Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Dual specificity protein kinase CLK3  

UniProtKB / Swiss-Prot ID :  CLK3_HUMAN

Gene Name (Synonyms) : 
CLK3  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Isoform 1: Nucleus. Cytoplasm (By similarity). Cytoplasmic vesicle, secretory vesicle, acrosome (By similarity). Isoform 2: Nucleus speckle. Note=Co- localizes with serine- and arginine-rich (SR) proteins in the nuclear speckles. 

Protein Function :  Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex. May be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing and can cause redistribution of SR proteins from speckles to a diffuse nucleoplasmic distribution. Phosphorylates SRSF1 and SRSF3. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells. 

Protein Sequence MPVLSARRRELADHAGSGRRSGPSPTARSGPHLSALRAQPARAAHLSGRGTYVRRDTAGGGPGQARPLGP...
Predicted Secondary Structure CCCCCCCCCCCCCCCCHHHCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCC...
Protein Variant
LocationDescription
486R -> C. VAR_040413
607Q -> R. VAR_045579
628R -> W. VAR_045580
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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
135PhosphoserineRGARSGEWG
CCCCCCCCC
40.30HPRD
Link
155PhosphotyrosineHCKRYRSPE
CCCCCEEEE
10.84PhosphoELM
Link
155PhosphotyrosineHCKRYRSPE
CCCCCEEEE
10.84Phosphositeplus
Link
155PhosphotyrosineHCKRYRSPE
CCCCCEEEE
10.84SysPTM
Link
155Phosphotyrosine.HCKRYRSPE
CCCCCEEEE
10.84UniProtKB
Link
157PhosphoserineKRYRSPEPD
CCCEEEEEE
25.36PhosphoELM
Link
157PhosphoserineKRYRSPEPD
CCCEEEEEE
25.36Phosphositeplus
Link
157PhosphoserineKRYRSPEPD
CCCEEEEEE
25.36SysPTM
Link
157Phosphoserine.KRYRSPEPD
CCCEEEEEE
25.36UniProtKB
Link
163PhosphotyrosineEPDPYLSYR
EEEEECCCC
18.70Phosphositeplus
Link
165PhosphoserineDPYLSYRWK
EEECCCCEE
13.55Phosphositeplus
Link
166PhosphotyrosinePYLSYRWKR
EECCCCEEE
20.21Phosphositeplus
Link
175PhosphoserineRRSYSREHE
EEEEEECCC
32.22Phosphositeplus
Link
197PhosphoserineRRSRSRSHD
CCHHHHHHH
39.11Phosphositeplus
Link
197PhosphoserineRRSRSRSHD
CCHHHHHHH
39.11SysPTM
Link
197Phosphoserine.RRSRSRSHD
CCHHHHHHH
39.11UniProtKB
Link
199PhosphoserineSRSRSHDRL
HHHHHHHHH
30.87PhosphoELM
Link
199PhosphoserineSRSRSHDRL
HHHHHHHHH
30.87Phosphositeplus
Link
199PhosphoserineSRSRSHDRL
HHHHHHHHH
30.87SysPTM
Link
199Phosphoserine.SRSRSHDRL
HHHHHHHHH
30.87UniProtKB
Link
215PhosphoserineERRDSDTYR
CCCCCCEEE
30.00PhosphoELM
Link
215PhosphoserineERRDSDTYR
CCCCCCEEE
30.00Phosphositeplus
Link
215Phosphoserine.ERRDSDTYR
CCCCCCEEE
30.00UniProtKB
Link
217PhosphothreonineRDSDTYRCE
CCCCEEEEE
19.47PhosphoELM
Link
218PhosphotyrosineDSDTYRCEE
CCCEEEEEE
20.46PhosphoELM
Link
220Carbamidation cysteineDTYRCEERS
CEEEEEEEE
4.48SysPTM
Link
224PhosphoserineCEERSPSFG
EEEEEEEEC
28.33PhosphoELM
Link
224PhosphoserineCEERSPSFG
EEEEEEEEC
28.33Phosphositeplus
Link
224PhosphoserineCEERSPSFG
EEEEEEEEC
28.33SysPTM
Link
224PhosphoserineCEERSPSFG
EEEEEEEEC
28.33SysPTM
Link
224Phosphoserine.CEERSPSFG
EEEEEEEEC
28.33UniProtKB
Link
226PhosphoserineERSPSFGED
EEEEEECCC
47.32PhosphoELM
Link
226PhosphoserineERSPSFGED
EEEEEECCC
47.32Phosphositeplus
Link
226PhosphoserineERSPSFGED
EEEEEECCC
47.32SysPTM
Link
226Phosphoserine.ERSPSFGED
EEEEEECCC
47.32UniProtKB
Link
280PhosphoserineSSKRSSRSV
HCCEEEECC
33.56Phosphositeplus
Link
281PhosphoserineSKRSSRSVE
CCEEEECCC
32.38Phosphositeplus
Link
283PhosphoserineRSSRSVEDD
EEEECCCCC
31.63Phosphositeplus
Link
283Phosphoserine.RSSRSVEDD
EEEECCCCC
31.63UniProtKB
Link
557Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KYFYKGGLV
36.28Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
Q4VX15_HUMANphysical interactionMINT-67663MINT16189514
CA063_HUMANphysical interactionEBI-754591
intact16189514
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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
"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 TYR-155; SER-157; SER-215;SER-224; SER-226 AND SER-283, AND MASS SPECTROMETRY.
"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 TYR-155; SER-157; SER-224AND SER-226, AND MASS SPECTROMETRY.
"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-157, 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 TYR-155; SER-197; SER-199;SER-224 AND SER-226, AND MASS SPECTROMETRY.
"Proteomics analysis of protein kinases by target class-selectiveprefractionation and tandem mass spectrometry.";
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R.,Keri G., Wehland J., Daub H.;
Mol. Cell. Proteomics 6:537-547(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures