UBC23_ARATH
ID UBC23_ARATH Reviewed; 1102 AA.
AC Q9ZVX1;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 141.
DE RecName: Full=Probable ubiquitin-conjugating enzyme E2 23;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme 23;
DE AltName: Full=Ubiquitin carrier protein 23;
GN Name=UBC23; OrderedLocusNames=At2g16920; ORFNames=F12A24.10;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
CC -!- FUNCTION: Accepts the ubiquitin from the E1 complex and catalyzes its
CC covalent attachment to other proteins. {ECO:0000250|UniProtKB:P42743}.
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};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; AC005167; AAC64223.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06554.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62201.1; -; Genomic_DNA.
DR PIR; H84545; H84545.
DR RefSeq; NP_001324377.1; NM_001335502.1.
DR RefSeq; NP_179284.1; NM_127245.3.
DR AlphaFoldDB; Q9ZVX1; -.
DR SMR; Q9ZVX1; -.
DR STRING; 3702.AT2G16920.1; -.
DR iPTMnet; Q9ZVX1; -.
DR PaxDb; Q9ZVX1; -.
DR PRIDE; Q9ZVX1; -.
DR ProteomicsDB; 228627; -.
DR EnsemblPlants; AT2G16920.1; AT2G16920.1; AT2G16920.
DR EnsemblPlants; AT2G16920.2; AT2G16920.2; AT2G16920.
DR GeneID; 816195; -.
DR Gramene; AT2G16920.1; AT2G16920.1; AT2G16920.
DR Gramene; AT2G16920.2; AT2G16920.2; AT2G16920.
DR KEGG; ath:AT2G16920; -.
DR Araport; AT2G16920; -.
DR TAIR; locus:2039380; AT2G16920.
DR eggNOG; KOG0895; Eukaryota.
DR HOGENOM; CLU_002088_0_0_1; -.
DR InParanoid; Q9ZVX1; -.
DR OMA; TIECRRE; -.
DR OrthoDB; 808738at2759; -.
DR PhylomeDB; Q9ZVX1; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9ZVX1; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZVX1; baseline and differential.
DR Genevisible; Q9ZVX1; AT.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 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..1102
FT /note="Probable ubiquitin-conjugating enzyme E2 23"
FT /id="PRO_0000345189"
FT DOMAIN 850..1010
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 25..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..90
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..695
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 936
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
SQ SEQUENCE 1102 AA; 122183 MW; DA2C11385355E8D9 CRC64;
MEHEQDDPGT STNVGVDSSV DDSMASLSIC DSEHPNIYRQ DIVKNKKTGS VGVVSEVAGD
SDSDSDISDE EEDDDDDEDN DDDDEDVEEG KKASEENVVN GDGEKKADGN YKCGALEGDQ
IRVLWMDNTE PVQDINDVTV IDRGFLHGDY VASASEPTGQ VGVVVDVNIS VDLLAPDGSI
HKDISTKNLK RVRDFAVGDY VVHGPWLGRI DDVLDNVTVL FDDGSMCKVL RVEPLRLKPI
PKNNLEEDAN FPYYPGQRVK ASSSSVFKNS RWLSGLWKPN RLEGTVTKVT AGSIFVYWIA
SAGFGPDSSV SPPEEQNPSN LTLLSCFTHA NWQVGDWCLL PSLNQSATIP LHKHVSKLRL
YDSQADRQQK IGRDLEDVQD EVSGKVEPAG ITAEALPKVT SDDPPQRNPS VSKEPVHEPW
PLHRKKIRKL VIRKDKKVKK KEESFEQALL VVNSRTRVDV SWQDGTIECR REAITLIPIE
TPGDHEFVSE QYVVEKTSDD GDNTTEPRRA GVVKNVNAKD RTASVRWLNP LRRAEEPREF
EKEEIVSVYE LEGHPDYDYC YGDVVVRLSP IAVALPASSP GNSFEEATQQ DNGYQDSESH
QEAKILVDKE ENEPSTDLSK LSWVGNITGL KDGDIEVTWA DGTISTVGPH AVYVVGRDDD
DESVAGESET SDAASWETLN DDDRGAPEIP EEDLGRSSSI EGNSDADIYA ENDSGRNGAL
ALPLAAIEFV TRLASGIFSR ARKSVDSSSS DYTVENVYKQ AESTNPSDET DSLDDPSPSK
VNVTDNCESK GTQANAKNIL SGETSTFLED EDKPVPSEGD SCSFRRFDIS QDPLDHHFLG
VDGQKTKERQ WFKKVDQDWK ILQNNLPDGI FVRAYEDRMD LLRAVIVGAF GTPYQDGLFF
FDFHLPSDYP SVPPSAYYHS GGWRLNPNLY EEGKVCLSLL NTWTGRGNEV WDPKSSSILQ
VLVSLQGLVL NSKPYFNEAG YDKQVGTAEG EKNSLGYNEN TFLLNCKTMM YLMRKPPKDF
EELIKDHFRK RGYYILKACD AYMKGYLIGS LTKDASVIDE RSSANSTSVG FKLMLAKIAP
KLFSALSEVG ADCNEFQHLQ QQ
