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O35235

- TNF11_MOUSE

UniProt

O35235 - TNF11_MOUSE

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Protein
Tumor necrosis factor ligand superfamily member 11
Gene
Tnfsf11, Opgl, Rankl, Trance
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Cytokine that binds to TNFRSF11B/OPG and to TNFRSF11A/RANK. Osteoclast differentiation and activation factor. Augments the ability of dendritic cells to stimulate naive T-cell proliferation. May be an important regulator of interactions between T-cells and dendritic cells and may play a role in the regulation of the T-cell-dependent immune response. May also play an important role in enhanced bone-resorption in humoral hypercalcemia of malignancy.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei138 – 1392Cleavage

GO - Molecular functioni

  1. protein binding Source: MGI
  2. tumor necrosis factor receptor superfamily binding Source: BHF-UCL

GO - Biological processi

  1. ERK1 and ERK2 cascade Source: DFLAT
  2. activation of JUN kinase activity Source: DFLAT
  3. bone resorption Source: MGI
  4. calcium ion homeostasis Source: MGI
  5. immune response Source: InterPro
  6. lymph node development Source: MGI
  7. mammary gland alveolus development Source: MGI
  8. mammary gland epithelial cell proliferation Source: MGI
  9. monocyte chemotaxis Source: Ensembl
  10. organ morphogenesis Source: MGI
  11. ossification Source: MGI
  12. osteoclast differentiation Source: UniProtKB
  13. osteoclast proliferation Source: MGI
  14. positive regulation of ERK1 and ERK2 cascade via TNFSF11-mediated signaling Source: Ensembl
  15. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: MGI
  16. positive regulation of JNK cascade Source: MGI
  17. positive regulation of NF-kappaB transcription factor activity Source: Ensembl
  18. positive regulation of T cell activation Source: Ensembl
  19. positive regulation of bone resorption Source: Ensembl
  20. positive regulation of corticotropin-releasing hormone secretion Source: BHF-UCL
  21. positive regulation of fever generation by positive regulation of prostaglandin secretion Source: BHF-UCL
  22. positive regulation of homotypic cell-cell adhesion Source: Ensembl
  23. positive regulation of osteoclast development Source: MGI
  24. positive regulation of osteoclast differentiation Source: MGI
  25. positive regulation of phosphorylation Source: DFLAT
  26. positive regulation of protein kinase B signaling Source: MGI
  27. positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  28. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  29. protein homooligomerization Source: MGI
  30. regulation of osteoclast differentiation Source: MGI
  31. tumor necrosis factor-mediated signaling pathway Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Cytokine, Developmental protein, Receptor

Keywords - Biological processi

Differentiation

Names & Taxonomyi

Protein namesi
Recommended name:
Tumor necrosis factor ligand superfamily member 11
Alternative name(s):
Osteoclast differentiation factor
Short name:
ODF
Osteoprotegerin ligand
Short name:
OPGL
Receptor activator of nuclear factor kappa-B ligand
Short name:
RANKL
TNF-related activation-induced cytokine
Short name:
TRANCE
CD_antigen: CD254
Cleaved into the following 2 chains:
Gene namesi
Name:Tnfsf11
Synonyms:Opgl, Rankl, Trance
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 14

Organism-specific databases

MGIiMGI:1100089. Tnfsf11.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4848Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei49 – 6921Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini70 – 316247Extracellular Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. extracellular space Source: UniProtKB-KW
  3. integral component of membrane Source: UniProtKB-KW
  4. intracellular Source: MGI
  5. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Secreted

Pathology & Biotechi

Involvement in diseasei

Deficiency in Tnfsf11 results in failure to form lobulo-alveolar mammary structures during pregnancy, resulting in death of newborns. Trance-deficient mice show severe osteopetrosis, with no osteoclasts, marrow spaces, or tooth eruption, and exhibit profound growth retardation at several skeletal sites, including the limbs, skull, and vertebrae and have marked chondrodysplasia, with thick, irregular growth plates and a relative increase in hypertrophic chondrocytes.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 316316Tumor necrosis factor ligand superfamily member 11, membrane form
PRO_0000034516Add
BLAST
Chaini139 – 316178Tumor necrosis factor ligand superfamily member 11, soluble form
PRO_0000034517Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi197 – 1971N-linked (GlcNAc...) Reviewed prediction
Glycosylationi262 – 2621N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

N-glycosylated.1 Publication
The soluble form of isoform 1 derives from the membrane form by proteolytic processing. The cleavage may be catalyzed by ADAM17. A further shorter soluble form was observed.

