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O00300

- TR11B_HUMAN

UniProt

O00300 - TR11B_HUMAN

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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

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
Complete GO annotation...

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
Complete GO annotation...

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. 1 Publication
Mutagenesisi116 – 1161E → A: Reduces affinity for TNFSF11. Decreases inhibition of osteoclast differentiation. 1 Publication
Mutagenesisi400 – 4012Missing: Abolishes dimerization.
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

BgeeiO00300.
CleanExiHS_TNFRSF11B.
ExpressionAtlasiO00300. baseline and differential.
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 – 313Combined sources
Beta strandi35 – 373Combined sources
Beta strandi40 – 423Combined sources
Beta strandi48 – 525Combined sources
Beta strandi56 – 583Combined sources
Beta strandi61 – 644Combined sources
Beta strandi91 – 955Combined sources
Beta strandi99 – 1013Combined sources
Beta strandi104 – 1074Combined sources
Beta strandi111 – 1144Combined sources
Beta strandi117 – 1204Combined sources
Beta strandi128 – 1325Combined sources
Beta strandi136 – 1383Combined sources
Beta strandi141 – 1444Combined sources
Beta strandi155 – 1573Combined sources
Beta strandi167 – 1715Combined sources

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.
GeneTreeiENSGT00760000119204.
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

        10         20         30         40         50
MNNLLCCALV FLDISIKWTT QETFPPKYLH YDEETSHQLL CDKCPPGTYL
60 70 80 90 100
KQHCTAKWKT VCAPCPDHYY TDSWHTSDEC LYCSPVCKEL QYVKQECNRT
110 120 130 140 150
HNRVCECKEG RYLEIEFCLK HRSCPPGFGV VQAGTPERNT VCKRCPDGFF
160 170 180 190 200
SNETSSKAPC RKHTNCSVFG LLLTQKGNAT HDNICSGNSE STQKCGIDVT
210 220 230 240 250
LCEEAFFRFA VPTKFTPNWL SVLVDNLPGT KVNAESVERI KRQHSSQEQT
260 270 280 290 300
FQLLKLWKHQ NKDQDIVKKI IQDIDLCENS VQRHIGHANL TFEQLRSLME
310 320 330 340 350
SLPGKKVGAE DIEKTIKACK PSDQILKLLS LWRIKNGDQD TLKGLMHALK
360 370 380 390 400
HSKTYHFPKT VTQSLKKTIR FLHSFTMYKL YQKLFLEMIG NQVQSVKISC

L
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.
GeneTreei ENSGT00760000119204.
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

Bgeei O00300.
CleanExi HS_TNFRSF11B.
ExpressionAtlasi O00300. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 132 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