DCN1_YEAST - dbPTM
DCN1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DCN1_YEAST
UniProt AC Q12395
Protein Name Defective in cullin neddylation protein 1
Gene Name DCN1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 269
Subcellular Localization
Protein Description 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..
Protein Sequence MSNNKIKRKDASPEQEAIESFTSLTKCDPKVSRKYLQRNHWNINYALNDYYDKEIGTFTDEVSTVAHPPVYPKELTQVFEHYINNNLFDIDSLVKFIEELGYNLEDLATLCLAHLLGYKKLEEPLKREDFLSTWFMQGCSTISDMQECIKTLDVKLHEDLQYFTQIYNYAFNLILDPNRKDIDTDEGIQYWKLFFQPEYPVRMEPDLLEAWFRFLRDEGKTTISKDTWRMLLLFFKRYPTIQKIISDYDETAAWPFIIDEFYECLQDQQ
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
12PhosphorylationKIKRKDASPEQEAIE
CCCCCCCCHHHHHHH
38.8221551504

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of DCN1_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DCN1_YEAST !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of DCN1_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RUB1_YEASTRUB1physical
15988528
UBI4P_YEASTUBI4physical
15988528
CDC53_YEASTCDC53physical
15988528
DCN1_YEASTDCN1physical
18206966
CDC53_YEASTCDC53physical
18206966
UBC12_YEASTUBC12physical
18206966
SEH1_YEASTSEH1genetic
19061648
PRP19_YEASTPRP19genetic
19061648
CWC27_YEASTCWC27genetic
19061648
LAG2_YEASTLAG2genetic
19942853
CDC53_YEASTCDC53physical
20832729
RTG3_YEASTRTG3genetic
21127252
MET18_YEASTMET18genetic
21127252
KCS1_YEASTKCS1genetic
21127252
RPH1_YEASTRPH1genetic
21127252
CDC53_YEASTCDC53physical
19942853
LAG2_YEASTLAG2physical
19942853
UBC12_YEASTUBC12physical
19942853
UBC12_HUMANUBE2Mphysical
15988528
UBC12_YEASTUBC12physical
20832729

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DCN1_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND MASSSPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND MASSSPECTROMETRY.

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