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Tumor necrosis factor receptor superfamily member 11B (Osteoclastogenesis inhibitory factor) (Osteoprotegerin)

 TR11B_HUMAN             Reviewed;         401 AA.
O00300; B2R9A8; O60236; Q53FX6; Q9UHP4;
27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
08-FEB-2011, sequence version 3.
28-FEB-2018, entry version 155.
RecName: Full=Tumor necrosis factor receptor superfamily member 11B;
AltName: Full=Osteoclastogenesis inhibitory factor;
AltName: Full=Osteoprotegerin;
Flags: Precursor;
Name=TNFRSF11B; Synonyms=OCIF, OPG;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LYS-3.
TISSUE=Kidney;
PubMed=9108485; DOI=10.1016/S0092-8674(00)80209-3;
Simonet W.S., Lacey D.L., Dunstan C.R., Kelley M., Chang M.-S.,
Luethy R., Nguyen H.Q., Wooden S., Bennett L., Boone T., Shimamoto G.,
Derose M., Elliott R., Colombero A., Tan H.-L., Trail G., Sullivan J.,
Davy E., Bucay N., Renshaw-Gegg L., Hughes T.M., Hill D., Pattison W.,
Campbell P., Sander S., Van G., Tarpley J., Derby P., Lee R.,
Suggs S., Boyle W.J.;
"Osteoprotegerin: a novel secreted protein involved in the regulation
of bone density.";
Cell 89:309-319(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LYS-3.
TISSUE=Lung cancer;
PubMed=9492069; DOI=10.1210/endo.139.3.5837;
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.;
"Identity of osteoclastogenesis inhibitory factor (OCIF) and
osteoprotegerin (OPG): a mechanism by which OPG/OCIF inhibits
osteoclastogenesis in vitro.";
Endocrinology 139:1329-1337(1998).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-3.
TISSUE=Placenta;
PubMed=9688283; DOI=10.1046/j.1432-1327.1998.2540685.x;
Morinaga T., Nakagawa N., Yasuda H., Tsuda E., Higashio K.;
"Cloning and characterization of the gene encoding human
osteoprotegerin/osteoclastogenesis-inhibitory factor.";
Eur. J. Biochem. 254:685-691(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LYS-3.
TISSUE=Kidney;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
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.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LYS-3 AND MET-104.
NIEHS SNPs program;
Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
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.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PROTEIN SEQUENCE OF 22-36 AND 378-401.
PubMed=9571159; DOI=10.1006/bbrc.1998.8443;
Tomoyasu A., Goto M., Fujise N., Mochizuki S., Yasuda H., Morinaga T.,
Tsuda E., Higashio K.;
"Characterization of monomeric and homodimeric forms of
osteoclastogenesis inhibitory factor.";
Biochem. Biophys. Res. Commun. 245:382-387(1998).
[10]
PROTEIN SEQUENCE OF 22-36.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 22-393.
TISSUE=Placenta;
PubMed=12110935;
He Z.-Y., Yang G.-Z., Zhang W.-J., Wu X.-F.;
"Cloning and expression of a novel mutated
osteoprogerin/osteoclastogenesis inhibitory factor gene.";
Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 31:680-684(1999).
[12]
PROTEIN SEQUENCE OF 242-255; 354-359 AND 369-378, AND FUNCTION.
PubMed=9168977; DOI=10.1006/bbrc.1997.6603;
Tsuda E., Goto M., Mochizuki S., Yano K., Kobayashi F., Morinaga T.,
Higashio K.;
"Isolation of a novel cytokine from human fibroblasts that
specifically inhibits osteoclastogenesis.";
Biochem. Biophys. Res. Commun. 234:137-142(1997).
[13]
INTERACTION WITH TNFSF10.
PubMed=9603945; DOI=10.1074/jbc.273.23.14363;
Emery J.G., McDonnell P., Burke M.B., Deen K.C., Lyn S., Silverman C.,
Dul E., Appelbaum E.R., Eichman C., DiPrinzio R., Dodds R.A.,
James I.E., Rosenberg M., Lee J.C., Young P.R.;
"Osteoprotegerin is a receptor for the cytotoxic ligand TRAIL.";
J. Biol. Chem. 273:14363-14367(1998).
[14]
CHARACTERIZATION, AND MUTAGENESIS OF CYS-400.
