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Protein

NEDD8-like protein RUB1

Gene

RUB1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Ubiquitin-like protein modifier that can be covalently attached to lysine residues of target proteins. Activated by the dimeric UBA3-ULA1 E1 enzyme and conjugated by the E2 UBC12 to substrate proteins. RUB1-conjugated (neddylated) substrate proteins include the cullins CDC53, RTT101 and CUL3, and the modification enhances the ubiquitin-ligase activity of the corresponding cullin-RING-based E3 ubiquitin-protein ligase complexes (CRLs).3 Publications

GO - Molecular functioni

  • protein tag Source: SGD

GO - Biological processi

  • protein neddylation Source: SGD
Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

BioCyciYEAST:G3O-29736-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
NEDD8-like protein RUB1
Alternative name(s):
Related to ubiquitin protein 1
Ubiquitin-like protein RUB1
Gene namesi
Name:RUB1
Ordered Locus Names:YDR139C
ORF Names:YD9302.15C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR139C.
SGDiS000002546. RUB1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7676NEDD8-like protein RUB1PRO_0000035979Add
BLAST
Propeptidei77 – 771CuratedPRO_0000035980

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki76 – 76Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)PROSITE-ProRule annotation

Keywords - PTMi

Isopeptide bond

Proteomic databases

MaxQBiQ03919.
PeptideAtlasiQ03919.

Interactioni

Subunit structurei

Interacts with CDC53 and DCN1.2 Publications

Protein-protein interaction databases

BioGridi32193. 45 interactions.
DIPiDIP-1627N.
IntActiQ03919. 8 interactions.
MINTiMINT-407484.

Structurei

3D structure databases

ProteinModelPortaliQ03919.
SMRiQ03919. Positions 1-76.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 7474Ubiquitin-likePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000233942.
InParanoidiQ03919.
KOiK12158.
OMAiQMNEDKT.
OrthoDBiEOG78SQXJ.

Family and domain databases

InterProiIPR019956. Ubiquitin.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
IPR000626. Ubiquitin_dom.
[Graphical view]
PfamiPF00240. ubiquitin. 1 hit.
[Graphical view]
PRINTSiPR00348. UBIQUITIN.
SMARTiSM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS00299. UBIQUITIN_1. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q03919-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIVKVKTLTG KEISVELKES DLVYHIKELL EEKEGIPPSQ QRLIFQGKQI
60 70
DDKLTVTDAH LVEGMQLHLV LTLRGGN
Length:77
Mass (Da):8,693
Last modified:November 1, 1996 - v1
Checksum:iF05DBF3C8E464FD1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y16890 Genomic DNA. Translation: CAA76516.1.
Z48179 Genomic DNA. Translation: CAA88221.1.
BK006938 Genomic DNA. Translation: DAA11982.1.
PIRiS51867.
RefSeqiNP_010423.4. NM_001180446.3.

Genome annotation databases

EnsemblFungiiYDR139C; YDR139C; YDR139C.
GeneIDi851717.
KEGGisce:YDR139C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y16890 Genomic DNA. Translation: CAA76516.1.
Z48179 Genomic DNA. Translation: CAA88221.1.
BK006938 Genomic DNA. Translation: DAA11982.1.
PIRiS51867.
RefSeqiNP_010423.4. NM_001180446.3.

3D structure databases

ProteinModelPortaliQ03919.
SMRiQ03919. Positions 1-76.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32193. 45 interactions.
DIPiDIP-1627N.
IntActiQ03919. 8 interactions.
MINTiMINT-407484.

Proteomic databases

MaxQBiQ03919.
PeptideAtlasiQ03919.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR139C; YDR139C; YDR139C.
GeneIDi851717.
KEGGisce:YDR139C.

Organism-specific databases

EuPathDBiFungiDB:YDR139C.
SGDiS000002546. RUB1.

Phylogenomic databases

HOGENOMiHOG000233942.
InParanoidiQ03919.
KOiK12158.
OMAiQMNEDKT.
OrthoDBiEOG78SQXJ.

Enzyme and pathway databases

BioCyciYEAST:G3O-29736-MONOMER.

Miscellaneous databases

NextBioi969415.
PROiQ03919.

Family and domain databases

InterProiIPR019956. Ubiquitin.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
IPR000626. Ubiquitin_dom.
[Graphical view]
PfamiPF00240. ubiquitin. 1 hit.
[Graphical view]
PRINTSiPR00348. UBIQUITIN.
SMARTiSM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS00299. UBIQUITIN_1. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel protein modification pathway related to the ubiquitin system."
    Liakopoulos D., Doenges G., Matuschewski K., Jentsch S.
    EMBO J. 17:2208-2214(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH CDC53, PROBABLE REMOVAL OF ASP-77.
    Strain: ATCC 200912 / DF5.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Modification of yeast Cdc53p by the ubiquitin-related protein Rub1p affects function of the SCFCdc4 complex."
    Lammer D., Mathias N., Laplaza J.M., Jiang W., Liu Y., Callis J., Goebl M., Estelle M.
    Genes Dev. 12:914-926(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NEDDYLATION OF CDC53.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "Saccharomyces cerevisiae ubiquitin-like protein Rub1 conjugates to cullin proteins Rtt101 and Cul3 in vivo."
    Laplaza J.M., Bostick M., Scholes D.T., Curcio M.J., Callis J.
    Biochem. J. 377:459-467(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NEDDYLATION OF RTT101 AND CUL3.
  7. "The conserved protein DCN-1/Dcn1p is required for cullin neddylation in C. elegans and S. cerevisiae."
    Kurz T., Oezlue N., Rudolf F., O'Rourke S.M., Luke B., Hofmann K., Hyman A.A., Bowerman B., Peter M.
    Nature 435:1257-1261(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DCN1.

Entry informationi

Entry nameiRUB1_YEAST
AccessioniPrimary (citable) accession number: Q03919
Secondary accession number(s): D6VSC2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1310 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.