dbPTM

CLK4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CLK4_HUMAN
UniProt AC	Q9HAZ1
Protein Name	Dual specificity protein kinase CLK4
Gene Name	CLK4
Organism	Homo sapiens (Human).
Sequence Length	481
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 and SRSF3. Required for the regulation of alternative splicing of MAPT/TAU. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells..
Protein Sequence	MRHSKRTHCPDWDSRESWGHESYRGSHKRKRRSHSSTQENRHCKPHHQFKESDCHYLEARSLNERDYRDRRYVDEYRNDYCEGYVPRHYHRDIESGYRIHCSKSSVRSRRSSPKRKRNRHCSSHQSRSKSHRRKRSRSIEDDEEGHLICQSGDVLRARYEIVDTLGEGAFGKVVECIDHGMDGMHVAVKIVKNVGRYREAARSEIQVLEHLNSTDPNSVFRCVQMLEWFDHHGHVCIVFELLGLSTYDFIKENSFLPFQIDHIRQMAYQICQSINFLHHNKLTHTDLKPENILFVKSDYVVKYNSKMKRDERTLKNTDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFQTHDSKEHLAMMERILGPIPQHMIQKTRKRKYFHHNQLDWDEHSSAGRYVRRRCKPLKEFMLCHDEEHEKLFDLVRRMLEYDPTQRITLDEALQHPFFDLLKKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MRHSKRTHCPD ----CCCCCCCCCCC	17.30	30576142
7	Phosphorylation	-MRHSKRTHCPDWDS -CCCCCCCCCCCCCC	31.41	30576142
14	Phosphorylation	THCPDWDSRESWGHE CCCCCCCCCCCCCCC	33.42	23927012
17	Phosphorylation	PDWDSRESWGHESYR CCCCCCCCCCCCCCC	36.93	23927012
22	Phosphorylation	RESWGHESYRGSHKR CCCCCCCCCCCCCCC	17.92	23927012
33	Phosphorylation	SHKRKRRSHSSTQEN CCCCCCCCCCCCHHC	31.58	30576142
35	Phosphorylation	KRKRRSHSSTQENRH CCCCCCCCCCHHCCC	36.01	30576142
36	Phosphorylation	RKRRSHSSTQENRHC CCCCCCCCCHHCCCC	28.78	30576142
37	Phosphorylation	KRRSHSSTQENRHCK CCCCCCCCHHCCCCC	42.81	30576142
72	Phosphorylation	RDYRDRRYVDEYRND CHHHCHHHHHHHHCC	17.10	27642862
76	Phosphorylation	DRRYVDEYRNDYCEG CHHHHHHHHCCCCCC	15.39	27642862
80	Phosphorylation	VDEYRNDYCEGYVPR HHHHHCCCCCCCCCC	8.92	29978859
95	Phosphorylation	HYHRDIESGYRIHCS CCCCCCCCCCEEEEC	41.27	27251275
102	Phosphorylation	SGYRIHCSKSSVRSR CCCEEEECHHHHHCC	22.78	27732954
104	Phosphorylation	YRIHCSKSSVRSRRS CEEEECHHHHHCCCC	20.12	27732954
105	Phosphorylation	RIHCSKSSVRSRRSS EEEECHHHHHCCCCC	25.86	24719451
108	Phosphorylation	CSKSSVRSRRSSPKR ECHHHHHCCCCCCCH	29.86	30576142
111	Phosphorylation	SSVRSRRSSPKRKRN HHHHCCCCCCCHHHC	50.29	30576142
112	Phosphorylation	SVRSRRSSPKRKRNR HHHCCCCCCCHHHCC	32.40	30576142
122	Phosphorylation	RKRNRHCSSHQSRSK HHHCCCCCCHHHHCH	25.40	-
123	Phosphorylation	KRNRHCSSHQSRSKS HHCCCCCCHHHHCHH	30.82	-
126	Phosphorylation	RHCSSHQSRSKSHRR CCCCCHHHHCHHHHH	32.85	-
128	Phosphorylation	CSSHQSRSKSHRRKR CCCHHHHCHHHHHHH	43.70	-
136	Phosphorylation	KSHRRKRSRSIEDDE HHHHHHHCCCCCCCC	33.15	23927012
138	Phosphorylation	HRRKRSRSIEDDEEG HHHHHCCCCCCCCCC	31.41	22167270
151	Phosphorylation	EGHLICQSGDVLRAR CCEEEECCCCHHHHE	32.33	33259812
189	Sumoylation	DGMHVAVKIVKNVGR CCHHHHHHHHHHHHH	31.85	-
189	Ubiquitination	DGMHVAVKIVKNVGR CCHHHHHHHHHHHHH	31.85	-
189	Sumoylation	DGMHVAVKIVKNVGR CCHHHHHHHHHHHHH	31.85	-
296	Ubiquitination	PENILFVKSDYVVKY HHHEEEECCCEEEEC	30.21	29967540
302	Ubiquitination	VKSDYVVKYNSKMKR ECCCEEEECCCCCCC	28.77	29967540
315	Ubiquitination	KRDERTLKNTDIKVV CCCCCHHCCCCEEEE	58.13	29967540
326	Phosphorylation	IKVVDFGSATYDDEH EEEEEECCCCCCCCC	19.89	29255136
328	Phosphorylation	VVDFGSATYDDEHHS EEEECCCCCCCCCCC	29.22	29255136
329	Phosphorylation	VDFGSATYDDEHHST EEECCCCCCCCCCCE	22.55	29255136
335	Phosphorylation	TYDDEHHSTLVSTRH CCCCCCCCEEEECCC	25.91	30266825
336	Phosphorylation	YDDEHHSTLVSTRHY CCCCCCCEEEECCCC	27.16	30266825
339	Phosphorylation	EHHSTLVSTRHYRAP CCCCEEEECCCCCCC	23.88	29255136
340	Phosphorylation	HHSTLVSTRHYRAPE CCCEEEECCCCCCCH	17.62	23401153
343	Phosphorylation	TLVSTRHYRAPEVIL EEEECCCCCCCHHHH	12.74	30576142
479	Ubiquitination	HPFFDLLKKK----- CHHHHHHHCC-----	66.85	-

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 CLK4_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CLK4_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 CLK4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CLASR_HUMAN	CLASRP	physical	12169693
RN181_HUMAN	RNF181	physical	21988832
SRRM2_HUMAN	SRRM2	physical	23602568
SAHH3_HUMAN	AHCYL2	physical	23602568
RASL2_HUMAN	RASA4	physical	23602568
TCP4_HUMAN	SUB1	physical	23602568
KR107_HUMAN	KRTAP10-7	physical	25416956
KR109_HUMAN	KRTAP10-9	physical	25416956
KR108_HUMAN	KRTAP10-8	physical	25416956
KR103_HUMAN	KRTAP10-3	physical	25416956

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 CLK4_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-136 AND SER-138, ANDMASS SPECTROMETRY.	19369195 [Abstract]
"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-136 AND SER-138, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"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-136 AND SER-138, ANDMASS SPECTROMETRY.	18691976 [Abstract]
"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 SER-138, AND MASSSPECTROMETRY.	17081983 [Abstract]