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Protein

Tumor necrosis factor receptor superfamily member 13B

Gene

TNFRSF13B

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

Functioni

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.2 Publications

GO - Molecular functioni

  1. receptor activity Source: ProtInc

GO - Biological processi

  1. B cell homeostasis Source: Ensembl
  2. cell surface receptor signaling pathway Source: ProtInc
  3. hematopoietic progenitor cell differentiation Source: Ensembl
  4. negative regulation of B cell proliferation Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Adaptive immunity, Immunity

Enzyme and pathway databases

SignaLinkiO14836.

Names & Taxonomyi

Protein namesi
Recommended name:
Tumor necrosis factor receptor superfamily member 13B
Alternative name(s):
Transmembrane activator and CAML interactor
CD_antigen: CD267
Gene namesi
Name:TNFRSF13B
Synonyms:TACI
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:18153. TNFRSF13B.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 165165ExtracellularSequence AnalysisAdd
BLAST
Transmembranei166 – 18621Helical; Signal-anchor for type III membrane proteinSequence AnalysisAdd
BLAST
Topological domaini187 – 293107CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. external side of plasma membrane Source: Ensembl
  2. integral component of plasma membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Immunodeficiency, common variable, 21 Publication

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

Disease descriptionA primary immunodeficiency characterized by antibody deficiency, hypogammaglobulinemia, recurrent bacterial infections and an inability to mount an antibody response to antigen. The defect results from a failure of B-cell differentiation and impaired secretion of immunoglobulins; the numbers of circulating B-cells is usually in the normal range, but can be low.

See also OMIM:240500
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti104 – 1041C → R in CVID2 and IGAD2. 1 Publication
Corresponds to variant rs34557412 [ dbSNP | Ensembl ].
VAR_024027
Natural varianti181 – 1811A → G in CVID2. 1 Publication
VAR_024028
Natural varianti202 – 2021R → H in CVID2. 1 Publication
VAR_024029
Immunoglobulin A deficiency 21 Publication

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

Disease descriptionSelective 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.

See also OMIM:609529
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti104 – 1041C → R in CVID2 and IGAD2. 1 Publication
Corresponds to variant rs34557412 [ dbSNP | Ensembl ].
VAR_024027

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi240500. phenotype.
609529. phenotype.
Orphaneti1572. Common variable immunodeficiency.
69127. Immunoglobulin A deficiency.
PharmGKBiPA38509.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 293293Tumor necrosis factor receptor superfamily member 13BPRO_0000058931Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi34 ↔ 47By similarity
Disulfide bondi50 ↔ 62By similarity
Disulfide bondi54 ↔ 66By similarity
Disulfide bondi71 ↔ 86
Disulfide bondi89 ↔ 100
Disulfide bondi93 ↔ 104
Glycosylationi128 – 1281N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiO14836.
PaxDbiO14836.
PRIDEiO14836.

PTM databases

PhosphoSiteiO14836.

Expressioni

Tissue specificityi

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.

Gene expression databases

BgeeiO14836.
CleanExiHS_TNFRSF13B.
ExpressionAtlasiO14836. baseline and differential.
GenevestigatoriO14836.

Organism-specific databases

HPAiHPA030453.

Interactioni

Subunit structurei

Binds TRAF2, TRAF5 and TRAF6. Binds the NH2-terminal domain of CAMLG with its C-terminus.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
MYD88Q9983612EBI-519160,EBI-447677
TNFSF13BQ9Y2757EBI-519160,EBI-519169

Protein-protein interaction databases

BioGridi117046. 12 interactions.
DIPiDIP-6224N.
IntActiO14836. 11 interactions.
STRINGi9606.ENSP00000261652.

Structurei

Secondary structure

1
293
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi73 – 753Combined sources
Beta strandi77 – 804Combined sources
Turni81 – 844Combined sources
Beta strandi85 – 884Combined sources
Helixi89 – 924Combined sources
Helixi98 – 1003Combined sources
Helixi101 – 1044Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XU1X-ray1.90R/S/T68-109[»]
1XUTNMR-A68-109[»]
ProteinModelPortaliO14836.
SMRiO14836. Positions 68-109.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO14836.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati33 – 6735TNFR-Cys 1Add
BLAST
Repeati70 – 10435TNFR-Cys 2Add
BLAST

Sequence similaritiesi

Contains 2 TNFR-Cys repeats.Curated

Keywords - Domaini

Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG43611.
GeneTreeiENSGT00390000013910.
HOGENOMiHOG000273905.
HOVERGENiHBG058015.
InParanoidiO14836.
KOiK05150.
OMAiCHTRTTV.
OrthoDBiEOG7W6WMN.
PhylomeDBiO14836.
TreeFamiTF337993.

Family and domain databases

InterProiIPR015384. TACI_Cys-rich-dom.
IPR022317. TNFR_13B.
[Graphical view]
PfamiPF09305. TACI-CRD2. 2 hits.
[Graphical view]
PRINTSiPR01963. TNFACTORR13B.
PROSITEiPS00652. TNFR_NGFR_1. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O14836-1) [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
MSGLGRSRRG GRSRVDQEER FPQGLWTGVA MRSCPEEQYW DPLLGTCMSC
60 70 80 90 100
KTICNHQSQR TCAAFCRSLS CRKEQGKFYD HLLRDCISCA SICGQHPKQC
110 120 130 140 150
AYFCENKLRS PVNLPPELRR QRSGEVENNS DNSGRYQGLE HRGSEASPAL
160 170 180 190 200
PGLKLSADQV ALVYSTLGLC LCAVLCCFLV AVACFLKKRG DPCSCQPRSR
210 220 230 240 250
PRQSPAKSSQ DHAMEAGSPV STSPEPVETC SFCFPECRAP TQESAVTPGT
260 270 280 290
PDPTCAGRWG CHTRTTVLQP CPHIPDSGLG IVCVPAQEGG PGA
Length:293
Mass (Da):31,816
Last modified:January 1, 1998 - v1
Checksum:i411799F3DE17A5EB
GO
Isoform 2 (identifier: O14836-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     21-67: FPQGLWTGVAMRSCPEEQYWDPLLGTCMSCKTICNHQSQRTCAAFCR → W

Show »
Length:247
Mass (Da):26,664
Checksum:i850E1F4C2578E8E6
GO
Isoform 3 (identifier: O14836-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     150-176: LPGLKLSADQVALVYSTLGLCLCAVLC → PRGCPAPGTRKSFWDKENFQGEGFHLG
     177-293: Missing.

Note: No experimental confirmation available.

Show »
Length:176
Mass (Da):19,865
Checksum:i4506764708AF788C
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti56 – 561H → N Found in a renal cell carcinoma sample; somatic mutation. 1 Publication
VAR_064758
Natural varianti104 – 1041C → R in CVID2 and IGAD2. 1 Publication
Corresponds to variant rs34557412 [ dbSNP | Ensembl ].
VAR_024027
Natural varianti181 – 1811A → G in CVID2. 1 Publication
VAR_024028
Natural varianti202 – 2021R → H in CVID2. 1 Publication
VAR_024029
Natural varianti251 – 2511P → L.1 Publication
Corresponds to variant rs34562254 [ dbSNP | Ensembl ].
VAR_052353

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei21 – 6747FPQGL…AAFCR → W in isoform 2. 2 PublicationsVSP_013798Add
BLAST
Alternative sequencei150 – 17627LPGLK…CAVLC → PRGCPAPGTRKSFWDKENFQ GEGFHLG in isoform 3. 1 PublicationVSP_054184Add
BLAST
Alternative sequencei177 – 293117Missing in isoform 3. 1 PublicationVSP_054185Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF023614 mRNA. Translation: AAC51790.1.
AY302137 mRNA. Translation: AAP57629.1.
AK301032 mRNA. Translation: BAH13394.1.
AK313302 mRNA. Translation: BAG36107.1.
CH471196 Genomic DNA. Translation: EAW55729.1.
BC109392 mRNA. Translation: AAI09393.1.
CCDSiCCDS11181.1. [O14836-1]
RefSeqiNP_036584.1. NM_012452.2. [O14836-1]
UniGeneiHs.158341.

Genome annotation databases

EnsembliENST00000261652; ENSP00000261652; ENSG00000240505. [O14836-1]
ENST00000583789; ENSP00000462952; ENSG00000240505. [O14836-2]
GeneIDi23495.
KEGGihsa:23495.
UCSCiuc002gqs.1. human. [O14836-1]
uc002gqt.1. human. [O14836-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

TNFRSF13Bbase

TNFRSF13B mutation db

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF023614 mRNA. Translation: AAC51790.1.
AY302137 mRNA. Translation: AAP57629.1.
AK301032 mRNA. Translation: BAH13394.1.
AK313302 mRNA. Translation: BAG36107.1.
CH471196 Genomic DNA. Translation: EAW55729.1.
BC109392 mRNA. Translation: AAI09393.1.
CCDSiCCDS11181.1. [O14836-1]
RefSeqiNP_036584.1. NM_012452.2. [O14836-1]
UniGeneiHs.158341.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XU1X-ray1.90R/S/T68-109[»]
1XUTNMR-A68-109[»]
ProteinModelPortaliO14836.
SMRiO14836. Positions 68-109.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117046. 12 interactions.
DIPiDIP-6224N.
IntActiO14836. 11 interactions.
STRINGi9606.ENSP00000261652.

