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Protein

Exosome complex component RRP43

Gene

EXOSC8

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

Functioni

Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. EXOSC8 binds to ARE-containing RNAs.2 Publications

GO - Molecular functioni

  • AU-rich element binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

rRNA processing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_18355. ATF4 activates genes.
REACT_20619. mRNA decay by 3' to 5' exoribonuclease.
REACT_24915. Butyrate Response Factor 1 (BRF1) destabilizes mRNA.
REACT_25042. KSRP destabilizes mRNA.
REACT_25064. Tristetraprolin (TTP) destabilizes mRNA.

Names & Taxonomyi

Protein namesi
Recommended name:
Exosome complex component RRP43
Alternative name(s):
Exosome component 8
Opa-interacting protein 2
Short name:
OIP-2
Ribosomal RNA-processing protein 43
p9
Gene namesi
Name:EXOSC8
Synonyms:OIP2, RRP43
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:17035. EXOSC8.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Nucleus 1 Publication
  • Nucleusnucleolus By similarity

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • exosome (RNase complex) Source: UniProtKB
  • nucleolus Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Exosome, Nucleus

Pathology & Biotechi

Involvement in diseasei

Pontocerebellar hypoplasia 1C (PCH1C)1 Publication

The disease is caused by mutations affecting the gene represented in this entry. EXOSC8 dysfunction causes myelin disruption through an imbalanced supply of myelin proteins due to dysregulation of their ARE-containing mRNAs (PubMed:24989451).

Disease descriptionA severe autosomal recessive neurodegenerative disease characterized by cerebellar and corpus callosum hypoplasia, abnormal myelination of the central nervous system, and spinal motor neuron disease. Affected individuals manifest failure to thrive, severe muscle weakness, spasticity and psychomotor retardation. Vision and hearing are impaired.

See also OMIM:616081
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2 – 21A → V in PCH1C. 1 Publication
VAR_072558
Natural varianti272 – 2721S → T in PCH1C. 1 Publication
VAR_072559

Keywords - Diseasei

Disease mutation, Neurodegeneration

Organism-specific databases

MIMi616081. phenotype.
Orphaneti2254. Pontocerebellar hypoplasia type 1.
PharmGKBiPA134922251.

Polymorphism and mutation databases

BioMutaiEXOSC8.
DMDMi21759409.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 276275Exosome complex component RRP43PRO_0000139967Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ96B26.
PaxDbiQ96B26.
PeptideAtlasiQ96B26.
PRIDEiQ96B26.

2D gel databases

SWISS-2DPAGEQ96B26.

PTM databases

PhosphoSiteiQ96B26.

Expressioni

Gene expression databases

BgeeiQ96B26.
CleanExiHS_EXOSC8.
ExpressionAtlasiQ96B26. baseline and differential.
GenevisibleiQ96B26. HS.

Organism-specific databases

HPAiCAB034240.
HPA039702.
HPA043942.

Interactioni

Subunit structurei

Component of the RNA exosome complex. Specifically part of the catalytically inactive RNA exosome core (Exo-9) complex which is believed to associate with catalytic subunits EXOSC10, and DIS3 or DIS3L in cytoplasmic- and nuclear-specific RNA exosome complex forms. Exo-9 is formed by a hexameric ring of RNase PH domain-containing subunits specifically containing the heterodimers EXOSC4-EXOSC9, EXOSC5-EXOSC8 and EXOSC6-EXOSC7, and peripheral S1 domain-containing components EXOSC1, EXOSC2 and EXOSC3 located on the top of the ring structure. Binds outer membrane protein opap from Neisseria gonorrhoeae.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AENQ8WTP83EBI-371922,EBI-8637627
ATF2P153363EBI-371922,EBI-1170906
COL23A1Q86Y223EBI-371922,EBI-373279
COX5AP206743EBI-371922,EBI-715032
DUSP23Q9BVJ73EBI-371922,EBI-724940
EXOSC3Q9NQT53EBI-371922,EBI-371866
EXOSC5Q9NQT49EBI-371922,EBI-371876
FAM90A1Q86YD73EBI-371922,EBI-6658203
FRG1Q143313EBI-371922,EBI-2515248
MORN4Q8WVZ33EBI-371922,EBI-10277137
OTUD4Q018043EBI-371922,EBI-1054396
RELQ048643EBI-371922,EBI-307352
SNRPCQ5TAL43EBI-371922,EBI-10246938
TCEA2Q155603EBI-371922,EBI-710310
TCEA2Q86VL03EBI-371922,EBI-10259904
TFAP4Q016643EBI-371922,EBI-2514218
TXNDC17Q9BRA23EBI-371922,EBI-1055906
TXNDC9O145303EBI-371922,EBI-707554

Protein-protein interaction databases

BioGridi116468. 60 interactions.
DIPiDIP-31133N.
IntActiQ96B26. 40 interactions.
MINTiMINT-4536555.
STRINGi9606.ENSP00000374354.