PubMed=9478964; DOI=10.1074/jbc.273.9.5117;
Yamaguchi K., Kinosaki M., Goto M., Kobayashi F., Tsuda E.,
Morinaga T., Higashio K.;
"Characterization of structural domains of human osteoclastogenesis
inhibitory factor.";
J. Biol. Chem. 273:5117-5123(1998).
[15]
REVIEW.
PubMed=11505389;
DOI=10.1002/1097-0142(20010801)92:3<460::AID-CNCR1344>3.0.CO;2-D;
Hofbauer L.C., Neubauer A., Heufelder A.E.;
"Receptor activator of nuclear factor-kappaB ligand and
osteoprotegerin: potential implications for the pathogenesis and
treatment of malignant bone diseases.";
Cancer 92:460-470(2001).
[16]
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, AND DISULFIDE
BONDS.
PubMed=22664871; DOI=10.4049/jimmunol.1103387;
Luan X., Lu Q., Jiang Y., Zhang S., Wang Q., Yuan H., Zhao W.,
Wang J., Wang X.;
"Crystal structure of human RANKL complexed with its decoy receptor
osteoprotegerin.";
J. Immunol. 189:245-252(2012).
[17]
VARIANT PDB5 ASP-182 DEL.
PubMed=12189164; DOI=10.1093/hmg/11.18.2119;
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.;
"A mutation in the gene TNFRSF11B encoding osteoprotegerin causes an
idiopathic hyperphosphatasia phenotype.";
Hum. Mol. Genet. 11:2119-2127(2002).
-!- FUNCTION: 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. {ECO:0000269|PubMed:22664871,
ECO:0000269|PubMed:9168977}.
-!- SUBUNIT: Homodimer. Interacts with TNFSF10 and TNFSF11.
{ECO:0000269|PubMed:22664871, ECO:0000269|PubMed:9603945}.
-!- INTERACTION:
O14788:TNFSF11; NbExp=3; IntAct=EBI-15481185, EBI-7404021;
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: 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.
-!- INDUCTION: Up-regulated by increasing calcium-concentration in the
medium and estrogens. Down-regulated by glucocorticoids.
-!- PTM: N-glycosylated. Contains sialic acid residues.
{ECO:0000269|PubMed:22664871}.
-!- PTM: The N-terminus is blocked.
-!- DISEASE: Paget disease of bone 5, juvenile-onset (PDB5)
[MIM:239000]: An autosomal recessive, juvenile-onset form of Paget
disease, a disorder of bone remodeling characterized by increased
bone turnover affecting one or more sites throughout the skeleton,
primarily the axial skeleton. Osteoclastic overactivity followed
by compensatory osteoblastic activity leads to a structurally
disorganized mosaic of bone (woven bone), which is mechanically
weaker, larger, less compact, more vascular, and more susceptible
to fracture than normal adult lamellar bone. PDB5 clinical
manifestations include short stature, progressive long bone
deformities, fractures, vertebral collapse, skull enlargement, and
hyperostosis with progressive deafness.
{ECO:0000269|PubMed:12189164}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/TNFRSF11BID42610ch8q24.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/tnfrsf11b/";
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EMBL; U94332; AAB53709.1; -; mRNA.
EMBL; AB002146; BAA25910.1; -; mRNA.
EMBL; AB008822; BAA32076.1; -; Genomic_DNA.
EMBL; AK313710; BAG36455.1; -; mRNA.
EMBL; AK223155; BAD96875.1; -; mRNA.
EMBL; AY466112; AAR23265.1; -; Genomic_DNA.
EMBL; AC107953; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP004283; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC030155; AAH30155.1; -; mRNA.
EMBL; AF134187; AAF20168.1; -; mRNA.
CCDS; CCDS6326.1; -.
RefSeq; NP_002537.3; NM_002546.3.
UniGene; Hs.81791; -.
PDB; 3URF; X-ray; 2.70 A; Z=22-186.
PDBsum; 3URF; -.
ProteinModelPortal; O00300; -.
SMR; O00300; -.
BioGrid; 111028; 2.
IntAct; O00300; 2.
STRING; 9606.ENSP00000297350; -.
iPTMnet; O00300; -.
PhosphoSitePlus; O00300; -.
BioMuta; TNFRSF11B; -.
PaxDb; O00300; -.
PeptideAtlas; O00300; -.
PRIDE; O00300; -.
Ensembl; ENST00000297350; ENSP00000297350; ENSG00000164761.
GeneID; 4982; -.
KEGG; hsa:4982; -.
UCSC; uc003yon.5; human.
