dbPTM

CLK2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
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

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Phosphorylation	-MPHPRRYHSSERGS -CCCCCCCCCCCCCC	13.82	22817900
9	Phosphorylation	PHPRRYHSSERGSRG CCCCCCCCCCCCCCC	25.59	28102081
10	Phosphorylation	HPRRYHSSERGSRGS CCCCCCCCCCCCCCC	20.28	28102081
14	Phosphorylation	YHSSERGSRGSYREH CCCCCCCCCCCHHHH	39.42	28102081
17	Phosphorylation	SERGSRGSYREHYRS CCCCCCCCHHHHHHH	21.65	27251275
18	Phosphorylation	ERGSRGSYREHYRSR CCCCCCCHHHHHHHH	23.89	29449344
34	Phosphorylation	HKRRRSRSWSSSSDR HHHHHCCCCCCCCHH	32.34	22817900
36	Phosphorylation	RRRSRSWSSSSDRTR HHHCCCCCCCCHHHH	22.91	28102081
37	Phosphorylation	RRSRSWSSSSDRTRR HHCCCCCCCCHHHHH	27.83	28102081
38	Phosphorylation	RSRSWSSSSDRTRRR HCCCCCCCCHHHHHH	30.64	28102081
39	Phosphorylation	SRSWSSSSDRTRRRR CCCCCCCCHHHHHHH	32.81	28102081
42	Phosphorylation	WSSSSDRTRRRRRED CCCCCHHHHHHHHHC	33.25	28102081
50	Phosphorylation	RRRRREDSYHVRSRS HHHHHHCCCCCCCCC	16.63	23401153
51	Phosphorylation	RRRREDSYHVRSRSS HHHHHCCCCCCCCCC	19.36	30266825
55	Phosphorylation	EDSYHVRSRSSYDDR HCCCCCCCCCCCCCC	35.11	24144214
57	Phosphorylation	SYHVRSRSSYDDRSS CCCCCCCCCCCCCCC	34.20	30576142
58	Phosphorylation	YHVRSRSSYDDRSSD CCCCCCCCCCCCCCC	31.32	25884760
59	Phosphorylation	HVRSRSSYDDRSSDR CCCCCCCCCCCCCCC	24.10	17384208
63	Phosphorylation	RSSYDDRSSDRRVYD CCCCCCCCCCCCCCC	43.51	25884760
64	Phosphorylation	SSYDDRSSDRRVYDR CCCCCCCCCCCCCCH	35.71	30576142
69	Phosphorylation	RSSDRRVYDRRYCGS CCCCCCCCCHHCCCC	11.26	17384208
73	Phosphorylation	RRVYDRRYCGSYRRN CCCCCHHCCCCCCCC	11.32	22210691
76	Phosphorylation	YDRRYCGSYRRNDYS CCHHCCCCCCCCCCC	16.35	27251275
77	Phosphorylation	DRRYCGSYRRNDYSR CHHCCCCCCCCCCCC	10.01	29449344
82	Phosphorylation	GSYRRNDYSRDRGDA CCCCCCCCCCCCCCC	14.78	18691976
83	Phosphorylation	SYRRNDYSRDRGDAY CCCCCCCCCCCCCCC	30.48	29214152
90	Phosphorylation	SRDRGDAYYDTDYRH CCCCCCCCCCCCCCC	13.45	27080861
91	Phosphorylation	RDRGDAYYDTDYRHS CCCCCCCCCCCCCCC	17.68	27732954
93	Phosphorylation	RGDAYYDTDYRHSYE CCCCCCCCCCCCCHH	20.86	28985074
95	Phosphorylation	DAYYDTDYRHSYEYQ CCCCCCCCCCCHHHH	16.59	27794612
98	Phosphorylation	YDTDYRHSYEYQREN CCCCCCCCHHHHHHC	15.63	23401153
99	Phosphorylation	DTDYRHSYEYQRENS CCCCCCCHHHHHHCC	16.72	21406692
101	Phosphorylation	DYRHSYEYQRENSSY CCCCCHHHHHHCCCH	12.49	19835603
106	Phosphorylation	YEYQRENSSYRSQRS HHHHHHCCCHHCHHH	24.80	19369195
127	Phosphorylation	RRRRRSRTFSRSSSQ HHHHHHHHHCCCCHH	27.49	22817900
127 (in isoform 2)	Phosphorylation	-	27.49	22210691
129 (in isoform 2)	Phosphorylation	-	30.55	22210691
131 (in isoform 2)	Phosphorylation	-	32.89	22210691
132 (in isoform 2)	Phosphorylation	-	32.67	22210691
133 (in isoform 2)	Phosphorylation	-	32.91	22210691
133	Phosphorylation	RTFSRSSSQHSSRRA HHHCCCCHHHHHCCC	32.91	25954137
133 (in isoform 3)	Phosphorylation	-	32.91	-
135 (in isoform 3)	Phosphorylation	-	29.68	-
136	Phosphorylation	SRSSSQHSSRRAKSV CCCCHHHHHCCCCCC	20.22	25954137
136 (in isoform 3)	Phosphorylation	-	20.22	-
137	Phosphorylation	RSSSQHSSRRAKSVE CCCHHHHHCCCCCCC	24.54	25954137
141 (in isoform 3)	Phosphorylation	-	53.90	25849741
142	Phosphorylation	HSSRRAKSVEDDAEG HHHCCCCCCCCCCCC	29.74	23401153
153	Phosphorylation	DAEGHLIYHVGDWLQ CCCCCEEEECHHHHH	9.23	30576142
167	Phosphorylation	QERYEIVSTLGEGTF HHHHHHHHHHCCCCC	24.47	22817900
332	Phosphorylation	VVDFGSATFDHEHHS EEEECCCCCCCCCCC	31.15	28348404
339	Phosphorylation	TFDHEHHSTIVSTRH CCCCCCCCEEEEECC	23.03	28348404
340	Phosphorylation	FDHEHHSTIVSTRHY CCCCCCCEEEEECCC	22.50	28348404
343	Phosphorylation	EHHSTIVSTRHYRAP CCCCEEEEECCCCCC	18.84	28348404
344	Phosphorylation	HHSTIVSTRHYRAPE CCCEEEEECCCCCCH	15.57	21082442
402	Phosphorylation	RILGPIPSRMIRKTR HHHCCCCHHHHHHHC	34.89	-
425	Phosphorylation	RLDWDENTSAGRYVR CCCCCCCCCHHHHHH	20.22	26657352
426	Phosphorylation	LDWDENTSAGRYVRE CCCCCCCCHHHHHHH	40.06	26657352
430	Phosphorylation	ENTSAGRYVRENCKP CCCCHHHHHHHHCHH	11.71	-
469	Phosphorylation	YEPAKRLTLGEALQH CCHHHCCCHHHHHCC	36.43	-
493	Phosphorylation	PPNKLWDSSRDISR- CCCCCCCCCCCCCC-	18.72	17192257
498	Phosphorylation	WDSSRDISR------ CCCCCCCCC------	35.91	25159151

