ID   UBC28_ARATH             Reviewed;         148 AA.
AC   Q94F47; Q9SH72;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 146.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 28;
DE            EC=2.3.2.23;
DE   AltName: Full=AtUBC9A {ECO:0000303|PubMed:12226665};
DE   AltName: Full=E2 ubiquitin-conjugating enzyme 28;
DE   AltName: Full=Ubiquitin carrier protein 28;
GN   Name=UBC28 {ECO:0000303|PubMed:16339806}; OrderedLocusNames=At1g64230;
GN   ORFNames=F22C12.2;
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 INTERACTION WITH SINAT5.
RX   PubMed=12226665; DOI=10.1038/nature00998;
RA   Xie Q., Guo H.-S., Dallman G., Fang S., Weissman A.M., Chua N.-H.;
RT   "SINAT5 promotes ubiquitin-related degradation of NAC1 to attenuate auxin
RT   signals.";
RL   Nature 419:167-170(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, GENE FAMILY, AND
RP   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=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   [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.
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   -!- SUBUNIT: Interacts with SINAT5. {ECO:0000269|PubMed:12226665}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q94F47-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Expressed in seeds, pistils, siliques, hypocotyls
CC       and leaves. {ECO:0000269|PubMed:16339806}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF24583.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF480945; AAM11574.1; -; mRNA.
DR   EMBL; DQ027041; AAY44867.1; -; mRNA.
DR   EMBL; AC007764; AAF24583.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE34212.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE34213.1; -; Genomic_DNA.
DR   EMBL; AF385718; AAK60309.1; -; mRNA.
DR   EMBL; AY133670; AAM91500.1; -; mRNA.
DR   PIR; D96666; D96666.
DR   RefSeq; NP_001031228.1; NM_001036151.1. [Q94F47-1]
DR   RefSeq; NP_564828.1; NM_105097.9. [Q94F47-1]
DR   AlphaFoldDB; Q94F47; -.
DR   SMR; Q94F47; -.
DR   BioGRID; 27949; 8.
DR   IntAct; Q94F47; 1.
DR   STRING; 3702.Q94F47; -.
DR   ProteomicsDB; 242818; -. [Q94F47-1]
DR   EnsemblPlants; AT1G64230.1; AT1G64230.1; AT1G64230. [Q94F47-1]
DR   EnsemblPlants; AT1G64230.2; AT1G64230.2; AT1G64230. [Q94F47-1]
DR   GeneID; 842728; -.
DR   Gramene; AT1G64230.1; AT1G64230.1; AT1G64230. [Q94F47-1]
DR   Gramene; AT1G64230.2; AT1G64230.2; AT1G64230. [Q94F47-1]
DR   KEGG; ath:AT1G64230; -.
DR   Araport; AT1G64230; -.
DR   TAIR; AT1G64230; UBC28.
DR   HOGENOM; CLU_030988_13_3_1; -.
DR   InParanoid; Q94F47; -.
DR   OMA; VHFTTRI; -.
DR   PhylomeDB; Q94F47; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q94F47; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q94F47; baseline and differential.
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; IEA:UniProtKB-EC.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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; PTHR24068:SF460; UBC CORE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR24068; UBIQUITIN-CONJUGATING ENZYME E2; 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; Q94F47; AT.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Nucleotide-binding; Reference proteome;
KW   Transferase; Ubl conjugation pathway.
FT   CHAIN           1..148
FT                   /note="Ubiquitin-conjugating enzyme E2 28"
FT                   /id="PRO_0000345193"
FT   DOMAIN          1..147
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   ACT_SITE        85
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT                   ECO:0000255|PROSITE-ProRule:PRU10133"
SQ   SEQUENCE   148 AA;  16510 MW;  D9F89BAF1801A83F CRC64;
     MASKRILKEL KDLQKDPPTS CSAGPVAEDM FHWQATIMGP SDSPYSGGVF LVTIHFPPDY
     PFKPPKVAFR TKVFHPNVNS NGSICLDILK EQWSPALTIS KVLLSICSLL TDPNPDDPLV
     PEIAHMYKTD RAKYESTARS WTQKYAMG
//