CLK1_HUMAN - dbPTM
CLK1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CLK1_HUMAN
UniProt AC P49759
Protein Name Dual specificity protein kinase CLK1
Gene Name CLK1
Organism Homo sapiens (Human).
Sequence Length 484
Subcellular Localization Nucleus.
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 and may be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing. Phosphorylates: SRSF1, SRSF3 and PTPN1. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells and adenovirus E1A pre-mRNA..
Protein Sequence MRHSKRTYCPDWDDKDWDYGKWRSSSSHKRRKRSHSSAQENKRCKYNHSKMCDSHYLESRSINEKDYHSRRYIDEYRNDYTQGCEPGHRQRDHESRYQNHSSKSSGRSGRSSYKSKHRIHHSTSHRRSHGKSHRRKRTRSVEDDEEGHLICQSGDVLSARYEIVDTLGEGAFGKVVECIDHKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTDPNSTFRCVQMLEWFEHHGHICIVFELLGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYTEAYNPKIKRDERTLINPDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMMERILGPLPKHMIQKTRKRKYFHHDRLDWDEHSSAGRYVSRRCKPLKEFMLSQDVEHERLFDLIQKMLEYDPAKRITLREALKHPFFDLLKKSI
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
15UbiquitinationYCPDWDDKDWDYGKW
CCCCCCCCCCCCCCC
59.2429967540
18 (in isoform 3)Phosphorylation-53.06-
21SumoylationDKDWDYGKWRSSSSH
CCCCCCCCCCCCCHH
32.95-
21UbiquitinationDKDWDYGKWRSSSSH
CCCCCCCCCCCCCHH
32.9529967540
21SumoylationDKDWDYGKWRSSSSH
CCCCCCCCCCCCCHH
32.95-
24PhosphorylationWDYGKWRSSSSHKRR
CCCCCCCCCCHHHHH
33.19-
34PhosphorylationSHKRRKRSHSSAQEN
HHHHHHCCCCHHHHH
30.6529514088
36PhosphorylationKRRKRSHSSAQENKR
HHHHCCCCHHHHHHH
28.7228985074
37 (in isoform 2)Phosphorylation-28.66-
37PhosphorylationRRKRSHSSAQENKRC
HHHCCCCHHHHHHHH
28.6617192257
50SumoylationRCKYNHSKMCDSHYL
HHCCCHHHHCCHHHH
35.68-
50UbiquitinationRCKYNHSKMCDSHYL
HHCCCHHHHCCHHHH
35.6829967540
50SumoylationRCKYNHSKMCDSHYL
HHCCCHHHHCCHHHH
35.68-
54PhosphorylationNHSKMCDSHYLESRS
CHHHHCCHHHHHCCC
14.7628555341
56PhosphorylationSKMCDSHYLESRSIN
HHHCCHHHHHCCCCC
19.00-
57UbiquitinationKMCDSHYLESRSINE
HHCCHHHHHCCCCCH
3.9429967540
59PhosphorylationCDSHYLESRSINEKD
CCHHHHHCCCCCHHH
28.8224247654
61 (in isoform 2)Phosphorylation-38.76-
61PhosphorylationSHYLESRSINEKDYH
HHHHHCCCCCHHHHH
38.7617192257
63UbiquitinationYLESRSINEKDYHSR
HHHCCCCCHHHHHHH
52.0629967540
65UbiquitinationESRSINEKDYHSRRY
HCCCCCHHHHHHHHH
60.1329967540
76PhosphorylationSRRYIDEYRNDYTQG
HHHHHHHHHCCCCCC
15.8029978859
80PhosphorylationIDEYRNDYTQGCEPG
HHHHHCCCCCCCCCC
12.4329978859
81PhosphorylationDEYRNDYTQGCEPGH
HHHHCCCCCCCCCCH
22.7325348954
92UbiquitinationEPGHRQRDHESRYQN
CCCHHHCCCHHHHCC
41.3829967540
98 (in isoform 3)Phosphorylation-39.8027642862
101PhosphorylationESRYQNHSSKSSGRS
HHHHCCCCCCCCCCC
47.19-
102PhosphorylationSRYQNHSSKSSGRSG
HHHCCCCCCCCCCCC
29.07-
103 (in isoform 3)Phosphorylation-52.2124719451
104PhosphorylationYQNHSSKSSGRSGRS
HCCCCCCCCCCCCCC
39.72-
107UbiquitinationHSSKSSGRSGRSSYK
CCCCCCCCCCCCCHH
37.5729967540
108PhosphorylationSSKSSGRSGRSSYKS
CCCCCCCCCCCCHHH
41.9226657352
122PhosphorylationSKHRIHHSTSHRRSH
HHCCCCCCHHHCCCC
19.9027732954
123PhosphorylationKHRIHHSTSHRRSHG
