UBC28_ARATH
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 25-MAY-2022, entry version 139.
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 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 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 Genevisible; Q94F47; 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 GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; 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 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