CTD; 4982; -.
DisGeNET; 4982; -.
EuPathDB; HostDB:ENSG00000164761.8; -.
GeneCards; TNFRSF11B; -.
H-InvDB; HIX0007748; -.
HGNC; HGNC:11909; TNFRSF11B.
MalaCards; TNFRSF11B; -.
MIM; 239000; phenotype.
MIM; 602643; gene.
neXtProt; NX_O00300; -.
OpenTargets; ENSG00000164761; -.
Orphanet; 2801; Juvenile Paget disease.
PharmGKB; PA36602; -.
eggNOG; ENOG410IFEM; Eukaryota.
eggNOG; ENOG4111PUQ; LUCA.
GeneTree; ENSGT00760000119204; -.
HOGENOM; HOG000273896; -.
HOVERGEN; HBG061495; -.
InParanoid; O00300; -.
KO; K05148; -.
OMA; SRQLMCD; -.
OrthoDB; EOG091G03XW; -.
PhylomeDB; O00300; -.
TreeFam; TF331157; -.
Reactome; R-HSA-5669034; TNFs bind their physiological receptors.
SIGNOR; O00300; -.
ChiTaRS; TNFRSF11B; human.
GeneWiki; Osteoprotegerin; -.
GenomeRNAi; 4982; -.
PRO; PR:O00300; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000164761; -.
CleanEx; HS_TNFRSF11B; -.
ExpressionAtlas; O00300; baseline and differential.
Genevisible; O00300; HS.
GO; GO:0005576; C:extracellular region; TAS:ProtInc.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:Ensembl.
GO; GO:0005125; F:cytokine activity; TAS:ProtInc.
GO; GO:0004872; F:receptor activity; TAS:ProtInc.
GO; GO:0005031; F:tumor necrosis factor-activated receptor activity; IBA:GO_Central.
GO; GO:0097190; P:apoptotic signaling pathway; IBA:GO_Central.
GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
GO; GO:0006955; P:immune response; IBA:GO_Central.
GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
GO; GO:0045779; P:negative regulation of bone resorption; IEA:Ensembl.
GO; GO:0042489; P:negative regulation of odontogenesis of dentin-containing tooth; IEA:Ensembl.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0046685; P:response to arsenic-containing substance; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IBA:GO_Central.
GO; GO:0032026; P:response to magnesium ion; IEA:Ensembl.
GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR000488; Death_domain.
InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
InterPro; IPR022323; TNFR_11.
InterPro; IPR017371; TNFR_11B.
InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
Pfam; PF00531; Death; 1.
Pfam; PF00020; TNFR_c6; 3.
PIRSF; PIRSF038065; TNFR_11B; 1.
PRINTS; PR01961; TNFACTORR11.
PRINTS; PR01975; TNFACTORR11B.
SMART; SM00005; DEATH; 1.
SMART; SM01411; Ephrin_rec_like; 2.
SMART; SM00208; TNFR; 4.
SUPFAM; SSF47986; SSF47986; 2.
PROSITE; PS00652; TNFR_NGFR_1; 1.
PROSITE; PS50050; TNFR_NGFR_2; 2.
1: Evidence at protein level;
3D-structure; Apoptosis; Complete proteome; Direct protein sequencing;
Disease mutation; Disulfide bond; Glycoprotein; Polymorphism;
Receptor; Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 21 {ECO:0000269|PubMed:15340161,
ECO:0000269|PubMed:9571159}.
CHAIN 22 401 Tumor necrosis factor receptor
superfamily member 11B.
/FTId=PRO_0000034587.
REPEAT 24 62 TNFR-Cys 1.
REPEAT 65 105 TNFR-Cys 2.
REPEAT 107 142 TNFR-Cys 3.
REPEAT 145 185 TNFR-Cys 4.
DOMAIN 198 269 Death 1.
DOMAIN 270 365 Death 2.
SITE 400 400 Involved in dimerization.
CARBOHYD 98 98 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 152 152 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 165 165 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 178 178 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:22664871}.
CARBOHYD 289 289 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 41 54 {ECO:0000255|PROSITE-ProRule:PRU00206,
ECO:0000269|PubMed:22664871}.
DISULFID 44 62 {ECO:0000255|PROSITE-ProRule:PRU00206,
ECO:0000269|PubMed:22664871}.
DISULFID 65 80 {ECO:0000255|PROSITE-ProRule:PRU00206,
ECO:0000269|PubMed:22664871}.
