RUB1_ORYSJ
ID RUB1_ORYSJ Reviewed; 153 AA.
AC P0C030; O82079; P03993; P69321; Q0J1Q2; Q652Q2; Q67UR4; Q69P70; Q6ATC2;
AC Q7XN78; Q8S5Y3; Q9AR09;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 03-AUG-2022, entry version 94.
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=OsRUB1;
DE AltName: Full=Ubiquitin-related protein 1;
DE Flags: Precursor;
GN Name=RUB1; Synonyms=NEDD8, UBQ4;
GN OrderedLocusNames=Os09g0420800, LOC_Os09g25320;
GN ORFNames=OJ1740_D06.1, P0668D04.32;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
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-48-linked is involved in protein degradation via the proteasome;
CC Lys-63-linked is involved in endocytosis, and DNA-damage responses.
CC Linear polymer chains formed via attachment by the initiator Met lead
CC to cell signaling. Ubiquitin is usually conjugated to Lys residues of
CC target proteins, however, in rare cases, conjugation to Cys or Ser
CC residues has been observed. When polyubiquitin is free (unanchored-
CC polyubiquitin), it also has distinct roles, such as in activation of
CC protein kinases, and in signaling (By similarity). {ECO:0000250}.
CC -!- FUNCTION: [NEDD8-like protein RUB1]: Appears to function as a stable
CC post-translational protein modifier.
CC -!- SUBCELLULAR LOCATION: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Ubiquitin is generally synthesized as a polyubiquitin
CC precursor with tandem head to tail repeats. Often, there is one to
CC three additional amino acids after the last repeat, removed in the
CC mature protein. Alternatively, ubiquitin extension protein is
CC synthesized as a single copy of ubiquitin fused to a ribosomal protein
CC (either L40 or S27A) or to an ubiquitin-related protein (either RUB1 or
CC RUB2). Following translation, extension protein is cleaved from
CC 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; AP005426; BAD33498.1; -; Genomic_DNA.
DR EMBL; AP005579; BAD33626.1; -; Genomic_DNA.
DR EMBL; AP008215; BAF25113.1; -; Genomic_DNA.
DR EMBL; AP014965; BAT08123.1; -; Genomic_DNA.
DR EMBL; AK099513; BAG94169.1; -; mRNA.
DR RefSeq; XP_015611997.1; XM_015756511.1.
DR AlphaFoldDB; P0C030; -.
DR SMR; P0C030; -.
DR STRING; 4530.OS09T0420800-01; -.
DR PaxDb; P0C030; -.
DR EnsemblPlants; Os09t0420800-01; Os09t0420800-01; Os09g0420800.
DR GeneID; 4347085; -.
DR Gramene; Os09t0420800-01; Os09t0420800-01; Os09g0420800.
DR KEGG; osa:4347085; -.
DR eggNOG; KOG0001; Eukaryota.
DR HOGENOM; CLU_010412_0_0_1; -.
DR InParanoid; P0C030; -.
DR OMA; ETQIVTC; -.
DR OrthoDB; 1536766at2759; -.
DR Proteomes; UP000000763; Chromosome 9.
DR Proteomes; UP000059680; Chromosome 9.
DR Genevisible; P0C030; OS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IEA:UniProt.
DR GO; GO:0031386; F:protein tag; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0019941; P:modification-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR CDD; cd01806; Ubl_NEDD8; 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 Pfam; PF00240; ubiquitin; 2.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM00213; UBQ; 2.
DR SUPFAM; SSF54236; SSF54236; 2.
DR PROSITE; PS00299; UBIQUITIN_1; 2.
DR PROSITE; PS50053; UBIQUITIN_2; 2.
PE 2: Evidence at transcript level;
KW Cytoplasm; Isopeptide bond; Nucleus; Reference proteome; Repeat;
KW Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..76
FT /note="Ubiquitin"
FT /id="PRO_0000396913"
FT CHAIN 77..152
FT /note="NEDD8-like protein RUB1"
FT /id="PRO_0000035973"
FT PROPEP 153
FT /evidence="ECO:0000305"
FT /id="PRO_0000035974"
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 48
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
FT CROSSLNK 63
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
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"
SQ SEQUENCE 153 AA; 17130 MW; 1929C1B3AEF7CAC9 CRC64;
MQIFVKTLTG KTITLEVESS DTIDNVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLADYN
IQKESTLHLV LRLRGGTMIK VKTLTGKEIE IDIEPTDTID RIKERVEEKE GIPPVQQRLI
YAGKQLADDK TAKDYNIEGG SVLHLVLALR GGY
