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Protein

Tumor necrosis factor receptor superfamily member 11A

Gene

TNFRSF11A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Receptor for TNFSF11/RANKL/TRANCE/OPGL; essential for RANKL-mediated osteoclastogenesis. Involved in the regulation of interactions between T-cells and dendritic cells.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi133 – 1331Sodium; via carbonyl oxygenBy similarity
Metal bindingi134 – 1341Sodium; via carbonyl oxygenBy similarity
Metal bindingi160 – 1601Sodium; via carbonyl oxygenBy similarity

GO - Molecular functioni

  1. cytokine binding Source: BHF-UCL
  2. metal ion binding Source: UniProtKB-KW
  3. receptor activity Source: ProtInc
  4. transmembrane signaling receptor activity Source: BHF-UCL
  5. tumor necrosis factor-activated receptor activity Source: BHF-UCL

GO - Biological processi

  1. adaptive immune response Source: BHF-UCL
  2. cell-cell signaling Source: ProtInc
  3. circadian temperature homeostasis Source: BHF-UCL
  4. lymph node development Source: Ensembl
  5. mammary gland alveolus development Source: Ensembl
  6. monocyte chemotaxis Source: BHF-UCL
  7. ossification Source: Ensembl
  8. osteoclast differentiation Source: BHF-UCL
  9. positive regulation of cell proliferation Source: ProtInc
  10. positive regulation of ERK1 and ERK2 cascade via TNFSF11-mediated signaling Source: BHF-UCL
  11. positive regulation of fever generation by positive regulation of prostaglandin secretion Source: BHF-UCL
  12. positive regulation of JUN kinase activity Source: BHF-UCL
  13. positive regulation of NF-kappaB transcription factor activity Source: BHF-UCL
  14. positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  15. response to cytokine Source: BHF-UCL
  16. response to interleukin-1 Source: BHF-UCL
  17. response to lipopolysaccharide Source: BHF-UCL
  18. response to radiation Source: Ensembl
  19. response to tumor necrosis factor Source: BHF-UCL
  20. signal transduction Source: ProtInc
  21. TNFSF11-mediated signaling pathway Source: BHF-UCL
  22. tumor necrosis factor-mediated signaling pathway Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Ligandi

Metal-binding, Sodium

Enzyme and pathway databases

SignaLinkiQ9Y6Q6.

Names & Taxonomyi

Protein namesi
Recommended name:
Tumor necrosis factor receptor superfamily member 11A
Alternative name(s):
Osteoclast differentiation factor receptor
Short name:
ODFR
Receptor activator of NF-KB
CD_antigen: CD265
Gene namesi
Name:TNFRSF11A
Synonyms:RANK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 18

Organism-specific databases

HGNCiHGNC:11908. TNFRSF11A.

Subcellular locationi

Isoform 1 : Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication
Isoform RANK-e5a : Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini30 – 212183ExtracellularSequence AnalysisAdd
BLAST
Transmembranei213 – 23321HelicalSequence AnalysisAdd
BLAST
Topological domaini234 – 616383CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. external side of plasma membrane Source: BHF-UCL
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

Familial expansile osteolysis1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionRare autosomal dominant bone disorder characterized by focal areas of increased bone remodeling. The osteolytic lesions develop usually in the long bones during early adulthood. FEO is often associated with early-onset deafness and loss of dentition.

See also OMIM:174810
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti21 – 211L → LLLCALL in FEO. 1 Publication
VAR_011517
Paget disease of bone 21 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionBone-remodeling disorder with clinical similarities to FEO. Unlike FEO, however, affected individuals have involvement of the axial skeleton with lesions in the spine, pelvis and skull.

