UBC20_ARATH
ID UBC20_ARATH Reviewed; 180 AA.
AC Q8L7T3; Q8L8L3; Q9C6Q4; Q9LPS2;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 20;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme 20;
DE AltName: Full=Ubiquitin carrier protein 20;
GN Name=UBC20; OrderedLocusNames=At1g50490; ORFNames=F11F12.16, F17J6.3;
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 [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12427990; DOI=10.1104/pp.011353;
RA Criqui M.C., de Almeida Engler J., Camasses A., Capron A., Parmentier Y.,
RA Inze D., Genschik P.;
RT "Molecular characterization of plant ubiquitin-conjugating enzymes
RT belonging to the UbcP4/E2-C/UBCx/UbcH10 gene family.";
RL Plant Physiol. 130:1230-1240(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION, GENE
RP FAMILY, AND NOMENCLATURE.
RX PubMed=16339806; DOI=10.1104/pp.105.067983;
RA Kraft E., Stone S.L., Ma L., Su N., Gao Y., Lau O.-S., Deng X.-W.,
RA Callis J.;
RT "Genome analysis and functional characterization of the E2 and RING-type E3
RT ligase ubiquitination enzymes of Arabidopsis.";
RL Plant Physiol. 139:1597-1611(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
RP DEVELOPMENTAL STAGE.
RX PubMed=15970679;
RA Fueloep K., Tarayre S., Kelemen Z., Horvath G., Kevei Z., Nikovics K.,
RA Bako L., Brown S., Kondorosi A., Kondorosi E.;
RT "Arabidopsis anaphase-promoting complexes: multiple activators and wide
RT range of substrates might keep APC perpetually busy.";
RL Cell Cycle 4:1084-1092(2005).
CC -!- FUNCTION: Accepts the ubiquitin from the E1 complex and catalyzes its
CC covalent attachment to other proteins. {ECO:0000269|PubMed:12427990,
CC ECO:0000269|PubMed:16339806}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-
CC activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-
CC conjugating enzyme]-L-cysteine.; EC=2.3.2.23;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-
CC ProRule:PRU10133};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues with cell division
CC activities and in mature leaves. {ECO:0000269|PubMed:12427990,
CC ECO:0000269|PubMed:16339806}.
CC -!- DEVELOPMENTAL STAGE: Expressed during the G2-M phases of the cell
CC cycle. {ECO:0000269|PubMed:15970679}.
CC -!- INDUCTION: By the herbicide isoxaben and by biotic stresses.
CC {ECO:0000269|PubMed:16339806}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF87880.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG51188.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY127574; AAM96887.1; -; mRNA.
DR EMBL; DQ027034; AAY44860.1; -; mRNA.
DR EMBL; AC012561; AAF87880.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC079279; AAG51188.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32556.1; -; Genomic_DNA.
DR EMBL; AK227382; BAE99389.1; -; mRNA.
DR EMBL; AY088923; AAM67229.1; -; mRNA.
DR EMBL; BT005855; AAO64790.1; -; mRNA.
DR PIR; D96541; D96541.
DR RefSeq; NP_564572.1; NM_103932.4.
DR AlphaFoldDB; Q8L7T3; -.
DR SMR; Q8L7T3; -.
DR STRING; 3702.AT1G50490.1; -.
DR PaxDb; Q8L7T3; -.
DR PRIDE; Q8L7T3; -.
DR ProteomicsDB; 242816; -.
DR EnsemblPlants; AT1G50490.1; AT1G50490.1; AT1G50490.
DR GeneID; 841471; -.
DR Gramene; AT1G50490.1; AT1G50490.1; AT1G50490.
DR KEGG; ath:AT1G50490; -.
DR Araport; AT1G50490; -.
DR TAIR; locus:2015819; AT1G50490.
DR eggNOG; KOG0421; Eukaryota.
DR HOGENOM; CLU_030988_9_2_1; -.
DR InParanoid; Q8L7T3; -.
DR OMA; WINQEEY; -.
DR OrthoDB; 1444506at2759; -.
DR PhylomeDB; Q8L7T3; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q8L7T3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8L7T3; baseline and differential.
DR Genevisible; Q8L7T3; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:TAIR.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IBA:GO_Central.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS00183; UBC_1; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cyclin; Nucleotide-binding; Reference proteome; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..180
FT /note="Ubiquitin-conjugating enzyme E2 20"
FT /id="PRO_0000345186"
FT DOMAIN 35..180
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 119
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
FT CONFLICT 72
FT /note="T -> I (in Ref. 6; AAM67229)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 180 AA; 19792 MW; 0FFFF2E7347D815B CRC64;
MAAVNGYQGN TPADPPASNG SKQPAAPTKT VDSQSVLKRL QSELMGLMMG GGPGISAFPE
EDNIFCWKGT ITGSKDTVFE GTEYRLSLSF SNDYPFKPPK VKFETCCFHP NVDVYGNICL
DILQDKWSSA YDVRTILLSI QSLLGEPNIS SPLNTQAAQL WSNQEEYRKM VEKLYKPPSA