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiO35235.

PTM databases

PhosphoSiteiO35235.

Miscellaneous databases

PMAP-CutDBQ3TWY5.

Expressioni

Tissue specificityi

Highly expressed in thymus and lymph nodes, but not in non-lymphoid tissues and is abundantly expressed in T-cells but not in B-cells. A high level expression is also seen in the trabecular bone and lung.

Gene expression databases

BgeeiO35235.
GenevestigatoriO35235.

Interactioni

Subunit structurei

Homotrimer. Interacts with TNFRSF11A and TNFRSF11B.3 Publications

Protein-protein interaction databases

DIPiDIP-59480N.
IntActiO35235. 1 interaction.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi164 – 1696
Helixi171 – 1733
Beta strandi177 – 1793
Beta strandi181 – 1833
Beta strandi186 – 1905
Beta strandi194 – 2018
Beta strandi204 – 2074
Beta strandi211 – 22414
Helixi225 – 2273
Beta strandi233 – 24816
Beta strandi251 – 26212
Beta strandi265 – 28218
Beta strandi286 – 2938
Helixi295 – 2973
Turni302 – 3043
Beta strandi305 – 3139

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IQAX-ray2.20A/B/C157-316[»]
1JTZX-ray2.60X/Y/Z156-316[»]
1S55X-ray1.90A/B/C161-316[»]
3ME2X-ray2.80A158-316[»]
3QBQX-ray2.50A/C157-316[»]
4E4DX-ray2.70X162-316[»]
4GIQX-ray2.70A158-316[»]
ProteinModelPortaliO35235.
SMRiO35235. Positions 161-316.

Miscellaneous databases

EvolutionaryTraceiO35235.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG40842.
GeneTreeiENSGT00530000063443.
HOGENOMiHOG000132981.
HOVERGENiHBG054257.
InParanoidiQ3TWY5.
KOiK05473.
OMAiLIPDSCK.
OrthoDBiEOG7V4B0Q.
TreeFamiTF332169.

Family and domain databases

Gene3Di2.60.120.40. 1 hit.
InterProiIPR006052. TNF_dom.
IPR017355. TNF_ligand_10/11.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view]
PfamiPF00229. TNF. 1 hit.
[Graphical view]
PIRSFiPIRSF038013. TNF10_TNF11. 1 hit.
SMARTiSM00207. TNF. 1 hit.
[Graphical view]
SUPFAMiSSF49842. SSF49842. 1 hit.
PROSITEiPS50049. TNF_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O35235-1) [UniParc]FASTAAdd to Basket

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

MRRASRDYGK YLRSSEEMGS GPGVPHEGPL HPAPSAPAPA PPPAASRSMF    50
LALLGLGLGQ VVCSIALFLY FRAQMDPNRI SEDSTHCFYR ILRLHENADL 100
QDSTLESEDT LPDSCRRMKQ AFQGAVQKEL QHIVGPQRFS GAPAMMEGSW 150
LDVAQRGKPE AQPFAHLTIN AASIPSGSHK VTLSSWYHDR GWAKISNMTL 200
SNGKLRVNQD GFYYLYANIC FRHHETSGSV PTDYLQLMVY VVKTSIKIPS 250
SHNLMKGGST KNWSGNSEFH FYSINVGGFF KLRAGEEISI QVSNPSLLDP 300
DQDATYFGAF KVQDID 316
Length:316
Mass (Da):35,003
Last modified:July 27, 2011 - v2
Checksum:i8AF3825F92E0A786
GO
Isoform 2 (identifier: O35235-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     14-44: SSEEMGSGPGVPHEGPLHPAPSAPAPAPPPA → TP

Show »
Length:287
Mass (Da):32,293
Checksum:i09000919EB550530
GO
Isoform 3 (identifier: O35235-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-117: Missing.

