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Protein

Cullin-8

Gene

RTT101

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

Functioni

Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes (CRLs), which mediate the ubiquitination of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The CRL associates with CDC34 as the E2 ubiquitin-conjugating enzyme. The functional specificity of the CRL depends on the type of the associated substrate receptor protein. RTT101(MMS1-MMS22) promotes fork progression through damaged DNA or natural pause sites by stabilizing replication proteins like the replication fork-pausing complex (FPC) and leading-strand polymerase at stalled replication forks. RTT101(MMS1-MMS22) ubiquitinates the acetylated histones H3K56ac-H4 at lysine residues H3K121, H3K122 and H3K125. Ubiquitination is required for efficient histone deposition during replication-coupled nucleosome assembly, probably by facilitating the transfer of H3-H4 from ASF1 to other chaperones involved in histone deposition. RTT101(MMS1-CRT10) may regulate nucleotide synthesis through transcriptional regulation of ribonucleotide reductase. RTT101(MMS1) is also involved in the non-functional rRNA decay (NRD) of 25S rRNA through the selective, ubiquitination-dependent degradation of nonfunctional ribosomal particles. Ubiquitinates the FACT (facilitiates chromatin transcription) complex subunit SPT16 in an MMS1-independent manner. Involved in regulation of Ty1 transposition and protects the genome from Ty1 integration upstream of tRNA genes.10 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Molecular functioni

  • ubiquitin-protein transferase activity Source: SGD

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • cell division Source: UniProtKB-KW
  • DNA repair Source: UniProtKB-KW
  • negative regulation of transposition, RNA-mediated Source: SGD
  • nonfunctional rRNA decay Source: SGD
  • regulation of mitotic nuclear division Source: SGD
  • replication fork processing Source: SGD
  • ubiquitin-dependent protein catabolic process Source: SGD
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, DNA damage, DNA repair, Ubl conjugation pathway

Enzyme and pathway databases

BioCyciYEAST:G3O-31511-MONOMER.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Cullin-8
Alternative name(s):
Cullin-C
Regulator of Ty1 transposition protein 101
Gene namesi
Name:RTT101
Synonyms:CUL8
Ordered Locus Names:YJL047C
ORF Names:J1166
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJL047C.
SGDiS000003583. RTT101.

Subcellular locationi

GO - Cellular componenti

  • Cul8-RING ubiquitin ligase complex Source: SGD
  • cytoplasm Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Delays anaphase progression.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi680 – 6867Missing : Disrupts interaction with HRT1 and prevents RUB1/NEDD8 modification. 1 Publication
Mutagenesisi791 – 7911K → A or R: Prevents RUB1/NEDD8 modification. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 842842Cullin-8PRO_0000119807Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki791 – 791Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)

Post-translational modificationi

Neddylated. HRT1-binding is necessary for RUB1/NEDD8 modification of RTT101. The modification enhances ubiquitin-ligase activity.1 Publication

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP47050.
PeptideAtlasiP47050.
PRIDEiP47050.

Interactioni

Subunit structurei

Component of multiple cullin-RING ligases (CRLs) composed of 4 subunits: the RING protein HRT1, the cullin RTT101, a linker protein MMS1, and one of many alternative substrate receptors belonging to a protein family described as DCAF (DDB1- and CUL4-associated factor). Component of a RTT101(MMS1-MMS22) complex with the substrate receptor MMS22. This complex further interacts with RTT107 and CTF4 to form RTT101-MMS1-MMS22-RTT107 and RTT101-MMS1-MMS22-CTF4 complexes respectively. Component of a RTT101(MSS1-CRT10) complex with the substrate receptor CRT10. Component of a RTT101(MSS1-ESC2) complex with the potential substrate receptor ESC2. Component of a RTT101(MSS1-ORC5) complex with the potential substrate receptor ORC5. Interacts (via C-ter) with HRT1; required for ubiquitin-ligase activity. Interacts (via N-ter) with MMS1.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MMS1Q062112EBI-25861,EBI-38894

Protein-protein interaction databases

BioGridi33708. 149 interactions.
DIPiDIP-2887N.
IntActiP47050. 14 interactions.
MINTiMINT-496763.

Structurei

3D structure databases

ProteinModelPortaliP47050.
SMRiP47050. Positions 773-842.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 5050Required for interaction with MMS1Add
BLAST

Sequence similaritiesi

Belongs to the cullin family.PROSITE-ProRule annotation

Phylogenomic databases

InParanoidiP47050.
OrthoDBiEOG71ZPBW.

Family and domain databases

Gene3Di1.10.10.10. 2 hits.
InterProiIPR016158. Cullin_homology.
IPR019559. Cullin_neddylation_domain.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
SMARTiSM00884. Cullin_Nedd8. 1 hit.
[Graphical view]
SUPFAMiSSF75632. SSF75632. 1 hit.
PROSITEiPS50069. CULLIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P47050-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MINESVSKRE GFHESISRET SASNALGLYN KFNDERNPRY RTMIAELHEF
60 70 80 90 100
FHLTLAETIT ETDVKELECN KEKAAKFRKL MPKMLNNCRE LTQRKSYIPY
110 120 130 140 150
NSEFNGNDEK QKKFQLLHQH QIVLSFQEFC DELAKLIIDA HVLSFLTRCD
160 170 180 190 200
YSYEIIPKNW TSFYKLFQYV MGAVGPIISY VPVNYPMIRK ELGFETLTIF
210 220 230 240 250
QYYDSKLFEC MKSHFGREFS TLVSATIHHY IHMFPITNTM LEKEVPMLRI
260 270 280 290 300
MSNCNFSIEG LSPKDFYMKT LRQYYCEESN LRPRLETFKN FKVLLTRNAL
310 320 330 340 350
LASLFSPEWV SDANDLFISH LLLNKKSISE YIEIGKDTYD EEKERYFKTE
360 370 380 390 400
THFSLLMFRN AFEAKNMLSK FKEFCDDAVS EKLKAAYGSN HDTERLFDEV
410 420 430 440 450
VQLANVDHLK IYSDSIEYHL CNLLGSTSKA IEQYVKYFES HLFIIVRKIK
460 470 480 490 500
TTKKDLPRDM KIKYLNENLP ILRLKFVNLP TFPNFFERSI FRKTILQSDQ
510 520 530 540 550
NSSFIKDILP VYKDSLMELF KQRIITNVSQ EDEMRYRDQY QPYLSQFFQP
560 570 580 590 600
VEVMADLRIK YASFLSFYEN IEAAVKFGKT YNENNSKSFF PLIFDRERIP
610 620 630 640 650
KVFQQSNEVK KNFVLPQEMD DTWNQFLRNY HEQNKVEDSD ASKKELYPMW
660 670 680 690 700
NLHHCEVESP YIIQDGTNLI FELTLFQTCV LTLFNESDHL TLQVISEQTK
710 720 730 740 750
LAYKDLALVL KSFCNYKILT RDIDNTYSIN ESFKPDMKKV KNGKLRVVLP
760 770 780 790 800
RTASLQSSNT GGERTSSAHH EGSNSQWTQE LLKACITRSV KSERNGLDYD
810 820 830 840
HLFETVKQQI KGFSVGEFKD ALAKLLRDKF ITRDESTATY KY
Length:842
Mass (Da):99,326
Last modified:February 1, 1996 - v1
Checksum:iA86A48F6DC6AF163
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY387707 Genomic DNA. Translation: AAQ91376.1.
Z49322 Genomic DNA. Translation: CAA89338.1.
BK006943 Genomic DNA. Translation: DAA08753.1.
PIRiS56819.
RefSeqiNP_012488.3. NM_001181480.3.

Genome annotation databases

EnsemblFungiiYJL047C; YJL047C; YJL047C.
GeneIDi853400.
KEGGisce:YJL047C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY387707 Genomic DNA. Translation: AAQ91376.1.
Z49322 Genomic DNA. Translation: CAA89338.1.
BK006943 Genomic DNA. Translation: DAA08753.1.
PIRiS56819.
RefSeqiNP_012488.3. NM_001181480.3.

3D structure databases

ProteinModelPortaliP47050.
SMRiP47050. Positions 773-842.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33708. 149 interactions.
DIPiDIP-2887N.
IntActiP47050. 14 interactions.
MINTiMINT-496763.

Proteomic databases

MaxQBiP47050.
PeptideAtlasiP47050.
PRIDEiP47050.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJL047C; YJL047C; YJL047C.
GeneIDi853400.
KEGGisce:YJL047C.

Organism-specific databases

EuPathDBiFungiDB:YJL047C.
SGDiS000003583. RTT101.

Phylogenomic databases

InParanoidiP47050.
OrthoDBiEOG71ZPBW.

Enzyme and pathway databases

UniPathwayiUPA00143.
BioCyciYEAST:G3O-31511-MONOMER.

Miscellaneous databases

PROiP47050.

Family and domain databases

Gene3Di1.10.10.10. 2 hits.
InterProiIPR016158. Cullin_homology.
IPR019559. Cullin_neddylation_domain.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
SMARTiSM00884. Cullin_Nedd8. 1 hit.
[Graphical view]
SUPFAMiSSF75632. SSF75632. 1 hit.
PROSITEiPS50069. CULLIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A role for Saccharomyces cerevisiae Cul8 ubiquitin ligase in proper anaphase progression."
    Michel J.J., McCarville J.F., Xiong Y.
    J. Biol. Chem. 278:22828-22837(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH HRT1, MUTAGENESIS OF 680-VAL--GLU-686 AND LYS-791, DISRUPTION PHENOTYPE.
  2. "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
    Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K.
    , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
    EMBO J. 15:2031-2049(1996) [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. "Multiple regulators of Ty1 transposition in Saccharomyces cerevisiae have conserved roles in genome maintenance."
    Scholes D.T., Banerjee M., Bowen B., Curcio M.J.
    Genetics 159:1449-1465(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. Cited for: SUBCELLULAR LOCATION [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: NEDDYLATION AT LYS-791, MUTAGENESIS OF LYS-791.
  7. "The cullin Rtt101p promotes replication fork progression through damaged DNA and natural pause sites."
    Luke B., Versini G., Jaquenoud M., Zaidi I.W., Kurz T., Pintard L., Pasero P., Peter M.
    Curr. Biol. 16:786-792(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Budding yeast Mms22 and Mms1 regulate homologous recombination induced by replisome blockage."
    Duro E., Vaisica J.A., Brown G.W., Rouse J.
    DNA Repair 7:811-818(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Rtt101 and Mms1 in budding yeast form a CUL4(DDB1)-like ubiquitin ligase that promotes replication through damaged DNA."
    Zaidi I.W., Rabut G., Poveda A., Scheel H., Malmstrom J., Ulrich H., Hofmann K., Pasero P., Peter M., Luke B.
    EMBO Rep. 9:1034-1040(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MMS1, IDENTIFICATION IN COMPLEXES WITH MMS22 AND CRT10.
  10. "Regulation of rtt107 recruitment to stalled DNA replication forks by the cullin rtt101 and the rtt109 acetyltransferase."
    Roberts T.M., Zaidi I.W., Vaisica J.A., Peter M., Brown G.W.
    Mol. Biol. Cell 19:171-180(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RTT107.
  11. "A role for ubiquitin in the clearance of nonfunctional rRNAs."
    Fujii K., Kitabatake M., Sakata T., Miyata A., Ohno M.
    Genes Dev. 23:963-974(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Cul8/Rtt101 forms a variety of protein complexes that regulate DNA damage response and transcriptional silencing."
    Mimura S., Yamaguchi T., Ishii S., Noro E., Katsura T., Obuse C., Kamura T.
    J. Biol. Chem. 285:9858-9867(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MMS1, IDENTIFICATION IN COMPLEXES WITH MMS22; RTT107; CTF4; ESC2 AND ORC5.
  13. "Ubiquitylation of FACT by the cullin-E3 ligase Rtt101 connects FACT to DNA replication."
    Han J., Li Q., McCullough L., Kettelkamp C., Formosa T., Zhang Z.
    Genes Dev. 24:1485-1490(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "Mms1 and Mms22 stabilize the replisome during replication stress."
    Vaisica J.A., Baryshnikova A., Costanzo M., Boone C., Brown G.W.
    Mol. Biol. Cell 22:2396-2408(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "A Cul4 E3 ubiquitin ligase regulates histone hand-off during nucleosome assembly."
    Han J., Zhang H., Zhang H., Wang Z., Zhou H., Zhang Z.
    Cell 155:817-829(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN UBIQUITINATION OF H3.

Entry informationi

Entry nameiCUL8_YEAST
AccessioniPrimary (citable) accession number: P47050
Secondary accession number(s): D6VWD7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: June 8, 2016
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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