CLK3_HUMAN - dbPTM
CLK3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CLK3_HUMAN
UniProt AC P49761
Protein Name Dual specificity protein kinase CLK3
Gene Name CLK3
Organism Homo sapiens (Human).
Sequence Length 638
Subcellular Localization Isoform 1: Nucleus. Cytoplasm. Cytoplasmic vesicle, secretory vesicle, acrosome.
Isoform 2: Nucleus speckle. Co-localizes with serine- and arginine-rich (SR) proteins in the nuclear speckles.
Protein Description 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 MPVLSARRRELADHAGSGRRSGPSPTARSGPHLSALRAQPARAAHLSGRGTYVRRDTAGGGPGQARPLGPPGTSLLGRGARRSGEGWCPGAFESGARAARPPSRVEPRLATAASREGAGLPRAEVAAGSGRGARSGEWGLAAAGAWETMHHCKRYRSPEPDPYLSYRWKRRRSYSREHEGRLRYPSRREPPPRRSRSRSHDRLPYQRRYRERRDSDTYRCEERSPSFGEDYYGPSRSRHRRRSRERGPYRTRKHAHHCHKRRTRSCSSASSRSQQSSKRSSRSVEDDKEGHLVCRIGDWLQERYEIVGNLGEGTFGKVVECLDHARGKSQVALKIIRNVGKYREAARLEINVLKKIKEKDKENKFLCVLMSDWFNFHGHMCIAFELLGKNTFEFLKENNFQPYPLPHVRHMAYQLCHALRFLHENQLTHTDLKPENILFVNSEFETLYNEHKSCEEKSVKNTSIRVADFGSATFDHEHHTTIVATRHYRPPEVILELGWAQPCDVWSIGCILFEYYRGFTLFQTHENREHLVMMEKILGPIPSHMIHRTRKQKYFYKGGLVWDENSSDGRYVKENCKPLKSYMLQDSLEHVQLFDLMRRMLEFDPAQRITLAEALLHPFFAGLTPEERSFHTSRNPSR
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
7 (in isoform 3)Phosphorylation-34.5118691976
7 (in isoform 2)Phosphorylation-34.5118691976
7 (in isoform 1)Phosphorylation-34.5118691976
9 (in isoform 1)Phosphorylation-37.4125849741
9 (in isoform 3)Phosphorylation-37.4125849741
9 (in isoform 2)Phosphorylation-37.4125849741
21PhosphorylationHAGSGRRSGPSPTAR
HCCCCCCCCCCCCCC		54.4127174698
24PhosphorylationSGRRSGPSPTARSGP
CCCCCCCCCCCCCCC		38.1127174698
26PhosphorylationRRSGPSPTARSGPHL
CCCCCCCCCCCCCCH		38.7527174698
29PhosphorylationGPSPTARSGPHLSAL
CCCCCCCCCCCHHHH		54.9627174698
34PhosphorylationARSGPHLSALRAQPA
CCCCCCHHHHHCCCC		23.4027174698
114PhosphorylationPRLATAASREGAGLP
HHHHHHHHHCCCCCC		28.5321964256
135PhosphorylationGSGRGARSGEWGLAA
CCCCCCCCCCCHHHH		40.3018691976
155PhosphorylationTMHHCKRYRSPEPDP
HHHHHHHCCCCCCCC		10.8422322096
157PhosphorylationHHCKRYRSPEPDPYL
HHHHHCCCCCCCCCH		25.3622322096
163PhosphorylationRSPEPDPYLSYRWKR
CCCCCCCCHHHHHHC		18.7022322096
165PhosphorylationPEPDPYLSYRWKRRR
CCCCCCHHHHHHCCC		13.5522322096
166PhosphorylationEPDPYLSYRWKRRRS
CCCCCHHHHHHCCCC		20.2122322096
173PhosphorylationYRWKRRRSYSREHEG
HHHHCCCCCCCCCCC		26.1628102081
174PhosphorylationRWKRRRSYSREHEGR
HHHCCCCCCCCCCCC		15.2223663014
175PhosphorylationWKRRRSYSREHEGRL
HHCCCCCCCCCCCCC		32.2228102081
184PhosphorylationEHEGRLRYPSRREPP
CCCCCCCCCCCCCCC		15.3428152594
186PhosphorylationEGRLRYPSRREPPPR
CCCCCCCCCCCCCCC		34.7326699800
195PhosphorylationREPPPRRSRSRSHDR
CCCCCCCCCCCCCCC		35.5730108239
197PhosphorylationPPPRRSRSRSHDRLP
CCCCCCCCCCCCCCC		39.1123401153
199PhosphorylationPRRSRSRSHDRLPYQ
CCCCCCCCCCCCCHH		30.8723401153
205PhosphorylationRSHDRLPYQRRYRER
CCCCCCCHHHHHHHH		21.1728152594
215PhosphorylationRYRERRDSDTYRCEE
HHHHHCCCCCCCCCC		30.0028176443
217PhosphorylationRERRDSDTYRCEERS
