ID RUB1_ARATH Reviewed; 156 AA. AC Q9SHE7; O80715; P59263; Q0WQU3; Q38875; Q9LDJ2; Q9LYW1; Q9M0W3; Q9M1P9; AC Q9S7X3; DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 10-AUG-2010, sequence version 3. DT 27-MAR-2024, entry version 151. DE RecName: Full=Ubiquitin-NEDD8-like protein RUB1; DE Contains: DE RecName: Full=Ubiquitin; DE Contains: DE RecName: Full=NEDD8-like protein RUB1; DE AltName: Full=Ubiquitin-related protein 1; DE Short=AtRUB1; DE Flags: Precursor; GN Name=RUB1; Synonyms=NEDD8, UBQ15; OrderedLocusNames=At1g31340; GN ORFNames=T19E23.13; 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=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 [2] 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 [3] 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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., Hayashizaki Y., RA 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 FUNCTION, AND INTERACTION WITH AXR1 AND ECR1. RX PubMed=9624055; DOI=10.1126/science.280.5370.1760; RA del Pozo J.C., Timpte C., Tan S., Callis J., Estelle M.; RT "The ubiquitin-related protein RUB1 and auxin response in Arabidopsis."; RL Science 280:1760-1763(1998). RN [6] RP FUNCTION. RX 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 protein RT RUB1."; RL Proc. Natl. Acad. Sci. U.S.A. 96:15342-15347(1999). RN [7] RP INTERACTION WITH ML3. RX PubMed=23903439; DOI=10.1104/pp.113.221341; RA Hakenjos J.P., Bejai S., Ranftl Q., Behringer C., Vlot A.C., Absmanner B., RA Hammes U., Heinzlmeir S., Kuster B., Schwechheimer C.; RT "ML3 is a NEDD8- and ubiquitin-modified protein."; RL Plant Physiol. 163:135-149(2013). RN [8] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 79-152, AND TISSUE SPECIFICITY. RX PubMed=9857029; DOI=10.1074/jbc.273.52.34976; RA Rao-Naik C., delaCruz W., Laplaza J.M., Tan S., Callis J., Fisher A.J.; RT "The rub family of ubiquitin-like proteins. Crystal structure of RT Arabidopsis rub1 and expression of multiple rubs in Arabidopsis."; RL J. Biol. Chem. 273:34976-34982(1998). CC -!- FUNCTION: Ubiquitin exists either covalently attached to another CC protein, or free (unanchored). When covalently bound, it is conjugated CC to target proteins via an isopeptide bond either as a monomer CC (monoubiquitin), a polymer linked via different Lys residues of the CC ubiquitin (polyubiquitin chains) or a linear polymer linked via the CC initiator Met of the ubiquitin (linear polyubiquitin chains). CC Polyubiquitin chains, when attached to a target protein, have different CC functions depending on the Lys residue of the ubiquitin that is linked: CC Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated CC degradation) and in cell-cycle regulation; Lys-29-linked is involved in CC lysosomal degradation; Lys-33-linked is involved in kinase CC modification; Lys-48-linked is involved in protein degradation via the CC proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage CC responses. Linear polymer chains formed via attachment by the initiator CC Met lead to cell signaling. Ubiquitin is usually conjugated to Lys CC residues of target proteins, however, in rare cases, conjugation to Cys CC or Ser residues has been observed. When polyubiquitin is free CC (unanchored-polyubiquitin), it also has distinct roles, such as in CC activation of protein kinases, and in signaling (By similarity). CC {ECO:0000250}. CC -!- FUNCTION: [NEDD8-like protein RUB1]: Appears to function as a stable CC post-translational protein modifier. An AMP-RUB1 intermediate is formed CC by an activating enzyme, distinct from the ubiquitin activating enzyme CC E1, which is composed of a heterodimer AXR1/ECR1. Auxin response is CC mediated, at least in part, through modification of the cullin AtCUL1 CC by the attachment of RUB1 to 'Lys-692'. {ECO:0000269|PubMed:10611386, CC ECO:0000269|PubMed:9624055}. CC -!- SUBUNIT: [NEDD8-like protein RUB1]: Forms a thiol ester with the CC heterodimer AXR1/ECR1, specifically with the 'Cys-215' of ECR1 CC (PubMed:9624055). Interacts with ML3 (PubMed:23903439). CC {ECO:0000269|PubMed:23903439, ECO:0000269|PubMed:9624055}. CC -!- SUBCELLULAR LOCATION: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus CC {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems and flowers. CC {ECO:0000269|PubMed:9857029}. CC -!- MISCELLANEOUS: Ubiquitin is encoded by 16 different genes. Ubiquitin is CC generally synthesized as a polyubiquitin precursor with tandem head to CC tail repeats. Often, there is one to three additional amino acids after CC the last repeat, removed in the mature protein. Alternatively, CC ubiquitin extension protein is synthesized as a single copy of CC ubiquitin fused to a ribosomal protein (either L40 or S27A) or to a CC ubiquitin-related protein (either RUB1 or RUB2). Following translation, CC extension protein is cleaved from ubiquitin. CC -!- SIMILARITY: Belongs to the ubiquitin family. {ECO:0000305}. 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; AC007654; AAF24594.1; -; Genomic_DNA. DR EMBL; CP002684; AEE31344.1; -; Genomic_DNA. DR EMBL; BT005749; AAO64156.1; -; mRNA. DR EMBL; BT006110; AAP04095.1; -; mRNA. DR EMBL; AK228591; BAF00506.1; -; mRNA. DR PIR; C86439; C86439. DR RefSeq; NP_564379.2; NM_102873.5. DR PDB; 1BT0; X-ray; 1.70 A; A=77-152. DR PDBsum; 1BT0; -. DR AlphaFoldDB; Q9SHE7; -. DR SMR; Q9SHE7; -. DR BioGRID; 25258; 4. DR STRING; 3702.Q9SHE7; -. DR PaxDb; 3702-AT1G31340-1; -. DR ProteomicsDB; 226614; -. DR EnsemblPlants; AT1G31340.1; AT1G31340.1; AT1G31340. DR GeneID; 840023; -. DR Gramene; AT1G31340.1; AT1G31340.1; AT1G31340. DR KEGG; ath:AT1G31340; -. DR Araport; AT1G31340; -. DR TAIR; AT1G31340; RUB1. DR eggNOG; KOG0001; Eukaryota. DR HOGENOM; CLU_010412_0_0_1; -. DR InParanoid; Q9SHE7; -. DR OMA; MMADYGI; -. DR OrthoDB; 2877552at2759; -. DR PhylomeDB; Q9SHE7; -. DR EvolutionaryTrace; Q9SHE7; -. DR PRO; PR:Q9SHE7; -. DR Proteomes; UP000006548; Chromosome 1. DR ExpressionAtlas; Q9SHE7; baseline and differential. DR GO; GO:0005829; C:cytosol; HDA:TAIR. DR GO; GO:0005634; C:nucleus; HDA:TAIR. DR GO; GO:0005886; C:plasma membrane; HDA:TAIR. DR GO; GO:0003729; F:mRNA binding; IDA:TAIR. DR GO; GO:0009693; P:ethylene biosynthetic process; IMP:TAIR. DR GO; GO:0045116; P:protein neddylation; TAS:TAIR. DR GO; GO:0009733; P:response to auxin; TAS:TAIR. DR CDD; cd01806; Ubl_NEDD8; 1. DR CDD; cd01803; Ubl_ubiquitin; 1. DR InterPro; IPR038738; Nedd8-like. DR InterPro; IPR000626; Ubiquitin-like_dom. DR InterPro; IPR029071; Ubiquitin-like_domsf. DR InterPro; IPR019954; Ubiquitin_CS. DR InterPro; IPR019956; Ubiquitin_dom. DR PANTHER; PTHR10666:SF465; POLYUBIQUITIN 3; 1. DR PANTHER; PTHR10666; UBIQUITIN; 1. DR Pfam; PF00240; ubiquitin; 2. DR PRINTS; PR00348; UBIQUITIN. DR SMART; SM00213; UBQ; 2. DR SUPFAM; SSF54236; Ubiquitin-like; 2. DR PROSITE; PS00299; UBIQUITIN_1; 2. DR PROSITE; PS50053; UBIQUITIN_2; 2. DR Genevisible; Q9SHE7; AT. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Isopeptide bond; Nucleus; Reference proteome; KW Repeat; Ubl conjugation pathway. FT CHAIN 1..76 FT /note="Ubiquitin" FT /id="PRO_0000396910" FT CHAIN 77..152 FT /note="NEDD8-like protein RUB1" FT /id="PRO_0000035965" FT PROPEP 153..156 FT /evidence="ECO:0000305" FT /id="PRO_0000035966" FT DOMAIN 1..76 FT /note="Ubiquitin-like 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214" FT DOMAIN 77..152 FT /note="Ubiquitin-like 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214" FT CROSSLNK 76 FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with FT K-? in acceptor proteins)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214" FT CROSSLNK 152 FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with FT K-? in acceptor proteins)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214" FT STRAND 78..82 FT /evidence="ECO:0007829|PDB:1BT0" FT STRAND 88..92 FT /evidence="ECO:0007829|PDB:1BT0" FT HELIX 99..110 FT /evidence="ECO:0007829|PDB:1BT0" FT HELIX 114..116 FT /evidence="ECO:0007829|PDB:1BT0" FT STRAND 117..121 FT /evidence="ECO:0007829|PDB:1BT0" FT HELIX 133..135 FT /evidence="ECO:0007829|PDB:1BT0" FT STRAND 142..147 FT /evidence="ECO:0007829|PDB:1BT0" SQ SEQUENCE 156 AA; 17397 MW; FA8D702BB9C1B3AE CRC64; MQIFVKTLTG KTITLEVESS DTIDNVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLADYN IQKESTLHLV LRLRGGTMIK VKTLTGKEIE IDIEPTDTID RIKERVEEKE GIPPVQQRLI YAGKQLADDK TAKDYNIEGG SVLHLVLALR GGFGLL //