ID   UBC13_ARATH             Reviewed;         166 AA.
AC   Q42541; Q4TYZ7;
DT   23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 158.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 13;
DE            EC=2.3.2.23;
DE   AltName: Full=E2 ubiquitin-conjugating enzyme 13;
DE   AltName: Full=Ubiquitin carrier protein 13;
DE   AltName: Full=Ubiquitin-protein ligase 13;
GN   Name=UBC13; OrderedLocusNames=At3g46460; ORFNames=F18L15.180;
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 [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=cv. Columbia; TISSUE=Seedling;
RX   PubMed=8647807; DOI=10.1074/jbc.271.21.12150;
RA   van Nocker S., Walker J.M., Vierstra R.D.;
RT   "The Arabidopsis thaliana UBC7/13/14 genes encode a family of
RT   multiubiquitin chain-forming E2 enzymes.";
RL   J. Biol. Chem. 271:12150-12158(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, 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=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   [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].
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).
CC   -!- FUNCTION: Accepts the ubiquitin from the E1 complex and catalyzes its
CC       covalent attachment to other proteins. Involved in the formation of
CC       multiubiquitin chains. Signal the protein for selective degradation.
CC       {ECO:0000269|PubMed:8647807}.
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   -!- 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}.
CC   -!- CAUTION: This protein has been named UBC13 according to the
CC       nomenclature proposed in PubMed:16339806, but it is not the same as the
CC       UBC13 described in several publications that correspond to the protein
CC       named UBC35 in our nomenclature. {ECO:0000305}.
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DR   EMBL; U33758; AAC49322.1; -; Genomic_DNA.
DR   EMBL; DQ027027; AAY44853.1; -; mRNA.
DR   EMBL; AL133298; CAB62037.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE78162.1; -; Genomic_DNA.
DR   EMBL; AY050368; AAK91385.1; -; mRNA.
DR   EMBL; AY094040; AAM16196.1; -; mRNA.
DR   PIR; T45703; T45703.
DR   RefSeq; NP_566884.1; NM_114513.6.
DR   AlphaFoldDB; Q42541; -.
DR   SMR; Q42541; -.
DR   BioGRID; 9116; 1.
DR   STRING; 3702.Q42541; -.
DR   PaxDb; 3702-AT3G46460-1; -.
DR   ProteomicsDB; 228650; -.
DR   EnsemblPlants; AT3G46460.1; AT3G46460.1; AT3G46460.
DR   GeneID; 823796; -.
DR   Gramene; AT3G46460.1; AT3G46460.1; AT3G46460.
DR   KEGG; ath:AT3G46460; -.
DR   Araport; AT3G46460; -.
DR   TAIR; AT3G46460; UBC13.
DR   eggNOG; KOG0425; Eukaryota.
DR   HOGENOM; CLU_030988_10_1_1; -.
DR   InParanoid; Q42541; -.
DR   OMA; NIDACKM; -.
DR   OrthoDB; 149628at2759; -.
DR   PhylomeDB; Q42541; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q42541; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q42541; baseline and differential.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IEA:UniProtKB-EC.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:TAIR.
DR   CDD; cd00195; UBCc; 1.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR023313; UBQ-conjugating_AS.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR24067; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR   PANTHER; PTHR24067:SF298; UBIQUITIN-CONJUGATING ENZYME E2 13-RELATED; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   SMART; SM00212; UBCc; 1.
DR   SUPFAM; SSF54495; UBC-like; 1.
DR   PROSITE; PS00183; UBC_1; 1.
DR   PROSITE; PS50127; UBC_2; 1.
DR   Genevisible; Q42541; AT.
PE   2: Evidence at transcript level;
KW   ATP-binding; Nucleotide-binding; Reference proteome; Transferase;
KW   Ubl conjugation pathway.
FT   CHAIN           1..166
FT                   /note="Ubiquitin-conjugating enzyme E2 13"
FT                   /id="PRO_0000082587"
FT   DOMAIN          4..164
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   ACT_SITE        89
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT                   ECO:0000255|PROSITE-ProRule:PRU10133"
SQ   SEQUENCE   166 AA;  18822 MW;  DCC26424275F275B CRC64;
     MNSQACLLLQ KQLKDLCKHP VDGFSAGLVD EKNIFEWSVT IIGPPDTLYE GGFFYAIMSF
     PQNYPNSPPT VRFTSDIWHP NVYPDGRVCI SILHPPGDDP SGYELASERW TPVHTVESIM
     LSIISMLSGP NDESPANVEA AKEWREKRDE FKKKVSRCVR KSQEMF
//