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Q9Y275

- TN13B_HUMAN

UniProt

Q9Y275 - TN13B_HUMAN

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Protein

Tumor necrosis factor ligand superfamily member 13B

Gene

TNFSF13B

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

Functioni

Cytokine that binds to TNFRSF13B/TACI and TNFRSF17/BCMA. TNFSF13/APRIL binds to the same 2 receptors. Together, they form a 2 ligands -2 receptors pathway involved in the stimulation of B- and T-cell function and the regulation of humoral immunity. A third B-cell specific BAFF-receptor (BAFFR/BR3) promotes the survival of mature B-cells and the B-cell response.1 Publication
Isoform 2 seems to inhibit isoform 1 secretion and bioactivity.By similarity
Isoform 3: Acts as a transcription factor for its own parent gene, in association with NF-kappa-B p50 subunit, at least in autoimmune and proliferative B-cell diseases. The presence of Delta4BAFF is essential for soluble BAFF release by IFNG/IFN-gamma-stimulated monocytes and for B-cell survival. It can directly or indirectly regulate the differential expression of a large number of genes involved in the innate immune response and the regulation of apoptosis.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei133 – 1342Cleavage

GO - Molecular functioni

  1. receptor binding Source: ProtInc

GO - Biological processi

  1. B cell costimulation Source: Ensembl
  2. B cell homeostasis Source: Ensembl
  3. cell proliferation Source: ProtInc
  4. immune response Source: InterPro
  5. immunoglobulin secretion Source: Ensembl
  6. positive regulation of B cell proliferation Source: Ensembl
  7. positive regulation of cell proliferation Source: ProtInc
  8. positive regulation of germinal center formation Source: Ensembl
  9. positive regulation of T cell proliferation Source: Ensembl
  10. signal transduction Source: ProtInc
  11. T cell costimulation Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Cytokine

Keywords - Biological processi

Immunity

Names & Taxonomyi

Protein namesi
Recommended name:
Tumor necrosis factor ligand superfamily member 13B
Alternative name(s):
B lymphocyte stimulator
Short name:
BLyS
B-cell-activating factor
BAFF
Dendritic cell-derived TNF-like molecule
TNF- and APOL-related leukocyte expressed ligand 1
Short name:
TALL-1
CD_antigen: CD257
Cleaved into the following 2 chains:
Gene namesi
Name:TNFSF13B
Synonyms:BAFF, BLYS, TALL1, TNFSF20, ZTNF4
ORF Names:UNQ401/PRO738
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 13

Organism-specific databases

HGNCiHGNC:11929. TNFSF13B.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProt
  2. extracellular space Source: UniProtKB-KW
  3. integral component of membrane Source: UniProtKB
  4. perinuclear region of cytoplasm Source: UniProt
  5. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA434.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 285285Tumor necrosis factor ligand superfamily member 13b, membrane formPRO_0000034528Add
BLAST
Chaini134 – 285152Tumor necrosis factor ligand superfamily member 13b, soluble formPRO_0000034529Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi124 – 1241N-linked (GlcNAc...)
Disulfide bondi232 ↔ 245
Glycosylationi242 – 2421N-linked (GlcNAc...) (high mannose)

Post-translational modificationi

The soluble form derives from the membrane form by proteolytic processing.
Isoform 2 is not efficiently shed from the membrane unlike isoform 1.By similarity
N-glycosylated.

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9Y275.
PRIDEiQ9Y275.

PTM databases

PhosphoSiteiQ9Y275.

Expressioni

Tissue specificityi

Abundantly expressed in peripheral blood Leukocytes and is specifically expressed in monocytes and macrophages. Also found in the spleen, lymph node, bone marrow, T-cells and dendritic cells. A lower expression seen in placenta, heart, lung, fetal liver, thymus, and pancreas. Isoform 2 is expressed in many myeloid cell lines.1 Publication

Inductioni

Up-regulated by exposure to IFNG/IFN-gamma. Down-regulated by phorbol myristate acetate/ionomycin treatment.

Gene expression databases

BgeeiQ9Y275.
CleanExiHS_TNFSF13B.
GenevestigatoriQ9Y275.

Organism-specific databases

HPAiCAB009188.

Interactioni

Subunit structurei

Homotrimer. Isoform 2 heteromultimerizes with isoform 1, probably limiting the amount of functional isoform 1 on the cell surface. Isoform 3 is unlikely form trimers or bind to BAFF receptors.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TNFRSF13BO148367EBI-519169,EBI-519160

Protein-protein interaction databases

BioGridi115915. 48 interactions.
DIPiDIP-6225N.
IntActiQ9Y275. 2 interactions.
STRINGi9606.ENSP00000365048.

