UBC9_ARATH
ID UBC9_ARATH Reviewed; 148 AA.
AC P35132; Q42014; Q4TZ01; Q8RXQ0; Q9FPH9;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 25-MAY-2022, entry version 167.
DE RecName: Full=SUMO-conjugating enzyme UBC9;
DE EC=2.3.2.-;
DE AltName: Full=RING-type E3 SUMO transferase UBC9;
DE AltName: Full=UBCAT4B;
DE AltName: Full=Ubiquitin carrier protein 9;
DE AltName: Full=Ubiquitin-conjugating enzyme E2 9;
DE AltName: Full=Ubiquitin-conjugating enzyme E2-17 kDa;
DE AltName: Full=Ubiquitin-protein ligase 9;
GN Name=UBC9; Synonyms=UBC4B; OrderedLocusNames=At4g27960; ORFNames=T13J8.70;
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] (ISOFORM 1).
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=8220461; DOI=10.1046/j.1365-313x.1993.03040545.x;
RA Girod P.-A., Carpenter T.B., van Nocker S., Sullivan M.L., Vierstra R.D.;
RT "Homologs of the essential ubiquitin conjugating enzymes UBC1, 4, and 5 in
RT yeast are encoded by a multigene family in Arabidopsis thaliana.";
RL Plant J. 3:545-552(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DEVELOPMENTAL STAGE, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=8078482; DOI=10.1007/bf00583906;
RA Genschik P., Durr A., Fleck J.;
RT "Differential expression of several E2-type ubiquitin carrier protein genes
RT at different developmental stages in Arabidopsis thaliana and Nicotiana
RT sylvestris.";
RL Mol. Gen. Genet. 244:548-556(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, GENE FAMILY,
RP 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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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] (ISOFORMS 1 AND 2).
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-82 (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=8281187; DOI=10.1046/j.1365-313x.1993.04061051.x;
RA Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M.,
RA Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., Guerrier D.,
RA Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., Raynal M.,
RA Cooke R., Grellet F., Delseny M., Parmentier Y., de Marcillac G., Gigot C.,
RA Fleck J., Philipps G., Axelos M., Bardet C., Tremousaygue D., Lescure B.;
RT "An inventory of 1152 expressed sequence tags obtained by partial
RT sequencing of cDNAs from Arabidopsis thaliana.";
RL Plant J. 4:1051-1061(1993).
RN [8]
RP INTERACTION WITH CHIP.
RX PubMed=16640601; DOI=10.1111/j.1365-313x.2006.02730.x;
RA Luo J., Shen G., Yan J., He C., Zhang H.;
RT "AtCHIP functions as an E3 ubiquitin ligase of protein phosphatase 2A
RT subunits and alters plant response to abscisic acid treatment.";
RL Plant J. 46:649-657(2006).
CC -!- FUNCTION: Accepts the ubiquitin-like protein SUMO/SMT3 from the E1
CC complex and catalyzes its covalent attachment to other proteins.
CC Mediates the selective degradation of short-lived and abnormal
CC proteins.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC -!- SUBUNIT: Interacts with CHIP. {ECO:0000269|PubMed:16640601}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P35132-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P35132-2; Sequence=VSP_008896;
CC -!- TISSUE SPECIFICITY: Highest expression in young stems and old leaves.
CC Lowest levels in floral buds, anthers and young leaves.
CC {ECO:0000269|PubMed:16339806}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated during senescence, but not during the
CC G0 to S phase transition. {ECO:0000269|PubMed:8078482}.
CC -!- INDUCTION: Not induced by heat shock or wounding.
CC {ECO:0000269|PubMed:8078482}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; Z14990; CAA78714.1; -; mRNA.
DR EMBL; X72626; CAA51201.1; -; mRNA.
DR EMBL; L00639; AAA32894.1; -; mRNA.
DR EMBL; DQ027023; AAY44849.1; -; mRNA.
DR EMBL; AL035524; CAB36765.1; -; Genomic_DNA.
DR EMBL; AL161572; CAB79598.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85413.1; -; Genomic_DNA.
DR EMBL; AF325019; AAG40371.1; -; mRNA.
DR EMBL; AY080741; AAL85988.1; -; mRNA.
DR EMBL; AY142644; AAN13102.1; -; mRNA.
DR EMBL; Z18473; CAA79198.1; -; mRNA.
DR PIR; S32674; S32674.
DR RefSeq; NP_567791.1; NM_118934.3.
DR RefSeq; NP_849462.1; NM_179131.3. [P35132-1]
DR AlphaFoldDB; P35132; -.
DR SMR; P35132; -.
DR BioGRID; 14196; 15.
DR IntAct; P35132; 7.
DR STRING; 3702.AT4G27960.2; -.
DR PaxDb; P35132; -.
DR EnsemblPlants; AT4G27960.1; AT4G27960.1; AT4G27960. [P35132-1]
DR GeneID; 828909; -.
DR Gramene; AT4G27960.1; AT4G27960.1; AT4G27960. [P35132-1]
DR KEGG; ath:AT4G27960; -.
DR Araport; AT4G27960; -.
DR eggNOG; KOG0417; Eukaryota.
DR HOGENOM; CLU_030988_13_3_1; -.
DR InParanoid; P35132; -.
DR OMA; RISWECT; -.
DR OrthoDB; 1337945at2759; -.
DR PhylomeDB; P35132; -.
DR UniPathway; UPA00886; -.
DR PRO; PR:P35132; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P35132; baseline and differential.
DR Genevisible; P35132; 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:0016925; P:protein sumoylation; IEA:UniProtKB-UniPathway.
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="SUMO-conjugating enzyme UBC9"
FT /id="PRO_0000082577"
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"
FT VAR_SEQ 1
FT /note="M -> MFFFFLIHLTIGLVFDCRVFNWNLDSGILEM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172,
FT ECO:0000303|PubMed:16339806"
FT /id="VSP_008896"
FT CONFLICT 65
FT /note="P -> H (in Ref. 6; AAL85988)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 148 AA; 16553 MW; 17F247FC1801BABD CRC64;
MASKRILKEL KDLQKDPPTS CSAGPVAEDM FHWQATIMGP SDSPYSGGVF LVTIHFPPDY
PFKPPKVAFR TKVFHPNINS NGSICLDILK EQWSPALTIS KVLLSICSLL TDPNPDDPLV
PEIAHMYKTD KNKYESTART WTQKYAMG