HCCCCCCHHHCCCCC
24.9727732954
124PhosphorylationHRIHHSTSHRRSHGK
CCCCCCHHHCCCCCC
20.2927732954
138PhosphorylationKSHRRKRTRSVEDDE
CCCCCCCCCCCCCCC
30.2630266825
140PhosphorylationHRRKRTRSVEDDEEG
CCCCCCCCCCCCCCC
29.2829255136
153PhosphorylationEGHLICQSGDVLSAR
CCEEEECCCCEEEEE
32.3329632367
158PhosphorylationCQSGDVLSARYEIVD
ECCCCEEEEEEEEEC
15.5620873877
174UbiquitinationLGEGAFGKVVECIDH
CCCCCCCEEEEEHHC
36.3329967540
180PhosphorylationGKVVECIDHKAGGRH
CEEEEEHHCCCCCCE
49.2233259812
180 (in isoform 3)Phosphorylation-49.2224719451
182 (in isoform 3)Phosphorylation-45.0024719451
182UbiquitinationVVECIDHKAGGRHVA
EEEEHHCCCCCCEEE
45.0029967540
191SumoylationGGRHVAVKIVKNVDR
CCCEEEEEECCCHHH
31.85-
191SumoylationGGRHVAVKIVKNVDR
CCCEEEEEECCCHHH
31.85-
191UbiquitinationGGRHVAVKIVKNVDR
CCCEEEEEECCCHHH
31.8529967540
216 (in isoform 3)Ubiquitination-48.67-
216UbiquitinationVLEHLNTTDPNSTFR
HHHHHCCCCCCCCCH
48.6729967540
220PhosphorylationLNTTDPNSTFRCVQM
HCCCCCCCCCHHHHH
34.0220071362
221PhosphorylationNTTDPNSTFRCVQML
CCCCCCCCCHHHHHH
23.0320071362
224UbiquitinationDPNSTFRCVQMLEWF
CCCCCCHHHHHHHHH
1.8629967540
233UbiquitinationQMLEWFEHHGHICIV
HHHHHHHHCCCEEEE
23.8229967540
285PhosphorylationFLHSNKLTHTDLKPE
CHHCCCCCCCCCCHH
25.0824719451
290UbiquitinationKLTHTDLKPENILFV
CCCCCCCCHHHEEEE
53.7729967540
299PhosphorylationENILFVQSDYTEAYN
HHEEEEECCCCHHHC
27.5524719451
302O-linked_GlycosylationLFVQSDYTEAYNPKI
EEEECCCCHHHCCCC
21.0930379171
305PhosphorylationQSDYTEAYNPKIKRD
ECCCCHHHCCCCCCC
26.2624719451
308UbiquitinationYTEAYNPKIKRDERT
CCHHHCCCCCCCCCC
58.1629967540
322SumoylationTLINPDIKVVDFGSA
CCCCCCCEEEEECCC
43.52-
327 (in isoform 3)Phosphorylation-16.3524719451
328PhosphorylationIKVVDFGSATYDDEH
CEEEEECCCCCCCCC
19.8929255136
330PhosphorylationVVDFGSATYDDEHHS
EEEECCCCCCCCCCC
29.2229255136
331PhosphorylationVDFGSATYDDEHHST
EEECCCCCCCCCCCC
22.5529255136
332UbiquitinationDFGSATYDDEHHSTL
EECCCCCCCCCCCCE
50.9329967540
337PhosphorylationTYDDEHHSTLVSTRH
CCCCCCCCCEEECCC
25.9130266825
338PhosphorylationYDDEHHSTLVSTRHY
CCCCCCCCEEECCCC
27.1630266825
341PhosphorylationEHHSTLVSTRHYRAP
CCCCCEEECCCCCCC
23.8829255136
341 (in isoform 3)Phosphorylation-23.8824719451
342PhosphorylationHHSTLVSTRHYRAPE
CCCCEEECCCCCCCH
17.6229255136
345PhosphorylationTLVSTRHYRAPEVIL
CEEECCCCCCCHHHH
12.7430576142
347 (in isoform 3)Phosphorylation-9.4624719451
350UbiquitinationRHYRAPEVILALGWS
CCCCCCHHHHHCCCC
4.1829967540
372 (in isoform 3)Phosphorylation-9.3024719451
400UbiquitinationRILGPLPKHMIQKTR
HHHCCCCHHHHHHHC
54.1929967540
442UbiquitinationPLKEFMLSQDVEHER
CHHHHCCCCCCCHHH
16.7329967540
464UbiquitinationMLEYDPAKRITLREA
HHCCCHHHCCCHHHH
50.1229967540
481UbiquitinationHPFFDLLKKSI----
CHHHHHHHHCC----
52.3429967540
506Ubiquitination-----------------------------
-----------------------------
29967540
506 (in isoform 3)Ubiquitination--
523Ubiquitination----------------------------------------------
----------------------------------------------
29967540

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

Oops, there are no upstream regulatory protein records of CLK1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CLK1_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 CLK1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BCLF1_HUMANBCLAF1physical
12890497
NCOR1_HUMANNCOR1physical
12890497
SRSF3_HUMANSRSF3physical
12890497
SAFB1_HUMANSAFBphysical
12890497
SRSF1_HUMANSRSF1physical
8798720
LC7L3_HUMANLUC7L3physical
12565863
SRSF1_HUMANSRSF1physical
12565863
PIAS4_HUMANPIAS4physical
15383276
ANM5_HUMANPRMT5physical
23455924
PDE9A_HUMANPDE9Aphysical
25416956
KR107_HUMANKRTAP10-7physical
25416956
PRP4B_HUMANPRPF4Bphysical
11418604
ABCAD_HUMANABCA13physical
26167880
ACOX2_HUMANACOX2physical
26167880
ANFY1_HUMANANKFY1physical
26167880
ARHGC_HUMANARHGEF12physical
26167880
ARPC4_HUMANARPC4physical
26167880
ARLY_HUMANASLphysical
26167880
ASXL3_HUMANASXL3physical
26167880
AT10A_HUMANATP10Aphysical
26167880
ATP4A_HUMANATP4Aphysical
26167880
CA094_HUMANC1orf94physical
26167880
CC067_HUMANC3orf67physical
26167880
ELP6_HUMANELP6physical
26167880
MTCL1_HUMANMTCL1physical
26167880
CDCP1_HUMANCDCP1physical
26167880
CAD23_HUMANCDH23physical
26167880
CDK12_HUMANCDK12physical
26167880
CELR3_HUMANCELSR3physical
26167880
CENPE_HUMANCENPEphysical
26167880
CEP95_HUMANCEP95physical
26167880
CKAP5_HUMANCKAP5physical
26167880
CLASR_HUMANCLASRPphysical
26167880
CLK1_HUMANCLK1physical
26167880
COCH_HUMANCOCHphysical
26167880
CRNL1_HUMANCRNKL1physical
26167880
CTND2_HUMANCTNND2physical
26167880
CUL3_HUMANCUL3physical
26167880
CWC27_HUMANCWC27physical
26167880
CP46A_HUMANCYP46A1physical
26167880
DBR1_HUMANDBR1physical
26167880
MYCPP_HUMANDENND4Aphysical
26167880
DJC13_HUMANDNAJC13physical
26167880
DJC24_HUMANDNAJC24physical
26167880
DPYD_HUMANDPYDphysical
26167880
DSC2_HUMANDSC2physical
26167880
ECE1_HUMANECE1physical
26167880
MICU3_HUMANMICU3physical
26167880
ENOA_HUMANENO1physical
26167880
ERFE_HUMANFAM132Bphysical
26167880
F16B2_HUMANFAM160B2physical
26167880
F1891_HUMANFAM189A1physical
26167880
FAT1_HUMANFAT1physical
26167880
FBF1_HUMANFBF1physical
26167880
GEMI5_HUMANGEMIN5physical
26167880
GRM6_HUMANGRM6physical
26167880
GSDMB_HUMANGSDMBphysical
26167880
HCDH_HUMANHADHphysical
26167880
H2B1K_HUMANHIST1H2BKphysical
26167880
ZEP1_HUMANHIVEP1physical
26167880
HNMT_HUMANHNMTphysical
26167880
ROA0_HUMANHNRNPA0physical
26167880
ROA1_HUMANHNRNPA1physical
26167880
ROA3_HUMANHNRNPA3physical
26167880
HRSL5_HUMANHRASLS5physical
26167880
HPBP1_HUMANHSPBP1physical
26167880
HTSF1_HUMANHTATSF1physical
26167880
IMDH2_HUMANIMPDH2physical
26167880
IP6K1_HUMANIP6K1physical
26167880
ITA5_HUMANITGA5physical
26167880
KTNA1_HUMANKATNA1physical
26167880
KHDR1_HUMANKHDRBS1physical
26167880
ICE1_HUMANICE1physical
26167880
KIF14_HUMANKIF14physical
26167880
KIF23_HUMANKIF23physical
26167880
K2C8_HUMANKRT8physical
26167880
LINES_HUMANLINSphysical
26167880
LMNA_HUMANLMNAphysical
26167880
MAP7_HUMANMAP7physical
26167880
MFS10_HUMANMFSD10physical
26167880
MKRN2_HUMANMKRN2physical
