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 DDX51  

UniProtKB / Swiss-Prot ID :  DDX51_HUMAN

Gene Name (Synonyms) : 
DDX51  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus, nucleolus (By similarity). 

Protein Function :  ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits (By similarity). 

Protein Sequence MALFYVARYPGPDAAAAAGPEGAEAGAHGRARALLERLQSRARERQQQREPAQTEAAASTEPATRRRRRP...
Predicted Secondary Structure CCEEEEHHCCCCHHHCCCCCCCCCCCCCCCHHHHHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCCCCCC...
Protein Variant
LocationDescription
41R -> Q (in dbSNP:rs17857214). VAR_055299
134E -> V (in dbSNP:rs17855642). VAR_055300
175Q -> K (in dbSNP:rs17855639). VAR_055301
249P -> L (in dbSNP:rs17857213). VAR_055302
295Q -> R (in dbSNP:rs1133690). VAR_055303
322A -> V (in dbSNP:rs60927391). VAR_061825
406Q -> K (in dbSNP:rs17853968). VAR_055304
652Q -> K (in dbSNP:rs17853969). VAR_055305
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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
Protein Variant
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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
83PhosphoserineAEPGSPEAP
CCCCCCHHH
30.22HPRD
Link-
83PhosphoserineAEPGSPEAP
CCCCCCHHH
30.22PhosphoELM
Link-
83PhosphoserineAEPGSPEAP
CCCCCCHHH
30.22Phosphositeplus
Link-
83PhosphoserineAEPGSPEAP
CCCCCCHHH
30.22SysPTM
Link-
83Phosphoserine.AEPGSPEAP
CCCCCCHHH
30.22UniProtKB
Link-
103PhosphoserineAGAESNEEA
CCCCCCCCC
49.35HPRD
Link-
103PhosphoserineAGAESNEEA
CCCCCCCCC
49.35PhosphoELM
Link-
103PhosphoserineAGAESNEEA
CCCCCCCCC
49.35Phosphositeplus
Link-
103PhosphoserineAGAESNEEA
CCCCCCCCC
49.35SysPTM
Link-
103Phosphoserine.AGAESNEEA
CCCCCCCCC
49.35UniProtKB
Link-
211Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PDLQKQLRA
HHHHHHHHH
59.61Phosphositeplus
Link-
255PhosphoserineDLCVSAPTG
CEEEECCCC
27.77HPRD
Link-
304PhosphotyrosineVFNIYTDAT
HHHHHHHHC
10.32Phosphositeplus
Link-
435PhosphothreonineSATLTQNPE
EECCCHHHH
23.19HPRD
Link-
435PhosphothreonineSATLTQNPE
EECCCHHHH
23.19Phosphositeplus
Link-
562PhosphothreonineLLISTDATA
EEEECCHHH
23.74HPRD
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
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83 AND SER-103, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83 AND SER-103, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures