UniProt ID | CLK2_HUMAN | |
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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. |
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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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
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 |
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 |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
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Oops, there are no SNP-PTM records of CLK2_HUMAN !! |
Kegg Disease | ||||||
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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. |
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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. | |
"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. |