UBC22_ARATH
ID UBC22_ARATH Reviewed; 251 AA.
AC Q9FF66;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 22;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme 22;
DE AltName: Full=Ubiquitin carrier protein 22;
GN Name=UBC22; OrderedLocusNames=At5g05080; ORFNames=MUG13.6;
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 [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION,
RP UBIQUITINATION, GENE 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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.
CC -!- FUNCTION: Accepts the ubiquitin from the E1 complex and catalyzes its
CC covalent attachment to other proteins. {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 seeds, pistils, siliques, hypocotyls
CC and leaves. {ECO:0000269|PubMed:16339806}.
CC -!- INDUCTION: By the herbicide isoxaben. {ECO:0000269|PubMed:16339806}.
CC -!- PTM: Self-ubiquitinated. {ECO:0000269|PubMed:16339806}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ027036; AAY44862.1; -; mRNA.
DR EMBL; AB005245; BAB11530.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90825.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90826.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM71122.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM71123.1; -; Genomic_DNA.
DR EMBL; AY116948; AAM51582.1; -; mRNA.
DR EMBL; AF428320; AAL16250.1; -; mRNA.
DR EMBL; AY088106; AAM65652.1; -; mRNA.
DR RefSeq; NP_001078530.1; NM_001085061.1.
DR RefSeq; NP_001332673.1; NM_001342802.1.
DR RefSeq; NP_001332674.1; NM_001342801.1.
DR RefSeq; NP_568148.1; NM_120590.3.
DR AlphaFoldDB; Q9FF66; -.
DR SMR; Q9FF66; -.
DR STRING; 3702.AT5G05080.1; -.
DR PaxDb; Q9FF66; -.
DR PRIDE; Q9FF66; -.
DR ProteomicsDB; 243216; -.
DR EnsemblPlants; AT5G05080.1; AT5G05080.1; AT5G05080.
DR EnsemblPlants; AT5G05080.2; AT5G05080.2; AT5G05080.
DR EnsemblPlants; AT5G05080.3; AT5G05080.3; AT5G05080.
DR EnsemblPlants; AT5G05080.4; AT5G05080.4; AT5G05080.
DR GeneID; 830390; -.
DR Gramene; AT5G05080.1; AT5G05080.1; AT5G05080.
DR Gramene; AT5G05080.2; AT5G05080.2; AT5G05080.
DR Gramene; AT5G05080.3; AT5G05080.3; AT5G05080.
DR Gramene; AT5G05080.4; AT5G05080.4; AT5G05080.
DR KEGG; ath:AT5G05080; -.
DR Araport; AT5G05080; -.
DR TAIR; locus:2175359; AT5G05080.
DR eggNOG; KOG0423; Eukaryota.
DR HOGENOM; CLU_030988_5_0_1; -.
DR InParanoid; Q9FF66; -.
DR OMA; TANKAFG; -.
DR OrthoDB; 1412570at2759; -.
DR PhylomeDB; Q9FF66; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9FF66; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FF66; baseline and differential.
DR Genevisible; Q9FF66; 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; Coiled coil; Nucleotide-binding; Reference proteome;
KW Transferase; Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..251
FT /note="Ubiquitin-conjugating enzyme E2 22"
FT /id="PRO_0000345188"
FT DOMAIN 10..156
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 230..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 230..251
FT /evidence="ECO:0000255"
FT ACT_SITE 94
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
SQ SEQUENCE 251 AA; 27399 MW; 3A335129A16D616E CRC64;
MASNENLPPN VIKQLAKELK SLDESPPDGI KVVVNDEDFS QICADIEGPV GTPYENGLFR
MKLALSHDFP HSPPKGYFMT KIFHPNVASN GEICVNTLKK DWNPSLGLRH VLSVVRCLLI
EPFPESALNE QAGKMLLENY DEYARHARLY TGIHAKPKPK FKTGAISEST TALNVGQTNN
ETPGAATAIP SSMTDIKRVT TSAQDQQHVA NVVVAASASV VTTTQKREAG LAKVQADKKK
VDARKKSLKR L