DISULFID 83 97 {ECO:0000255|PROSITE-ProRule:PRU00206,
ECO:0000269|PubMed:22664871}.
DISULFID 87 105 {ECO:0000255|PROSITE-ProRule:PRU00206,
ECO:0000269|PubMed:22664871}.
DISULFID 107 118 {ECO:0000255|PROSITE-ProRule:PRU00206,
ECO:0000269|PubMed:22664871}.
DISULFID 124 142 {ECO:0000255|PROSITE-ProRule:PRU00206,
ECO:0000269|PubMed:22664871}.
DISULFID 145 160 {ECO:0000255|PROSITE-ProRule:PRU00206,
ECO:0000269|PubMed:22664871}.
DISULFID 166 185 {ECO:0000255|PROSITE-ProRule:PRU00206,
ECO:0000269|PubMed:22664871}.
VARIANT 3 3 N -> K (in dbSNP:rs2073618).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:9108485,
ECO:0000269|PubMed:9492069,
ECO:0000269|PubMed:9688283,
ECO:0000269|Ref.6}.
/FTId=VAR_013439.
VARIANT 104 104 V -> M (in dbSNP:rs11573906).
{ECO:0000269|Ref.6}.
/FTId=VAR_018957.
VARIANT 182 182 Missing (in PDB5).
{ECO:0000269|PubMed:12189164}.
/FTId=VAR_019413.
MUTAGEN 78 79 DE->AA: Decreases inhibition of
osteoclast differentiation.
{ECO:0000269|PubMed:22664871}.
MUTAGEN 116 116 E->A: Reduces affinity for TNFSF11.
Decreases inhibition of osteoclast
differentiation.
{ECO:0000269|PubMed:22664871}.
MUTAGEN 400 401 Missing: Abolishes dimerization.
MUTAGEN 400 400 C->S: Abolishes dimerization.
{ECO:0000269|PubMed:9478964}.
CONFLICT 263 263 D -> A (in Ref. 1; AAB53709).
{ECO:0000305}.
STRAND 29 31 {ECO:0000244|PDB:3URF}.
STRAND 35 37 {ECO:0000244|PDB:3URF}.
STRAND 40 42 {ECO:0000244|PDB:3URF}.
STRAND 48 52 {ECO:0000244|PDB:3URF}.
STRAND 56 58 {ECO:0000244|PDB:3URF}.
STRAND 61 64 {ECO:0000244|PDB:3URF}.
STRAND 91 95 {ECO:0000244|PDB:3URF}.
STRAND 99 101 {ECO:0000244|PDB:3URF}.
STRAND 104 107 {ECO:0000244|PDB:3URF}.
STRAND 111 114 {ECO:0000244|PDB:3URF}.
STRAND 117 120 {ECO:0000244|PDB:3URF}.
STRAND 128 132 {ECO:0000244|PDB:3URF}.
STRAND 136 138 {ECO:0000244|PDB:3URF}.
STRAND 141 144 {ECO:0000244|PDB:3URF}.
STRAND 155 157 {ECO:0000244|PDB:3URF}.
STRAND 167 171 {ECO:0000244|PDB:3URF}.
SEQUENCE 401 AA; 46026 MW; 2A23AC07BFA1E2DE CRC64;
MNNLLCCALV FLDISIKWTT QETFPPKYLH YDEETSHQLL CDKCPPGTYL KQHCTAKWKT
VCAPCPDHYY TDSWHTSDEC LYCSPVCKEL QYVKQECNRT HNRVCECKEG RYLEIEFCLK
HRSCPPGFGV VQAGTPERNT VCKRCPDGFF SNETSSKAPC RKHTNCSVFG LLLTQKGNAT
HDNICSGNSE STQKCGIDVT LCEEAFFRFA VPTKFTPNWL SVLVDNLPGT KVNAESVERI
KRQHSSQEQT FQLLKLWKHQ NKDQDIVKKI IQDIDLCENS VQRHIGHANL TFEQLRSLME
SLPGKKVGAE DIEKTIKACK PSDQILKLLS LWRIKNGDQD TLKGLMHALK HSKTYHFPKT
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Fax 0032 16 50 90 45
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GENTAUR Ltd.
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SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

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Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
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Genprice Inc, Logistics
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Genprice Inc, Invoices and accounting
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Kuiper 1
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ГЕНТАУЪР БЪЛГАРИЯ
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GENTAUR Poland Sp. z o.o.


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