ID   UBC15_ARATH             Reviewed;         161 AA.
AC   P42743; O48952; Q67XR1; Q9MAK4;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2002, sequence version 2.
DT   27-MAR-2024, entry version 164.
DE   RecName: Full=Ubiquitin-conjugating enzyme 15;
DE            EC=2.3.2.23;
DE   AltName: Full=E2 ubiquitin-conjugating enzyme 15;
DE   AltName: Full=PM42;
DE   AltName: Full=Ubiquitin carrier protein;
DE   AltName: Full=Ubiquitin-conjugating enzyme E2-18 kDa 15;
DE   AltName: Full=Ubiquitin-protein ligase;
GN   Name=UBC15; Synonyms=UBC2-1; OrderedLocusNames=At1g45050;
GN   ORFNames=F27F5.13;
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], AND FUNCTION.
RC   STRAIN=cv. Landsberg erecta; TISSUE=Leaf;
RX   PubMed=8219072; DOI=10.1007/bf00029013;
RA   Bartling D., Rehling P., Weiler E.W.;
RT   "Functional expression and molecular characterization of AtUBC2-1, a novel
RT   ubiquitin-conjugating enzyme (E2) from Arabidopsis thaliana.";
RL   Plant Mol. Biol. 23:387-396(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Kim C.J., Chen H., Quinitio C., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (JUL-2006) 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:8219072}.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF69157.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; X68306; CAA48378.1; -; mRNA.
DR   EMBL; AF028338; AAC39324.1; -; Genomic_DNA.
DR   EMBL; DQ027029; AAY44855.1; -; mRNA.
DR   EMBL; AC007915; AAF69157.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE32077.1; -; Genomic_DNA.
DR   EMBL; BT026105; ABG48461.1; -; mRNA.
DR   EMBL; AK176757; BAD44520.1; -; mRNA.
DR   PIR; C96509; C96509.
DR   PIR; S39483; S39483.
DR   RefSeq; NP_564493.1; NM_103582.4.
DR   AlphaFoldDB; P42743; -.
DR   SMR; P42743; -.
DR   BioGRID; 26297; 3.
DR   STRING; 3702.P42743; -.
DR   PaxDb; 3702-AT1G45050-1; -.
DR   ProteomicsDB; 228715; -.
DR   EnsemblPlants; AT1G45050.1; AT1G45050.1; AT1G45050.
DR   GeneID; 841072; -.
DR   Gramene; AT1G45050.1; AT1G45050.1; AT1G45050.
DR   KEGG; ath:AT1G45050; -.
DR   Araport; AT1G45050; -.
DR   TAIR; AT1G45050; ATUBC2-1.
DR   eggNOG; KOG0427; Eukaryota.
DR   HOGENOM; CLU_030988_15_1_1; -.
DR   InParanoid; P42743; -.
DR   OMA; CANARIT; -.
DR   OrthoDB; 452at2759; -.
DR   PhylomeDB; P42743; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:P42743; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; P42743; baseline and differential.
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:SF373; UBIQUITIN-CONJUGATING ENZYME E2 W; 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; P42743; AT.
PE   2: Evidence at transcript level;
KW   ATP-binding; Nucleotide-binding; Reference proteome; Transferase;
KW   Ubl conjugation pathway.
FT   CHAIN           1..161
FT                   /note="Ubiquitin-conjugating enzyme 15"
FT                   /id="PRO_0000082575"
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"
FT   CONFLICT        33
FT                   /note="T -> S (in Ref. 1; CAA48378)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   161 AA;  18262 MW;  60C7F34A9574FB68 CRC64;
     MTSSSAPSRK ALSKIACNRL QKELSEWQLN PPTGFRHKVT DNLQKWTIDV TGAPGTLYAN
     ETYQLQVEFP EHYPMEAPQV VFVSPAPSHP HIYSNGHICL DILYDSWSPA MTVNSVCISI
     LSMLSSSPAK QRPADNDRYV KNCKNGRSPK ETRWWFHDDK V
//