Combined sources8
Helixi177 – 179Combined sources3
Beta strandi186 – 193Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2Q1MX-ray2.30A74-199[»]
2R30X-ray3.20A74-199[»]
2R32X-ray1.95A74-199[»]
3B93X-ray2.20A/B/C72-199[»]
3B94X-ray2.50A/B/C/D72-199[»]
ProteinModelPortaliQ9UNG2.
SMRiQ9UNG2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UNG2.

Family & Domainsi

Sequence similaritiesi

Belongs to the tumor necrosis factor family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410J65W. Eukaryota.
ENOG41117Z4. LUCA.
GeneTreeiENSGT00390000002560.
HOGENOMiHOG000026597.
HOVERGENiHBG061857.
InParanoidiQ9UNG2.
KOiK05479.
OMAiTYKEPAP.
OrthoDBiEOG091G0U1B.
PhylomeDBiQ9UNG2.
TreeFamiTF338614.

Family and domain databases

Gene3Di2.60.120.40. 1 hit.
InterProiIPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view]
SUPFAMiSSF49842. SSF49842. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9UNG2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLHPSPITC EFLFSTALIS PKMCLSHLEN MPLSHSRTQG AQRSSWKLWL
60 70 80 90 100
FCSIVMLLFL CSFSWLIFIF LQLETAKEPC MAKFGPLPSK WQMASSEPPC
110 120 130 140 150
VNKVSDWKLE ILQNGLYLIY GQVAPNANYN DVAPFEVRLY KNKDMIQTLT
160 170 180 190
NKSKIQNVGG TYELHVGDTI DLIFNSEHQV LKNNTYWGII LLANPQFIS
Length:199
Mass (Da):22,724
Last modified:March 8, 2011 - v2
Checksum:iC83A94645745DA58
GO

Sequence cautioni

The sequence AAH93986 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAI12033 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAQ89227 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAG36082 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence EAW90937 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL031599 Genomic DNA. Translation: CAP58846.1.
CH471067 Genomic DNA. Translation: EAW90937.1. Different initiation.
BC069111 mRNA. Translation: AAH69111.1.
BC069319 mRNA. Translation: AAH69319.1.
BC093986 mRNA. Translation: AAH93986.1. Different initiation.
BC112032 mRNA. Translation: AAI12033.1. Different initiation.
AK313273 mRNA. Translation: BAG36082.1. Different initiation.
AY358868 mRNA. Translation: AAQ89227.1. Different initiation.
AF125303 mRNA. Translation: AAD22634.1.
AF117713 mRNA. Translation: AAD19695.1.
CCDSiCCDS1305.2.
RefSeqiNP_005083.2. NM_005092.3.
UniGeneiHs.248197.

Genome annotation databases

EnsembliENST00000404377; ENSP00000385470; ENSG00000120337.
GeneIDi8995.
KEGGihsa:8995.
UCSCiuc001giu.3. human.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL031599 Genomic DNA. Translation: CAP58846.1.
CH471067 Genomic DNA. Translation: EAW90937.1. Different initiation.
BC069111 mRNA. Translation: AAH69111.1.
BC069319 mRNA. Translation: AAH69319.1.
BC093986 mRNA. Translation: AAH93986.1. Different initiation.
BC112032 mRNA. Translation: AAI12033.1. Different initiation.
AK313273 mRNA. Translation: BAG36082.1. Different initiation.
AY358868 mRNA. Translation: AAQ89227.1. Different initiation.
AF125303 mRNA. Translation: AAD22634.1.
AF117713 mRNA. Translation: AAD19695.1.
CCDSiCCDS1305.2.
RefSeqiNP_005083.2. NM_005092.3.
UniGeneiHs.248197.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2Q1MX-ray2.30A74-199[»]
2R30X-ray3.20A74-199[»]
2R32X-ray1.95A74-199[»]
3B93X-ray2.20A/B/C72-199[»]
3B94X-ray2.50A/B/C/D72-199[»]
ProteinModelPortaliQ9UNG2.
SMRiQ9UNG2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29882N.
DIP-6243N.
STRINGi9606.ENSP00000385470.

Polymorphism and mutation databases

BioMutaiTNFSF18.
DMDMi325511353.

Proteomic databases

PaxDbiQ9UNG2.
PeptideAtlasiQ9UNG2.
PRIDEiQ9UNG2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000404377; ENSP00000385470; ENSG00000120337.
GeneIDi8995.
KEGGihsa:8995.
UCSCiuc001giu.3. human.

Organism-specific databases

CTDi8995.
DisGeNETi8995.
GeneCardsiTNFSF18.
H-InvDBHIX0028550.
HGNCiHGNC:11932. TNFSF18.
HPAiHPA012699.
MIMi603898. gene.
neXtProtiNX_Q9UNG2.
OpenTargetsiENSG00000120337.
PharmGKBiPA36624.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410J65W. Eukaryota.
ENOG41117Z4. LUCA.
GeneTreeiENSGT00390000002560.
HOGENOMiHOG000026597.
HOVERGENiHBG061857.
InParanoidiQ9UNG2.
KOiK05479.
OMAiTYKEPAP.
OrthoDBiEOG091G0U1B.
PhylomeDBiQ9UNG2.
TreeFamiTF338614.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000120337-MONOMER.
ReactomeiR-HSA-5669034. TNFs bind their physiological receptors.

Miscellaneous databases

EvolutionaryTraceiQ9UNG2.
GeneWikiiTNFSF18.
GenomeRNAii8995.
PROiQ9UNG2.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000120337.
CleanExiHS_TNFSF18.
ExpressionAtlasiQ9UNG2. baseline and differential.
GenevisibleiQ9UNG2. HS.

Family and domain databases

Gene3Di2.60.120.40. 1 hit.
InterProiIPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view]
SUPFAMiSSF49842. SSF49842. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiTNF18_HUMAN
AccessioniPrimary (citable) accession number: Q9UNG2
Secondary accession number(s): A9IQG8, O95852, Q6ISV1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: March 8, 2011
Last modified: November 30, 2016
This is version 122 of the entry and version 2 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

Caution

It is uncertain whether Met-1 or Met-23 is the initiator.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.