Show »
Length:199
Mass (Da):22,150
Checksum:i401C13EB5E8CE166
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 117117Missing in isoform 3.
VSP_006448Add
BLAST
Alternative sequencei14 – 4431SSEEM…APPPA → TP in isoform 2.
VSP_006449Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti99 – 991D → G in AAC71061. 1 Publication
Sequence conflicti99 – 991D → G in AAC40113. 1 Publication
Sequence conflicti99 – 991D → G in BAA25425. 1 Publication
Sequence conflicti99 – 991D → G in BAA36970. 1 Publication
Sequence conflicti99 – 991D → G in BAA97257. 1 Publication
Sequence conflicti99 – 991D → G in BAA97259. 1 Publication
Sequence conflicti141 – 1433Missing in BAA36970. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF013170 mRNA. Translation: AAC71061.1.
AF019048 mRNA. Translation: AAB86812.1.
AF053713 mRNA. Translation: AAC40113.1.
AB008426 mRNA. Translation: BAA25425.1.
AB022039 Genomic DNA. Translation: BAA36970.1.
AB032771 mRNA. Translation: BAA97257.1.
AB032772 mRNA. Translation: BAA97258.1.
AB036798 mRNA. Translation: BAA97259.1.
AK159498 mRNA. Translation: BAE35131.1.
CCDSiCCDS27294.1. [O35235-1]
RefSeqiNP_035743.2. NM_011613.3. [O35235-1]
UniGeneiMm.249221.

Genome annotation databases

EnsembliENSMUST00000022592; ENSMUSP00000022592; ENSMUSG00000022015. [O35235-1]
GeneIDi21943.
KEGGimmu:21943.
UCSCiuc007ush.1. mouse. [O35235-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF013170 mRNA. Translation: AAC71061.1 .
AF019048 mRNA. Translation: AAB86812.1 .
AF053713 mRNA. Translation: AAC40113.1 .
AB008426 mRNA. Translation: BAA25425.1 .
AB022039 Genomic DNA. Translation: BAA36970.1 .
AB032771 mRNA. Translation: BAA97257.1 .
AB032772 mRNA. Translation: BAA97258.1 .
AB036798 mRNA. Translation: BAA97259.1 .
AK159498 mRNA. Translation: BAE35131.1 .
CCDSi CCDS27294.1. [O35235-1 ]
RefSeqi NP_035743.2. NM_011613.3. [O35235-1 ]
UniGenei Mm.249221.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1IQA X-ray 2.20 A/B/C 157-316 [» ]
1JTZ X-ray 2.60 X/Y/Z 156-316 [» ]
1S55 X-ray 1.90 A/B/C 161-316 [» ]
3ME2 X-ray 2.80 A 158-316 [» ]
3QBQ X-ray 2.50 A/C 157-316 [» ]
4E4D X-ray 2.70 X 162-316 [» ]
4GIQ X-ray 2.70 A 158-316 [» ]
ProteinModelPortali O35235.
SMRi O35235. Positions 161-316.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-59480N.
IntActi O35235. 1 interaction.

PTM databases

PhosphoSitei O35235.

Proteomic databases

PRIDEi O35235.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000022592 ; ENSMUSP00000022592 ; ENSMUSG00000022015 . [O35235-1 ]
GeneIDi 21943.
KEGGi mmu:21943.
UCSCi uc007ush.1. mouse. [O35235-1 ]

Organism-specific databases

CTDi 8600.
MGIi MGI:1100089. Tnfsf11.

Phylogenomic databases

eggNOGi NOG40842.
GeneTreei ENSGT00530000063443.
HOGENOMi HOG000132981.
HOVERGENi HBG054257.
InParanoidi Q3TWY5.
KOi K05473.
OMAi LIPDSCK.
OrthoDBi EOG7V4B0Q.
TreeFami TF332169.

Miscellaneous databases

ChiTaRSi TNFSF11. mouse.
EvolutionaryTracei O35235.
NextBioi 301584.
PMAP-CutDB Q3TWY5.
PROi O35235.
SOURCEi Search...

Gene expression databases

Bgeei O35235.
Genevestigatori O35235.

Family and domain databases

Gene3Di 2.60.120.40. 1 hit.
InterProi IPR006052. TNF_dom.
IPR017355. TNF_ligand_10/11.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view ]
Pfami PF00229. TNF. 1 hit.
[Graphical view ]
PIRSFi PIRSF038013. TNF10_TNF11. 1 hit.
SMARTi SM00207. TNF. 1 hit.
[Graphical view ]
SUPFAMi SSF49842. SSF49842. 1 hit.
PROSITEi PS50049. TNF_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "TRANCE is a novel ligand of the tumor necrosis factor receptor family that activates c-Jun N-terminal kinase in T cells."
    Wong B.R., Rho J., Arron J., Robinson E., Orlinick J., Chao M., Kalachikov S., Cayani E., Bartlett F.S. III, Frankel W.N., Lee S.Y., Choi Y.
    J. Biol. Chem. 272:25190-25194(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Hybridoma.
  2. "A homologue of the TNF receptor and its ligand enhance T-cell growth and dendritic-cell function."
    Anderson D.M., Maraskovsky E., Billingsley W.L., Dougall W.C., Tometsko M.E., Roux E.R., Teepe M.C., DuBose R.F., Cosman D., Galibert L.
    Nature 390:175-179(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Thymic lymphoma.
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Bone marrow.
  4. "Osteoclast differentiation factor is a ligand for osteoprotegerin/osteoclastogenesis-inhibitory factor and is identical to TRANCE/RANKL."
    Yasuda H., Shima N., Nakagawa N., Yamaguchi K., Kinosaki M., Mochizuki S., Tomoyasu A., Yano K., Goto M., Murakami A., Tsuda E., Morinaga T., Higashio K., Udagawa N., Takahashi N., Suda T.
    Proc. Natl. Acad. Sci. U.S.A. 95:3597-3602(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Bone marrow stroma.
  5. "Cloning and characterization of the gene encoding mouse osteoclast differentiation factor."
    Kodaira K., Kodaira K., Mizuno A., Yasuda H., Shima N., Murakami A., Ueda M., Higashio K.
    Gene 230:121-127(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    Strain: 129.
  6. "Determination of three isoforms of the receptor activator of nuclear factor-kappaB ligand and their differential expression in bone and thymus."
    Ikeda T., Kasai M., Utsuyama M., Hirokawa K.
    Endocrinology 142:1419-1426(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
  7. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
  8. "Evidence for a role of a tumor necrosis factor-alpha (TNF-alpha)-converting enzyme-like protease in shedding of TRANCE, a TNF family member involved in osteoclastogenesis and dendritic cell survival."
    Lum L., Wong B.R., Josien R., Becherer J.D., Erdjument-Bromage H., Schloendorff J., Tempst P., Choi Y., Blobel C.P.
    J. Biol. Chem. 274:13613-13618(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 139-147, PROTEOLYTIC PROCESSING, GLYCOSYLATION.
  9. "Crystal structure of the TRANCE/RANKL cytokine reveals determinants of receptor-ligand specificity."
    Lam J., Nelson C.A., Ross F.P., Teitelbaum S.L., Fremont D.H.
    J. Clin. Invest. 108:971-979(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 158-316, SUBUNIT.
  10. "Crystal structure of the extracellular domain of mouse RANK ligand at 2.2-A resolution."
    Ito S., Wakabayashi K., Ubukata O., Hayashi S., Okada F., Hata T.
    J. Biol. Chem. 277:6631-6636(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 137-316, SUBUNIT.
  11. "Structural and functional insights of RANKL-RANK interaction and signaling."
    Liu C., Walter T.S., Huang P., Zhang S., Zhu X., Wu Y., Wedderburn L.R., Tang P., Owens R.J., Stuart D.I., Ren J., Gao B.
    J. Immunol. 184:6910-6919(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 158-316 IN COMPLEX WITH TNFRSF11A, INTERACTION WITH TNFRSF11A, SUBUNIT.
  12. "RANKL employs distinct binding modes to engage RANK and the osteoprotegerin decoy receptor."
    Nelson C.A., Warren J.T., Wang M.W., Teitelbaum S.L., Fremont D.H.
    Structure 20:1971-1982(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 162-316 IN COMPLEX WITH TNFRSF11B.

Entry informationi

Entry nameiTNF11_MOUSE
AccessioniPrimary (citable) accession number: O35235
Secondary accession number(s): O35306
, Q3TWY5, Q9JJK8, Q9JJK9, Q9R1Y0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi