Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O00300

- TR11B_HUMAN

UniProt

O00300 - TR11B_HUMAN

Protein

Tumor necrosis factor receptor superfamily member 11B

Gene

TNFRSF11B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 3 (08 Feb 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Acts as decoy receptor for TNFSF11/RANKL and thereby neutralizes its function in osteoclastogenesis. Inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local ratio between TNFSF11 and TNFRSF11B. May also play a role in preventing arterial calcification. May act as decoy receptor for TNFSF10/TRAIL and protect against apoptosis. TNFSF10/TRAIL binding blocks the inhibition of osteoclastogenesis.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei400 – 4001Involved in dimerization

    GO - Molecular functioni

    1. cytokine activity Source: ProtInc
    2. receptor activity Source: ProtInc

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. extracellular matrix organization Source: Ensembl
    3. negative regulation of bone resorption Source: Ensembl
    4. negative regulation of odontogenesis of dentin-containing tooth Source: Ensembl
    5. response to arsenic-containing substance Source: Ensembl
    6. response to drug Source: Ensembl
    7. response to estrogen Source: Ensembl
    8. response to magnesium ion Source: Ensembl
    9. response to nutrient Source: Ensembl
    10. signal transduction Source: ProtInc
    11. skeletal system development Source: ProtInc

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Apoptosis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tumor necrosis factor receptor superfamily member 11B
    Alternative name(s):
    Osteoclastogenesis inhibitory factor
    Osteoprotegerin
    Gene namesi
    Name:TNFRSF11B
    Synonyms:OCIF, OPG
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:11909. TNFRSF11B.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: ProtInc
    2. extracellular space Source: BHF-UCL
    3. proteinaceous extracellular matrix Source: Ensembl

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Juvenile Paget disease (JPD) [MIM:239000]: Rare autosomal recessive osteopathy that presents in infancy or early childhood. The disorder is characterized by rapidly remodeling woven bone, osteopenia, debilitating fractures, and deformities due to a markedly accelerated rate of bone remodeling throughout the skeleton. Approximately 40 cases of JPD have been reported worldwide. Unless it is treated with drugs that block osteoclast-mediated skeletal resorption, the disease can be fatal.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti182 – 1821Missing in JPD. 1 Publication
    VAR_019413

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi78 – 792DE → AA: Decreases inhibition of osteoclast differentiation.
    Mutagenesisi116 – 1161E → A: Reduces affinity for TNFSF11. Decreases inhibition of osteoclast differentiation. 1 Publication
    Mutagenesisi400 – 4012Missing: Abolishes dimerization. 1 Publication
    Mutagenesisi400 – 4001C → S: Abolishes dimerization. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi239000. phenotype.
    Orphaneti2801. Juvenile Paget disease.
    PharmGKBiPA36602.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 21212 PublicationsAdd
    BLAST
    Chaini22 – 401380Tumor necrosis factor receptor superfamily member 11BPRO_0000034587Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi41 ↔ 541 PublicationPROSITE-ProRule annotation
    Disulfide bondi44 ↔ 621 PublicationPROSITE-ProRule annotation
    Disulfide bondi65 ↔ 801 PublicationPROSITE-ProRule annotation
    Disulfide bondi83 ↔ 971 PublicationPROSITE-ProRule annotation
    Disulfide bondi87 ↔ 1051 PublicationPROSITE-ProRule annotation
    Glycosylationi98 – 981N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi107 ↔ 1181 PublicationPROSITE-ProRule annotation
    Disulfide bondi124 ↔ 1421 PublicationPROSITE-ProRule annotation
    Disulfide bondi145 ↔ 1601 PublicationPROSITE-ProRule annotation
    Glycosylationi152 – 1521N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi165 – 1651N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi166 ↔ 1851 PublicationPROSITE-ProRule annotation
    Glycosylationi178 – 1781N-linked (GlcNAc...)1 Publication
    Glycosylationi289 – 2891N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated. Contains sialic acid residues.1 Publication
    The N-terminus is blocked.

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiO00300.
    PRIDEiO00300.

    PTM databases

    PhosphoSiteiO00300.

    Expressioni

    Tissue specificityi

    Highly expressed in adult lung, heart, kidney, liver, spleen, thymus, prostate, ovary, small intestine, thyroid, lymph node, trachea, adrenal gland, testis, and bone marrow. Detected at very low levels in brain, placenta and skeletal muscle. Highly expressed in fetal kidney, liver and lung.

    Inductioni

    Up-regulated by increasing calcium-concentration in the medium and estrogens. Down-regulated by glucocorticoids.

    Gene expression databases

    ArrayExpressiO00300.
    BgeeiO00300.
    CleanExiHS_TNFRSF11B.
    GenevestigatoriO00300.

    Organism-specific databases

    HPAiHPA027013.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with TNFSF10 and TNFSF11.2 Publications

    Protein-protein interaction databases

    BioGridi111028. 2 interactions.
    STRINGi9606.ENSP00000297350.

    Structurei

    Secondary structure

    1
    401
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi29 – 313
    Beta strandi35 – 373
    Beta strandi40 – 423
    Beta strandi48 – 525
    Beta strandi56 – 583
    Beta strandi61 – 644
    Beta strandi91 – 955
    Beta strandi99 – 1013
    Beta strandi104 – 1074
    Beta strandi111 – 1144
    Beta strandi117 – 1204
    Beta strandi128 – 1325
    Beta strandi136 – 1383
    Beta strandi141 – 1444
    Beta strandi155 – 1573
    Beta strandi167 – 1715

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3URFX-ray2.70Z22-186[»]
    ProteinModelPortaliO00300.
    SMRiO00300. Positions 26-186.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati24 – 6239TNFR-Cys 1Add
    BLAST
    Repeati65 – 10541TNFR-Cys 2Add
    BLAST
    Repeati107 – 14236TNFR-Cys 3Add
    BLAST
    Repeati145 – 18541TNFR-Cys 4Add
    BLAST
    Domaini198 – 26972Death 1Add
    BLAST
    Domaini270 – 36596Death 2Add
    BLAST

    Sequence similaritiesi

    Contains 2 death domains.Curated
    Contains 4 TNFR-Cys repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG80702.
    HOGENOMiHOG000273896.
    HOVERGENiHBG061495.
    InParanoidiO00300.
    KOiK05148.
    OMAiDIDLCEN.
    OrthoDBiEOG786H2Q.
    PhylomeDBiO00300.
    TreeFamiTF331157.

    Family and domain databases

    Gene3Di1.10.533.10. 1 hit.
    InterProiIPR011029. DEATH-like_dom.
    IPR000488. Death_domain.
    IPR001368. TNFR/NGFR_Cys_rich_reg.
    IPR022323. TNFR_11.
    IPR017371. TNFR_11B.
    [Graphical view]
    PfamiPF00531. Death. 1 hit.
    PF00020. TNFR_c6. 2 hits.
    [Graphical view]
    PIRSFiPIRSF038065. TNFR_11B. 1 hit.
    PRINTSiPR01961. TNFACTORR11.
    PR01975. TNFACTORR11B.
    SMARTiSM00208. TNFR. 4 hits.
    [Graphical view]
    SUPFAMiSSF47986. SSF47986. 2 hits.
    PROSITEiPS00652. TNFR_NGFR_1. 1 hit.
    PS50050. TNFR_NGFR_2. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    O00300-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNNLLCCALV FLDISIKWTT QETFPPKYLH YDEETSHQLL CDKCPPGTYL    50
    KQHCTAKWKT VCAPCPDHYY TDSWHTSDEC LYCSPVCKEL QYVKQECNRT 100
    HNRVCECKEG RYLEIEFCLK HRSCPPGFGV VQAGTPERNT VCKRCPDGFF 150
    SNETSSKAPC RKHTNCSVFG LLLTQKGNAT HDNICSGNSE STQKCGIDVT 200
    LCEEAFFRFA VPTKFTPNWL SVLVDNLPGT KVNAESVERI KRQHSSQEQT 250
    FQLLKLWKHQ NKDQDIVKKI IQDIDLCENS VQRHIGHANL TFEQLRSLME 300
    SLPGKKVGAE DIEKTIKACK PSDQILKLLS LWRIKNGDQD TLKGLMHALK 350
    HSKTYHFPKT VTQSLKKTIR FLHSFTMYKL YQKLFLEMIG NQVQSVKISC 400
    L 401
    Length:401
    Mass (Da):46,026
    Last modified:February 8, 2011 - v3
    Checksum:i2A23AC07BFA1E2DE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti263 – 2631D → A in AAB53709. (PubMed:9108485)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti3 – 31N → K.5 Publications
    Corresponds to variant rs2073618 [ dbSNP | Ensembl ].
    VAR_013439
    Natural varianti104 – 1041V → M.1 Publication
    Corresponds to variant rs11573906 [ dbSNP | Ensembl ].
    VAR_018957
    Natural varianti182 – 1821Missing in JPD. 1 Publication
    VAR_019413

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U94332 mRNA. Translation: AAB53709.1.
    AB002146 mRNA. Translation: BAA25910.1.
    AB008822 Genomic DNA. Translation: BAA32076.1.
    AK313710 mRNA. Translation: BAG36455.1.
    AK223155 mRNA. Translation: BAD96875.1.
    AY466112 Genomic DNA. Translation: AAR23265.1.
    AC107953 Genomic DNA. No translation available.
    AP004283 Genomic DNA. No translation available.
    BC030155 mRNA. Translation: AAH30155.1.
    AF134187 mRNA. Translation: AAF20168.1.
    CCDSiCCDS6326.1.
    RefSeqiNP_002537.3. NM_002546.3.
    UniGeneiHs.81791.

    Genome annotation databases

    EnsembliENST00000297350; ENSP00000297350; ENSG00000164761.
    GeneIDi4982.
    KEGGihsa:4982.
    UCSCiuc003yon.4. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U94332 mRNA. Translation: AAB53709.1 .
    AB002146 mRNA. Translation: BAA25910.1 .
    AB008822 Genomic DNA. Translation: BAA32076.1 .
    AK313710 mRNA. Translation: BAG36455.1 .
    AK223155 mRNA. Translation: BAD96875.1 .
    AY466112 Genomic DNA. Translation: AAR23265.1 .
    AC107953 Genomic DNA. No translation available.
    AP004283 Genomic DNA. No translation available.
    BC030155 mRNA. Translation: AAH30155.1 .
    AF134187 mRNA. Translation: AAF20168.1 .
    CCDSi CCDS6326.1.
    RefSeqi NP_002537.3. NM_002546.3.
    UniGenei Hs.81791.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3URF X-ray 2.70 Z 22-186 [» ]
    ProteinModelPortali O00300.
    SMRi O00300. Positions 26-186.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111028. 2 interactions.
    STRINGi 9606.ENSP00000297350.

    PTM databases

    PhosphoSitei O00300.

    Proteomic databases

    PaxDbi O00300.
    PRIDEi O00300.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000297350 ; ENSP00000297350 ; ENSG00000164761 .
    GeneIDi 4982.
    KEGGi hsa:4982.
    UCSCi uc003yon.4. human.

    Organism-specific databases

    CTDi 4982.
    GeneCardsi GC08M119935.
    H-InvDB HIX0007748.
    HGNCi HGNC:11909. TNFRSF11B.
    HPAi HPA027013.
    MIMi 239000. phenotype.
    602643. gene.
    neXtProti NX_O00300.
    Orphaneti 2801. Juvenile Paget disease.
    PharmGKBi PA36602.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG80702.
    HOGENOMi HOG000273896.
    HOVERGENi HBG061495.
    InParanoidi O00300.
    KOi K05148.
    OMAi DIDLCEN.
    OrthoDBi EOG786H2Q.
    PhylomeDBi O00300.
    TreeFami TF331157.

    Miscellaneous databases

    GeneWikii Osteoprotegerin.
    GenomeRNAii 4982.
    NextBioi 19182.
    PROi O00300.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O00300.
    Bgeei O00300.
    CleanExi HS_TNFRSF11B.
    Genevestigatori O00300.

    Family and domain databases

    Gene3Di 1.10.533.10. 1 hit.
    InterProi IPR011029. DEATH-like_dom.
    IPR000488. Death_domain.
    IPR001368. TNFR/NGFR_Cys_rich_reg.
    IPR022323. TNFR_11.
    IPR017371. TNFR_11B.
    [Graphical view ]
    Pfami PF00531. Death. 1 hit.
    PF00020. TNFR_c6. 2 hits.
    [Graphical view ]
    PIRSFi PIRSF038065. TNFR_11B. 1 hit.
    PRINTSi PR01961. TNFACTORR11.
    PR01975. TNFACTORR11B.
    SMARTi SM00208. TNFR. 4 hits.
    [Graphical view ]
    SUPFAMi SSF47986. SSF47986. 2 hits.
    PROSITEi PS00652. TNFR_NGFR_1. 1 hit.
    PS50050. TNFR_NGFR_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LYS-3.
      Tissue: Kidney.
    2. "Identity of osteoclastogenesis inhibitory factor (OCIF) and osteoprotegerin (OPG): a mechanism by which OPG/OCIF inhibits osteoclastogenesis in vitro."
      Yasuda H., Shima N., Nakagawa N., Mochizuki S., Yano K., Fujise N., Sato Y., Goto M., Yamaguchi K., Kuriyama M., Kanno T., Murakami A., Tsuda E., Morinaga T., Higashio K.
      Endocrinology 139:1329-1337(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LYS-3.
      Tissue: Lung cancer.
    3. "Cloning and characterization of the gene encoding human osteoprotegerin/osteoclastogenesis-inhibitory factor."
      Morinaga T., Nakagawa N., Yasuda H., Tsuda E., Higashio K.
      Eur. J. Biochem. 254:685-691(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LYS-3.
      Tissue: Placenta.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT LYS-3.
      Tissue: Kidney.
    5. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Lung.
    6. NIEHS SNPs program
      Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LYS-3 AND MET-104.
    7. "DNA sequence and analysis of human chromosome 8."
      Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
      , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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: Eye.
    9. "Characterization of monomeric and homodimeric forms of osteoclastogenesis inhibitory factor."
      Tomoyasu A., Goto M., Fujise N., Mochizuki S., Yasuda H., Morinaga T., Tsuda E., Higashio K.
      Biochem. Biophys. Res. Commun. 245:382-387(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 22-36 AND 378-401.
    10. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
      Zhang Z., Henzel W.J.
      Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 22-36.
    11. "Cloning and expression of a novel mutated osteoprogerin/osteoclastogenesis inhibitory factor gene."
      He Z.-Y., Yang G.-Z., Zhang W.-J., Wu X.-F.
      Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 31:680-684(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 22-393.
      Tissue: Placenta.
    12. "Isolation of a novel cytokine from human fibroblasts that specifically inhibits osteoclastogenesis."
      Tsuda E., Goto M., Mochizuki S., Yano K., Kobayashi F., Morinaga T., Higashio K.
      Biochem. Biophys. Res. Commun. 234:137-142(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 242-255; 354-359 AND 369-378, FUNCTION.
    13. Cited for: INTERACTION WITH TNFSF10.
    14. "Characterization of structural domains of human osteoclastogenesis inhibitory factor."
      Yamaguchi K., Kinosaki M., Goto M., Kobayashi F., Tsuda E., Morinaga T., Higashio K.
      J. Biol. Chem. 273:5117-5123(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, MUTAGENESIS OF CYS-400.
    15. "Receptor activator of nuclear factor-kappaB ligand and osteoprotegerin: potential implications for the pathogenesis and treatment of malignant bone diseases."
      Hofbauer L.C., Neubauer A., Heufelder A.E.
      Cancer 92:460-470(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    16. "Crystal structure of human RANKL complexed with its decoy receptor osteoprotegerin."
      Luan X., Lu Q., Jiang Y., Zhang S., Wang Q., Yuan H., Zhao W., Wang J., Wang X.
      J. Immunol. 189:245-252(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 22-186 IN COMPLEX WITH TNFSF11, INTERACTION WITH TNFSF11, SUBUNIT, FUNCTION, MUTAGENESIS OF 78-ASP-GLU-79 AND GLU-116, GLYCOSYLATION AT ASN-178, DISULFIDE BONDS.
    17. "A mutation in the gene TNFRSF11B encoding osteoprotegerin causes an idiopathic hyperphosphatasia phenotype."
      Cundy T., Hegde M., Naot D., Chong B., King A., Wallace R., Mulley J., Love D.R., Seidel J., Fawkner M., Banovic T., Callon K.E., Grey A.B., Reid I.R., Middleton-Hardie C.A., Cornish J.
      Hum. Mol. Genet. 11:2119-2127(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT JPD ASP-182 DEL.

    Entry informationi

    Entry nameiTR11B_HUMAN
    AccessioniPrimary (citable) accession number: O00300
    Secondary accession number(s): B2R9A8
    , O60236, Q53FX6, Q9UHP4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 27, 2002
    Last sequence update: February 8, 2011
    Last modified: October 1, 2014
    This is version 131 of the entry and version 3 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

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 8
      Human chromosome 8: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3