UBC19_ARATH
ID UBC19_ARATH Reviewed; 181 AA.
AC Q9LJZ5; A8MSD2;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 19;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme 19;
DE AltName: Full=Ubiquitin carrier protein 19;
GN Name=UBC19; OrderedLocusNames=At3g20060; ORFNames=MAL21.6;
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] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, INDUCTION, AND MUTAGENESIS OF CYS-120.
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] (ISOFORM 1), 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Quinitio C., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
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. Part of the anaphase-promoting
CC complex (APC). May have a key function during cell cycle and be
CC involved in cyclin B1 degradation. {ECO:0000269|PubMed:12427990}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12427990}. Nucleus
CC {ECO:0000269|PubMed:12427990}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LJZ5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LJZ5-2; Sequence=VSP_034927;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues with cell division
CC activities and in mature leaves. {ECO:0000269|PubMed:12427990}.
CC -!- DEVELOPMENTAL STAGE: Expressed during the G1-S phases of the cell
CC cycle. {ECO:0000269|PubMed:15970679}.
CC -!- INDUCTION: Not induced by heat shock, dark to light transition,
CC proteasome inhibitor MG132 or geldanamycin.
CC {ECO:0000269|PubMed:12427990}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; AY127573; AAM96886.1; -; mRNA.
DR EMBL; DQ027033; AAY44859.1; -; mRNA.
DR EMBL; AP000383; BAB01863.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76325.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76326.1; -; Genomic_DNA.
DR EMBL; BT025536; ABF58954.1; -; mRNA.
DR RefSeq; NP_001078192.1; NM_001084723.1. [Q9LJZ5-2]
DR RefSeq; NP_566653.1; NM_112897.4. [Q9LJZ5-1]
DR AlphaFoldDB; Q9LJZ5; -.
DR SMR; Q9LJZ5; -.
DR BioGRID; 6877; 1.
DR IntAct; Q9LJZ5; 1.
DR STRING; 3702.AT3G20060.1; -.
DR PaxDb; Q9LJZ5; -.
DR PRIDE; Q9LJZ5; -.
DR ProteomicsDB; 228716; -. [Q9LJZ5-1]
DR EnsemblPlants; AT3G20060.1; AT3G20060.1; AT3G20060. [Q9LJZ5-1]
DR EnsemblPlants; AT3G20060.2; AT3G20060.2; AT3G20060. [Q9LJZ5-2]
DR GeneID; 821545; -.
DR Gramene; AT3G20060.1; AT3G20060.1; AT3G20060. [Q9LJZ5-1]
DR Gramene; AT3G20060.2; AT3G20060.2; AT3G20060. [Q9LJZ5-2]
DR KEGG; ath:AT3G20060; -.
DR Araport; AT3G20060; -.
DR TAIR; locus:2087620; AT3G20060.
DR eggNOG; KOG0421; Eukaryota.
DR HOGENOM; CLU_030988_9_2_1; -.
DR InParanoid; Q9LJZ5; -.
DR OMA; HPNVDMS; -.
DR PhylomeDB; Q9LJZ5; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9LJZ5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LJZ5; baseline and differential.
DR Genevisible; Q9LJZ5; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
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:0031145; P:anaphase-promoting complex-dependent catabolic process; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEP:TAIR.
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 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 Alternative splicing; ATP-binding; Cytoplasm; Nucleotide-binding; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation pathway.
FT CHAIN 1..181
FT /note="Ubiquitin-conjugating enzyme E2 19"
FT /id="PRO_0000345185"
FT DOMAIN 36..181
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 ACT_SITE 120
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT VAR_SEQ 1..45
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_034927"
FT MUTAGEN 120
FT /note="C->A: Unable to form a complex with ubiquitin."
FT /evidence="ECO:0000269|PubMed:12427990"
FT MUTAGEN 120
FT /note="C->S: Formation of a stable oxygen-ester bond with
FT ubiquitin."
FT /evidence="ECO:0000269|PubMed:12427990"
SQ SEQUENCE 181 AA; 19999 MW; D4E5C632112D3796 CRC64;
MATVNGYTGN TPAATTPAAT GSKQSAPPTK TVDSHSVLKR LQSELMGLMM GADPGISAFP
EEDNIFCWKG TITGSKDTVF EGTEYRLSLT FSNDYPFKSP KVKFETCCFH PNVDLYGNIC
LDILQDKWSS AYDVRTILLS IQSLLGEPNI SSPLNNQAAQ LWSNQEEYRK MVEKLYKPLN
A