HHHCCCCCCCCCCCC		19.4727273156
218PhosphorylationERRDSDTYRCEERSP
HHCCCCCCCCCCCCC		20.4630576142
220CarbamidationRDSDTYRCEERSPSF
CCCCCCCCCCCCCCC		4.4817322306
224PhosphorylationTYRCEERSPSFGEDY
CCCCCCCCCCCCCCC		28.3322167270
226PhosphorylationRCEERSPSFGEDYYG
CCCCCCCCCCCCCCC		47.3222167270
231PhosphorylationSPSFGEDYYGPSRSR
CCCCCCCCCCCCHHH		13.1528450419
232PhosphorylationPSFGEDYYGPSRSRH
CCCCCCCCCCCHHHH		34.5828450419
235PhosphorylationGEDYYGPSRSRHRRR
CCCCCCCCHHHHHHH		38.2323927012
237PhosphorylationDYYGPSRSRHRRRSR
CCCCCCHHHHHHHHH		36.4526552605
243PhosphorylationRSRHRRRSRERGPYR
HHHHHHHHHHCCCCH		36.3628102081
265PhosphorylationCHKRRTRSCSSASSR
HHHCCCCCCCCCHHH		20.1029978859
267PhosphorylationKRRTRSCSSASSRSQ
HCCCCCCCCCHHHHH		30.1329978859
268PhosphorylationRRTRSCSSASSRSQQ
CCCCCCCCCHHHHHH		36.1829978859
270PhosphorylationTRSCSSASSRSQQSS
CCCCCCCHHHHHHCC		28.3829978859
271PhosphorylationRSCSSASSRSQQSSK
CCCCCCHHHHHHCCC		35.3529978859
273PhosphorylationCSSASSRSQQSSKRS
CCCCHHHHHHCCCCC		34.2229978859
276PhosphorylationASSRSQQSSKRSSRS
CHHHHHHCCCCCCCC		30.1429978859
277PhosphorylationSSRSQQSSKRSSRSV
HHHHHHCCCCCCCCC		27.9629978859
280PhosphorylationSQQSSKRSSRSVEDD
HHHCCCCCCCCCCCC		33.5623927012
281PhosphorylationQQSSKRSSRSVEDDK
HHCCCCCCCCCCCCC		32.3823927012
283PhosphorylationSSKRSSRSVEDDKEG
CCCCCCCCCCCCCCC		31.6329255136
288UbiquitinationSRSVEDDKEGHLVCR
CCCCCCCCCCCEEEE		77.30-
314PhosphorylationVGNLGEGTFGKVVEC
EEECCCCHHHHHHHH		25.55-
317UbiquitinationLGEGTFGKVVECLDH
CCCCHHHHHHHHHHH		38.63-
328SumoylationCLDHARGKSQVALKI
HHHHCCCCHHHHHHH		31.96-
328UbiquitinationCLDHARGKSQVALKI
HHHHCCCCHHHHHHH		31.96-
334UbiquitinationGKSQVALKIIRNVGK
CCHHHHHHHHHHHCH		26.75-
354UbiquitinationRLEINVLKKIKEKDK
HHHHHHHHHHHHHHC		48.44-
386 (in isoform 3)Ubiquitination-6.5421906983
396UbiquitinationKNTFEFLKENNFQPY
CCHHHHHHHCCCCCC		64.81-
409 (in isoform 1)Ubiquitination-15.7221906983
433SumoylationQLTHTDLKPENILFV
CCCCCCCCHHHEEEE		53.7717000644
453PhosphorylationTLYNEHKSCEEKSVK
HHHHCCCCHHHHCCC		28.7729083192
458PhosphorylationHKSCEEKSVKNTSIR
CCCHHHHCCCCCEEE		41.4229083192
460UbiquitinationSCEEKSVKNTSIRVA
CHHHHCCCCCEEEEE		62.69-
462PhosphorylationEEKSVKNTSIRVADF
HHHCCCCCEEEEEEC		21.5829083192
463PhosphorylationEKSVKNTSIRVADFG
HHCCCCCEEEEEECC		20.1429083192
553UbiquitinationIHRTRKQKYFYKGGL
HCCCCCCCEEEECCE		40.12-
557UbiquitinationRKQKYFYKGGLVWDE
CCCCEEEECCEECCC		36.282190698
557 (in isoform 4)Ubiquitination-36.2821906983
566PhosphorylationGLVWDENSSDGRYVK
CEECCCCCCCCCCCC		27.9720873877
567PhosphorylationLVWDENSSDGRYVKE
EECCCCCCCCCCCCC		56.5220873877
573UbiquitinationSSDGRYVKENCKPLK
CCCCCCCCCCCCCCC		33.98-
577UbiquitinationRYVKENCKPLKSYML
CCCCCCCCCCCHHHC		66.04-
580UbiquitinationKENCKPLKSYMLQDS
CCCCCCCCHHHCHHH		48.33-
637PhosphorylationFHTSRNPSR------
CCCCCCCCC------		54.9224719451
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
157SPhosphorylationKinaseCHEK1O14757
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CLK3_HUMAN !!
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 CLK3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RSRP1_HUMANRSRP1physical
16189514
A4_HUMANAPPphysical
21832049
SUV91_HUMANSUV39H1physical
23455924
SLAF7_HUMANSLAMF7physical
21988832
FKBP5_HUMANFKBP5physical
23602568
SRRM2_HUMANSRRM2physical
23602568
TNPO3_HUMANTNPO3physical
23602568
PSME3_HUMANPSME3physical
23602568
BCLF1_HUMANBCLAF1physical
23602568
RBBP6_HUMANRBBP6physical
23602568
PABP1_HUMANPABPC1physical
23602568
IMB1_HUMANKPNB1physical
23602568
HNRPC_HUMANHNRNPCphysical
23602568
SRSF7_HUMANSRSF7physical
23602568
LBR_HUMANLBRphysical
23602568
PABP4_HUMANPABPC4physical
23602568
P53_HUMANTP53physical
23602568
CLK3_HUMANCLK3physical
23602568
TRA2B_HUMANTRA2Bphysical
23602568
TRA2A_HUMANTRA2Aphysical
23602568
SCRIB_HUMANSCRIBphysical
23602568
LARP1_HUMANLARP1physical
23602568
USP9X_HUMANUSP9Xphysical
23602568
ANM1_HUMANPRMT1physical
23602568
LRRC1_HUMANLRRC1physical
23602568
IMA5_HUMANKPNA1physical
23602568
UBP7_HUMANUSP7physical
23602568
GPTC8_HUMANGPATCH8physical
23602568
TR150_HUMANTHRAP3physical
23602568
IMA1_HUMANKPNA2physical
23602568
UBP11_HUMANUSP11physical
23602568
F192A_HUMANFAM192Aphysical
23602568
ANM5_HUMANPRMT5physical
23455924
CLK3_HUMANCLK3physical
25416956
HXB6_HUMANHOXB6physical
25416956
HXB7_HUMANHOXB7physical
25416956
OAS2_HUMANOAS2physical
25416956
RBY1A_HUMANRBMY1A1physical
25416956
SDCB1_HUMANSDCBPphysical
25416956
SRPK2_HUMANSRPK2physical
25416956
ZN263_HUMANZNF263physical
25416956
RBMX_HUMANRBMXphysical
25416956
RSRP1_HUMANRSRP1physical
25416956
RBY1F_HUMANRBMY1Fphysical
25416956
KR103_HUMANKRTAP10-3physical
25416956
GPTC8_HUMANGPATCH8physical
28514442
CLK2_HUMANCLK2physical
28514442
ZCH18_HUMANZC3H18physical
28514442
JMJD6_HUMANJMJD6physical
28514442
FKBP5_HUMANFKBP5physical
28514442
USP9Y_HUMANUSP9Yphysical
28514442
PR38B_HUMANPRPF38Bphysical
28514442
PININ_HUMANPNNphysical
28514442
SRS12_HUMANSRSF12physical
28514442
ZC3HD_HUMANZC3H13physical
28514442
RU17_HUMANSNRNP70physical
28514442
SRSF8_HUMANSRSF8physical
28514442
PPIG_HUMANPPIGphysical
28514442
RBBP6_HUMANRBBP6physical
28514442
PPHLN_HUMANPPHLN1physical
28514442
YTDC1_HUMANYTHDC1physical
28514442
SIR1_HUMANSIRT1physical
28514442
VIR_HUMANKIAA1429physical
28514442
UBE2O_HUMANUBE2Ophysical
28514442
HS90A_HUMANHSP90AA1physical
28514442
MEPCE_HUMANMEPCEphysical
28514442
ZN638_HUMANZNF638physical
28514442
SAFB2_HUMANSAFB2physical
28514442
TNPO3_HUMANTNPO3physical
28514442
LRRC1_HUMANLRRC1physical
28514442
PSME3_HUMANPSME3physical
28514442
GEMI2_HUMANGEMIN2physical
28514442
CDC37_HUMANCDC37physical
28514442
SRRM2_HUMANSRRM2physical
28514442
SRS10_HUMANSRSF10physical
28514442
SAHH3_HUMANAHCYL2physical
28514442
F192A_HUMANFAM192Aphysical
28514442
HS90B_HUMANHSP90AB1physical
28514442
SRSF1_HUMANSRSF1physical
28514442
TOPRS_HUMANTOPORSphysical
28514442
NRDC_HUMANNRD1physical
28514442
SCRIB_HUMANSCRIBphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CLK3_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.
"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.
"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.
"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.
"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.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory