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Q92630

- DYRK2_HUMAN

UniProt

Q92630 - DYRK2_HUMAN

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Protein

Dual specificity tyrosine-phosphorylation-regulated kinase 2

Gene

DYRK2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Serine/threonine-protein kinase involved in the regulation of the mitotic cell cycle, cell proliferation, apoptosis, organization of the cytoskeleton and neurite outgrowth. Functions in part via its role in ubiquitin-dependent proteasomal protein degradation. Functions downstream of ATM and phosphorylates p53/TP53 at 'Ser-46', and thereby contributes to the induction of apoptosis in response to DNA damage. Phosphorylates NFATC1, and thereby inhibits its accumulation in the nucleus and its transcription factor activity. Phosphorylates EIF2B5 at 'Ser-544', enabling its subsequent phosphorylation and inhibition by GSK3B. Likewise, phosphorylation of NFATC1, CRMP2/DPYSL2 and CRMP4/DPYSL3 promotes their subsequent phosphorylation by GSK3B. May play a general role in the priming of GSK3 substrates. Inactivates GYS1 by phosphorylation at 'Ser-641', and potentially also a second phosphorylation site, thus regulating glycogen synthesis. Mediates EDVP E3 ligase complex formation and is required for the phosphorylation and subsequent degradation of KATNA1. Phosphorylates TERT at 'Ser-457', promoting TERT ubiquitination by the EDVP complex. Phosphorylates SIAH2, and thereby increases its ubiquitin ligase activity. Promotes the proteasomal degradation of MYC and JUN, and thereby regulates progress through the mitotic cell cycle and cell proliferation. Promotes proteasomal degradation of GLI2 and GLI3, and thereby plays a role in smoothened and sonic hedgehog signaling. Plays a role in cytoskeleton organization and neurite outgrowth via its phosphorylation of DCX and DPYSL2. Phosphorylates CRMP2/DPYSL2, CRMP4/DPYSL3, DCX, EIF2B5, EIF4EBP1, GLI2, GLI3, GYS1, JUN, MDM2, MYC, NFATC1, p53/TP53, TAU/MAPT and KATNA1. Can phosphorylate histone H1, histone H3 and histone H2B (in vitro). Can phosphorylate CARHSP1 (in vitro).14 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Cofactori

Magnesium.1 Publication
Manganese.1 Publication

Enzyme regulationi

Activated by autophosphorylation on the second tyrosine residue in the Tyr-X-Tyr motif in the activation loop. Inhibited by acridine analogs, purvalanol, and barely by harmine. Inhibited by leucettine and leucettine derivatives.4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei251 – 2511ATPCurated
Active sitei348 – 3481Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi228 – 2369ATPCurated
Nucleotide bindingi301 – 3044ATPCurated

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. magnesium ion binding Source: UniProtKB
  3. manganese ion binding Source: UniProtKB
  4. protein serine/threonine/tyrosine kinase activity Source: UniProtKB-EC
  5. protein serine/threonine kinase activity Source: UniProtKB
  6. protein tyrosine kinase activity Source: UniProtKB
  7. ubiquitin binding Source: UniProtKB

GO - Biological processi

  1. cellular response to DNA damage stimulus Source: UniProtKB
  2. intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: UniProtKB
  3. negative regulation of NFAT protein import into nucleus Source: UniProtKB
  4. peptidyl-tyrosine phosphorylation Source: GOC
  5. positive regulation of glycogen biosynthetic process Source: UniProtKB
  6. protein phosphorylation Source: UniProtKB
  7. smoothened signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Apoptosis, Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Magnesium, Manganese, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.12.1. 2681.
SignaLinkiQ92630.

Names & Taxonomyi

Protein namesi
Recommended name:
Dual specificity tyrosine-phosphorylation-regulated kinase 2 (EC:2.7.12.1)
Gene namesi
Name:DYRK2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:3093. DYRK2.

Subcellular locationi

Cytoplasm. Nucleus
Note: Translocates into the nucleus following DNA damage.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: UniProtKB
  3. ribonucleoprotein complex Source: Ensembl
  4. ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi106 – 1061T → A: Impaired ATM-mediated phosphorylation, reduced affinity with MDM2 and altered MDM2-triggered ubiquitination. 1 Publication
Mutagenesisi189 – 1913KKR → NNN: Impaired nuclear translocation. 1 Publication
Mutagenesisi251 – 2511K → R: Abolishes protein serine/threonine kinase activity. 1 Publication
Mutagenesisi442 – 4421S → A: Impaired ATM-mediated phosphorylation, reduced affinity with MDM2 and altered MDM2-triggered ubiquitination. 1 Publication

Organism-specific databases

PharmGKBiPA27550.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 601601Dual specificity tyrosine-phosphorylation-regulated kinase 2PRO_0000085936Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei106 – 1061Phosphothreonine; by ATM1 Publication
Modified residuei381 – 3811Phosphothreonine; by MAP3K101 Publication
Modified residuei382 – 3821Phosphotyrosine; by autocatalysis1 Publication
Modified residuei442 – 4421Phosphoserine; by ATM1 Publication
Modified residuei449 – 4491Phosphoserine; by MAP3K101 Publication