See also OMIM:602080
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti21 – 211L → LALLLLCALL in PDB2. 1 Publication
VAR_011516
Osteopetrosis, autosomal recessive 71 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA rare genetic disease characterized by abnormally dense bone, due to defective resorption of immature bone. Osteopetrosis occurs in two forms: a severe autosomal recessive form occurring in utero, infancy, or childhood, and a benign autosomal dominant form occurring in adolescence or adulthood. Recessive osteopetrosis commonly manifests in early infancy with macrocephaly, feeding difficulties, evolving blindness and deafness, bone marrow failure, severe anemia, and hepatosplenomegaly. Deafness and blindness are generally thought to represent effects of pressure on nerves. OPTB7 is characterized by paucity of osteoclasts, suggesting a molecular defect in osteoclast development. OPTB7 is associated with hypogammaglobulinemia.

See also OMIM:612301
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti53 – 531G → R in OPTB7; two patients with osteoclast-poor osteopetrosis. 1 Publication
VAR_046788
Natural varianti129 – 1291R → C in OPTB7; a patient with osteoclast-poor osteopetrosis. 1 Publication
VAR_046789
Natural varianti170 – 1701R → G in OPTB7; two siblings with osteoclast-poor osteopetrosis. 1 Publication
VAR_046791
Natural varianti175 – 1751C → R in OPTB7; two patients with osteoclast-poor osteopetrosis. 1 Publication
VAR_046792
Natural varianti244 – 2441A → S in OPTB7; one patient with osteoclast-poor osteopetrosis. 1 Publication
VAR_046793

Keywords - Diseasei

Deafness, Disease mutation, Osteopetrosis

Organism-specific databases

MIMi174810. phenotype.
602080. phenotype.
612301. phenotype.
Orphaneti85195. Familial expansile osteolysis.
178389. Osteopetrosis - hypogammaglobulinemia.
PharmGKBiPA36601.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929Sequence AnalysisAdd
BLAST
Chaini30 – 616587Tumor necrosis factor receptor superfamily member 11APRO_0000034585Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi34 ↔ 46PROSITE-ProRule annotation
Disulfide bondi47 ↔ 60PROSITE-ProRule annotation
Disulfide bondi50 ↔ 68PROSITE-ProRule annotation
Disulfide bondi71 ↔ 86PROSITE-ProRule annotation
Disulfide bondi92 ↔ 112PROSITE-ProRule annotation
Glycosylationi105 – 1051N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi114 ↔ 127PROSITE-ProRule annotation
Disulfide bondi124 ↔ 126PROSITE-ProRule annotation
Disulfide bondi133 ↔ 151PROSITE-ProRule annotation
Disulfide bondi154 ↔ 169PROSITE-ProRule annotation
Glycosylationi174 – 1741N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi175 ↔ 194PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ9Y6Q6.
PaxDbiQ9Y6Q6.
PRIDEiQ9Y6Q6.

PTM databases

PhosphoSiteiQ9Y6Q6.

Expressioni

Tissue specificityi

Ubiquitous expression with high levels in skeletal muscle, thymus, liver, colon, small intestine and adrenal gland.

Gene expression databases

BgeeiQ9Y6Q6.
CleanExiHS_TNFRSF11A.
GenevestigatoriQ9Y6Q6.

Organism-specific databases

HPAiCAB010391.
HPA027728.

Interactioni

Subunit structurei

Binds to the clefts between the subunits of the TNFSF11 ligand trimer to form a heterohexamer (By similarity). Interacts with TRAF1, TRAF2, TRAF3, TRAF5 and TRAF6. Interacts (via cytoplasmic domain) with GAB2.By similarity2 Publications

Protein-protein interaction databases

BioGridi114320. 10 interactions.
IntActiQ9Y6Q6. 4 interactions.
STRINGi9606.ENSP00000269485.

Structurei

Secondary structure

1
616
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi345 – 3484Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LB5X-ray2.40B342-349[»]
ProteinModelPortaliQ9Y6Q6.
SMRiQ9Y6Q6. Positions 32-198.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati34 – 6835TNFR-Cys 1Add
BLAST
Repeati71 – 11242TNFR-Cys 2Add
BLAST
Repeati114 – 15138TNFR-Cys 3Add
BLAST
Repeati154 – 19441TNFR-Cys 4Add
BLAST

Sequence similaritiesi

Contains 4 TNFR-Cys repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG45473.
GeneTreeiENSGT00760000119204.
HOGENOMiHOG000154659.
HOVERGENiHBG079274.
InParanoidiQ9Y6Q6.
KOiK05147.
OMAiCPHWAAS.
OrthoDBiEOG786H2Q.
PhylomeDBiQ9Y6Q6.

Family and domain databases

InterProiIPR001368. TNFR/NGFR_Cys_rich_reg.
IPR022323. TNFR_11.
IPR022361. TNFR_11A.
[Graphical view]
PfamiPF00020. TNFR_c6. 1 hit.
[Graphical view]
PRINTSiPR01961. TNFACTORR11.
PR01974. TNFACTORR11A.
SMARTiSM00208. TNFR. 4 hits.
[Graphical view]
PROSITEiPS00652. TNFR_NGFR_1. 1 hit.
PS50050. TNFR_NGFR_2. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

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

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Y6Q6-1) [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

        10         20         30         40         50
MAPRARRRRP LFALLLLCAL LARLQVALQI APPCTSEKHY EHLGRCCNKC
60 70 80 90 100
EPGKYMSSKC TTTSDSVCLP CGPDEYLDSW NEEDKCLLHK VCDTGKALVA
110 120 130 140 150
VVAGNSTTPR RCACTAGYHW SQDCECCRRN TECAPGLGAQ HPLQLNKDTV
160 170 180 190 200
CKPCLAGYFS DAFSSTDKCR PWTNCTFLGK RVEHHGTEKS DAVCSSSLPA
210 220 230 240 250
RKPPNEPHVY LPGLIILLLF ASVALVAAII FGVCYRKKGK ALTANLWHWI
260 270 280 290 300
NEACGRLSGD KESSGDSCVS THTANFGQQG ACEGVLLLTL EEKTFPEDMC
310 320 330 340 350
YPDQGGVCQG TCVGGGPYAQ GEDARMLSLV SKTEIEEDSF RQMPTEDEYM
360 370 380 390 400
DRPSQPTDQL LFLTEPGSKS TPPFSEPLEV GENDSLSQCF TGTQSTVGSE
410 420 430 440 450
SCNCTEPLCR TDWTPMSSEN YLQKEVDSGH CPHWAASPSP NWADVCTGCR
460 470 480 490 500
NPPGEDCEPL VGSPKRGPLP QCAYGMGLPP EEEASRTEAR DQPEDGADGR
510 520 530 540 550
LPSSARAGAG SGSSPGGQSP ASGNVTGNSN STFISSGQVM NFKGDIIVVY
560 570 580 590 600
VSQTSQEGAA AAAEPMGRPV QEETLARRDS FAGNGPRFPD PCGGPEGLRE
610
PEKASRPVQE QGGAKA
Length:616
Mass (Da):66,034
Last modified:November 1, 1999 - v1
Checksum:iE3DE9A7A08196F81
GO
Isoform 2 (identifier: Q9Y6Q6-2) [UniParc]FASTAAdd to basket

Also known as: delta7,8,9

The sequence of this isoform differs from the canonical sequence as follows:
     206-522: Missing.

Show »
Length:299
Mass (Da):32,318
Checksum:i0EF38515CF29F18D
GO
Isoform 3 (identifier: Q9Y6Q6-3) [UniParc]FASTAAdd to basket

Also known as: delta8,9

The sequence of this isoform differs from the canonical sequence as follows:
     244-522: Missing.

Show »
Length:337
Mass (Da):36,399
Checksum:i9200CEF495CCF5B3
GO
Isoform 4 (identifier: Q9Y6Q6-4) [UniParc]FASTAAdd to basket

Also known as: delta9

The sequence of this isoform differs from the canonical sequence as follows:
     263-263: S → M
     264-616: Missing.

Show »
Length:263
Mass (Da):28,965
Checksum:iA6E72E8DEFA676C2
GO
Isoform 5 (identifier: Q9Y6Q6-5) [UniParc]FASTAAdd to basket

Also known as: exon9a

The sequence of this isoform differs from the canonical sequence as follows:
     523-616: GNVTGNSNST...PVQEQGGAKA → D

Show »
Length:523
Mass (Da):56,402
Checksum:i653957CFE411BEB5
GO
Isoform RANK-e5a (identifier: Q9Y6Q6-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     143-157: LQLNKDTVCKPCLAG → C

Note: Reduced abilitity to bind RANKL and to activate NF-kappaB as compared to isoform 1.

Show »
Length:602
Mass (Da):64,552
Checksum:i820338A19FAE9D03
GO

Sequence cautioni

The sequence BAD92999.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti21 – 211L → LALLLLCALL in PDB2. 1 Publication
VAR_011516
Natural varianti21 – 211L → LLLCALL in FEO. 1 Publication
VAR_011517
Natural varianti53 – 531G → R in OPTB7; two patients with osteoclast-poor osteopetrosis. 1 Publication
VAR_046788
Natural varianti129 – 1291R → C in OPTB7; a patient with osteoclast-poor osteopetrosis. 1 Publication
VAR_046789
Natural varianti141 – 1411H → Y.
Corresponds to variant rs35211496 [ dbSNP | Ensembl ].
VAR_046790
Natural varianti170 – 1701R → G in OPTB7; two siblings with osteoclast-poor osteopetrosis. 1 Publication
VAR_046791
Natural varianti175 – 1751C → R in OPTB7; two patients with osteoclast-poor osteopetrosis. 1 Publication
VAR_046792
Natural varianti192 – 1921A → V.1 Publication
Corresponds to variant rs1805034 [ dbSNP | Ensembl ].
VAR_011518
Natural varianti244 – 2441A → S in OPTB7; one patient with osteoclast-poor osteopetrosis. 1 Publication
VAR_046793

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei143 – 15715LQLNK…PCLAG → C in isoform RANK-e5a. 1 PublicationVSP_054179Add
BLAST
Alternative sequencei206 – 522317Missing in isoform 2. 2 PublicationsVSP_046901Add
BLAST
Alternative sequencei244 – 522279Missing in isoform 3. 1 PublicationVSP_054180Add
BLAST
Alternative sequencei263 – 2631S → M in isoform 4. 1 PublicationVSP_054181
Alternative sequencei264 – 616353Missing in isoform 4. 1 PublicationVSP_054182Add
BLAST
Alternative sequencei523 – 61694GNVTG…GGAKA → D in isoform 5. 1 PublicationVSP_054183Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF018253 mRNA. Translation: AAB86809.1.
HF584702 mRNA. Translation: CCQ44072.1.
HE647782 mRNA. Translation: CCF23032.1.
HE649916 mRNA. Translation: CCF55033.1.
HE649917 mRNA. Translation: CCF55034.1.
HE659518 mRNA. Translation: CCF77738.1.
AB209762 mRNA. Translation: BAD92999.1. Different initiation.
CCDSiCCDS11980.1. [Q9Y6Q6-1]
CCDS59324.1. [Q9Y6Q6-2]
CCDS74227.1. [Q9Y6Q6-4]
CCDS74228.1. [Q9Y6Q6-3]
RefSeqiNP_001257878.1. NM_001270949.1. [Q9Y6Q6-4]
NP_001257879.1. NM_001270950.1. [Q9Y6Q6-3]
NP_001257880.1. NM_001270951.1. [Q9Y6Q6-2]
NP_001265197.1. NM_001278268.1. [Q9Y6Q6-6]
NP_003830.1. NM_003839.3. [Q9Y6Q6-1]
XP_005266834.1. XM_005266777.1. [Q9Y6Q6-5]
UniGeneiHs.204044.
Hs.621477.

Genome annotation databases

EnsembliENST00000269485; ENSP00000269485; ENSG00000141655. [Q9Y6Q6-2]
ENST00000586569; ENSP00000465500; ENSG00000141655. [Q9Y6Q6-1]
ENST00000616710; ENSP00000479567; ENSG00000141655. [Q9Y6Q6-4]
ENST00000617039; ENSP00000482466; ENSG00000141655. [Q9Y6Q6-3]
GeneIDi8792.
KEGGihsa:8792.
UCSCiuc002lin.4. human. [Q9Y6Q6-1]

Polymorphism databases

DMDMi19924309.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF018253 mRNA. Translation: AAB86809.1.
HF584702 mRNA. Translation: CCQ44072.1.
HE647782 mRNA. Translation: CCF23032.1.
HE649916 mRNA. Translation: CCF55033.1.
HE649917 mRNA. Translation: CCF55034.1.
HE659518 mRNA. Translation: CCF77738.1.
AB209762 mRNA. Translation: BAD92999.1. Different initiation.
CCDSiCCDS11980.1. [Q9Y6Q6-1]
CCDS59324.1. [Q9Y6Q6-2]
CCDS74227.1. [Q9Y6Q6-4]
CCDS74228.1. [Q9Y6Q6-3]
RefSeqiNP_001257878.1. NM_001270949.1. [Q9Y6Q6-4]
NP_001257879.1. NM_001270950.1. [Q9Y6Q6-3]
NP_001257880.1. NM_001270951.1. [Q9Y6Q6-2]
NP_001265197.1. NM_001278268.1. [Q9Y6Q6-6]
NP_003830.1. NM_003839.3. [Q9Y6Q6-1]
XP_005266834.1. XM_005266777.1. [Q9Y6Q6-5]
UniGeneiHs.204044.
Hs.621477.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LB5X-ray2.40B342-349[»]
ProteinModelPortaliQ9Y6Q6.
SMRiQ9Y6Q6. Positions 32-198.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114320. 10 interactions.
IntActiQ9Y6Q6. 4 interactions.
STRINGi9606.ENSP00000269485.

Chemistry

GuidetoPHARMACOLOGYi1881.

PTM databases

PhosphoSiteiQ9Y6Q6.

Polymorphism databases

DMDMi19924309.

Proteomic databases

MaxQBiQ9Y6Q6.
PaxDbiQ9Y6Q6.
PRIDEiQ9Y6Q6.

Protocols and materials databases

DNASUi8792.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000269485; ENSP00000269485; ENSG00000141655. [Q9Y6Q6-2]
ENST00000586569; ENSP00000465500; ENSG00000141655. [Q9Y6Q6-1]
ENST00000616710; ENSP00000479567; ENSG00000141655. [Q9Y6Q6-4]
ENST00000617039; ENSP00000482466; ENSG00000141655. [Q9Y6Q6-3]
GeneIDi8792.
KEGGihsa:8792.
UCSCiuc002lin.4. human. [Q9Y6Q6-1]

Organism-specific databases

CTDi8792.
GeneCardsiGC18P059992.
HGNCiHGNC:11908. TNFRSF11A.
HPAiCAB010391.
HPA027728.
MIMi174810. phenotype.
602080. phenotype.
603499. gene.
612301. phenotype.
neXtProtiNX_Q9Y6Q6.
Orphaneti85195. Familial expansile osteolysis.
178389. Osteopetrosis - hypogammaglobulinemia.
PharmGKBiPA36601.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG45473.
GeneTreeiENSGT00760000119204.
HOGENOMiHOG000154659.
HOVERGENiHBG079274.
InParanoidiQ9Y6Q6.
KOiK05147.
OMAiCPHWAAS.
OrthoDBiEOG786H2Q.
PhylomeDBiQ9Y6Q6.

Enzyme and pathway databases

SignaLinkiQ9Y6Q6.

Miscellaneous databases

ChiTaRSiTNFRSF11A. human.
GeneWikiiRANK.
GenomeRNAii8792.
NextBioi32972.
PROiQ9Y6Q6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y6Q6.
CleanExiHS_TNFRSF11A.
GenevestigatoriQ9Y6Q6.

Family and domain databases

InterProiIPR001368. TNFR/NGFR_Cys_rich_reg.
IPR022323. TNFR_11.
IPR022361. TNFR_11A.
[Graphical view]
PfamiPF00020. TNFR_c6. 1 hit.
[Graphical view]
PRINTSiPR01961. TNFACTORR11.
PR01974. TNFACTORR11A.
SMARTiSM00208. TNFR. 4 hits.
[Graphical view]
PROSITEiPS00652. TNFR_NGFR_1. 1 hit.
PS50050. TNFR_NGFR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: Dendritic cell.
  2. "Alternative splicing generates a truncated isoform of human TNFRSF11A (RANK) with an altered capacity to activate NF-kappaB."
    Sirinian C., Papanastasiou A.D., Zarkadis I.K., Kalofonos H.P.
    Gene 525:124-129(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM RANK-E5A), SUBCELLULAR LOCATION (ISOFORMS 1 AND RANK-E5A), ALTERNATIVE SPLICING.
    Tissue: Blood.
  3. "Alternative splicing generates multiple human TNFRSF11A (RANK) isoforms."
    Papanastasiou A.D., Sirinian C., Kalofonos H.P.
    Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), NUCLEOTIDE SEQUENCE [MRNA] OF 159-523 (ISOFORM 5), ALTERNATIVE SPLICING.
    Tissue: Blood.
  4. "Homo sapiens protein coding cDNA."
    Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  5. "RANK is the essential signaling receptor for osteoclast differentiation factor in osteoclastogenesis."
    Nakagawa N., Kinosaki M., Yamaguchi K., Shima N., Yasuda H., Yano K., Morinaga T., Higashio K.
    Biochem. Biophys. Res. Commun. 253:395-400(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "The TRAF family of signal transducers mediates NF-kappaB activation by the TRANCE receptor."
    Wong B.R., Josien R., Lee S.Y., Vologodskaia M., Steinman R.M., Choi Y.
    J. Biol. Chem. 273:28355-28359(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRAF1; TRAF2; TRAF3; TRAF5 AND TRAF6.
  7. "The molecular scaffold Gab2 is a crucial component of RANK signaling and osteoclastogenesis."
    Wada T., Nakashima T., Oliveira-dos-Santos A.J., Gasser J., Hara H., Schett G., Penninger J.M.
    Nat. Med. 11:394-399(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GAB2.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Mutations in TNFRSF11A, affecting the signal peptide of RANK, cause familial expansile osteolysis."
    Hughes A.E., Ralston S.H., Marken J., Bell C., MacPherson H., Wallace R.G.H., van Hul W., Whyte M.P., Nakatsuka K., Hovy L., Anderson D.M.
    Nat. Genet. 24:45-48(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT FEO LEU-LEU-CYS-ALA-LEU-LEU-21 INS, VARIANT PDB2 ALA-LEU-LEU-LEU-LEU-CYS-ALA-LEU-LEU-21 INS, VARIANT VAL-192.
  10. Cited for: VARIANTS OPTB7 ARG-53; CYS-129; GLY-170; ARG-175 AND SER-244.

Entry informationi

Entry nameiTNR11_HUMAN
AccessioniPrimary (citable) accession number: Q9Y6Q6
Secondary accession number(s): I4EC36
, I4EC38, I4EC39, I7JE63, N0GVH0, Q59EP9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: November 1, 1999
Last modified: March 4, 2015
This is version 134 of the entry and version 1 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, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.