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Protein

Defective in cullin neddylation protein 1

Gene

DCN1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Required for neddylation of cullin components of SCF-type E3 ubiquitin ligase complexes. Neddylation of cullins play an essential role in the regulation of SCF-type complexes activity. Does not act by preventing deneddylation, but rather facilitates neddylation, possibly by acting with HRT1/RBX1 to recruit the Nedd8-charged E2 UBC12 to the cullin component of SCF-type complexes.1 Publication

GO - Molecular functioni

  • cullin family protein binding Source: SGD
  • protein binding, bridging Source: SGD
  • ubiquitin binding Source: UniProtKB
  • ubiquitin conjugating enzyme binding Source: SGD
  • ubiquitin-like protein binding Source: SGD

GO - Biological processi

  • positive regulation of ubiquitin-protein transferase activity Source: SGD
  • protein neddylation Source: SGD
Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

BioCyciYEAST:G3O-32270-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Defective in cullin neddylation protein 1
Gene namesi
Name:DCN1
Ordered Locus Names:YLR128W
ORF Names:L3111
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR128W.
SGDiS000004118. DCN1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 269269Defective in cullin neddylation protein 1PRO_0000129518Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei12 – 121PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ12395.

PTM databases

iPTMnetiQ12395.

Interactioni

Subunit structurei

Interacts with the cullin CDC53. Interacts with ubiquitin via its UBA-like domain. Interacts with RUB1/NEDD8.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC53Q120183EBI-29871,EBI-4321

GO - Molecular functioni

  • cullin family protein binding Source: SGD
  • protein binding, bridging Source: SGD
  • ubiquitin binding Source: UniProtKB
  • ubiquitin conjugating enzyme binding Source: SGD
  • ubiquitin-like protein binding Source: SGD

Protein-protein interaction databases

BioGridi31397. 27 interactions.
DIPiDIP-1238N.
IntActiQ12395. 1 interaction.
MINTiMINT-410699.

Structurei

Secondary structure

1
269
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi13 – 2513Combined sources
Helixi29 – 379Combined sources
Turni38 – 414Combined sources
Helixi43 – 5412Combined sources
Helixi59 – 613Combined sources
Helixi73 – 8210Combined sources
Helixi90 – 10011Combined sources
Helixi107 – 1159Combined sources
Helixi127 – 13610Combined sources
Helixi142 – 15817Combined sources
Helixi160 – 17415Combined sources
Beta strandi180 – 1834Combined sources
Helixi184 – 19411Combined sources
Beta strandi199 – 2013Combined sources
Helixi205 – 21814Combined sources
Beta strandi222 – 2243Combined sources
Helixi225 – 23713Combined sources
Helixi241 – 2477Combined sources
Beta strandi252 – 2543Combined sources
Helixi256 – 26712Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IS9X-ray1.92A66-269[»]
2L4ENMR-A6-62[»]
2L4FNMR-A6-62[»]
3BQ3X-ray1.90A1-269[»]
3O2PX-ray2.23A70-269[»]
3O6BX-ray3.10A/C/E/G/I70-269[»]
3TDIX-ray2.30A/B70-269[»]
ProteinModelPortaliQ12395.
SMRiQ12395. Positions 6-269.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12395.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 5138UBA-likeAdd
BLAST
Domaini70 – 266197DCUN1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 DCUN1 domain.PROSITE-ProRule annotation
Contains 1 UBA-like domain.Curated

Phylogenomic databases

GeneTreeiENSGT00550000074529.
HOGENOMiHOG000112177.
InParanoidiQ12395.
KOiK17822.
OMAiIASEQWR.
OrthoDBiEOG7HQNM2.

Family and domain databases

InterProiIPR014764. DCN-prot.
IPR005176. PONY_dom.
IPR009060. UBA-like.
[Graphical view]
PANTHERiPTHR12281. PTHR12281. 1 hit.
PfamiPF03556. Cullin_binding. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
PROSITEiPS51229. DCUN1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q12395-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNNKIKRKD ASPEQEAIES FTSLTKCDPK VSRKYLQRNH WNINYALNDY
60 70 80 90 100
YDKEIGTFTD EVSTVAHPPV YPKELTQVFE HYINNNLFDI DSLVKFIEEL
110 120 130 140 150
GYNLEDLATL CLAHLLGYKK LEEPLKREDF LSTWFMQGCS TISDMQECIK
160 170 180 190 200
TLDVKLHEDL QYFTQIYNYA FNLILDPNRK DIDTDEGIQY WKLFFQPEYP
210 220 230 240 250
VRMEPDLLEA WFRFLRDEGK TTISKDTWRM LLLFFKRYPT IQKIISDYDE
260
TAAWPFIIDE FYECLQDQQ
Length:269
Mass (Da):32,204
Last modified:November 1, 1996 - v1
Checksum:iCBD829C941466180
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X89514 Genomic DNA. Translation: CAA61706.1.
Z73300 Genomic DNA. Translation: CAA97697.1.
U53877 Genomic DNA. Translation: AAB82374.1.
X91258 Genomic DNA. Translation: CAA62639.1.
BK006945 Genomic DNA. Translation: DAA09439.1.
PIRiS59316.
RefSeqiNP_013229.1. NM_001182015.1.

Genome annotation databases

EnsemblFungiiYLR128W; YLR128W; YLR128W.
GeneIDi850819.
KEGGisce:YLR128W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X89514 Genomic DNA. Translation: CAA61706.1.
Z73300 Genomic DNA. Translation: CAA97697.1.
U53877 Genomic DNA. Translation: AAB82374.1.
X91258 Genomic DNA. Translation: CAA62639.1.
BK006945 Genomic DNA. Translation: DAA09439.1.
PIRiS59316.
RefSeqiNP_013229.1. NM_001182015.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IS9X-ray1.92A66-269[»]
2L4ENMR-A6-62[»]
2L4FNMR-A6-62[»]
3BQ3X-ray1.90A1-269[»]
3O2PX-ray2.23A70-269[»]
3O6BX-ray3.10A/C/E/G/I70-269[»]
3TDIX-ray2.30A/B70-269[»]
ProteinModelPortaliQ12395.
SMRiQ12395. Positions 6-269.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31397. 27 interactions.
DIPiDIP-1238N.
IntActiQ12395. 1 interaction.
MINTiMINT-410699.

PTM databases

iPTMnetiQ12395.

Proteomic databases

MaxQBiQ12395.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR128W; YLR128W; YLR128W.
GeneIDi850819.
KEGGisce:YLR128W.

Organism-specific databases

EuPathDBiFungiDB:YLR128W.
SGDiS000004118. DCN1.

Phylogenomic databases

GeneTreeiENSGT00550000074529.
HOGENOMiHOG000112177.
InParanoidiQ12395.
KOiK17822.
OMAiIASEQWR.
OrthoDBiEOG7HQNM2.

Enzyme and pathway databases

BioCyciYEAST:G3O-32270-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ12395.
PROiQ12395.

Family and domain databases

InterProiIPR014764. DCN-prot.
IPR005176. PONY_dom.
IPR009060. UBA-like.
[Graphical view]
PANTHERiPTHR12281. PTHR12281. 1 hit.
PfamiPF03556. Cullin_binding. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
PROSITEiPS51229. DCUN1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis of a 37.6 kbp cosmid clone from the right arm of Saccharomyces cerevisiae chromosome XII, carrying YAP3, HOG1, SNR6, tRNA-Arg3 and 23 new open reading frames, among which several homologies to proteins involved in cell division control and to mammalian growth factors and other animal proteins are found."
    Verhasselt P., Volckaert G.
    Yeast 13:241-250(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 90840 / EAY235 / FY23.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "Skp1 forms multiple protein complexes, including RAVE, a regulator of V-ATPase assembly."
    Seol J.H., Shevchenko A., Shevchenko A., Deshaies R.J.
    Nat. Cell Biol. 3:384-391(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDC53.
  5. "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: FUNCTION, INTERACTION WITH UBIQUITIN AND NEDD8.
  6. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "N-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex."
    Scott D.C., Monda J.K., Bennett E.J., Harper J.W., Schulman B.A.
    Science 334:674-678(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 70-269 IN COMPLEX WITH UBC12.

Entry informationi

Entry nameiDCN1_YEAST
AccessioniPrimary (citable) accession number: Q12395
Secondary accession number(s): D6VYC3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 129 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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 XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: 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.