Reviewed, UniProtKB/Swiss-Prot Q12395 (DCN1_YEAST)

Names and origin

Protein names

Recommended name:
    Defective in cullin neddylation protein 1

Gene names

Name:	DCN1
Ordered Locus Names:	YLR128W
ORF Names:	L3111

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	269 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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. Ref.4
Subunit structure	Interacts with the cullin CDC53. Interacts with ubiquitin via its UBA-like domain. Interacts with RUB1/NEDD8. Ref.4 Ref.3
Sequence similarities	Contains 1 DCUN1 domain. Contains 1 UBA-like domain.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of ubiquitin-protein ligase activity Ref.4 Inferred from mutant phenotype. Source: SGD protein neddylation Ref.4 Inferred from direct assay. Source: SGD
Molecular function	enzyme activator activity Ref.4 Inferred from mutant phenotype. Source: SGD ubiquitin binding Ref.4 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDC53	Q12018	2	EBI-29871,EBI-4321

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 269

269

Defective in cullin neddylation protein 1

PRO_0000129518

Regions

Domain

14 – 51

38

UBA-like

Domain

70 – 266

197

DCUN1

Amino acid modifications

Modified residue

12

1

Phosphoserine Ref.5 Ref.6

Secondary structure

1

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269

Helix Strand Turn

Details...

Helix

13 – 25

13

Helix

29 – 37

9

Turn

38 – 41

4

Helix

43 – 54

12

Helix

73 – 82

10

Helix

90 – 100

11

Helix

107 – 116

10

Helix

127 – 136

10

Helix

142 – 158

17

Helix

160 – 174

15

Beta strand

180 – 183

4

Helix

184 – 194

11

Helix

205 – 217

13

Helix

225 – 237

13

Helix

241 – 247

7

Helix

256 – 267

12

Sequences

	Sequence		Length	Mass (Da)
	Q12395-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: CBD829C941466180	FASTA	269	32,204
	10 20 30 40 50 60 MSNNKIKRKD ASPEQEAIES FTSLTKCDPK VSRKYLQRNH WNINYALNDY YDKEIGTFTD 70 80 90 100 110 120 EVSTVAHPPV YPKELTQVFE HYINNNLFDI DSLVKFIEEL GYNLEDLATL CLAHLLGYKK 130 140 150 160 170 180 LEEPLKREDF LSTWFMQGCS TISDMQECIK TLDVKLHEDL QYFTQIYNYA FNLILDPNRK 190 200 210 220 230 240 DIDTDEGIQY WKLFFQPEYP VRMEPDLLEA WFRFLRDEGK TTISKDTWRM LLLFFKRYPT 250 260 IQKIISDYDE TAAWPFIIDE FYECLQDQQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 9090053] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 90840 / EAY235 / FY23.
[2]	"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: 9169871] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"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: 11283612] [Abstract] Cited for: INTERACTION WITH CDC53.
[4]	"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: 15988528] [Abstract] Cited for: FUNCTION, INTERACTION WITH UBIQUITIN AND NEDD8.
[5]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, MASS SPECTROMETRY.
[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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X89514 Genomic DNA. Translation: CAA61706.1.
Z73300 Genomic DNA. Translation: CAA97697.1.
U53877 Genomic DNA. Translation: AAB82374.1.
X91258 Genomic DNA. Translation: CAA62639.1.

PIR

S59316.

RefSeq

NP_013229.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2IS9	X-ray	1.92	A	66-269	[»]
3BQ3	X-ray	1.90	A	1-269	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:1238N.

IntAct

Q12395. 3 interactions.

Genome annotation databases

Ensembl

YLR128W. Saccharomyces cerevisiae. [Contig view]

GeneID

850819.

GenomeReviews

Gene locus YLR128W in contig Y13138_GR.

KEGG

sce:YLR128W.

NMPDR

fig|4932.3.peg.4222.

Organism-specific databases

CYGD

YLR128w.

SGD

S000004118. DCN1.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

Q12395.

OMA

Q12395. NFVEFAR.

Gene expression databases

ArrayExpress

Q12395.

GermOnline

YLR128W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR014764. DCN.
IPR005176. DUF298.
[Graphical view]

PANTHER

PTHR12281. DUF298. 1 hit.

Pfam

PF03556. DUF298. 1 hit.
[Graphical view]

PROSITE

PS51229. DCUN1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

967064.

Entry information

Entry name

DCN1_YEAST

Accession

Primary (citable) accession number: Q12395

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)