Structurei

Secondary structure

1
285
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi146 – 1516
Beta strandi158 – 1603
Beta strandi163 – 1653
Beta strandi168 – 18114
Beta strandi184 – 1874
Beta strandi191 – 20111
Beta strandi205 – 21511
Beta strandi225 – 23511
Beta strandi238 – 2403
Beta strandi243 – 25311
Beta strandi258 – 2658
Turni274 – 2763
Beta strandi277 – 2837

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JH5X-ray3.00A/B/C/D/E/F/G/H/I/J142-285[»]
1KD7X-ray2.80A/B/C/K/L/M133-285[»]
1KXGX-ray2.00A/B/C/D/E/F134-285[»]
1OQDX-ray2.60A/B/C/D/E/F/G/H/I/J142-285[»]
1OQEX-ray2.50A/B/C/D/E/F/G/H/I/J142-285[»]
1OSGX-ray3.00A/B/C/D/E/F82-285[»]
1OTZX-ray3.300/1/2/3/4/5/6/7/8/9/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d/e/f/g/h/i/j/k/l/m/n/o/p/q/r/s/t/u/v/w/x138-285[»]
3V56X-ray3.00A/B/C/D/E/F82-285[»]
ProteinModelPortaliQ9Y275.
SMRiQ9Y275. Positions 142-285.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y275.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4646CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini68 – 285218ExtracellularSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei47 – 6721Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Sequence similaritiesi

Belongs to the tumor necrosis factor family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG47835.
GeneTreeiENSGT00530000063837.
HOGENOMiHOG000036810.
HOVERGENiHBG061472.
InParanoidiQ9Y275.
KOiK05476.
OMAiILPQKES.
OrthoDBiEOG7T4MM3.
PhylomeDBiQ9Y275.
TreeFamiTF332331.

Family and domain databases

Gene3Di2.60.120.40. 1 hit.
InterProiIPR006052. TNF_dom.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view]
PfamiPF00229. TNF. 1 hit.
[Graphical view]
SMARTiSM00207. TNF. 1 hit.
[Graphical view]
SUPFAMiSSF49842. SSF49842. 1 hit.
PROSITEiPS50049. TNF_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Y275-1) [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
MDDSTEREQS RLTSCLKKRE EMKLKECVSI LPRKESPSVR SSKDGKLLAA
60 70 80 90 100
TLLLALLSCC LTVVSFYQVA ALQGDLASLR AELQGHHAEK LPAGAGAPKA
110 120 130 140 150
GLEEAPAVTA GLKIFEPPAP GEGNSSQNSR NKRAVQGPEE TVTQDCLQLI
160 170 180 190 200
ADSETPTIQK GSYTFVPWLL SFKRGSALEE KENKILVKET GYFFIYGQVL
210 220 230 240 250
YTDKTYAMGH LIQRKKVHVF GDELSLVTLF RCIQNMPETL PNNSCYSAGI
260 270 280
AKLEEGDELQ LAIPRENAQI SLDGDVTFFG ALKLL
Length:285
Mass (Da):31,223
Last modified:November 1, 1999 - v1
Checksum:i48ED0D7AB38C8867
GO
Isoform 2 (identifier: Q9Y275-2) [UniParc]FASTAAdd to Basket

Also known as: DeltaBAFF

The sequence of this isoform differs from the canonical sequence as follows:
     142-160: Missing.

Show »
Length:266
Mass (Da):29,137
Checksum:i6BD06F90061152C6
GO
Isoform 3 (identifier: Q9Y275-3) [UniParc]FASTAAdd to Basket

Also known as: Delta4BAFF

The sequence of this isoform differs from the canonical sequence as follows:
     162-164: SYT → FIY
     165-285: Missing.