Chemistry

GuidetoPHARMACOLOGYi1885.

PTM databases

PhosphoSiteiO14836.

Proteomic databases

MaxQBiO14836.
PaxDbiO14836.
PRIDEiO14836.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261652; ENSP00000261652; ENSG00000240505. [O14836-1]
ENST00000583789; ENSP00000462952; ENSG00000240505. [O14836-2]
GeneIDi23495.
KEGGihsa:23495.
UCSCiuc002gqs.1. human. [O14836-1]
uc002gqt.1. human. [O14836-2]

Organism-specific databases

CTDi23495.
GeneCardsiGC17M016832.
GeneReviewsiTNFRSF13B.
H-InvDBHIX0173687.
HGNCiHGNC:18153. TNFRSF13B.
HPAiHPA030453.
MIMi240500. phenotype.
604907. gene.
609529. phenotype.
neXtProtiNX_O14836.
Orphaneti1572. Common variable immunodeficiency.
69127. Immunoglobulin A deficiency.
PharmGKBiPA38509.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG43611.
GeneTreeiENSGT00390000013910.
HOGENOMiHOG000273905.
HOVERGENiHBG058015.
InParanoidiO14836.
KOiK05150.
OMAiCHTRTTV.
OrthoDBiEOG7W6WMN.
PhylomeDBiO14836.
TreeFamiTF337993.

Enzyme and pathway databases

SignaLinkiO14836.

Miscellaneous databases

ChiTaRSiTNFRSF13B. human.
EvolutionaryTraceiO14836.
GeneWikiiTNFRSF13B.
GenomeRNAii23495.
NextBioi35480074.
PROiO14836.
SOURCEiSearch...

Gene expression databases

BgeeiO14836.
CleanExiHS_TNFRSF13B.
ExpressionAtlasiO14836. baseline and differential.
GenevestigatoriO14836.

Family and domain databases

InterProiIPR015384. TACI_Cys-rich-dom.
IPR022317. TNFR_13B.
[Graphical view]
PfamiPF09305. TACI-CRD2. 2 hits.
[Graphical view]
PRINTSiPR01963. TNFACTORR13B.
PROSITEiPS00652. TNFR_NGFR_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "NF-AT activation induced by a CAML-interacting member of the tumor necrosis factor receptor superfamily."
    von Buelow G.-U., Bram R.J.
    Science 278:138-141(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: B-cell.
  2. Zhou G., Ke R., Li H., Zheng G., Shen C., Lin L., Yang S.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  3. "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] (ISOFORMS 1 AND 3), VARIANT LEU-251.
    Tissue: Spleen.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 2).
  6. "Tumor necrosis factor (TNF) receptor superfamily member TACI is a high affinity receptor for TNF family members APRIL and BLyS."
    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.
    J. Biol. Chem. 275:35478-35485(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. Cited for: FUNCTION.
  8. "TACI is a TRAF-interacting receptor for TALL-1, a tumor necrosis factor family member involved in B cell regulation."
    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.
    J. Exp. Med. 192:137-143(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRAF2 AND TRAF5.
  9. "Structures of APRIL-receptor complexes: like BCMA, TACI employs only a single cysteine-rich domain for high affinity ligand binding."
    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.
    J. Biol. Chem. 280:7218-7227(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 68-109 IN COMPLEX WITH MOUSE TNFSF13, STRUCTURE BY NMR OF 68-109.
  10. "TACI is mutant in common variable immunodeficiency and IgA deficiency."
    Castigli E., Wilson S.A., Garibyan L., Rachid R., Bonilla F., Schneider L., Geha R.S.
    Nat. Genet. 37:829-834(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT IGAD2 ARG-104, VARIANTS CVID2 ARG-104; GLY-181 AND HIS-202.
  11. Cited for: VARIANT ASN-56.

Entry informationi

Entry nameiTR13B_HUMAN
AccessioniPrimary (citable) accession number: O14836
Secondary accession number(s): B2R8B0
, B7Z6V8, Q32LX4, Q7Z6F5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: January 1, 1998
Last modified: February 4, 2015
This is version 132 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 17
    Human chromosome 17: 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.