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P36941 (TNR3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Tumor necrosis factor receptor superfamily member 3
Alternative name(s):
Lymphotoxin-beta receptor
Tumor necrosis factor C receptor
Tumor necrosis factor receptor 2-related protein
Tumor necrosis factor receptor type III
Short name=TNF-RIII
Short name=TNFR-III
Gene names
Name:LTBR
Synonyms:D12S370, TNFCR, TNFR3, TNFRSF3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length435 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for the heterotrimeric lymphotoxin containing LTA and LTB, and for TNFS14/LIGHT. Promotes apoptosis via TRAF3 and TRAF5. May play a role in the development of lymphoid organs. Ref.4 Ref.6

Subunit structure

Self-associates. Associates with TRAF3, TRAF4 and TRAF5. Interacts with HCV core protein. Ref.7 Ref.8 Ref.9 Ref.10

Subcellular location

Membrane; Single-pass type I membrane protein.

Sequence similarities

Contains 4 TNFR-Cys repeats.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-3509981,EBI-3509981
ZMYND11Q153265EBI-3509981,EBI-2799565

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Potential
Chain31 – 435405Tumor necrosis factor receptor superfamily member 3
PRO_0000034552

Regions

Topological domain31 – 227197Extracellular Potential
Transmembrane228 – 24821Helical; Potential
Topological domain249 – 435187Cytoplasmic Potential
Repeat42 – 8140TNFR-Cys 1
Repeat82 – 12443TNFR-Cys 2
Repeat125 – 16844TNFR-Cys 3
Repeat169 – 21143TNFR-Cys 4

Amino acid modifications

Modified residue3231Phosphoserine Ref.11
Glycosylation401N-linked (GlcNAc...) Potential
Glycosylation1771N-linked (GlcNAc...) Potential
Disulfide bond43 ↔ 58 By similarity
Disulfide bond59 ↔ 72 By similarity
Disulfide bond62 ↔ 80 By similarity
Disulfide bond83 ↔ 98 By similarity
Disulfide bond101 ↔ 116 By similarity
Disulfide bond104 ↔ 124 By similarity
Disulfide bond126 ↔ 132 By similarity
Disulfide bond139 ↔ 148 By similarity
Disulfide bond142 ↔ 167 By similarity
Disulfide bond170 ↔ 185 By similarity

Natural variations

Natural variant2741V → I.
Corresponds to variant rs35681405 [ dbSNP | Ensembl ].
VAR_052346

Sequences

Sequence LengthMass (Da)Tools
P36941 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 624626E6022F656F

FASTA43546,709
        10         20         30         40         50         60 
MLLPWATSAP GLAWGPLVLG LFGLLAASQP QAVPPYASEN QTCRDQEKEY YEPQHRICCS 

        70         80         90        100        110        120 
RCPPGTYVSA KCSRIRDTVC ATCAENSYNE HWNYLTICQL CRPCDPVMGL EEIAPCTSKR 

       130        140        150        160        170        180 
KTQCRCQPGM FCAAWALECT HCELLSDCPP GTEAELKDEV GKGNNHCVPC KAGHFQNTSS 

       190        200        210        220        230        240 
PSARCQPHTR CENQGLVEAA PGTAQSDTTC KNPLEPLPPE MSGTMLMLAV LLPLAFFLLL 

       250        260        270        280        290        300 
ATVFSCIWKS HPSLCRKLGS LLKRRPQGEG PNPVAGSWEP PKAHPYFPDL VQPLLPISGD 

       310        320        330        340        350        360 
VSPVSTGLPA APVLEAGVPQ QQSPLDLTRE PQLEPGEQSQ VAHGTNGIHV TGGSMTITGN 

       370        380        390        400        410        420 
IYIYNGPVLG GPPGPGDLPA TPEPPYPIPE EGDPGPPGLS TPHQEDGKAW HLAETEHCGA 

