ID RCE1_ARATH Reviewed; 184 AA. AC Q9SDY5; O23202; Q0WLB1; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 22-JUL-2008, entry version 49. DE RecName: Full=NEDD8-conjugating enzyme Ubc12; DE EC=6.3.2.-; DE AltName: Full=RUB1-conjugating enzyme 1; DE AltName: Full=RUB1-protein ligase 1; DE AltName: Full=RUB1 carrier protein 1; GN Name=RCE1; OrderedLocusNames=At4g36800; ORFNames=C7A10.560; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION. RX MEDLINE=20079655; PubMed=10611386; DOI=10.1073/pnas.96.26.15342; RA del Pozo J.C., Estelle M.; RT "The Arabidopsis cullin AtCUL1 is modified by the ubiquitin-related RT protein RUB1."; RL Proc. Natl. Acad. Sci. U.S.A. 96:15342-15347(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=20083488; PubMed=10617198; DOI=10.1038/47134; RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., RA Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., RA Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., RA Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M., RA Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., RA Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., RA Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., RA Langham S.-A., McCullagh B., Bilham L., Robben J., RA van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., RA Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., RA Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., RA Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., RA Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., RA De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., RA van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., RA Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., RA Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., RA Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., RA Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., RA Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., RA Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., RA Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., RA Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., RA Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., RA Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., RA Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., RA Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., RA Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., RA Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., RA Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., RA Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., RA 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., RA Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., RA Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., RA Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., RA Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., RA Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., RA Chen E., Marra M.A., Martienssen R., McCombie W.R.; RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis RT thaliana."; RL Nature 402:769-777(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). 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., RA Hayashizaki Y., Shinozaki K.; RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. RN [5] RP TISSUE SPECIFICITY, FUNCTION, AND INTERACTION WITH RBX1. RX MEDLINE=22568282; PubMed=12682009; DOI=10.1093/emboj/cdg190; RA Dharmasiri S., Dharmasiri N., Hellmann H., Estelle M.; RT "The RUB/Nedd8 conjugation pathway is required for early development RT in Arabidopsis."; RL EMBO J. 22:1762-1770(2003). CC -!- FUNCTION: Accepts the ubiquitin-like protein NEDD8/RUB1 from the CC ECR1-AXR1 E1 complex and catalyzes its covalent attachment to CC other proteins. CC -!- CATALYTIC ACTIVITY: ATP + NEDD8 + protein lysine = AMP + CC diphosphate + protein N-NEDD8yllysine. CC -!- PATHWAY: Protein modification; protein neddylation. CC -!- SUBUNIT: Interacts with RBX1. CC -!- INTERACTION: CC P42744:AXR1; NbExp=1; IntAct=EBI-595116, EBI-595161; CC Q94AH6:CUL1; NbExp=1; IntAct=EBI-595116, EBI-532411; CC Q940X7:RBX1A; NbExp=2; IntAct=EBI-595116, EBI-532404; CC Q570C0:TIR1; NbExp=1; IntAct=EBI-595116, EBI-307183; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9SDY5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9SDY5-2; Sequence=VSP_034924; CC Note=May be due to intron retention. No experimental CC confirmation available; CC -!- TISSUE SPECIFICITY: Expressed in shoot, root and floral meristems, CC and in vascular tissues of leaves. CC -!- MISCELLANEOUS: Reduction in RCE1 levels leads to reduced organ CC length and defects in gravitropism. CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. CC UBC12 subfamily. CC -!- SEQUENCE CAUTION: CC Sequence=CAB16820.1; Type=Erroneous gene model prediction; CC Sequence=CAB80346.1; Type=Erroneous gene model prediction; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF202771; AAF19827.1; -; mRNA. DR EMBL; Z99708; CAB16820.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL161590; CAB80346.1; ALT_SEQ; Genomic_DNA. DR EMBL; AY048210; AAK82473.1; -; mRNA. DR EMBL; AY097381; AAM19897.1; -; mRNA. DR EMBL; AK230295; BAF02096.1; -; mRNA. DR PIR; E85434; E85434. DR HSSP; P52490; 1JAT. DR IntAct; Q9SDY5; -. DR GenomeReviews; CT486007_GR; AT4G36800. DR TAIR; At4g36800; -. DR GermOnline; AT4G36800; Arabidopsis thaliana. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR InterPro; IPR015580; Ubc12. DR InterPro; IPR016135; UBQ-conjugat/RWD-like. DR InterPro; IPR000608; UBQ-conjugat_E2. DR Gene3D; G3DSA:3.10.110.10; UBQ-conjugat_E2; 1. DR PANTHER; PTHR11621:SF17; Ubc12; 1. DR PANTHER; PTHR11621; UBQ-conjugat_E2; 1. DR Pfam; PF00179; UQ_con; 1. DR ProDom; PD000461; UBQ_conjugat; 1. DR SMART; SM00212; UBCc; 1. DR PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1. DR PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1. PE 1: Evidence at protein level; KW Alternative splicing; Complete proteome; Ligase; KW Ubl conjugation pathway. FT CHAIN 1 184 NEDD8-conjugating enzyme Ubc12. FT /FTId=PRO_0000082494. FT ACT_SITE 113 113 Glycyl thioester intermediate (By FT similarity). FT VAR_SEQ 102 184 YHPNIDLEGNVCLNILREDWKPVLNINTVIYGLFHLFTEPN FT SEDPLNHDAAAVLRDNPKLFETNVRRAMTGGYVGQTFFPRC FT I -> GLSSFYMPYIVYSFYFKIVCVVETLCWFSCLGLSSQ FT YRFGRKRLPEHL (in isoform 2). FT /FTId=VSP_034924. SQ SEQUENCE 184 AA; 20787 MW; 9F541991CED5C1E4 CRC64; MIGLFKVKEK QREQAQNATR GGASVKKQSA GELRLHKDIS ELNLPSSCSI SFPNGKDDLM NFEVSIKPDD GYYHNGTFVF TFQVSPVYPH EAPKVKCKTK VYHPNIDLEG NVCLNILRED WKPVLNINTV IYGLFHLFTE PNSEDPLNHD AAAVLRDNPK LFETNVRRAM TGGYVGQTFF PRCI //