UBC18_ARATH
ID UBC18_ARATH Reviewed; 161 AA.
AC Q9FMM0; O48954;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Probable ubiquitin-conjugating enzyme E2 18;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme 18;
DE AltName: Full=Ubiquitin carrier protein 18;
GN Name=UBC18; OrderedLocusNames=At5g42990; ORFNames=MBD2.19;
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], 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=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(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 [GENOMIC DNA] OF 65-161.
RC STRAIN=cv. Columbia;
RA Yan N., Doelling J., Vierstra R.D.;
RT "A new family of ubiquitin-conjugating enzymes (E2S) AtUBC15/16/17/18 in
RT Arabidopsis thaliana.";
RL (er) Plant Gene Register PGR97-174(1997).
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, ECO:0000255|PROSITE-
CC ProRule:PRU10133};
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; DQ027032; AAY44858.1; -; mRNA.
DR EMBL; AB008264; BAB09201.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94898.1; -; Genomic_DNA.
DR EMBL; AY058137; AAL25553.1; -; mRNA.
DR EMBL; AY101537; AAM26658.1; -; mRNA.
DR EMBL; AF028341; AAC39327.1; -; mRNA.
DR PIR; T52052; T52052.
DR RefSeq; NP_568619.1; NM_123665.5.
DR AlphaFoldDB; Q9FMM0; -.
DR SMR; Q9FMM0; -.
DR BioGRID; 19564; 7.
DR IntAct; Q9FMM0; 4.
DR STRING; 3702.AT5G42990.1; -.
DR PaxDb; Q9FMM0; -.
DR PRIDE; Q9FMM0; -.
DR ProteomicsDB; 243238; -.
DR EnsemblPlants; AT5G42990.1; AT5G42990.1; AT5G42990.
DR GeneID; 834314; -.
DR Gramene; AT5G42990.1; AT5G42990.1; AT5G42990.
DR KEGG; ath:AT5G42990; -.
DR Araport; AT5G42990; -.
DR TAIR; locus:2159981; AT5G42990.
DR eggNOG; KOG0427; Eukaryota.
DR HOGENOM; CLU_030988_15_1_1; -.
DR InParanoid; Q9FMM0; -.
DR OMA; YNTQRPR; -.
DR OrthoDB; 1522577at2759; -.
DR PhylomeDB; Q9FMM0; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9FMM0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FMM0; baseline and differential.
DR Genevisible; Q9FMM0; 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:0000209; P:protein polyubiquitination; 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; Nucleotide-binding; Reference proteome; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..161
FT /note="Probable ubiquitin-conjugating enzyme E2 18"
FT /id="PRO_0000345184"
FT DOMAIN 15..161
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 99
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
SQ SEQUENCE 161 AA; 18372 MW; 04A773CB44F5F60E CRC64;
MTSSSSPSRK ALSKIACNRL QKELSEWQVN PPTGFKHRVT DNLQKWVIEV TGAPGTLYAN
ETYNLQVEFP QHYPMEAPQV IFVPPAPLHP HIYSNGHICL DILYDSWSPA MTVSSVCISI
LSMLSSSPEK QRPTDNDRYV KNCKNGRSPK ETRWWFHDDK V
