Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  ATP-dependent RNA helicase DED1  

UniProtKB / Swiss-Prot ID :  DED1_YEAST

Gene Name (Synonyms) : 
DED1, SPP81 YOR204W  

Species :  Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). 

Subcellular Localization :  Cytoplasm. 

Protein Function :  ATP-binding RNA helicase involved in translation initiation. Remodels RNA in response to ADP and ATP concentrations by facilitating disruption, but also formation of RNA duplexes. Has weak ATP-dependent affinity for dsRNA, but strong ATP- dependent affinity for ssRNA. Acts as a virus host factor involved in the replication of the MBV and the L-A viruses by promoting the negative-strand RNA synthesis. May be involved in recognition of the preinitiation complex and DNA binding of the RNA polymerase III and play a role in mRNA splicing. 

Protein Sequence MAELSEQVQNLSINDNNENGYVPPHLRGKPRSARNNSSNYNNNNGGYNGGRGGGSFFSNNRRGGYGNGGF...
Predicted Secondary Structure CCCHHHHHCCCCCCCCCCCCCCCHHHCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
210PhosphoserineKTGPSPQPE
HCCCCCCCC
37.20SysPTM
Link-
210Phosphoserine.KTGPSPQPE
HCCCCCCCC
37.20UniProtKB
Link-
263PhosphoserineVYGGSPIGN
EECCCCHHH
14.69SysPTM
Link-
263Phosphoserine.VYGGSPIGN
EECCCCHHH
14.69UniProtKB
Link-
535PhosphoserineDAMMSAPGS
HHHHHHHHH
20.44SysPTM
Link-
535Phosphoserine.DAMMSAPGS
HHHHHHHHH
20.44UniProtKB
Link-
539PhosphoserineSAPGSRSNS
HHHHHHHHH
31.32SysPTM
Link-
539Phosphoserine.SAPGSRSNS
HHHHHHHHH
31.32UniProtKB
Link-
541PhosphoserinePGSRSNSRR
HHHHHHHHH
40.63SysPTM
Link-
541Phosphoserine.PGSRSNSRR
HHHHHHHHH
40.63UniProtKB
Link-
543PhosphoserineSRSNSRRGG
HHHHHHHHC
25.30SysPTM
Link-
543Phosphoserine.SRSNSRRGG
HHHHHHHHC
25.30UniProtKB
Link-
572PhosphoserineGSSRSRDNS
CCCCCCCCC
46.03SysPTM
Link-
572Phosphoserine.GSSRSRDNS
CCCCCCCCC
46.03UniProtKB
Link-
576PhosphoserineSRDNSFRGG
CCCCCCCCC
22.17SysPTM
Link-
576Phosphoserine.SRDNSFRGG
CCCCCCCCC
22.17UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-535; SER-539 ANDSER-576, AND MASS SPECTROMETRY.
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-535; SER-539; SER-543;SER-572 AND SER-576, AND MASS SPECTROMETRY.
"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-541, AND MASSSPECTROMETRY.
"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-210; SER-263; SER-535;SER-539; SER-541 AND SER-543, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures