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O35235

- TNF11_MOUSE

UniProt

O35235 - TNF11_MOUSE

Protein

Tumor necrosis factor ligand superfamily member 11

Gene

Tnfsf11

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    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. activation of JUN kinase activity Source: DFLAT
    2. bone resorption Source: MGI
    3. calcium ion homeostasis Source: MGI
    4. ERK1 and ERK2 cascade Source: DFLAT
    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 bone resorption Source: Ensembl
    15. positive regulation of corticotropin-releasing hormone secretion Source: BHF-UCL
    16. positive regulation of ERK1 and ERK2 cascade via TNFSF11-mediated signaling Source: Ensembl
    17. positive regulation of fever generation by positive regulation of prostaglandin secretion Source: BHF-UCL
    18. positive regulation of homotypic cell-cell adhesion Source: Ensembl
    19. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: MGI
    20. positive regulation of JNK cascade Source: MGI
    21. positive regulation of NF-kappaB transcription factor activity Source: Ensembl
    22. positive regulation of osteoclast development Source: MGI
    23. positive regulation of osteoclast differentiation Source: MGI
    24. positive regulation of phosphorylation Source: DFLAT
    25. positive regulation of protein kinase B signaling Source: MGI
    26. positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
    27. positive regulation of T cell activation Source: Ensembl
    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

    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

    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

    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 formPRO_0000034516Add
    BLAST
    Chaini139 – 316178Tumor necrosis factor ligand superfamily member 11, soluble formPRO_0000034517Add
    BLAST

    Amino acid modifications

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

    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.1 Publication

    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.4 Publications

    Protein-protein interaction databases

    DIPiDIP-59480N.
    IntActiO35235. 1 interaction.

    Structurei

    Secondary structure

    1
    316
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO35235.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 4848CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini70 – 316247ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei49 – 6921Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the tumor necrosis factor family.Curated

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti99 – 991D → G in AAC71061. (PubMed:9312132)Curated
    Sequence conflicti99 – 991D → G in AAC40113. (PubMed:9568710)Curated
    Sequence conflicti99 – 991D → G in BAA25425. (PubMed:9520411)Curated
    Sequence conflicti99 – 991D → G in BAA36970. (PubMed:10196481)Curated
    Sequence conflicti99 – 991D → G in BAA97257. (PubMed:11250921)Curated
    Sequence conflicti99 – 991D → G in BAA97259. (PubMed:11250921)Curated
    Sequence conflicti141 – 1433Missing in BAA36970. (PubMed:10196481)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 117117Missing in isoform 3. 1 PublicationVSP_006448Add
    BLAST
    Alternative sequencei14 – 4431SSEEM…APPPA → TP in isoform 2. 1 PublicationVSP_006449Add
    BLAST

    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

    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: October 1, 2014
    This is version 144 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

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