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Protein

Ubiquitin domain-containing protein DSK2a

Gene

DSK2A

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Binds and presumably selects ubiquitin-conjugates for destruction. Prefers multiubiquitin chains rather than single ubiquitins, with a binding affinity for 'Lys-48'-linked ubiquitin chains. Acts as a ubiquitin receptor that associates with the 26S proteasomal docking subunit RPN10 for the indirect recognition of ubiquitinated substrates of ubiquitin/26S proteasome-mediated proteolysis (UPP).2 Publications

GO - Molecular functioni

  • polyubiquitin binding Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin domain-containing protein DSK2a
Gene namesi
Name:DSK2A
Ordered Locus Names:At2g17190
ORF Names:T23A1.5
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRiAT2G17190.

Subcellular locationi

  • Nucleus 1 Publication
  • Cytoplasm 1 Publication

GO - Cellular componenti

  • cytosol Source: TAIR
  • nucleus Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi61 – 611I → A: Abolishes interaction with RPN13. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 538538Ubiquitin domain-containing protein DSK2aPRO_0000423179Add
BLAST

Proteomic databases

PaxDbiQ9SII9.
PRIDEiQ9SII9.

Expressioni

Tissue specificityi

Ubiquitous with a strong expression level in inflorescence.1 Publication

Gene expression databases

GenevisibleiQ9SII9. AT.

Interactioni

Subunit structurei

Interacts with 'Lys-48'-linked polyubiquitin chains via its UBA domain. Interacts with RPN10 and RPN13. Interacts with PEX2 and PEX12.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PEX2Q9CA863EBI-6860633,EBI-4470254

GO - Molecular functioni

  • polyubiquitin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi1581. 3 interactions.
IntActiQ9SII9. 3 interactions.
STRINGi3702.AT2G17190.1.

Structurei

3D structure databases

ProteinModelPortaliQ9SII9.
SMRiQ9SII9. Positions 20-88, 492-535.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 9376Ubiquitin-likePROSITE-ProRule annotationAdd
BLAST
Domaini138 – 17942STI1 1Add
BLAST
Domaini192 – 23140STI1 2Add
BLAST
Domaini357 – 39438STI1 3Add
BLAST
Domaini398 – 43336STI1 4Add
BLAST
Domaini491 – 53545UBAPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 4 STI1 domains.Curated
Contains 1 UBA domain.PROSITE-ProRule annotation
Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0010. Eukaryota.
COG5272. LUCA.
HOGENOMiHOG000234878.
InParanoidiQ9SII9.
KOiK04523.
OMAiPPGINTD.
PhylomeDBiQ9SII9.

Family and domain databases

InterProiIPR006636. STI1_HS-bd.
IPR015940. UBA.
IPR009060. UBA-like.
IPR015496. Ubiquilin.
IPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_dom.
[Graphical view]
PANTHERiPTHR10677. PTHR10677. 1 hit.
PfamiPF00627. UBA. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]
SMARTiSM00727. STI1. 4 hits.
SM00165. UBA. 1 hit.
SM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50030. UBA. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9SII9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGGEADSRQP LTAEGVAVAV NVRCSNGTKF SVTTSLDSTV ESFKELIAQN
60 70 80 90 100
SDVPANQQRL IYKGRILKDD QTLLSYGLQA DHTVHMVRGF VPSSPSAPAA
110 120 130 140 150
NAGNQTTAPQ AVGSNDSSNL GGGESLFPGL GFNPLGGGNA MAGLFGSGLP
160 170 180 190 200
DLEQAQQQLA QNPNMIREMM NTPAIQNLMN NPEFMRSMIM NNPQMRELVD
210 220 230 240 250
RNPELGHVLN DPSILRQTLE AARNPELMRE MMRNTDRAMS NIESMPEGFN
260 270 280 290 300
MLRRMYENVQ EPLMNATTMS ENAGNNTSSN PFAALLGNQG VTTQGSDTSN
310 320 330 340 350
NISAPNAETG TPNANPLPNP WGATAGQTTA PGRTNAGLGG LGGLGGLGGL
360 370 380 390 400
GMLGADSPLG ATPDASQLSQ ILQNPAMSQM MQSVLSNPQY MNQLMSLNPQ
410 420 430 440 450
LRSMLDMNPQ LREMMQNPDF LRQFSSPEMM QQMMSLQQSL FSQNRNTAGQ
460 470 480 490 500
DPTQTGAATG TANNGGLDLL MNMFGSLGAG GLSGTNQPNV PPEERFATQL
510 520 530
QQLQEMGFYD RAENIRALLA TNGNVNAAVE RLLGSIGQ
Length:538
Mass (Da):57,285
Last modified:June 1, 2002 - v2
Checksum:iAF2BF2BF36413DBD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC007127 Genomic DNA. Translation: AAD25137.2.
CP002685 Genomic DNA. Translation: AEC06596.1.
AF360159 mRNA. Translation: AAK25869.1.
AY042828 mRNA. Translation: AAK68768.1.
AY081450 mRNA. Translation: AAM10012.1.
AY113886 mRNA. Translation: AAM44934.1.
AK228616 mRNA. Translation: BAF00527.1.
PIRiB84549.
RefSeqiNP_565407.1. NM_127273.3.
UniGeneiAt.21851.

