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UniProtKB/Swiss-Prot entry O14836


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name TR13B_HUMAN
Primary accession number O14836
Secondary accession numbers B2R8B0 Q7Z6F5
Integrated into Swiss-Prot on May 27, 2002
Sequence was last modified on January 1, 1998 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 78)
Name and origin of the protein
Protein name Tumor necrosis factor receptor superfamily member 13B
Synonyms Transmembrane activator and CAML interactor
CD267 antigen
Gene name
Name: TNFRSF13B
Synonyms: TACI
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=B-cell;
DOI=10.1126/science.278.5335.138; PubMed=9311921 [NCBI, ExPASy, EBI, Israel, Japan]
von Buelow G.-U., Bram R.J.;
"NF-AT activation induced by a CAML-interacting member of the tumor necrosis factor receptor superfamily.";
Science 278:138-141(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Zhou G., Ke R., Li H., Zheng G., Shen C., Lin L., Yang S.;
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LEU-251.
TISSUE=Spleen;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[4]
FUNCTION.
DOI=10.1074/jbc.M005224200; PubMed=10956646 [NCBI, ExPASy, EBI, Israel, Japan]
Wu Y., Bressette D., Carrell J.A., Kaufman T., Feng P., Taylor K., Gan Y., Cho Y.H., Garcia A.D., Gollatz E., Dimke D., LaFleur D., Migone T.S., Nardelli B., Wei P., Ruben S.M., Ullrich S.J., Olsen H.S., Kanakaraj P., Moore P.A., Baker K.P.;
"Tumor necrosis factor (TNF) receptor superfamily member TACI is a high affinity receptor for TNF family members APRIL and BLyS.";
J. Biol. Chem. 275:35478-35485(2000).
[5]
FUNCTION.
DOI=10.1038/79802; PubMed=10973284 [NCBI, ExPASy, EBI, Israel, Japan]
Yu G., Boone T., Delaney J., Hawkins N., Kelley M.J., Ramakrishnan M., McCabe S., Qiu W.R., Kornuc M., Xia X.-Z., Guo J., Stolina M., Boyle W.J., Sarosi I., Hsu H., Senaldi G., Theill L.E.;
"APRIL and TALL-I and receptors BCMA and TACI: system for regulating humoral immunity.";
Nat. Immunol. 1:252-256(2000).
[6]
INTERACTION WITH TRAF2 AND TRAF5.
DOI=10.1084/jem.192.1.137; PubMed=10880535 [NCBI, ExPASy, EBI, Israel, Japan]
Xia X.-Z., Treanor J., Senaldi G., Khare S.D., Boone T., Kelley M., Theill L.E., Colombero A., Solovyev I., Lee F., McCabe S., Elliott R., Miner K., Hawkins N., Guo J., Stolina M., Yu G., Wang J., Delaney J., Meng S.-Y., Boyle W.J., Hsu H.;
"TACI is a TRAF-interacting receptor for TALL-1, a tumor necrosis factor family member involved in B cell regulation.";
J. Exp. Med. 192:137-143(2000).
[7]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 68-109 IN COMPLEX WITH MOUSE TNFSF13, AND STRUCTURE BY NMR OF 68-109.
DOI=10.1074/jbc.M411714200; PubMed=15542592 [NCBI, ExPASy, EBI, Israel, Japan]
Hymowitz S.G., Patel D.R., Wallweber H.J., Runyon S., Yan M., Yin J., Shriver S.K., Gordon N.C., Pan B., Skelton N.J., Kelley R.F., Starovasnik M.A.;
"Structures of APRIL-receptor complexes: like BCMA, TACI employs only a single cysteine-rich domain for high affinity ligand binding.";
J. Biol. Chem. 280:7218-7227(2005).
[8]
VARIANT CVID/IGAD2 ARG-104, AND VARIANTS CVID GLY-181 AND HIS-202.
DOI=10.1038/ng1601; PubMed=16007086 [NCBI, ExPASy, EBI, Israel, Japan]
Castigli E., Wilson S.A., Garibyan L., Rachid R., Bonilla F., Schneider L., Geha R.S.;
"TACI is mutant in common variable immunodeficiency and IgA deficiency.";
Nat. Genet. 37:829-834(2005).
Comments
  • FUNCTION: Receptor for TNFSF13/APRIL and TNFSF13B/TALL1/BAFF/BLYS that binds both ligands with similar high affinity. Mediates calcineurin-dependent activation of NF-AT, as well as activation of NF-kappa-B and AP-1. Involved in the stimulation of B- and T-cell function and the regulation of humoral immunity.
  • SUBUNIT: Binds TRAF2, TRAF5 and TRAF6. Binds the NH2-terminal domain of CAMLG with its C-terminus.
  • INTERACTION:
    O75888:TNFSF13; NbExp=1; IntAct=EBI-519160, EBI-519208;
    Q9Y275:TNFSF13B; NbExp=4; IntAct=EBI-519160, EBI-519169;
  • SUBCELLULAR LOCATION: Membrane; Single-pass type III membrane protein.
  • ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.
    Name1
    Isoform IDO14836-1
    This is the isoform sequence displayed in this entry.
    Name2
    Isoform IDO14836-2
    Features which should be applied to build the isoform sequence: VSP_013798.
  • TISSUE SPECIFICITY: Highly expressed in spleen, thymus, small intestine and peripheral blood leukocytes. Expressed in resting B-cells and activated T-cells, but not in resting T-cells.
  • DISEASE: Defects in TNFRSF13B are a cause of common variable immunodeficiency (CVID) [MIM:240500]. CVID is characterized by a deficiency in all immunoglobulin (Ig) isotypes. Individuals with CVID suffer from recurrent sinopulmonary and gastrointestinal infections and have an increased incidence of autoimmune disorders and of lymphoid and non-lymphoid malignancies. There is evidence for a global isotype switching defect in some individuals with CVID. But CVID is a complex and heterogeneous disease in which defects in B-cell survival, number of circulating CD27+ memory B-cells (including IgM+CD27+ B-cells), B-cell activation after antigen receptor cross-linking, T-cell signaling and cytokine expression have been observed.
  • DISEASE: Defects in TNFRSF13B are a cause of immunoglobulin A deficiency 2 (IGAD2) [MIM:609529]. Selective deficiency of immunoglobulin A (IGAD) is the most common form of primary immunodeficiency, with an incidence of approximately 1 in 600 individuals in the western world. Individuals with symptomatic IGAD often have deficiency of IgG subclasses or decreased antibody response to carbohydrate antigens such as pneumococcal polysaccharide vaccine. Individuals with IGAD also suffer from recurrent sinopulmonary and gastrointestinal infections and have an increased incidence of autoimmune disorders and of lymphoid and non-lymphoid malignancies. In vitro studies have suggested that some individuals with IGAD have impaired isotype class switching to IgA and others may have a post-switch defect. IGAD and CVID have been known to coexist in families. Some individuals initially present with IGAD1 and then develop CVID. These observations suggest that some cases of IGAD and CVID may have a common etiology.
  • SIMILARITY: Contains 2 TNFR-Cys repeats.
  • WEB RESOURCE: Name=TNFRSF13Bbase; Note=TNFRSF13B mutation db; URL="http://bioinf.uta.fi/TNFRSF13Bbase/";.
  • WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=TNFRSF13B";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF023614; AAC51790.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY302137; AAP57629.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK313302; BAG36107.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00018362; -.
IPI00385403; -.
RefSeq NP_036584.1; -.
UniGene Hs.158341
3D structure databases
PDB
1XU1; X-ray; 1.90 A; R/S/T=68-109.[ExPASy / RCSB / EBI]
1XUT; NMR; -; A=68-109.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1XU1; -.
1XUT; -.
ModBase O14836.
Protein-protein interaction databases
IntAct O14836; 3.
Enzyme and pathway databases
Pathway_Interaction_DB syndecan_2_pathway; Syndecan-2-mediated signaling events.
syndecan_4_pathway; Syndecan-4-mediated signaling events.
Organism-specific databases
GeneCards GC17M016783; -.
H-InvDB HIX0013576; -.
HGNC HGNC:18153; TNFRSF13B.
GenAtlas TNFRSF13B.
MIM 240500; phenotype. [NCBI / EBI]
604907; gene. [NCBI / EBI]
609529; phenotype. [NCBI / EBI]
Orphanet 1572; Common variable immunodeficiency.
69127; Immunoglobulin A deficiency.
PharmGKB PA38509; -.
Gene expression databases
ArrayExpress O14836; -.
Bgee O14836; -.
CleanEx HS_TNFRSF13B; -.
GermOnline ENSG00000108516; Homo sapiens.
Ontologies
GO
GO:0005887; Cellular component: integral to plasma membrane (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0004872; Molecular function: receptor activity (traceable author statement from ProtInc).
GO:0007166; Biological process: cell surface receptor linked signal transduction (traceable author statement from ProtInc).
GO:0006955; Biological process: immune response (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR015384; TACI-CRD2.
IPR001368; TNFR_Cys_rich_reg.
Graphical view of domain structure.
Pfam PF09305; TACI-CRD2; 1.
Pfam graphical view of domain structure.
PROSITE PS00652; TNFR_NGFR_1; 1.
PS50050; TNFR_NGFR_2; FALSE_NEG.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE O14836; -.
Genome annotation databases
Ensembl ENSG00000108516; Homo sapiens. [Contig view]
GeneID 23495; -.
KEGG hsa:23495; -.
Phylogenomic databases
HOGENOM O14836; -.
HOVERGEN O14836; -.
OMA O14836; FPECRAP.
Other
NextBio 45863; -.
SOURCE TNFRSF13B; Homo sapiens.
ProtoNet O14836.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Disease mutation; Disulfide bond; Glycoprotein; Immune response; Membrane; Polymorphism; Receptor; Repeat; Signal-anchor; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   293  293     Tumor necrosis factor receptor superfamily member 13B. PRO_0000058931
TOPO_DOM   1   165  165     Extracellular (Potential). 
TRANSMEM   166   186  21     Signal-anchor for type III membrane protein (Potential). 
TOPO_DOM   187   293  107     Cytoplasmic (Potential). 
REPEAT   33    67  35     TNFR-Cys 1. 
REPEAT   70   104  35     TNFR-Cys 2. 
CARBOHYD   128   128        N-linked (GlcNAc...) (Potential). 
DISULFID   34    47        By similarity. 
DISULFID   50    62        By similarity. 
DISULFID   54    66        By similarity. 
DISULFID   71    86         
DISULFID   89   100         
DISULFID   93   104         
VAR_SEQ   21    67        FPQGLWTGVAMRSCPEEQYWDPLLGTCMSCKTICNHQSQR TCAAFCR -> W (in isoform 2). VSP_013798
VARIANT   104   104  1     C -> R (in CVID and IGAD2). VAR_024027 [3D]
VARIANT   181   181  1     A -> G (in CVID). VAR_024028 
VARIANT   202   202  1     R -> H (in CVID). VAR_024029 
VARIANT   251   251  1     P -> L (in dbSNP:rs34562254 [NCBI]). VAR_052353 
HELIX   73    75  3      
STRAND   77    80  4      
TURN   81    84  4      
STRAND   85    88  4      
HELIX   89    92  4      
HELIX   98   100  3      
HELIX   101   104  4      
Sequence information
Length: 293 AA [This is the length of the unprocessed precursor] Molecular weight: 31816 Da [This is the MW of the unprocessed precursor] CRC64: 411799F3DE17A5EB [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSGLGRSRRG GRSRVDQEER FPQGLWTGVA MRSCPEEQYW DPLLGTCMSC KTICNHQSQR 

        70         80         90        100        110        120 
TCAAFCRSLS CRKEQGKFYD HLLRDCISCA SICGQHPKQC AYFCENKLRS PVNLPPELRR 

       130        140        150        160        170        180 
QRSGEVENNS DNSGRYQGLE HRGSEASPAL PGLKLSADQV ALVYSTLGLC LCAVLCCFLV 

       190        200        210        220        230        240 
AVACFLKKRG DPCSCQPRSR PRQSPAKSSQ DHAMEAGSPV STSPEPVETC SFCFPECRAP 

       250        260        270        280        290 
TQESAVTPGT PDPTCAGRWG CHTRTTVLQP CPHIPDSGLG IVCVPAQEGG PGA 

O14836 in FASTA format

View entry in raw text format (no links)
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