DSK2A_ARATH
ID DSK2A_ARATH Reviewed; 538 AA.
AC Q9SII9; Q9C5L7;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 25-MAY-2022, entry version 150.
DE RecName: Full=Ubiquitin domain-containing protein DSK2a;
GN Name=DSK2A; OrderedLocusNames=At2g17190; ORFNames=T23A1.5;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, INTERACTION WITH RPN10 AND RPN13, AND MUTAGENESIS OF ILE-61.
RX PubMed=20059542; DOI=10.1111/j.1742-4658.2009.07531.x;
RA Fatimababy A.S., Lin Y.L., Usharani R., Radjacommare R., Wang H.T.,
RA Tsai H.L., Lee Y., Fu H.;
RT "Cross-species divergence of the major recognition pathways of
RT ubiquitylated substrates for ubiquitin/26S proteasome-mediated
RT proteolysis.";
RL FEBS J. 277:796-816(2010).
RN [6]
RP REVIEW.
RX PubMed=20399133; DOI=10.1016/j.tplants.2010.03.004;
RA Fu H., Lin Y.L., Fatimababy A.S.;
RT "Proteasomal recognition of ubiquitylated substrates.";
RL Trends Plant Sci. 15:375-386(2010).
RN [7]
RP FUNCTION, AND POLYUBIQUITIN BINDING.
RX PubMed=21764993; DOI=10.1105/tpc.111.086702;
RA Lin Y.-L., Sung S.-C., Tsai H.-L., Yu T.-T., Radjacommare R., Usharani R.,
RA Fatimababy A.S., Lin H.-Y., Wang Y.-Y., Fu H.;
RT "The defective proteasome but not substrate recognition function is
RT responsible for the null phenotypes of the Arabidopsis proteasome subunit
RT RPN10.";
RL Plant Cell 23:2754-2773(2011).
RN [8]
RP INTERACTION WITH PEX2 AND PEX12, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=23336935; DOI=10.1111/jipb.12014;
RA Kaur N., Zhao Q., Xie Q., Hu J.;
RT "Arabidopsis RING peroxins are E3 ubiquitin ligases that interact with two
RT homologous ubiquitin receptor proteins(F).";
RL J. Integr. Plant Biol. 55:108-120(2013).
CC -!- FUNCTION: Binds and presumably selects ubiquitin-conjugates for
CC destruction. Prefers multiubiquitin chains rather than single
CC ubiquitins, with a binding affinity for 'Lys-48'-linked ubiquitin
CC chains. Acts as a ubiquitin receptor that associates with the 26S
CC proteasomal docking subunit RPN10 for the indirect recognition of
CC ubiquitinated substrates of ubiquitin/26S proteasome-mediated
CC proteolysis (UPP). {ECO:0000269|PubMed:20059542,
CC ECO:0000269|PubMed:21764993}.
CC -!- SUBUNIT: Interacts with 'Lys-48'-linked polyubiquitin chains via its
CC UBA domain. Interacts with RPN10 and RPN13. Interacts with PEX2 and
CC PEX12. {ECO:0000269|PubMed:20059542, ECO:0000269|PubMed:23336935}.
CC -!- INTERACTION:
CC Q9SII9; Q9CA86: PEX2; NbExp=3; IntAct=EBI-6860633, EBI-4470254;
CC Q9SII9; Q8RUC6: RUB2; NbExp=3; IntAct=EBI-6860633, EBI-25522172;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23336935}. Cytoplasm
CC {ECO:0000269|PubMed:23336935}.
CC -!- TISSUE SPECIFICITY: Ubiquitous with a strong expression level in
CC inflorescence. {ECO:0000269|PubMed:23336935}.
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DR EMBL; AC007127; AAD25137.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC06596.1; -; Genomic_DNA.
DR EMBL; AF360159; AAK25869.1; -; mRNA.
DR EMBL; AY042828; AAK68768.1; -; mRNA.
DR EMBL; AY081450; AAM10012.1; -; mRNA.
DR EMBL; AY113886; AAM44934.1; -; mRNA.
DR EMBL; AK228616; BAF00527.1; -; mRNA.
DR PIR; B84549; B84549.
DR RefSeq; NP_565407.1; NM_127273.4.
DR AlphaFoldDB; Q9SII9; -.
DR SMR; Q9SII9; -.
DR BioGRID; 1581; 4.
DR IntAct; Q9SII9; 4.
DR STRING; 3702.AT2G17190.1; -.
DR PaxDb; Q9SII9; -.
DR PRIDE; Q9SII9; -.
DR ProteomicsDB; 222182; -.
DR EnsemblPlants; AT2G17190.1; AT2G17190.1; AT2G17190.
DR GeneID; 816224; -.
DR Gramene; AT2G17190.1; AT2G17190.1; AT2G17190.
DR KEGG; ath:AT2G17190; -.
DR Araport; AT2G17190; -.
DR TAIR; locus:2059677; AT2G17190.
DR eggNOG; KOG0010; Eukaryota.
DR HOGENOM; CLU_024293_4_0_1; -.
DR InParanoid; Q9SII9; -.
DR OMA; GMNASNF; -.
DR OrthoDB; 1553668at2759; -.
DR PhylomeDB; Q9SII9; -.
DR PRO; PR:Q9SII9; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SII9; baseline and differential.
DR Genevisible; Q9SII9; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR InterPro; IPR006636; STI1_HS-bd.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF00627; UBA; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00727; STI1; 4.
DR SMART; SM00165; UBA; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Reference proteome; Repeat.
FT CHAIN 1..538
FT /note="Ubiquitin domain-containing protein DSK2a"
FT /id="PRO_0000423179"
FT DOMAIN 18..93
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 138..179
FT /note="STI1 1"
FT DOMAIN 192..231
FT /note="STI1 2"
FT DOMAIN 357..394
FT /note="STI1 3"
FT DOMAIN 398..433
FT /note="STI1 4"
FT DOMAIN 491..535
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT REGION 95..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 61
FT /note="I->A: Abolishes interaction with RPN13."
FT /evidence="ECO:0000269|PubMed:20059542"
SQ SEQUENCE 538 AA; 57285 MW; AF2BF2BF36413DBD CRC64;
MGGEADSRQP LTAEGVAVAV NVRCSNGTKF SVTTSLDSTV ESFKELIAQN SDVPANQQRL
IYKGRILKDD QTLLSYGLQA DHTVHMVRGF VPSSPSAPAA NAGNQTTAPQ AVGSNDSSNL
GGGESLFPGL GFNPLGGGNA MAGLFGSGLP DLEQAQQQLA QNPNMIREMM NTPAIQNLMN
NPEFMRSMIM NNPQMRELVD RNPELGHVLN DPSILRQTLE AARNPELMRE MMRNTDRAMS
NIESMPEGFN MLRRMYENVQ EPLMNATTMS ENAGNNTSSN PFAALLGNQG VTTQGSDTSN
NISAPNAETG TPNANPLPNP WGATAGQTTA PGRTNAGLGG LGGLGGLGGL GMLGADSPLG
ATPDASQLSQ ILQNPAMSQM MQSVLSNPQY MNQLMSLNPQ LRSMLDMNPQ LREMMQNPDF
LRQFSSPEMM QQMMSLQQSL FSQNRNTAGQ DPTQTGAATG TANNGGLDLL MNMFGSLGAG
GLSGTNQPNV PPEERFATQL QQLQEMGFYD RAENIRALLA TNGNVNAAVE RLLGSIGQ
