UBC11_ARATH
ID UBC11_ARATH Reviewed; 148 AA.
AC P35134; Q4TYZ9; Q9M9J1;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2001, sequence version 2.
DT 25-MAY-2022, entry version 163.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 11;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme 11;
DE AltName: Full=Ubiquitin carrier protein 11;
DE AltName: Full=Ubiquitin-conjugating enzyme E2-17 kDa 11;
DE AltName: Full=Ubiquitin-protein ligase 11;
GN Name=UBC11; OrderedLocusNames=At3g08690; ORFNames=F17O14.16;
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, INDUCTION, GENE FAMILY, AND
RP 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
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 [4]
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 [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 31-148.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=8220461; DOI=10.1046/j.1365-313x.1993.03040545.x;
RA Girod P.-A., Carpenter T.B., van Nocker S., Sullivan M.L., Vierstra R.D.;
RT "Homologs of the essential ubiquitin conjugating enzymes UBC1, 4, and 5 in
RT yeast are encoded by a multigene family in Arabidopsis thaliana.";
RL Plant J. 3:545-552(1993).
RN [8]
RP INTERACTION WITH MBR1 AND MBR2.
RX PubMed=22992513; DOI=10.1104/pp.112.205500;
RA Inigo S., Giraldez A.N., Chory J., Cerdan P.D.;
RT "Proteasome-mediated turnover of Arabidopsis MED25 is coupled to the
RT activation of FLOWERING LOCUS T transcription.";
RL Plant Physiol. 160:1662-1673(2012).
CC -!- FUNCTION: Accepts the ubiquitin from the E1 complex and catalyzes its
CC covalent attachment to other proteins. Mediates the selective
CC degradation of short-lived and abnormal proteins.
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 -!- SUBUNIT: Interacts with the E3 ubiquitin-protein ligases MBR1 and MBR2.
CC {ECO:0000269|PubMed:22992513}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Mainly in petals.
CC -!- INDUCTION: Up-regulated by syringolin, a cell death-inducing chemical.
CC {ECO:0000269|PubMed:16339806}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; DQ027025; AAY44851.1; -; mRNA.
DR EMBL; AC012562; AAG51362.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74664.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74665.1; -; Genomic_DNA.
DR EMBL; AY063869; AAL36225.1; -; mRNA.
DR EMBL; AY091223; AAM14162.1; -; mRNA.
DR EMBL; AY086109; AAM63316.1; -; mRNA.
DR EMBL; AK228254; BAF00202.1; -; mRNA.
DR EMBL; Z14992; CAA78716.1; -; mRNA.
DR EMBL; L00641; AAA32896.1; -; mRNA.
DR PIR; S32673; S32673.
DR RefSeq; NP_001189841.1; NM_001202912.1.
DR RefSeq; NP_566331.1; NM_111703.4.
DR AlphaFoldDB; P35134; -.
DR SMR; P35134; -.
DR BioGRID; 5351; 7.
DR IntAct; P35134; 3.
DR STRING; 3702.AT3G08690.2; -.
DR PaxDb; P35134; -.
DR PRIDE; P35134; -.
DR EnsemblPlants; AT3G08690.1; AT3G08690.1; AT3G08690.
DR EnsemblPlants; AT3G08690.2; AT3G08690.2; AT3G08690.
DR GeneID; 820016; -.
DR Gramene; AT3G08690.1; AT3G08690.1; AT3G08690.
DR Gramene; AT3G08690.2; AT3G08690.2; AT3G08690.
DR KEGG; ath:AT3G08690; -.
DR Araport; AT3G08690; -.
DR TAIR; locus:2077773; AT3G08690.
DR eggNOG; KOG0417; Eukaryota.
DR HOGENOM; CLU_030988_13_3_1; -.
DR InParanoid; P35134; -.
DR OMA; NTHAREW; -.
DR OrthoDB; 1337945at2759; -.
DR PhylomeDB; P35134; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:P35134; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P35134; baseline and differential.
DR Genevisible; P35134; 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; IDA:TAIR.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:TAIR.
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 1: Evidence at protein level;
KW ATP-binding; Nucleotide-binding; Reference proteome; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..148
FT /note="Ubiquitin-conjugating enzyme E2 11"
FT /id="PRO_0000082579"
FT DOMAIN 1..147
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 85
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
SQ SEQUENCE 148 AA; 16551 MW; 74A0991115BA50EA CRC64;
MASKRILKEL KDLQKDPPSN CSAGPVAEDM FHWQATIMGP PESPYAGGVF LVSIHFPPDY
PFKPPKVSFK TKVYHPNINS NGSICLDILK EQWSPALTIS KVLLSICSLL TDPNPDDPLV
PEIAHMYKTD RSKYESTARS WTQKYAMG