Structurei

Secondary structure

1
276
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 199Combined sources
Beta strandi37 – 393Combined sources
Beta strandi43 – 5311Combined sources
Beta strandi56 – 6611Combined sources
Beta strandi71 – 733Combined sources
Beta strandi80 – 845Combined sources
Beta strandi87 – 893Combined sources
Beta strandi95 – 973Combined sources
Helixi100 – 11617Combined sources
Helixi121 – 1244Combined sources
Beta strandi126 – 1283Combined sources
Beta strandi133 – 14311Combined sources
Helixi150 – 16112Combined sources
Beta strandi172 – 1754Combined sources
Beta strandi194 – 2007Combined sources
Turni202 – 2043Combined sources
Beta strandi207 – 2093Combined sources
Turni212 – 2165Combined sources
Beta strandi219 – 2268Combined sources
Beta strandi232 – 2387Combined sources
Helixi245 – 26723Combined sources
Turni268 – 2736Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NN6X-ray3.35C1-276[»]
ProteinModelPortaliQ96B26.
SMRiQ96B26. Positions 7-275.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96B26.

Family & Domainsi

Sequence similaritiesi

Belongs to the RNase PH family.Curated

Phylogenomic databases

eggNOGiCOG2123.
GeneTreeiENSGT00530000063093.
HOGENOMiHOG000229504.
HOVERGENiHBG051522.
InParanoidiQ96B26.
KOiK12586.
OMAiAKLQDCI.
OrthoDBiEOG7D59PC.
PhylomeDBiQ96B26.
TreeFamiTF320415.

Family and domain databases

Gene3Di3.30.230.70. 1 hit.
InterProiIPR001247. ExoRNase_PH_dom1.
IPR015847. ExoRNase_PH_dom2.
IPR027408. PNPase/RNase_PH_dom.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PfamiPF01138. RNase_PH. 1 hit.
PF03725. RNase_PH_C. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 2 hits.
SSF55666. SSF55666. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q96B26-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAGFKTVEP LEYYRRFLKE NCRPDGRELG EFRTTTVNIG SISTADGSAL
60 70 80 90 100
VKLGNTTVIC GVKAEFAAPS TDAPDKGYVV PNVDLPPLCS SRFRSGPPGE
110 120 130 140 150
EAQVASQFIA DVIENSQIIQ KEDLCISPGK LVWVLYCDLI CLDYDGNILD
160 170 180 190 200
ACTFALLAAL KNVQLPEVTI NEETALAEVN LKKKSYLNIR THPVATSFAV
210 220 230 240 250
FDDTLLIVDP TGEEEHLATG TLTIVMDEEG KLCCLHKPGG SGLTGAKLQD
260 270
CMSRAVTRHK EVKKLMDEVI KSMKPK
Length:276
Mass (Da):30,040
Last modified:December 1, 2001 - v1
Checksum:iFC8F5BAE74A1FF55
GO

Sequence cautioni

The sequence CAI14013.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence EAX08581.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti265 – 27612LMDEV…SMKPK → TDG in AAC39558 (PubMed:9466265).CuratedAdd
BLAST

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2 – 21A → V in PCH1C. 1 Publication
VAR_072558
Natural varianti272 – 2721S → T in PCH1C. 1 Publication
VAR_072559

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL138706 Genomic DNA. Translation: CAI14013.1. Sequence problems.
CH471075 Genomic DNA. Translation: EAX08581.1. Sequence problems.
BC020773 mRNA. Translation: AAH20773.1.
AF025438 mRNA. Translation: AAC39558.1.
CCDSiCCDS31958.1.
RefSeqiNP_852480.1. NM_181503.2.
UniGeneiHs.294041.

Genome annotation databases

EnsembliENST00000389704; ENSP00000374354; ENSG00000120699.
GeneIDi11340.
KEGGihsa:11340.
UCSCiuc001uwa.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL138706 Genomic DNA. Translation: CAI14013.1. Sequence problems.
CH471075 Genomic DNA. Translation: EAX08581.1. Sequence problems.
BC020773 mRNA. Translation: AAH20773.1.
AF025438 mRNA. Translation: AAC39558.1.
CCDSiCCDS31958.1.
RefSeqiNP_852480.1. NM_181503.2.
UniGeneiHs.294041.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NN6X-ray3.35C1-276[»]
ProteinModelPortaliQ96B26.
SMRiQ96B26. Positions 7-275.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116468. 60 interactions.
DIPiDIP-31133N.
IntActiQ96B26. 40 interactions.
MINTiMINT-4536555.
STRINGi9606.ENSP00000374354.

PTM databases

PhosphoSiteiQ96B26.

Polymorphism and mutation databases

BioMutaiEXOSC8.
DMDMi21759409.

2D gel databases

SWISS-2DPAGEQ96B26.

Proteomic databases

MaxQBiQ96B26.
PaxDbiQ96B26.
PeptideAtlasiQ96B26.
PRIDEiQ96B26.

Protocols and materials databases

DNASUi11340.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000389704; ENSP00000374354; ENSG00000120699.
GeneIDi11340.
KEGGihsa:11340.
UCSCiuc001uwa.3. human.

Organism-specific databases

CTDi11340.
GeneCardsiGC13P037572.
HGNCiHGNC:17035. EXOSC8.
HPAiCAB034240.
HPA039702.
HPA043942.
MIMi606019. gene.
616081. phenotype.
neXtProtiNX_Q96B26.
Orphaneti2254. Pontocerebellar hypoplasia type 1.
PharmGKBiPA134922251.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2123.
GeneTreeiENSGT00530000063093.
HOGENOMiHOG000229504.
HOVERGENiHBG051522.
InParanoidiQ96B26.
KOiK12586.
OMAiAKLQDCI.
OrthoDBiEOG7D59PC.
PhylomeDBiQ96B26.
TreeFamiTF320415.

Enzyme and pathway databases

ReactomeiREACT_18355. ATF4 activates genes.
REACT_20619. mRNA decay by 3' to 5' exoribonuclease.
REACT_24915. Butyrate Response Factor 1 (BRF1) destabilizes mRNA.
REACT_25042. KSRP destabilizes mRNA.
REACT_25064. Tristetraprolin (TTP) destabilizes mRNA.

Miscellaneous databases

EvolutionaryTraceiQ96B26.
GeneWikiiExosome_component_8.
GenomeRNAii11340.
NextBioi43089.
PROiQ96B26.
SOURCEiSearch...

Gene expression databases

BgeeiQ96B26.
CleanExiHS_EXOSC8.
ExpressionAtlasiQ96B26. baseline and differential.
GenevisibleiQ96B26. HS.

Family and domain databases

Gene3Di3.30.230.70. 1 hit.
InterProiIPR001247. ExoRNase_PH_dom1.
IPR015847. ExoRNase_PH_dom2.
IPR027408. PNPase/RNase_PH_dom.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PfamiPF01138. RNase_PH. 1 hit.
PF03725. RNase_PH_C. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 2 hits.
SSF55666. SSF55666. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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].
    Tissue: Uterus.
  4. "Using the yeast two-hybrid system to identify human epithelial cell proteins that bind gonococcal Opa proteins: intracellular gonococci bind pyruvate kinase via their Opa proteins and require host pyruvate for growth."
    Williams J.M., Chen G.-C., Zhu L., Rest R.F.
    Mol. Microbiol. 27:171-186(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-276.
  5. "AU binding proteins recruit the exosome to degrade ARE-containing mRNAs."
    Chen C.-Y., Gherzi R., Ong S.-E., Chan E.L., Raijmakers R., Pruijn G.J.M., Stoecklin G., Moroni C., Mann M., Karin M.
    Cell 107:451-464(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE RNA EXOSOME CORE COMPLEX.
  6. "Protein-protein interactions between human exosome components support the assembly of RNase PH-type subunits into a six-membered PNPase-like ring."
    Raijmakers R., Vree Egberts W., van Venrooij W.J., Pruijn G.J.M.
    J. Mol. Biol. 323:653-663(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN INTERACTION.
  7. "A protein interaction framework for human mRNA degradation."
    Lehner B., Sanderson C.M.
    Genome Res. 14:1315-1323(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN INTERACTION.
  8. "Sequence-specific RNA binding mediated by the RNase PH domain of components of the exosome."
    Anderson J.R., Mukherjee D., Muthukumaraswamy K., Moraes K.C., Wilusz C.J., Wilusz J.
    RNA 12:1810-1816(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ARE-CONTAINING MRNA-BINDING.
  9. "Human cell growth requires a functional cytoplasmic exosome, which is involved in various mRNA decay pathways."
    van Dijk E.L., Schilders G., Pruijn G.J.
    RNA 13:1027-1035(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MRNA DEGRADATION, SUBCELLULAR LOCATION.
  10. "Dis3-like 1: a novel exoribonuclease associated with the human exosome."
    Staals R.H., Bronkhorst A.W., Schilders G., Slomovic S., Schuster G., Heck A.J., Raijmakers R., Pruijn G.J.
    EMBO J. 29:2358-2367(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE RNA EXOSOME COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  13. Cited for: INVOLVEMENT IN PCH1C, VARIANTS PCH1C VAL-2 AND THR-272.
  14. "Reconstitution, activities, and structure of the eukaryotic RNA exosome."
    Liu Q., Greimann J.C., Lima C.D.
    Cell 127:1223-1237(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS), LACK OF CATALYTIC ACTIVITY, RECONSTITUTION OF THE RNA EXOSOME CORE COMPLEX.
  15. Erratum
    Liu Q., Greimann J.C., Lima C.D.
    Cell 131:188-189(2007)

Entry informationi

Entry nameiEXOS8_HUMAN
AccessioniPrimary (citable) accession number: Q96B26
Secondary accession number(s): O43480, Q5TBA5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: December 1, 2001
Last modified: July 22, 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

Caution

The six exosome core subunits containing a RNase PH-domain are not phosphorolytically active.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.