26167880
M3K21_HUMANKIAA1804physical
26167880
MTBP_HUMANMTBPphysical
26167880
MYOM1_HUMANMYOM1physical
26167880
NUCL_HUMANNCLphysical
26167880
NF1_HUMANNF1physical
26167880
NPM_HUMANNPM1physical
26167880
NU153_HUMANNUP153physical
26167880
PATZ1_HUMANPATZ1physical
26167880
PHF3_HUMANPHF3physical
26167880
PHLB2_HUMANPHLDB2physical
26167880
PI42B_HUMANPIP4K2Bphysical
26167880
PK1L1_HUMANPKD1L1physical
26167880
PXDC2_HUMANPLXDC2physical
26167880
LIPB2_HUMANPPFIBP2physical
26167880
PPHLN_HUMANPPHLN1physical
26167880
PPIG_HUMANPPIGphysical
26167880
PP1B_HUMANPPP1CBphysical
26167880
PRDX5_HUMANPRDX5physical
26167880
PRKDC_HUMANPRKDCphysical
26167880
PR38A_HUMANPRPF38Aphysical
26167880
PTN22_HUMANPTPN22physical
26167880
RD21L_HUMANRAD21L1physical
26167880
RAPH1_HUMANRAPH1physical
26167880
RASLC_HUMANRASL12physical
26167880
RBBP6_HUMANRBBP6physical
26167880
RBM15_HUMANRBM15physical
26167880
RBM39_HUMANRBM39physical
26167880
RBMX_HUMANRBMXphysical
26167880
REV1_HUMANREV1physical
26167880
RLF_HUMANRLFphysical
26167880
RL5_HUMANRPL5physical
26167880
RS4Y1_HUMANRPS4Y1physical
26167880
RUSD3_HUMANRPUSD3physical
26167880
SAM9L_HUMANSAMD9Lphysical
26167880
SCAR3_HUMANSCARA3physical
26167880
SPI2_HUMANSERPINI2physical
26167880
SF3B1_HUMANSF3B1physical
26167880
SMBT2_HUMANSFMBT2physical
26167880
SRSF5_HUMANSRSF5physical
26167880
SRSF6_HUMANSRSF6physical
26167880
SRSF7_HUMANSRSF7physical
26167880
SHRM1_HUMANSHROOM1physical
26167880
S35D3_HUMANSLC35D3physical
26167880
SLFN5_HUMANSLFN5physical
26167880
MINT_HUMANSPENphysical
26167880
SPTN4_HUMANSPTBN4physical
26167880
SRRM1_HUMANSRRM1physical
26167880
SRRM2_HUMANSRRM2physical
26167880
SSBP3_HUMANSSBP3physical
26167880
STIP1_HUMANSTIP1physical
26167880
STK31_HUMANSTK31physical
26167880
SVOP_HUMANSVOPphysical
26167880
TEX11_HUMANTEX11physical
26167880
TR150_HUMANTHRAP3physical
26167880
THY1_HUMANTHY1physical
26167880
ZO2_HUMANTJP2physical
26167880
TLN2_HUMANTLN2physical
26167880
LAP2A_HUMANTMPOphysical
26167880
LAP2B_HUMANTMPOphysical
26167880
TMPS2_HUMANTMPRSS2physical
26167880
TNIP2_HUMANTNIP2physical
26167880
PRPK_HUMANTP53RKphysical
26167880
TRA2A_HUMANTRA2Aphysical
26167880
TRA2B_HUMANTRA2Bphysical
26167880
UN13B_HUMANUNC13Bphysical
26167880
VWA7_HUMANVWA7physical
26167880
CF251_HUMANWDR66physical
26167880
YTDC1_HUMANYTHDC1physical
26167880
ZC3HD_HUMANZC3H13physical
26167880
ZCH18_HUMANZC3H18physical
26167880
ZMY10_HUMANZMYND10physical
26167880
ZN148_HUMANZNF148physical
26167880

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 CLK1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 SER-61; THR-138; SER-140;THR-330; THR-338 AND SER-341, 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 THR-138 AND SER-140, ANDMASS 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 SER-37; SER-61; THR-138;SER-140; SER-341 AND THR-342, AND MASS SPECTROMETRY.
"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 THR-138 AND SER-140, ANDMASS SPECTROMETRY.

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