Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P41273 (TNFL9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tumor necrosis factor ligand superfamily member 9
Alternative name(s):
4-1BB ligand
Short name=4-1BBL
Gene names
Name:TNFSF9
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length254 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cytokine that binds to TNFRSF9. Induces the proliferation of activated peripheral blood T-cells. May have a role in activation-induced cell death (AICD). May play a role in cognate interactions between T-cells and B-cells/macrophages. Ref.3

Subunit structure

Homotrimer. Ref.3

Subcellular location

Membrane; Single-pass type II membrane protein.

Tissue specificity

Expressed in brain, placenta, lung, skeletal muscle and kidney.

Sequence similarities

Belongs to the tumor necrosis factor family.

Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   Molecular functionCytokine
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Traceable author statement Ref.1. Source: ProtInc

cell proliferation

Traceable author statement Ref.1. Source: ProtInc

cell-cell signaling

Traceable author statement Ref.1. Source: ProtInc

immune response

Inferred from electronic annotation. Source: InterPro

myeloid dendritic cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of activated T cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of cytotoxic T cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of interferon-gamma production

Inferred from electronic annotation. Source: Ensembl

positive regulation of interleukin-12 production

Inferred from electronic annotation. Source: Ensembl

positive regulation of interleukin-6 production

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentextracellular space

Inferred from electronic annotation. Source: UniProtKB-KW

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionreceptor binding

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 254254Tumor necrosis factor ligand superfamily member 9
PRO_0000185501

Regions

Topological domain1 – 2828Cytoplasmic Potential
Transmembrane29 – 4921Helical; Signal-anchor for type II membrane protein; Potential
Topological domain50 – 254205Extracellular Potential
Compositional bias35 – 417Poly-Leu

Natural variations

Natural variant171P → A.
Corresponds to variant rs442511 [ dbSNP | Ensembl ].
VAR_011928

Secondary structure

............................. 254
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P41273 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 827551F34563E508

FASTA25426,625
        10         20         30         40         50         60 
MEYASDASLD PEAPWPPAPR ARACRVLPWA LVAGLLLLLL LAAACAVFLA CPWAVSGARA 

        70         80         90        100        110        120 
SPGSAASPRL REGPELSPDD PAGLLDLRQG MFAQLVAQNV LLIDGPLSWY SDPGLAGVSL 

       130        140        150        160        170        180 
TGGLSYKEDT KELVVAKAGV YYVFFQLELR RVVAGEGSGS VSLALHLQPL RSAAGAAALA 

       190        200        210        220        230        240 
LTVDLPPASS EARNSAFGFQ GRLLHLSAGQ RLGVHLHTEA RARHAWQLTQ GATVLGLFRV 

       250 
TPEIPAGLPS PRSE 

« Hide

References

« Hide 'large scale' references
[1]"Molecular and biological characterization of human 4-1BB and its ligand."
Alderson M.R., Smith C.A., Tough T.W., Davis-Smith T., Armitage R.J., Falk B., Roux E., Baker E., Sutherland G.R., Din W.S., Goodwin R.G.
Eur. J. Immunol. 24:2219-2227(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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].
Tissue: Lung.
[3]"The structure of the trimer of human 4-1BB ligand is unique among members of the tumor necrosis factor superfamily."
Won E.Y., Cha K., Byun J.S., Kim D.U., Shin S., Ahn B., Kim Y.H., Rice A.J., Walz T., Kwon B.S., Cho H.S.
J. Biol. Chem. 285:9202-9210(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 80-246, FUNCTION, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U03398 mRNA. Translation: AAA53134.1.
BC104805 mRNA. Translation: AAI04806.1.
BC104807 mRNA. Translation: AAI04808.1.
PIRI38427.
RefSeqNP_003802.1. NM_003811.3.
UniGeneHs.1524.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2X29X-ray2.30A80-246[»]
ProteinModelPortalP41273.
SMRP41273. Positions 80-246.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114281. 6 interactions.
DIPDIP-3020N.
STRING9606.ENSP00000245817.

PTM databases

PhosphoSiteP41273.

Polymorphism databases

DMDM728739.

Proteomic databases

PaxDbP41273.
PRIDEP41273.

Protocols and materials databases

DNASU8744.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000245817; ENSP00000245817; ENSG00000125657.
GeneID8744.
KEGGhsa:8744.
UCSCuc002mfh.2. human.

Organism-specific databases

CTD8744.
GeneCardsGC19P006531.
HGNCHGNC:11939. TNFSF9.
HPAHPA041376.
MIM606182. gene.
neXtProtNX_P41273.
PharmGKBPA36629.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG41045.
HOGENOMHOG000154658.
HOVERGENHBG079273.
InParanoidP41273.
KOK05472.
OMANSAFGFR.
OrthoDBEOG7HQNB2.
PhylomeDBP41273.
TreeFamTF338523.

Gene expression databases

BgeeP41273.
CleanExHS_TNFSF9.
GenevestigatorP41273.

Family and domain databases

Gene3D2.60.120.40. 1 hit.
InterProIPR021184. TNF_CS.
IPR006052. TNF_dom.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view]
PfamPF00229. TNF. 1 hit.
[Graphical view]
SMARTSM00207. TNF. 1 hit.
[Graphical view]
SUPFAMSSF49842. SSF49842. 1 hit.
PROSITEPS00251. TNF_1. 1 hit.
PS50049. TNF_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTNFSF9. human.
EvolutionaryTraceP41273.
GenomeRNAi8744.
NextBio32809.
PROP41273.
SOURCESearch...

Entry information

Entry nameTNFL9_HUMAN
AccessionPrimary (citable) accession number: P41273
Secondary accession number(s): Q2M3S2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: February 19, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM