UBC25_ARATH
ID UBC25_ARATH Reviewed; 609 AA.
AC Q9LUQ5; Q4TYY6; Q9M7X2;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Probable ubiquitin-conjugating enzyme E2 25;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme 25;
DE AltName: Full=Ubiquitin carrier protein 25;
GN Name=UBC25; OrderedLocusNames=At3g15355; ORFNames=MJK13.1;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
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).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 351-609, 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).
CC -!- FUNCTION: Accepts the ubiquitin from the E1 complex and catalyzes its
CC covalent attachment to other proteins. {ECO:0000250|UniProtKB:P42743}.
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};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB022218; BAB02364.1; -; Genomic_DNA.
DR EMBL; AP000413; BAB02364.1; JOINED; Genomic_DNA.
DR EMBL; AC024081; AAF35401.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75657.1; -; Genomic_DNA.
DR EMBL; AF361806; AAK32819.1; -; mRNA.
DR EMBL; AY059155; AAL15380.1; -; mRNA.
DR EMBL; DQ027038; AAY44864.1; -; mRNA.
DR RefSeq; NP_188154.1; NM_112402.3.
DR AlphaFoldDB; Q9LUQ5; -.
DR SMR; Q9LUQ5; -.
DR STRING; 3702.AT3G15355.1; -.
DR PaxDb; Q9LUQ5; -.
DR PRIDE; Q9LUQ5; -.
DR ProteomicsDB; 228657; -.
DR EnsemblPlants; AT3G15355.1; AT3G15355.1; AT3G15355.
DR GeneID; 820772; -.
DR Gramene; AT3G15355.1; AT3G15355.1; AT3G15355.
DR KEGG; ath:AT3G15355; -.
DR Araport; AT3G15355; -.
DR TAIR; locus:2090096; AT3G15355.
DR eggNOG; KOG0895; Eukaryota.
DR HOGENOM; CLU_025097_5_1_1; -.
DR InParanoid; Q9LUQ5; -.
DR OMA; NTCRVKR; -.
DR OrthoDB; 808738at2759; -.
DR PhylomeDB; Q9LUQ5; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9LUQ5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LUQ5; baseline and differential.
DR Genevisible; Q9LUQ5; 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:0006301; P:postreplication repair; IBA:GO_Central.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Nucleotide-binding; Reference proteome; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..609
FT /note="Probable ubiquitin-conjugating enzyme E2 25"
FT /id="PRO_0000345190"
FT DOMAIN 332..492
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 70..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 418
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
SQ SEQUENCE 609 AA; 67769 MW; 94A2C2E839DED309 CRC64;
MEPNVVEIAT PPAASCSRIR TPTKAETPEV IDVEEYDLQN GGVPNGNNVD YKNKGKAIDF
DSMSYGDYGE EDEYAVGSPG DDYGYPESSP LSNSLLDPES LIYEDDENYS EQYDFEMEAE
PDNYSMYQDL FDGKDIPTGV EVSMDWFPNS ADKESASSSK SSHANNGNNS SKKATKASGI
HSQFSSDMET PVAQPWNALP HKAEGVIPNS AYALPQNSKA FQPPYAVHYS ALKTAFSNYL
QPQTPDTVLG EAPAPAAGSS GLLPPNTPGF KSNAARFKEE PPILPPDDSR VKRNMEDYLG
LYLFFKRFDI VEDFSDHHYA SKGTTSKQHS KDWAKRIQDE WRILEKDLPE MIFVRAYESR
MDLLRAVIIG AQGTPYHDGL FFFDIFFPDT YPSTPPIVHY HSGGLRINPN LYNCGKVCLS
LLGTWSGNQR EKWIPNTSTM LQVLVSIQGL ILNQKPYFNE PGYERSAGSA HGESTSKAYS
ENTFILSLKT MVYTMRRPPK YFEDFAYGHF FSCAHDVLKA CNAYRNGATP GYLVKGAPDV
EENSAGMSSL KFRTDVATFV ETVLLKEFIL LGVLGLEPEE EEKTPETIIV AESSKCTRSR
SKRDRVSSS