Show »
Length:164
Mass (Da):17,578
Checksum:iF74F5E404973B730
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti105 – 1051A → T.1 Publication
Corresponds to variant rs201543678 [ dbSNP | Ensembl ].
VAR_013483

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei142 – 16019Missing in isoform 2. 1 PublicationVSP_041183Add
BLAST
Alternative sequencei162 – 1643SYT → FIY in isoform 3. 1 PublicationVSP_047591
Alternative sequencei165 – 285121Missing in isoform 3. 1 PublicationVSP_047592Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF136293 mRNA. Translation: AAD29421.1.
AF116456 mRNA. Translation: AAD25356.1.
AF132600 mRNA. Translation: AAD21092.1.
AY302751 mRNA. Translation: AAP83164.1.
HM636064 mRNA. Translation: ADK91575.1.
AF186114 mRNA. Translation: AAF01432.1.
AF134715 mRNA. Translation: AAF60219.1.
AY129225 mRNA. Translation: AAN08421.1.
EF064706 Genomic DNA. Translation: ABK41889.1.
AY358881 mRNA. Translation: AAQ89240.1.
CR541818 mRNA. Translation: CAG46617.1.
AL157762 Genomic DNA. Translation: CAH70631.1.
CH471085 Genomic DNA. Translation: EAX09099.1.
BC020674 mRNA. Translation: AAH20674.1.
AB073225 Genomic DNA. Translation: BAB90856.1.
CCDSiCCDS45067.1. [Q9Y275-2]
CCDS9509.1. [Q9Y275-1]
RefSeqiNP_001139117.1. NM_001145645.2. [Q9Y275-2]
NP_006564.1. NM_006573.4. [Q9Y275-1]
UniGeneiHs.525157.

Genome annotation databases

EnsembliENST00000375887; ENSP00000365048; ENSG00000102524. [Q9Y275-1]
ENST00000430559; ENSP00000389540; ENSG00000102524. [Q9Y275-2]
ENST00000542136; ENSP00000445334; ENSG00000102524. [Q9Y275-3]
GeneIDi10673.
KEGGihsa:10673.
UCSCiuc001vqr.3. human. [Q9Y275-1]
uc010agj.3. human. [Q9Y275-2]

Polymorphism databases

DMDMi13124573.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Protein Spotlight

Proteic grace - Issue 77 of December 2006

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF136293 mRNA. Translation: AAD29421.1 .
AF116456 mRNA. Translation: AAD25356.1 .
AF132600 mRNA. Translation: AAD21092.1 .
AY302751 mRNA. Translation: AAP83164.1 .
HM636064 mRNA. Translation: ADK91575.1 .
AF186114 mRNA. Translation: AAF01432.1 .
AF134715 mRNA. Translation: AAF60219.1 .
AY129225 mRNA. Translation: AAN08421.1 .
EF064706 Genomic DNA. Translation: ABK41889.1 .
AY358881 mRNA. Translation: AAQ89240.1 .
CR541818 mRNA. Translation: CAG46617.1 .
AL157762 Genomic DNA. Translation: CAH70631.1 .
CH471085 Genomic DNA. Translation: EAX09099.1 .
BC020674 mRNA. Translation: AAH20674.1 .
AB073225 Genomic DNA. Translation: BAB90856.1 .
CCDSi CCDS45067.1. [Q9Y275-2 ]
CCDS9509.1. [Q9Y275-1 ]
RefSeqi NP_001139117.1. NM_001145645.2. [Q9Y275-2 ]
NP_006564.1. NM_006573.4. [Q9Y275-1 ]
UniGenei Hs.525157.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1JH5 X-ray 3.00 A/B/C/D/E/F/G/H/I/J 142-285 [» ]
1KD7 X-ray 2.80 A/B/C/K/L/M 133-285 [» ]
1KXG X-ray 2.00 A/B/C/D/E/F 134-285 [» ]
1OQD X-ray 2.60 A/B/C/D/E/F/G/H/I/J 142-285 [» ]
1OQE X-ray 2.50 A/B/C/D/E/F/G/H/I/J 142-285 [» ]
1OSG X-ray 3.00 A/B/C/D/E/F 82-285 [» ]
1OTZ X-ray 3.30 0/1/2/3/4/5/6/7/8/9/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d/e/f/g/h/i/j/k/l/m/n/o/p/q/r/s/t/u/v/w/x 138-285 [» ]
3V56 X-ray 3.00 A/B/C/D/E/F 82-285 [» ]
ProteinModelPortali Q9Y275.
SMRi Q9Y275. Positions 142-285.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115915. 48 interactions.
DIPi DIP-6225N.
IntActi Q9Y275. 2 interactions.
STRINGi 9606.ENSP00000365048.

Chemistry

ChEMBLi CHEMBL2364158.
DrugBanki DB08879. Belimumab.

PTM databases

PhosphoSitei Q9Y275.

Polymorphism databases

DMDMi 13124573.

Proteomic databases

PaxDbi Q9Y275.
PRIDEi Q9Y275.

