CLK2_HUMAN - dbPTM
CLK2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CLK2_HUMAN
UniProt AC P49760
Protein Name Dual specificity protein kinase CLK2
Gene Name CLK2
Organism Homo sapiens (Human).
Sequence Length 499
Subcellular Localization Isoform 1: Nucleus. Nucleus speckle. Inhibition of phosphorylation at Ser-142 results in accumulation in the nuclear speckle..
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. Acts as a suppressor of hepatic gluconeogenesis and glucose output by repressing PPARGC1A transcriptional activity on gluconeogenic genes via its phosphorylation. Phosphorylates PPP2R5B thereby stimulating the assembly of PP2A phosphatase with the PPP2R5B-AKT1 complex leading to dephosphorylation of AKT1. Phosphorylates: PTPN1, SRSF1 and SRSF3. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells..
Protein Sequence MPHPRRYHSSERGSRGSYREHYRSRKHKRRRSRSWSSSSDRTRRRRREDSYHVRSRSSYDDRSSDRRVYDRRYCGSYRRNDYSRDRGDAYYDTDYRHSYEYQRENSSYRSQRSSRRKHRRRRRRSRTFSRSSSQHSSRRAKSVEDDAEGHLIYHVGDWLQERYEIVSTLGEGTFGRVVQCVDHRRGGARVALKIIKNVEKYKEAARLEINVLEKINEKDPDNKNLCVQMFDWFDYHGHMCISFELLGLSTFDFLKDNNYLPYPIHQVRHMAFQLCQAVKFLHDNKLTHTDLKPENILFVNSDYELTYNLEKKRDERSVKSTAVRVVDFGSATFDHEHHSTIVSTRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLFQTHDNREHLAMMERILGPIPSRMIRKTRKQKYFYRGRLDWDENTSAGRYVRENCKPLRRYLTSEAEEHHQLFDLIESMLEYEPAKRLTLGEALQHPFFARLRAEPPNKLWDSSRDISR
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
7Phosphorylation-MPHPRRYHSSERGS
-CCCCCCCCCCCCCC
13.8222817900
9PhosphorylationPHPRRYHSSERGSRG
CCCCCCCCCCCCCCC
25.5928102081
10PhosphorylationHPRRYHSSERGSRGS
CCCCCCCCCCCCCCC
20.2828102081
14PhosphorylationYHSSERGSRGSYREH
CCCCCCCCCCCHHHH
39.4228102081
17PhosphorylationSERGSRGSYREHYRS
CCCCCCCCHHHHHHH
21.6527251275
18PhosphorylationERGSRGSYREHYRSR
CCCCCCCHHHHHHHH
23.8929449344
34PhosphorylationHKRRRSRSWSSSSDR
HHHHHCCCCCCCCHH
32.3422817900
36PhosphorylationRRRSRSWSSSSDRTR
HHHCCCCCCCCHHHH
22.9128102081
37PhosphorylationRRSRSWSSSSDRTRR
HHCCCCCCCCHHHHH
27.8328102081
38PhosphorylationRSRSWSSSSDRTRRR
HCCCCCCCCHHHHHH
30.6428102081
39PhosphorylationSRSWSSSSDRTRRRR
CCCCCCCCHHHHHHH
32.8128102081
42PhosphorylationWSSSSDRTRRRRRED
CCCCCHHHHHHHHHC
33.2528102081
50PhosphorylationRRRRREDSYHVRSRS
HHHHHHCCCCCCCCC
16.6323401153
51PhosphorylationRRRREDSYHVRSRSS
HHHHHCCCCCCCCCC
19.3630266825
55PhosphorylationEDSYHVRSRSSYDDR
HCCCCCCCCCCCCCC
35.1124144214
57PhosphorylationSYHVRSRSSYDDRSS
CCCCCCCCCCCCCCC
34.2030576142
58PhosphorylationYHVRSRSSYDDRSSD
CCCCCCCCCCCCCCC
31.3225884760
59PhosphorylationHVRSRSSYDDRSSDR
CCCCCCCCCCCCCCC
24.1017384208
63PhosphorylationRSSYDDRSSDRRVYD
CCCCCCCCCCCCCCC
43.5125884760
64PhosphorylationSSYDDRSSDRRVYDR
CCCCCCCCCCCCCCH
35.7130576142
69PhosphorylationRSSDRRVYDRRYCGS
CCCCCCCCCHHCCCC
11.2617384208
73PhosphorylationRRVYDRRYCGSYRRN
CCCCCHHCCCCCCCC
11.3222210691
76PhosphorylationYDRRYCGSYRRNDYS
CCHHCCCCCCCCCCC
16.3527251275
77PhosphorylationDRRYCGSYRRNDYSR
CHHCCCCCCCCCCCC
10.0129449344
82PhosphorylationGSYRRNDYSRDRGDA
CCCCCCCCCCCCCCC
14.7818691976
83PhosphorylationSYRRNDYSRDRGDAY
CCCCCCCCCCCCCCC
30.4829214152
90PhosphorylationSRDRGDAYYDTDYRH
CCCCCCCCCCCCCCC
13.4527080861
91PhosphorylationRDRGDAYYDTDYRHS
CCCCCCCCCCCCCCC
17.6827732954
93PhosphorylationRGDAYYDTDYRHSYE
CCCCCCCCCCCCCHH
20.8628985074
95PhosphorylationDAYYDTDYRHSYEYQ
CCCCCCCCCCCHHHH
16.5927794612
98PhosphorylationYDTDYRHSYEYQREN
CCCCCCCCHHHHHHC
15.6323401153
99PhosphorylationDTDYRHSYEYQRENS
CCCCCCCHHHHHHCC
16.7221406692
101PhosphorylationDYRHSYEYQRENSSY
CCCCCHHHHHHCCCH
12.4919835603
106PhosphorylationYEYQRENSSYRSQRS
HHHHHHCCCHHCHHH
24.8019369195
127PhosphorylationRRRRRSRTFSRSSSQ
HHHHHHHHHCCCCHH
27.4922817900
127 (in isoform 2)Phosphorylation-27.4922210691
129 (in isoform 2)Phosphorylation-30.5522210691
131 (in isoform 2)Phosphorylation-32.8922210691
132 (in isoform 2)Phosphorylation-32.6722210691
133 (in isoform 2)Phosphorylation-32.9122210691
133PhosphorylationRTFSRSSSQHSSRRA
HHHCCCCHHHHHCCC
32.9125954137
133 (in isoform 3)Phosphorylation-32.91-
135 (in isoform 3)Phosphorylation-29.68-
136PhosphorylationSRSSSQHSSRRAKSV
CCCCHHHHHCCCCCC
20.2225954137
136 (in isoform 3)Phosphorylation-20.22-
137PhosphorylationRSSSQHSSRRAKSVE
CCCHHHHHCCCCCCC
24.5425954137
141 (in isoform 3)Phosphorylation-53.9025849741
142PhosphorylationHSSRRAKSVEDDAEG
HHHCCCCCCCCCCCC
29.7423401153
153PhosphorylationDAEGHLIYHVGDWLQ
CCCCCEEEECHHHHH
9.2330576142
167PhosphorylationQERYEIVSTLGEGTF
HHHHHHHHHHCCCCC
24.4722817900
332PhosphorylationVVDFGSATFDHEHHS
EEEECCCCCCCCCCC
31.1528348404
339PhosphorylationTFDHEHHSTIVSTRH
CCCCCCCCEEEEECC
23.0328348404
340PhosphorylationFDHEHHSTIVSTRHY
CCCCCCCEEEEECCC
22.5028348404
343PhosphorylationEHHSTIVSTRHYRAP
CCCCEEEEECCCCCC
18.8428348404
344PhosphorylationHHSTIVSTRHYRAPE
CCCEEEEECCCCCCH
15.5721082442
402PhosphorylationRILGPIPSRMIRKTR
HHHCCCCHHHHHHHC
34.89-
425PhosphorylationRLDWDENTSAGRYVR
CCCCCCCCCHHHHHH
20.2226657352
426PhosphorylationLDWDENTSAGRYVRE
CCCCCCCCHHHHHHH
40.0626657352
430PhosphorylationENTSAGRYVRENCKP
CCCCHHHHHHHHCHH
11.71-
469PhosphorylationYEPAKRLTLGEALQH
CCHHHCCCHHHHHCC
36.43-
493PhosphorylationPPNKLWDSSRDISR-
CCCCCCCCCCCCCC-
18.7217192257
498PhosphorylationWDSSRDISR------
CCCCCCCCC------
35.9125159151

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
34SPhosphorylationKinaseAKT1P31749
Uniprot
98SPhosphorylationKinaseCLK2P49760
GPS
127TPhosphorylationKinaseAKT1P31749
Uniprot
142SPhosphorylationKinaseCLK2P49760
GPS
344TPhosphorylationKinaseAKT2P31751
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
34SPhosphorylation

20682768
127TPhosphorylation

20682768
142SPhosphorylation

20682768
344TPhosphorylation

20682768

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 CLK2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CLK3_HUMANCLK3physical
16189514
FANCM_HUMANFANCMphysical
18995830
AKT1_HUMANAKT1physical
20682768
RU17_HUMANSNRNP70physical
21988832
PININ_HUMANPNNphysical
23602568
HNRPM_HUMANHNRNPMphysical
23602568
LUC7L_HUMANLUC7Lphysical
23602568
TNPO3_HUMANTNPO3physical
23602568
CLK2_HUMANCLK2physical
23602568
HUWE1_HUMANHUWE1physical
23602568
PSME3_HUMANPSME3physical
23602568
SK2L2_HUMANSKIV2L2physical
23602568
ZCHC8_HUMANZCCHC8physical
23602568
BCLF1_HUMANBCLAF1physical
23602568
CPSF1_HUMANCPSF1physical
23602568
FIP1_HUMANFIP1L1physical
23602568
RBBP6_HUMANRBBP6physical
23602568
WDR33_HUMANWDR33physical
23602568
PPHLN_HUMANPPHLN1physical
23602568
RBM7_HUMANRBM7physical
23602568
ACINU_HUMANACIN1physical
23602568
PABP1_HUMANPABPC1physical
23602568
SETD2_HUMANSETD2physical
23602568
PKP2_HUMANPKP2physical
23602568
TR150_HUMANTHRAP3physical
23602568
CPSF2_HUMANCPSF2physical
23602568
RBM39_HUMANRBM39physical
23602568
SON_HUMANSONphysical
23602568
ZNF30_HUMANZNF30physical
23602568
HNRPF_HUMANHNRNPFphysical
23602568
CPSF4_HUMANCPSF4physical
23602568
CDN2A_HUMANCDKN2Aphysical
23602568
ARF_HUMANCDKN2Aphysical
23602568
CLK2_HUMANCLK2physical
25416956
CLK3_HUMANCLK3physical
25416956
ECE1_HUMANECE1physical
25416956
TRI27_HUMANTRIM27physical
25416956
SDCB1_HUMANSDCBPphysical
25416956
SRPK2_HUMANSRPK2physical
25416956
U2AF1_HUMANU2AF1physical
25416956
UBC9_HUMANUBE2Iphysical
25416956
U2AFM_HUMANZRSR2physical
25416956
RBM39_HUMANRBM39physical
25416956
ZN263_HUMANZNF263physical
25416956
SRRM1_HUMANSRRM1physical
25416956
RNPS1_HUMANRNPS1physical
25416956
KLHL2_HUMANKLHL2physical
25416956
ZN473_HUMANZNF473physical
25416956
RM04_HUMANMRPL4physical
25416956
LUZP4_HUMANLUZP4physical
25416956
RSRP1_HUMANRSRP1physical
25416956
ZN398_HUMANZNF398physical
25416956
GMCL1_HUMANGMCL1physical
25416956
SNIP1_HUMANSNIP1physical
25416956
CPSF7_HUMANCPSF7physical
25416956
ZN394_HUMANZNF394physical
25416956
LNX1_HUMANLNX1physical
25416956
PR38A_HUMANPRPF38Aphysical
25416956
YTDC1_HUMANYTHDC1physical
25416956
BRCA1_HUMANBRCA1physical
25184681
CLK3_HUMANCLK3physical
21516116
SRPK2_HUMANSRPK2physical
21516116
SNIP1_HUMANSNIP1physical
21516116
RSRP1_HUMANRSRP1physical
28514442
NKTR_HUMANNKTRphysical
28514442
CLK1_HUMANCLK1physical
28514442
SETD2_HUMANSETD2physical
28514442
PPHLN_HUMANPPHLN1physical
28514442
RBBP6_HUMANRBBP6physical
28514442
RMXL1_HUMANRBMXL1physical
28514442
SRSF8_HUMANSRSF8physical
28514442
CLASR_HUMANCLASRPphysical
28514442
YTDC1_HUMANYTHDC1physical
28514442
GPTC8_HUMANGPATCH8physical
28514442
ZN638_HUMANZNF638physical
28514442
BCLF1_HUMANBCLAF1physical
28514442
ACINU_HUMANACIN1physical
28514442
SRS12_HUMANSRSF12physical
28514442
SRS10_HUMANSRSF10physical
28514442
NCOA5_HUMANNCOA5physical
28514442
NCBP3_HUMANC17orf85physical
28514442
WDR33_HUMANWDR33physical
28514442
GPAM1_HUMANGPALPP1physical
28514442
ZC3HE_HUMANZC3H14physical
28514442
TR150_HUMANTHRAP3physical
28514442
REPI1_HUMANREPIN1physical
28514442
SRRT_HUMANSRRTphysical
28514442
ZCHC8_HUMANZCCHC8physical
28514442
CASC3_HUMANCASC3physical
28514442
SRRM1_HUMANSRRM1physical
28514442
RNPS1_HUMANRNPS1physical
28514442
PRP4B_HUMANPRPF4Bphysical
28514442
PTN1_HUMANPTPN1physical
10480872
CLK2_HUMANCLK2physical
10480872
KC1D_RATCsnk1dphysical
17594292

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 CLK2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphorylation of CLK2 at serine 34 and threonine 127 by AKTcontrols cell survival after ionizing radiation.";
Nam S.Y., Seo H.H., Park H.S., An S., Kim J.Y., Yang K.H., Kim C.S.,Jeong M., Jin Y.W.;
J. Biol. Chem. 285:31157-31163(2010).
Cited for: PHOSPHORYLATION AT SER-34 AND THR-127, AND INTERACTION WITH AKT1.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-7; SER-50; SER-83;SER-106; SER-142; TYR-153; SER-167 AND SER-493, 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 SER-142, 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 TYR-51; SER-98; SER-142 ANDSER-493, AND MASS SPECTROMETRY.

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