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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: -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 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

Keywordsi

Biological processUbl conjugation pathway

Enzyme and pathway databases

BioCyciYEAST:G3O-32270-MONOMER
ReactomeiR-SCE-8951664 Neddylation

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001295181 – 269Defective in cullin neddylation protein 1Add BLAST269

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei12PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ12395
PaxDbiQ12395
PRIDEiQ12395

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 conjugating enzyme binding Source: SGD
  • ubiquitin-like protein binding Source: SGD

Protein-protein interaction databases

BioGridi31397, 37 interactors
DIPiDIP-1238N
IntActiQ12395, 1 interactor
MINTiQ12395
STRINGi4932.YLR128W

Structurei

Secondary structure

1269
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi13 – 25Combined sources13
Helixi29 – 37Combined sources9
Turni38 – 41Combined sources4
Helixi43 – 54Combined sources12
Helixi59 – 61Combined sources3
Helixi73 – 82Combined sources10
Helixi90 – 100Combined sources11
Helixi107 – 115Combined sources9
Helixi127 – 136Combined sources10
Helixi142 – 158Combined sources17
Helixi160 – 174Combined sources15
Beta strandi180 – 183Combined sources4
Helixi184 – 194Combined sources11
Beta strandi199 – 201Combined sources3
Helixi205 – 218Combined sources14
Beta strandi222 – 224Combined sources3
Helixi225 – 237Combined sources13
Helixi241 – 247Combined sources7
Beta strandi252 – 254Combined sources3
Helixi256 – 267Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12395

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini14 – 51UBA-likeAdd BLAST38
Domaini70 – 266DCUN1PROSITE-ProRule annotationAdd BLAST197

Phylogenomic databases

GeneTreeiENSGT00550000074529
HOGENOMiHOG000112177
InParanoidiQ12395
KOiK17822
OMAiMITDDMS
OrthoDBiEOG092C3OM7

Family and domain databases

InterProiView protein in InterPro
IPR014764 DCN-prot
IPR005176 PONY_dom
IPR009060 UBA-like_sf
PANTHERiPTHR12281 PTHR12281, 1 hit
PfamiView protein in Pfam
PF03556 Cullin_binding, 1 hit
SUPFAMiSSF46934 SSF46934, 1 hit
PROSITEiView protein in PROSITE
PS51229 DCUN1, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiDCN1_YEAST
AccessioniPrimary (citable) accession number: Q12395
Secondary accession number(s): D6VYC3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: November 1, 1996
Last modified: February 28, 2018
This is version 141 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health