(data stored in ACNUC21429 zone)

SWISSPROT: 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   11-DEC-2019, entry version 141.
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       Q9CA86:PEX2; NbExp=3; IntAct=EBI-6860633, EBI-4470254;
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}.
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   SMR; Q9SII9; -.
DR   BioGrid; 1581; 3.
DR   IntAct; Q9SII9; 3.
DR   STRING; 3702.AT2G17190.1; -.
DR   PaxDb; Q9SII9; -.
DR   PRIDE; Q9SII9; -.
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   eggNOG; COG5272; LUCA.
DR   HOGENOM; HOG000234878; -.
DR   InParanoid; Q9SII9; -.
DR   KO; K04523; -.
DR   OMA; AGMFNTP; -.
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; IPR015496; Ubiquilin.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR10677; PTHR10677; 1.
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;
DR   PRODOM; Q9SII9.
DR   SWISS-2DPAGE; Q9SII9.
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   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
//

If you have problems or comments...

PBIL Back to PBIL home page