RUB1_YEAST
ID RUB1_YEAST Reviewed; 77 AA.
AC Q03919; D6VSC2;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=NEDD8-like protein RUB1;
DE AltName: Full=Related to ubiquitin protein 1;
DE AltName: Full=Ubiquitin-like protein RUB1;
DE Flags: Precursor;
GN Name=RUB1; OrderedLocusNames=YDR139C; ORFNames=YD9302.15C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH CDC53, AND
RP PROBABLE REMOVAL OF ASP-77.
RC STRAIN=ATCC 200912 / DF5;
RX PubMed=9545234; DOI=10.1093/emboj/17.8.2208;
RA Liakopoulos D., Doenges G., Matuschewski K., Jentsch S.;
RT "A novel protein modification pathway related to the ubiquitin system.";
RL EMBO J. 17:2208-2214(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION IN NEDDYLATION OF CDC53.
RX PubMed=9531531; DOI=10.1101/gad.12.7.914;
RA Lammer D., Mathias N., Laplaza J.M., Jiang W., Liu Y., Callis J., Goebl M.,
RA Estelle M.;
RT "Modification of yeast Cdc53p by the ubiquitin-related protein Rub1p
RT affects function of the SCFCdc4 complex.";
RL Genes Dev. 12:914-926(1998).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP FUNCTION IN NEDDYLATION OF RTT101 AND CUL3.
RX PubMed=14519104; DOI=10.1042/bj20030755;
RA Laplaza J.M., Bostick M., Scholes D.T., Curcio M.J., Callis J.;
RT "Saccharomyces cerevisiae ubiquitin-like protein Rub1 conjugates to cullin
RT proteins Rtt101 and Cul3 in vivo.";
RL Biochem. J. 377:459-467(2004).
RN [7]
RP INTERACTION WITH DCN1.
RX PubMed=15988528; DOI=10.1038/nature03662;
RA Kurz T., Oezlue N., Rudolf F., O'Rourke S.M., Luke B., Hofmann K.,
RA Hyman A.A., Bowerman B., Peter M.;
RT "The conserved protein DCN-1/Dcn1p is required for cullin neddylation in C.
RT elegans and S. cerevisiae.";
RL Nature 435:1257-1261(2005).
CC -!- FUNCTION: Ubiquitin-like protein modifier that can be covalently
CC attached to lysine residues of target proteins. Activated by the
CC dimeric UBA3-ULA1 E1 enzyme and conjugated by the E2 UBC12 to substrate
CC proteins. RUB1-conjugated (neddylated) substrate proteins include the
CC cullins CDC53, RTT101 and CUL3, and the modification enhances the
CC ubiquitin-ligase activity of the corresponding cullin-RING-based E3
CC ubiquitin-protein ligase complexes (CRLs).
CC {ECO:0000269|PubMed:14519104, ECO:0000269|PubMed:9531531,
CC ECO:0000269|PubMed:9545234}.
CC -!- SUBUNIT: Interacts with CDC53 and DCN1. {ECO:0000269|PubMed:15988528,
CC ECO:0000269|PubMed:9545234}.
CC -!- MISCELLANEOUS: Present with 1310 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Y16890; CAA76516.1; -; Genomic_DNA.
DR EMBL; Z48179; CAA88221.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11982.1; -; Genomic_DNA.
DR PIR; S51867; S51867.
DR RefSeq; NP_010423.4; NM_001180446.3.
DR AlphaFoldDB; Q03919; -.
DR SMR; Q03919; -.
DR BioGRID; 32193; 72.
DR DIP; DIP-1627N; -.
DR IntAct; Q03919; 9.
DR MINT; Q03919; -.
DR STRING; 4932.YDR139C; -.
DR iPTMnet; Q03919; -.
DR MaxQB; Q03919; -.
DR PaxDb; Q03919; -.
DR PRIDE; Q03919; -.
DR EnsemblFungi; YDR139C_mRNA; YDR139C; YDR139C.
DR GeneID; 851717; -.
DR KEGG; sce:YDR139C; -.
DR SGD; S000002546; RUB1.
DR VEuPathDB; FungiDB:YDR139C; -.
DR eggNOG; KOG0001; Eukaryota.
DR GeneTree; ENSGT00940000155856; -.
DR HOGENOM; CLU_010412_6_4_1; -.
DR InParanoid; Q03919; -.
DR OMA; YAGKQMA; -.
DR BioCyc; YEAST:G3O-29736-MON; -.
DR Reactome; R-SCE-5689603; UCH proteinases.
DR Reactome; R-SCE-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-SCE-8951664; Neddylation.
DR PRO; PR:Q03919; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q03919; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031386; F:protein tag; IDA:SGD.
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:0045116; P:protein neddylation; IDA:SGD.
DR GO; GO:0030162; P:regulation of proteolysis; 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; 1.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS00299; UBIQUITIN_1; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW Isopeptide bond; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..76
FT /note="NEDD8-like protein RUB1"
FT /id="PRO_0000035979"
FT PROPEP 77
FT /evidence="ECO:0000305"
FT /id="PRO_0000035980"
FT DOMAIN 1..74
FT /note="Ubiquitin-like"
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"
SQ SEQUENCE 77 AA; 8693 MW; F05DBF3C8E464FD1 CRC64;
MIVKVKTLTG KEISVELKES DLVYHIKELL EEKEGIPPSQ QRLIFQGKQI DDKLTVTDAH
LVEGMQLHLV LTLRGGN