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
34	S	Phosphorylation	Kinase	AKT1	P31749	Uniprot
98	S	Phosphorylation	Kinase	CLK2	P49760	GPS
127	T	Phosphorylation	Kinase	AKT1	P31749	Uniprot
142	S	Phosphorylation	Kinase	CLK2	P49760	GPS
344	T	Phosphorylation	Kinase	AKT2	P31751	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
34	S	Phosphorylation	20682768
Phosphorylation on Ser-34 and Thr-127 by AKT1 is induced by ionizing radiation or insulin.
127	T	Phosphorylation	20682768
Phosphorylation on Ser-34 and Thr-127 by AKT1 is induced by ionizing radiation or insulin.
142	S	Phosphorylation	20682768
The phosphorylation status at Ser-142 influences its subnuclear localization; inhibition of phosphorylation at Ser-142 results in accumulation in the nuclear speckle.
344	T	Phosphorylation	20682768
Phosphorylation at Thr-344 by PKB/AKT2 induces its kinase activity which is required for its stability.

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
CLK3_HUMAN	CLK3	physical	16189514
FANCM_HUMAN	FANCM	physical	18995830
AKT1_HUMAN	AKT1	physical	20682768
RU17_HUMAN	SNRNP70	physical	21988832
PININ_HUMAN	PNN	physical	23602568
HNRPM_HUMAN	HNRNPM	physical	23602568
LUC7L_HUMAN	LUC7L	physical	23602568
TNPO3_HUMAN	TNPO3	physical	23602568
CLK2_HUMAN	CLK2	physical	23602568
HUWE1_HUMAN	HUWE1	physical	23602568
PSME3_HUMAN	PSME3	physical	23602568
SK2L2_HUMAN	SKIV2L2	physical	23602568
ZCHC8_HUMAN	ZCCHC8	physical	23602568
BCLF1_HUMAN	BCLAF1	physical	23602568
CPSF1_HUMAN	CPSF1	physical	23602568
FIP1_HUMAN	FIP1L1	physical	23602568
RBBP6_HUMAN	RBBP6	physical	23602568
WDR33_HUMAN	WDR33	physical	23602568
PPHLN_HUMAN	PPHLN1	physical	23602568
RBM7_HUMAN	RBM7	physical	23602568
ACINU_HUMAN	ACIN1	physical	23602568
PABP1_HUMAN	PABPC1	physical	23602568
SETD2_HUMAN	SETD2	physical	23602568
PKP2_HUMAN	PKP2	physical	23602568
TR150_HUMAN	THRAP3	physical	23602568
CPSF2_HUMAN	CPSF2	physical	23602568
RBM39_HUMAN	RBM39	physical	23602568
SON_HUMAN	SON	physical	23602568
ZNF30_HUMAN	ZNF30	physical	23602568
HNRPF_HUMAN	HNRNPF	physical	23602568
CPSF4_HUMAN	CPSF4	physical	23602568
CDN2A_HUMAN	CDKN2A	physical	23602568
ARF_HUMAN	CDKN2A	physical	23602568
CLK2_HUMAN	CLK2	physical	25416956
CLK3_HUMAN	CLK3	physical	25416956
ECE1_HUMAN	ECE1	physical	25416956
TRI27_HUMAN	TRIM27	physical	25416956
SDCB1_HUMAN	SDCBP	physical	25416956
SRPK2_HUMAN	SRPK2	physical	25416956
U2AF1_HUMAN	U2AF1	physical	25416956
UBC9_HUMAN	UBE2I	physical	25416956
U2AFM_HUMAN	ZRSR2	physical	25416956
RBM39_HUMAN	RBM39	physical	25416956
ZN263_HUMAN	ZNF263	physical	25416956
SRRM1_HUMAN	SRRM1	physical	25416956
RNPS1_HUMAN	RNPS1	physical	25416956
KLHL2_HUMAN	KLHL2	physical	25416956
ZN473_HUMAN	ZNF473	physical	25416956
RM04_HUMAN	MRPL4	physical	25416956
LUZP4_HUMAN	LUZP4	physical	25416956
RSRP1_HUMAN	RSRP1	physical	25416956
ZN398_HUMAN	ZNF398	physical	25416956
GMCL1_HUMAN	GMCL1	physical	25416956
SNIP1_HUMAN	SNIP1	physical	25416956
CPSF7_HUMAN	CPSF7	physical	25416956
ZN394_HUMAN	ZNF394	physical	25416956
LNX1_HUMAN	LNX1	physical	25416956
PR38A_HUMAN	PRPF38A	physical	25416956
YTDC1_HUMAN	YTHDC1	physical	25416956
BRCA1_HUMAN	BRCA1	physical	25184681
CLK3_HUMAN	CLK3	physical	21516116
SRPK2_HUMAN	SRPK2	physical	21516116
SNIP1_HUMAN	SNIP1	physical	21516116
RSRP1_HUMAN	RSRP1	physical	28514442
NKTR_HUMAN	NKTR	physical	28514442
CLK1_HUMAN	CLK1	physical	28514442
SETD2_HUMAN	SETD2	physical	28514442
PPHLN_HUMAN	PPHLN1	physical	28514442
RBBP6_HUMAN	RBBP6	physical	28514442
RMXL1_HUMAN	RBMXL1	physical	28514442
SRSF8_HUMAN	SRSF8	physical	28514442
CLASR_HUMAN	CLASRP	physical	28514442
YTDC1_HUMAN	YTHDC1	physical	28514442
GPTC8_HUMAN	GPATCH8	physical	28514442
ZN638_HUMAN	ZNF638	physical	28514442
BCLF1_HUMAN	BCLAF1	physical	28514442
ACINU_HUMAN	ACIN1	physical	28514442
SRS12_HUMAN	SRSF12	physical	28514442
SRS10_HUMAN	SRSF10	physical	28514442
NCOA5_HUMAN	NCOA5	physical	28514442
NCBP3_HUMAN	C17orf85	physical	28514442
WDR33_HUMAN	WDR33	physical	28514442
GPAM1_HUMAN	GPALPP1	physical	28514442
ZC3HE_HUMAN	ZC3H14	physical	28514442
TR150_HUMAN	THRAP3	physical	28514442
REPI1_HUMAN	REPIN1	physical	28514442
SRRT_HUMAN	SRRT	physical	28514442
ZCHC8_HUMAN	ZCCHC8	physical	28514442
CASC3_HUMAN	CASC3	physical	28514442
SRRM1_HUMAN	SRRM1	physical	28514442
RNPS1_HUMAN	RNPS1	physical	28514442
PRP4B_HUMAN	PRPF4B	physical	28514442
PTN1_HUMAN	PTPN1	physical	10480872
CLK2_HUMAN	CLK2	physical	10480872
KC1D_RAT	Csnk1d	physical	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

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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.	20682768 [Abstract]
"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.	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-142, AND MASSSPECTROMETRY.	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 TYR-51; SER-98; SER-142 ANDSER-493, AND MASS SPECTROMETRY.	18691976 [Abstract]

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