ID   DSK2B_ARATH             Reviewed;         551 AA.
AC   Q9SII8; Q94C51;
DT   24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 141.
DE   RecName: Full=Ubiquitin domain-containing protein DSK2b;
GN   Name=DSK2B; OrderedLocusNames=At2g17200; ORFNames=T23A1.6;
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   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   [5]
RP   FUNCTION, POLYUBIQUITIN BINDING, INTERACTION WITH RPN10, AND MUTAGENESIS OF
RP   ILE-61 AND VAL-87.
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   [6]
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:21764993}.
CC   -!- SUBUNIT: Interacts with 'Lys-48'-linked polyubiquitin chains via its
CC       UBA domain. Interacts with RPN10 via its ubiquitin-like domain.
CC       Interacts with PEX2 and PEX12. {ECO:0000269|PubMed:21764993,
CC       ECO:0000269|PubMed:23336935}.
CC   -!- INTERACTION:
CC       Q9SII8; Q9CA86: PEX2; NbExp=4; IntAct=EBI-4433040, EBI-4470254;
CC       Q9SII8; P55034: RPN10; NbExp=2; IntAct=EBI-4433040, EBI-2620423;
CC       Q9SII8; O48726: RPN13; NbExp=5; IntAct=EBI-4433040, EBI-7710745;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23336935}. Cytoplasm
CC       {ECO:0000269|PubMed:23336935}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:23336935}.
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DR   EMBL; AC007127; AAD25138.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC06597.1; -; Genomic_DNA.
DR   EMBL; AY035177; AAK59681.1; -; mRNA.
DR   EMBL; AY142486; AAN13037.1; -; mRNA.
DR   PIR; C84549; C84549.
DR   RefSeq; NP_179311.1; NM_127274.3.
DR   AlphaFoldDB; Q9SII8; -.
DR   SMR; Q9SII8; -.
DR   BioGRID; 1582; 9.
DR   IntAct; Q9SII8; 10.
DR   MINT; Q9SII8; -.
DR   STRING; 3702.AT2G17200.1; -.
DR   PaxDb; Q9SII8; -.
DR   PRIDE; Q9SII8; -.
DR   ProteomicsDB; 221909; -.
DR   EnsemblPlants; AT2G17200.1; AT2G17200.1; AT2G17200.
DR   GeneID; 816225; -.
DR   Gramene; AT2G17200.1; AT2G17200.1; AT2G17200.
DR   KEGG; ath:AT2G17200; -.
DR   Araport; AT2G17200; -.
DR   TAIR; locus:2059682; AT2G17200.
DR   eggNOG; KOG0010; Eukaryota.
DR   HOGENOM; CLU_024293_4_0_1; -.
DR   InParanoid; Q9SII8; -.
DR   OMA; GMDMFGP; -.
DR   OrthoDB; 1553668at2759; -.
DR   PhylomeDB; Q9SII8; -.
DR   PRO; PR:Q9SII8; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9SII8; baseline and differential.
DR   Genevisible; Q9SII8; 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..551
FT                   /note="Ubiquitin domain-containing protein DSK2b"
FT                   /id="PRO_0000423180"
FT   DOMAIN          18..93
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          143..184
FT                   /note="STI1 1"
FT   DOMAIN          197..236
FT                   /note="STI1 2"
FT   DOMAIN          373..410
FT                   /note="STI1 3"
FT   DOMAIN          414..449
FT                   /note="STI1 4"
FT   DOMAIN          504..548
FT                   /note="UBA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT   REGION          88..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          294..336
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          455..475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..126
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         61
FT                   /note="I->A: Strongly reduces interaction with RPN10."
FT                   /evidence="ECO:0000269|PubMed:21764993"
FT   MUTAGEN         87
FT                   /note="V->A: Abolishes interaction with RPN10."
FT                   /evidence="ECO:0000269|PubMed:21764993"
FT   CONFLICT        345
FT                   /note="D -> N (in Ref. 3; AAK59681)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   551 AA;  58054 MW;  EFE8FA99BED21974 CRC64;
     MGGEGDSSQP QSGEGEAVAV NIRCSNGTKF SVKTSLDSTV ESFKELVAQS SDVPANQQRL
     IYKGRILKDD QTLLSYGLQA DHTIHMVRGS APSSAPPPAP AASQTTAPSV TRGVGSDNSS
     NLGGASPGES LFPGLGFNPL GGGNAMSGLF GAGLPDLVQT QQQLAQNPNM IRDMMNTPAI
     QNLMNNPEFM RSMIMNNPQM RELVDRNPEL GHVLNDPSIL RQTLEAARNP ELMREMMRNT
     DRAMSNIESM PEGFNMLRRM YENVQEPLMN ATTMSGNAGN NTGSNPFAAL LGNQGVTTQG
     SDASNNSSTP NAGTGTIPNA NPLPNPWGAT GGQTTAPGRT NVGGDARSPG LGGLGGLGSL
     GGLGGLGMLG ADSPLGATPD ASQLSQLLQN PAISQMMQSV FSNPQYMNQL MSLNPQLRSM
     LDSNPQLREM MQNPDFLRQF SSPEMMQQMM TLQQSLSQNR NTASQDAGQT GAATGNNGGL
     DLLMNMFGSL GAGGLSGTNQ SNVPPEERYA TQLQQLQEMG FYDRAENIRA LLATNGNVNA
     AVERLLGSIG Q