Sequence of DYRK2_HUMAN
EC Number:2.7.12.1
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate
Other sequences found for EC No. 2.7.12.1
General information:
Sequence
0 MLTRKPSAAA PAAYPTGRGG DSAVRQLQAS PGLGAGATRS GVGTGPPSPI ALPPLRASNA
60 AAAAHTIGGS KHTMNDHLHV GSHAHGQIQV QQLFEDNSNK RTVLTTQPNG LTTVGKTGLP
120 VVPERQLDSI HRRQGSSTSL KSMEGMGKVK ATPMTPEQAM KQYMQKLTAF EHHEIFSYPE
180 IYFLGLNAKK RQGMTGGPNN GGYDDDQGSY VQVPHDHVAY RYEVLKVIGK GSFGQVVKAY
240 DHKVHQHVAL KMVRNEKRFH RQAAEEIRIL EHLRKQDKDN TMNVIHMLEN FTFRNHICMT
300 FELLSMNLYE LIKKNKFQGF SLPLVRKFAH SILQCLDALH KNRIIHCDLK PENILLKQQG
360 RSGIKVIDFG SSCYEHQRVY TYIQSRFYRA PEVILGARYG MPIDMWSLGC ILAELLTGYP
420 LLPGEDEGDQ LACMIELLGM PSQKLLDASK RAKNFVSSKG YPRYCTVTTL SDGSVVLNGG
480 RSRRGKLRGP PESREWGNAL KGCDDPLFLD FLKQCLEWDP AVRMTPGQAL RHPWLRRRLP
540 KPPTGEKTSV KRITESTGAI TSISKLPPPS SSASKLRTNL AQMTDANGNI QQRTVLPKLV
600 S
Download this sequence
in fasta formatDownload all sequences for 2.7.12.1
in fasta format
in csv (Excel, OpenOffice) formatSequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
155726
Becker W.,Weber Y.,Wetzel K.,Eirmbter K.,Tejedor F.J.,Joost H.-G.
Sequence characteristics, subcellular localization, and substrate specificity of DYRK-related kinases, a novel family of dual specificity protein kinases.
J. Biol. Chem.
273
25893-25902
1998
155727
Ota T.,Suzuki Y.,Nishikawa T.,Otsuki T.,Sugiyama T.,Irie R.,Wakamatsu A.,Hayashi K.,Sato H.,Nagai K.,Kimura K.,Makita H.,Sekine M.,Obayashi M.,Nishi T.,Shibahara T.,Tanaka T.,Ishii S.,Yamamoto J.,Saito K.,Kawai Y.,Isono Y.,Nakamura Y.,Nagahari K.,Murakami K.,Yasuda T.,Iwayanagi T.,Wagatsuma M.,Shiratori A.,Sudo H.,Hosoiri T.,Kaku Y.,Kodaira H.,Kondo H.,Sugawara M.,Takahashi M.,Kanda K.,Yokoi T.,Furuya T.,Kikkawa E.,Omura Y.,Abe K.,Kamihara K.,Katsuta N.,Sato K.,Tanikawa M.,Yamazaki M.,Ninomiya K.,Ishibashi T.,Yamashita H.,Murakawa K.,Fujimori K.,Tanai H.,Kimata M.,Watanabe M.,Hiraoka S.,Chiba Y.,Ishida S.,Ono Y.,Takiguchi S.,Watanabe S.,Yosida M.,Hotuta T.,Kusano J.,Kanehori K.,Takahashi-Fujii A.,Hara H.,Tanase T.-O.,Nomura Y.,Togiya S.,Komai F.,Hara R.,Takeuchi K.,Arita M.,Imose N.,Musashino K.,Yuuki H.,Oshima A.,Sasaki N.,Aotsuka S.,Yoshikawa Y.,Matsunawa H.,Ichihara T.,Shiohata N.,Sano S.,Moriya S.,Momiyama H.,Satoh N.,Takami S.,Terashima Y.,Suzuki O.,Nakagawa S.,Senoh A.,Mizoguchi H.,Goto Y.,Shimizu F.,Wakebe H.,Hishigaki H.,Watanabe T.,Sugiyama A.,Takemoto M.,Kawakami B.,Yamazaki M.,Watanabe K.,Kumagai A.,Itakura S.,Fukuzumi Y.,Fujimori Y.,Komiyama M.,Tashiro H.,Tanigami A.,Fujiwara T.,Ono T.,Yamada K.,Fujii Y.,Ozaki K.,Hirao M.,Ohmori Y.,Kawabata A.,Hikiji T.,Kobatake N.,Inagaki H.,Ikema Y.,Okamoto S.,Okitani R.,Kawakami T.,Noguchi S.,Itoh T.,Shigeta K.,Senba T.,Matsumura K.,Nakajima Y.,Mizuno T.,Morinaga M.,Sasaki M.,Togashi T.,Oyama M.,Hata H.,Watanabe M.,Komatsu T.,Mizushima-Sugano J.,Satoh T.,Shirai Y.,Takahashi Y.,Nakagawa K.,Okumura K.,Nagase T.,Nomura N.,Kikuchi H.,Masuho Y.,Yamashita R.,Nakai K.,Yada T.,Nakamura Y.,Ohara O.,Isogai T.,Sugano S.
Complete sequencing and characterization of 21,243 full-length human cDNAs.
Nat. Genet.
36
40-45
2004
155729
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
155731
Woods Y.L.,Cohen P.,Becker W.,Jakes R.,Goedert M.,Wang X.,Proud C.G.
The kinase DYRK phosphorylates protein-synthesis initiation factor eIF2Bepsilon at Ser539 and the microtubule-associated protein tau at Thr212: potential role for DYRK as a glycogen synthase kinase 3-priming kinase.
Biochem. J.
355
609-615
2001
155732
Miller C.T.,Aggarwal S.,Lin T.K.,Dagenais S.L.,Contreras J.I.,Orringer M.B.,Glover T.W.,Beer D.G.,Lin L.
Amplification and overexpression of the dual-specificity tyrosine-(Y)-phosphorylation regulated kinase 2 (DYRK2) gene in esophageal and lung adenocarcinomas.
Cancer Res.
63
4136-4143
2003
155733
Wang X.,Li W.,Parra J.L.,Beugnet A.,Proud C.G.
The C terminus of initiation factor 4E-binding protein 1 contains multiple regulatory features that influence its function and phosphorylation.
Mol. Cell. Biol.
23
1546-1557
2003
155734
Skurat A.V.,Dietrich A.D.
Phosphorylation of Ser640 in muscle glycogen synthase by DYRK family protein kinases.
J. Biol. Chem.
279
2490-2498
2004
155735
de Graaf K.,Hekerman P.,Spelten O.,Herrmann A.,Packman L.C.,Bussow K.,Muller-Newen G.,Becker W.
Characterization of cyclin L2, a novel cyclin with an arginine/serine-rich domain: phosphorylation by DYRK1A and colocalization with splicing factors.
J. Biol. Chem.
279
4612-4624
2004
155736
Auld G.C.,Campbell D.G.,Morrice N.,Cohen P.
Identification of calcium-regulated heat-stable protein of 24 kDa (CRHSP24) as a physiological substrate for PKB and RSK using KESTREL.
Biochem. J.
389
775-783
2005
155737
Cole A.R.,Causeret F.,Yadirgi G.,Hastie C.J.,McLauchlan H.,McManus E.J.,Hernandez F.,Eickholt B.J.,Nikolic M.,Sutherland C.
Distinct priming kinases contribute to differential regulation of collapsin response mediator proteins by glycogen synthase kinase-3 in vivo.
J. Biol. Chem.
281
16591-16598
2006
155738
Gwack Y.,Sharma S.,Nardone J.,Tanasa B.,Iuga A.,Srikanth S.,Okamura H.,Bolton D.,Feske S.,Hogan P.G.,Rao A.
A genome-wide Drosophila RNAi screen identifies DYRK-family kinases as regulators of NFAT.
Nature
441
646-650
2006
155739
Taira N.,Nihira K.,Yamaguchi T.,Miki Y.,Yoshida K.
DYRK2 is targeted to the nucleus and controls p53 via Ser46 phosphorylation in the apoptotic response to DNA damage.
Mol. Cell
25
725-738
2007
155740
Yoshida K.
Role for DYRK family kinases on regulation of apoptosis.
Biochem. Pharmacol.
76
1389-1394
2008
155741
Varjosalo M.,Bjorklund M.,Cheng F.,Syvanen H.,Kivioja T.,Kilpinen S.,Sun Z.,Kallioniemi O.,Stunnenberg H.G.,He W.W.,Ojala P.,Taipale J.
Application of active and kinase-deficient kinome collection for identification of kinases regulating hedgehog signaling.
Cell
133
537-548
2008
155742
Yoshida K.
Nuclear trafficking of pro-apoptotic kinases in response to DNA damage.
Trends Mol. Med.
14
305-313
2008
155743
Goeckler N.,Jofre G.,Papadopoulos C.,Soppa U.,Tejedor F.J.,Becker W.
Harmine specifically inhibits protein kinase DYRK1A and interferes with neurite formation.
FEBS J.
276
6324-6337
2009
155744
Maddika S.,Chen J.
Protein kinase DYRK2 is a scaffold that facilitates assembly of an E3 ligase.
Nat. Cell Biol.
11
409-419
2009
155745
Cuny G.D.,Robin M.,Ulyanova N.P.,Patnaik D.,Pique V.,Casano G.,Liu J.-F.,Lin X.,Xian J.,Glicksman M.A.,Stein R.L.,Higgins J.M.G.
Structure-activity relationship study of acridine analogs as haspin and DYRK2 kinase inhibitors.
Bioorg. Med. Chem. Lett.
20
3491-3494
2010
155746
Taira N.,Yamamoto H.,Yamaguchi T.,Miki Y.,Yoshida K.
ATM augments nuclear stabilization of DYRK2 by inhibiting MDM2 in the apoptotic response to DNA damage.
J. Biol. Chem.
285
4909-4919
2010
155747
Taira N.,Mimoto R.,Kurata M.,Yamaguchi T.,Kitagawa M.,Miki Y.,Yoshida K.
DYRK2 priming phosphorylation of c-Jun and c-Myc modulates cell cycle progression in human cancer cells.
J. Clin. Invest.
122
859-872
2012
155748
Perez M.,Garcia-Limones C.,Zapico I.,Marina A.,Schmitz M.L.,Munoz E.,Calzado M.A.
Mutual regulation between SIAH2 and DYRK2 controls hypoxic and genotoxic signaling pathways.
J. Mol. Cell Biol.
4
316-330
2012
155749
Jung H.Y.,Wang X.,Jun S.,Park J.I.
Dyrk2-associated EDD-DDB1-VprBP E3 ligase inhibits telomerase by TERT degradation.
J. Biol. Chem.
288
7252-7262
2013
155750
Zhou H.,Di Palma S.,Preisinger C.,Peng M.,Polat A.N.,Heck A.J.,Mohammed S.
Toward a comprehensive characterization of a human cancer cell phosphoproteome.
J. Proteome Res.
12
260-271
2013
155752
Tahtouh T.,Elkins J.M.,Filippakopoulos P.,Soundararajan M.,Burgy G.,Durieu E.,Cochet C.,Schmid R.S.,Lo D.C.,Delhommel F.,Oberholzer A.E.,Pearl L.H.,Carreaux F.,Bazureau J.P.,Knapp S.,Meijer L.
Selectivity, cocrystal structures, and neuroprotective properties of leucettines, a family of protein kinase inhibitors derived from the marine sponge alkaloid leucettamine B.
J. Med. Chem.
55
9312-9330
2012
155753
Soundararajan M.,Roos A.K.,Savitsky P.,Filippakopoulos P.,Kettenbach A.N.,Olsen J.V.,Gerber S.A.,Eswaran J.,Knapp S.,Elkins J.M.
Structures of Down syndrome kinases, DYRKs, reveal mechanisms of kinase activation and substrate recognition.
Structure
21
986-996
2013
155754
Greenman C.,Stephens P.,Smith R.,Dalgliesh G.L.,Hunter C.,Bignell G.,Davies H.,Teague J.,Butler A.,Stevens C.,Edkins S.,O'Meara S.,Vastrik I.,Schmidt E.E.,Avis T.,Barthorpe S.,Bhamra G.,Buck G.,Choudhury B.,Clements J.,Cole J.,Dicks E.,Forbes S.,Gray K.,Halliday K.,Harrison R.,Hills K.,Hinton J.,Jenkinson A.,Jones D.,Menzies A.,Mironenko T.,Perry J.,Raine K.,Richardson D.,Shepherd R.,Small A.,Tofts C.,Varian J.,Webb T.,West S.,Widaa S.,Yates A.,Cahill D.P.,Louis D.N.,Goldstraw P.,Nicholson A.G.,Brasseur F.,Looijenga L.,Weber B.L.,Chiew Y.-E.,DeFazio A.,Greaves M.F.,Green A.R.,Campbell P.,Birney E.,Easton D.F.,Chenevix-Trench G.,Tan M.-H.,Khoo S.K.,Teh B.T.,Yuen S.T.,Leung S.Y.,Wooster R.,Futreal P.A.,Stratton M.R.
Patterns of somatic mutation in human cancer genomes.
Nature
446
153-158
2007