       430 
TPSNRGPRNQ FITHD 

« Hide

References

« Hide 'large scale' references
[1]"Construction and evaluation of a hncDNA library of human 12p transcribed sequences derived from a somatic cell hybrid."
Baens M., Chaffanet M., Cassiman J.-J., van den Berghe H., Marynen P.
Genomics 16:214-218(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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.
[4]"A lymphotoxin-beta-specific receptor."
Crowe P.D., VanArsdale T.L., Walter B.N., Ware C.F., Hession C., Ehrenfels B., Browning J.L., Din W.S., Goodwin R.G., Smith C.A.
Science 264:707-710(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"The cytoplasmic domain of the lymphotoxin-beta receptor mediates cell death in HeLa cells."
Wu M.-Y., Wang P.-Y., Han S.-H., Hsieh S.-L.
J. Biol. Chem. 274:11868-11873(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[6]"The lymphotoxin-beta receptor is necessary and sufficient for LIGHT-mediated apoptosis of tumor cells."
Rooney I.A., Butrovich K.D., Glass A.A., Borboroglu S., Benedict C.A., Whitbeck J.C., Cohen G.H., Eisenberg R.J., Ware C.F.
J. Biol. Chem. 275:14307-14315(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"TRAF5, an activator of NF-kappaB and putative signal transducer for the lymphotoxin-beta receptor."
Nakano H., Oshima H., Chung W., Williams-Abbott L., Ware C.F., Yagita H., Okumura K.
J. Biol. Chem. 271:14661-14664(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRAF3.
[8]"Hepatitis C virus core protein interacts with the cytoplasmic tail of lymphotoxin-beta receptor."
Matsumoto M., Hsieh T.-Y., Zhu N., VanArsdale T., Hwang S.B., Jeng K.-S., Gorbalenya A.E., Lo S.-Y., Ou J.-H., Ware C.F., Lai M.M.C.
J. Virol. 71:1301-1309(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HCV CORE PROTEIN.
[9]"TRAF-4 expression in epithelial progenitor cells. Analysis in normal adult, fetal, and tumor tissues."
Krajewska M., Krajewski S., Zapata J.M., VanArsdale T., Gascoyne R.D., Berern K., McFadden D., Shabaik A., Hugh J., Reynolds A., Clevenger C.V., Reed J.C.
Am. J. Pathol. 152:1549-1561(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRAF4.
[10]"Cloning and characterization of a cDNA encoding the human homolog of tumor necrosis factor receptor-associated factor 5 (TRAF5)."
Mizushima S., Fujita M., Ishida T., Azuma S., Kato K., Hirai M., Otsuka M., Yamamoto T., Inoue J.
Gene 207:135-140(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRAF5.
[11]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[12]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L04270 mRNA. Translation: AAA36757.1.
CH471116 Genomic DNA. Translation: EAW88801.1.
CH471116 Genomic DNA. Translation: EAW88802.1.
BC026262 mRNA. Translation: AAH26262.1.
IPIIPI00006097.
PIRI54182.
RefSeqNP_001257916.1. NM_001270987.1.
NP_002333.1. NM_002342.2.
UniGeneHs.1116.
Hs.591047.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1RF3X-ray3.50B385-408[»]
ProteinModelPortalP36941.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-2928N.
IntActP36941. 6 interactions.
STRING9606.ENSP00000228918.

PTM databases

PhosphoSiteP36941.

Polymorphism databases

DMDM549090.

Proteomic databases

PaxDbP36941.
PeptideAtlasP36941.
PRIDEP36941.

Protocols and materials databases

DNASU4055.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000228918; ENSP00000228918; ENSG00000111321.
GeneID4055.
KEGGhsa:4055.
UCSCuc001qny.1. human.

Organism-specific databases

CTD4055.
GeneCardsGC12P006467.
HGNCHGNC:6718. LTBR.
HPACAB026202.
MIM600979. gene.
neXtProtNX_P36941.
PharmGKBPA30481.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG38845.
HOGENOMHOG000294180.
HOVERGENHBG023187.
InParanoidP36941.
KOK03159.
OMATVTGNIY.
OrthoDBEOG41ZFC0.
PhylomeDBP36941.

Gene expression databases

ArrayExpressP36941.
BgeeP36941.
CleanExHS_LTBR.
GenevestigatorP36941.
GermOnlineENSG00000111321. Homo sapiens.

Family and domain databases

InterProIPR001368. TNFR/NGFR_Cys_rich_reg.
IPR017349. TNFR_3_LTBR.
[Graphical view]
PfamPF00020. TNFR_c6. 2 hits.
[Graphical view]
PIRSFPIRSF037999. TNFR_3_LTBR. 1 hit.
PRINTSPR01920. TNFACTORR3.
SMARTSM00208. TNFR. 4 hits.
[Graphical view]
PROSITEPS00652. TNFR_NGFR_1. 2 hits.
PS50050. TNFR_NGFR_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChEMBLCHEMBL1250360.
ChiTaRSLTBR. human.
EvolutionaryTraceP36941.
GenomeRNAi4055.
NextBio15888.
SOURCESearch...

Entry information

Entry nameTNR3_HUMAN
AccessionPrimary (citable) accession number: P36941
Secondary accession number(s): D3DUR2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: May 1, 2013
This is version 130 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.

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Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families