Protocols and materials databases

DNASUi 10673.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000375887 ; ENSP00000365048 ; ENSG00000102524 . [Q9Y275-1 ]
ENST00000430559 ; ENSP00000389540 ; ENSG00000102524 . [Q9Y275-2 ]
ENST00000542136 ; ENSP00000445334 ; ENSG00000102524 . [Q9Y275-3 ]
GeneIDi 10673.
KEGGi hsa:10673.
UCSCi uc001vqr.3. human. [Q9Y275-1 ]
uc010agj.3. human. [Q9Y275-2 ]

Organism-specific databases

CTDi 10673.
GeneCardsi GC13P108903.
HGNCi HGNC:11929. TNFSF13B.
HPAi CAB009188.
MIMi 603969. gene.
neXtProti NX_Q9Y275.
PharmGKBi PA434.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG47835.
GeneTreei ENSGT00530000063837.
HOGENOMi HOG000036810.
HOVERGENi HBG061472.
InParanoidi Q9Y275.
KOi K05476.
OMAi ILPQKES.
OrthoDBi EOG7T4MM3.
PhylomeDBi Q9Y275.
TreeFami TF332331.

Miscellaneous databases

EvolutionaryTracei Q9Y275.
GeneWikii B-cell_activating_factor.
GenomeRNAii 10673.
NextBioi 35496036.
PROi Q9Y275.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y275.
CleanExi HS_TNFSF13B.
Genevestigatori Q9Y275.

Family and domain databases

Gene3Di 2.60.120.40. 1 hit.
InterProi IPR006052. TNF_dom.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view ]
Pfami PF00229. TNF. 1 hit.
[Graphical view ]
SMARTi SM00207. TNF. 1 hit.
[Graphical view ]
SUPFAMi SSF49842. SSF49842. 1 hit.
PROSITEi PS50049. TNF_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "TALL-1 is a novel member of the TNF family that is down-regulated by mitogens."
    Shu H.-B., Hu W.-H., Johnson H.
    J. Leukoc. Biol. 65:680-683(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 134-148.
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Monocyte and Neutrophil.
  4. "DeltaBAFF, an alternate splice isoform that regulates receptor binding and biopresentation of the B cell survival cytokine, BAFF."
    Gavin A.L., Ait-Azzouzene D., Ware C.F., Nemazee D.
    J. Biol. Chem. 278:38220-38228(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, SUBUNIT.
  5. "The complexity of the BAFF TNF-family members: implications for autoimmunity."
    Lahiri A., Pochard P., Le Pottier L., Tobon G.J., Bendaoud B., Youinou P., Pers J.O.
    J. Autoimmun. 39:189-198(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION (ISOFORM 3), SUBUNIT, ALTERNATIVE SPLICING.
  6. "Homo sapiens homolog of tumor necrosis factor."
    Farrah T., Gross J., Piddington C., O'Hara P.
    Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  7. "A novel dendritic cell-derived TNF-like molecule."
    Zhang W., Wan T., Yu Y., Cao X.
    Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Dendritic cell.
  8. Gao H., He F., Li R.
    Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  9. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  11. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  12. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  13. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  14. "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] (ISOFORM 1).
    Tissue: Placenta.
  15. "New polymorphisms of human BLyS gene."
    Kawasaki A., Tsuchiya N., Fukazawa T., Hashimoto H., Tokunaga K.
    Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-135, VARIANT THR-105.
  16. Cited for: FUNCTION.
  17. "Crystal structure of sTALL-1 reveals a virus-like assembly of TNF family ligands."
    Liu Y., Xu L., Opalka N., Kappler J., Shu H.-B., Zhang G.
    Cell 108:383-394(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 142-285.
  18. "Crystal structure of extracellular human BAFF, a TNF family member that stimulates B lymphocytes."
    Karpusas M., Cachero T.G., Qian F., Boriack-Sjodin A., Mullen C., Strauch K., Hsu Y.-M., Kalled S.L.
    J. Mol. Biol. 315:1145-1154(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 136-285.
  19. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 134-285.

Entry informationi

Entry nameiTN13B_HUMAN
AccessioniPrimary (citable) accession number: Q9Y275
Secondary accession number(s): E0ADT7, Q6FHD6, Q7Z5J2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: November 1, 1999
Last modified: October 29, 2014
This is version 156 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, Direct protein sequencing, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 13
    Human chromosome 13: 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. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  8. SIMILARITY comments
    Index of protein domains and families

External Data

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