Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  H/ACA ribonucleoprotein complex subunit 4  

UniProtKB / Swiss-Prot ID :  DKC1_MOUSE

Gene Name (Synonyms) : 
Dkc1  

Species :  Mus musculus (Mouse). 

Subcellular Localization :  Nucleus, nucleolus. Nucleus, Cajal body. Note=Also localized to Cajal bodies (coiled bodies). 

Protein Function :  Required for ribosome biogenesis and telomere maintenance. Probable catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Each rRNA can contain up to 100 pseudouridine ('psi') residues, which may serve to stabilize the conformation of rRNAs. Also required for correct processing or intranuclear trafficking of TERC, the RNA component of the telomerase reverse transcriptase (TERT) holoenzyme. 

Protein Sequence MADAEVITFPKKHKKKKDRKPLQEDDVAEIQHAEEFLIKPESKVAQLDTSQWPLLLKNFDKLNVRTAHYT...
Predicted Secondary Structure CCCCCEEECCHHHHHHHHCCCCCCCHHHHHHHCCCEEECCCCCCCCCCCHHCCHHHHHHHHHHHCCCCCC...
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
89PhosphothreonineDYIRTGFIN
HHHHCCEEE
27.21Phosphositeplus
Link-
98PhosphoserineLDKPSNPSS
EECCCCCCH
68.09Phosphositeplus
Link-
102PhosphoserineSNPSSHEVV
CCCCHHHHH
25.56Phosphositeplus
Link-
420PhosphoserineYIDYSDSGK
CCCCCCCCC
22.88Phosphositeplus
Link-
451PhosphoserineRKRDSESES
HHCCCCCCC
47.24PhosphoELM
Link-
451PhosphoserineRKRDSESES
HHCCCCCCC
47.24Phosphositeplus
Link-
451PhosphoserineRKRDSESES
HHCCCCCCC
47.24SysPTM
Link-
451Phosphoserine.RKRDSESES
HHCCCCCCC
47.24UniProtKB
Link-
453PhosphoserineRDSESESDE
CCCCCCCCC
46.48PhosphoELM
Link-
453PhosphoserineRDSESESDE
CCCCCCCCC
46.48Phosphositeplus
Link-
453PhosphoserineRDSESESDE
CCCCCCCCC
46.48SysPTM
Link-
453Phosphoserine.RDSESESDE
CCCCCCCCC
46.48UniProtKB
Link-
455PhosphoserineSESESDETP
CCCCCCCCC
50.45Phosphositeplus
Link-
455PhosphoserineSESESDETP
CCCCCCCCC
50.45SysPTM
Link-
455Phosphoserine.SESESDETP
CCCCCCCCC
50.45UniProtKB
Link-
458PhosphothreonineESDETPTVP
CCCCCCCCC
29.29Phosphositeplus
Link-
458Phosphothreonine.ESDETPTVP
CCCCCCCCC
29.29UniProtKB
Link-
477PhosphothreonineKKPKTVLES
HCCCCHHHC
38.56Phosphositeplus
Link-
481PhosphoserineTVLESGGET
CHHHCCCCC
48.19PhosphoELM
Link-
481PhosphoserineTVLESGGET
CHHHCCCCC
48.19Phosphositeplus
Link-
481Phosphoserine.TVLESGGET
CHHHCCCCC
48.19UniProtKB
Link-
485PhosphothreonineSGGETGDGD
CCCCCCCCC
43.79Phosphositeplus
Link-
508PhosphoserineVEEMSE
HHHHCC
43.35PhosphoELM
Link-
508PhosphoserineVEEMSE
HHHHCC
43.35Phosphositeplus
Link-
508Phosphoserine.VEEMSE
HHHHCC
43.35UniProtKB
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
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451; SER-453 ANDTHR-458, AND MASS SPECTROMETRY.
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-508, AND MASSSPECTROMETRY.
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451; SER-453; SER-455AND SER-508, AND MASS SPECTROMETRY.
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-508, AND MASSSPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, AND MASSSPECTROMETRY.
"A differential phosphoproteomic analysis of retinoic acid-treated P19cells.";
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
J. Proteome Res. 6:3174-3186(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451; SER-453 ANDSER-455, AND MASS SPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451; SER-453 ANDSER-481, 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