Genome annotation databases

EnsemblPlantsiAT2G17190.1; AT2G17190.1; AT2G17190.
GeneIDi816224.
GrameneiAT2G17190.1; AT2G17190.1; AT2G17190.
KEGGiath:AT2G17190.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC007127 Genomic DNA. Translation: AAD25137.2.
CP002685 Genomic DNA. Translation: AEC06596.1.
AF360159 mRNA. Translation: AAK25869.1.
AY042828 mRNA. Translation: AAK68768.1.
AY081450 mRNA. Translation: AAM10012.1.
AY113886 mRNA. Translation: AAM44934.1.
AK228616 mRNA. Translation: BAF00527.1.
PIRiB84549.
RefSeqiNP_565407.1. NM_127273.3.
UniGeneiAt.21851.

3D structure databases

ProteinModelPortaliQ9SII9.
SMRiQ9SII9. Positions 20-88, 492-535.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi1581. 3 interactions.
IntActiQ9SII9. 3 interactions.
STRINGi3702.AT2G17190.1.

Proteomic databases

PaxDbiQ9SII9.
PRIDEiQ9SII9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G17190.1; AT2G17190.1; AT2G17190.
GeneIDi816224.
GrameneiAT2G17190.1; AT2G17190.1; AT2G17190.
KEGGiath:AT2G17190.

Organism-specific databases

TAIRiAT2G17190.

Phylogenomic databases

eggNOGiKOG0010. Eukaryota.
COG5272. LUCA.
HOGENOMiHOG000234878.
InParanoidiQ9SII9.
KOiK04523.
OMAiPPGINTD.
PhylomeDBiQ9SII9.

Miscellaneous databases

PROiQ9SII9.

Gene expression databases

GenevisibleiQ9SII9. AT.

Family and domain databases

InterProiIPR006636. STI1_HS-bd.
IPR015940. UBA.
IPR009060. UBA-like.
IPR015496. Ubiquilin.
IPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_dom.
[Graphical view]
PANTHERiPTHR10677. PTHR10677. 1 hit.
PfamiPF00627. UBA. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]
SMARTiSM00727. STI1. 4 hits.
SM00165. UBA. 1 hit.
SM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50030. UBA. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Cross-species divergence of the major recognition pathways of ubiquitylated substrates for ubiquitin/26S proteasome-mediated proteolysis."
    Fatimababy A.S., Lin Y.L., Usharani R., Radjacommare R., Wang H.T., Tsai H.L., Lee Y., Fu H.
    FEBS J. 277:796-816(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RPN10 AND RPN13, MUTAGENESIS OF ILE-61.
  6. "Proteasomal recognition of ubiquitylated substrates."
    Fu H., Lin Y.L., Fatimababy A.S.
    Trends Plant Sci. 15:375-386(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  7. "The defective proteasome but not substrate recognition function is responsible for the null phenotypes of the Arabidopsis proteasome subunit RPN10."
    Lin Y.L., Sung S.C., Tsai H.L., Yu T.T., Radjacommare R., Usharani R., Fatimababy A.S., Lin H.Y., Wang Y.Y., Fu H.
    Plant Cell 23:2754-2773(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, POLYUBIQUITIN BINDING.
  8. "Arabidopsis RING peroxins are E3 ubiquitin ligases that interact with two homologous ubiquitin receptor proteins(F)."
    Kaur N., Zhao Q., Xie Q., Hu J.
    J. Integr. Plant Biol. 55:108-120(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PEX2 AND PEX12, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiDSK2A_ARATH
AccessioniPrimary (citable) accession number: Q9SII9
Secondary accession number(s): Q9C5L7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 24, 2013
Last sequence update: June 1, 2002
Last modified: February 17, 2016
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.