Post-translational modificationi

Autophosphorylates cotranslationally on the second tyrosine residue in the Tyr-X-Tyr motif in the activation loop, but once mature, does not have any protein tyrosine kinase activity. Phosphorylated at Thr-106 and Ser-442 by ATM in response to genotoxic stress.1 Publication
Under normal conditions, polyubiquitinated in the nucleus by MDM2, leading to its proteasomal degradation. Phosphorylation on Thr-106 and Ser-442 by ATM in response to genotoxic stress disrupts MDM2 binding and prevents MDM2-mediated ubiquitination and subsequent proteasomal degradation. Polyubiquitinated by SIAH2, leading to its proteasomal degradation. Polyubiquitinated by SIAH2 occurs under normal conditions, and is enhanced in response to hypoxia.2 Publications

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ92630.
PRIDEiQ92630.

PTM databases

PhosphoSiteiQ92630.

Expressioni

Tissue specificityi

Testis, after the onset of spermatogenesis.1 Publication

Inductioni

Accumulates in nucleus upon DNA damage. Induced in both esophageal and lung adenocarcinomas.2 Publications

Gene expression databases

BgeeiQ92630.
CleanExiHS_DYRK2.
ExpressionAtlasiQ92630. baseline and differential.
GenevestigatoriQ92630.

Organism-specific databases

HPAiHPA027230.
HPA056902.

Interactioni

Subunit structurei

Component of an E3 ligase complex containing DYRK2, EDD/UBR5, DDB1 and VPRBP (EDVP complex). Interacts directly with EDD/UBR5, DDB1 and VPRBP. Interacts with SIAH2 and MDM2. Interacts with MAP3K10 and NFATC1. May also interact with CCNL2.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DYRK4Q9NR203EBI-749432,EBI-3914009

Protein-protein interaction databases

BioGridi114023. 45 interactions.
IntActiQ92630. 5 interactions.
MINTiMINT-1469581.
STRINGi9606.ENSP00000342105.

Structurei

Secondary structure

1
601
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi149 – 1524
Helixi156 – 1638
Helixi164 – 1663
Helixi169 – 1746
Helixi175 – 1773
Beta strandi179 – 1813
Helixi198 – 2014
Beta strandi206 – 2083
Turni219 – 2213
Beta strandi222 – 24120
Turni242 – 2454
Beta strandi246 – 2538
Helixi257 – 27418
Beta strandi287 – 2937
Beta strandi296 – 3016
Helixi308 – 3147
Turni315 – 3173
Helixi322 – 34221
Helixi351 – 3533
Beta strandi354 – 3585
Beta strandi364 – 3663
Helixi375 – 3773
Helixi386 – 3883
Helixi391 – 3955
Helixi402 – 41716
Helixi427 – 43812
Helixi443 – 4475
Helixi452 – 4554
Beta strandi467 – 4693
Beta strandi475 – 4773
Helixi496 – 4994
Turni500 – 5023
Helixi506 – 51510
Turni520 – 5223
Helixi526 – 5305
Turni533 – 5353

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3K2LX-ray2.36A146-552[»]
3KVWX-ray2.28A146-552[»]
4AZFX-ray2.55A146-540[»]
ProteinModelPortaliQ92630.
SMRiQ92630. Positions 146-543.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92630.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini222 – 535314Protein kinasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi189 – 1913Nuclear localization signal1 Publication

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119032.
HOGENOMiHOG000220863.
HOVERGENiHBG051426.
InParanoidiQ92630.
KOiK08825.
OMAiHTIGGSK.
OrthoDBiEOG77127N.
PhylomeDBiQ92630.
TreeFamiTF314624.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q92630-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLTRKPSAAA PAAYPTGRGG DSAVRQLQAS PGLGAGATRS GVGTGPPSPI
60 70 80 90 100
ALPPLRASNA AAAAHTIGGS KHTMNDHLHV GSHAHGQIQV QQLFEDNSNK
110 120 130 140 150
RTVLTTQPNG LTTVGKTGLP VVPERQLDSI HRRQGSSTSL KSMEGMGKVK
160 170 180 190 200
ATPMTPEQAM KQYMQKLTAF EHHEIFSYPE IYFLGLNAKK RQGMTGGPNN
210 220 230 240 250
GGYDDDQGSY VQVPHDHVAY RYEVLKVIGK GSFGQVVKAY DHKVHQHVAL
260 270 280 290 300
KMVRNEKRFH RQAAEEIRIL EHLRKQDKDN TMNVIHMLEN FTFRNHICMT
310 320 330 340 350
FELLSMNLYE LIKKNKFQGF SLPLVRKFAH SILQCLDALH KNRIIHCDLK
360 370 380 390 400
PENILLKQQG RSGIKVIDFG SSCYEHQRVY TYIQSRFYRA PEVILGARYG
410 420 430 440 450
MPIDMWSLGC ILAELLTGYP LLPGEDEGDQ LACMIELLGM PSQKLLDASK
460 470 480 490 500
RAKNFVSSKG YPRYCTVTTL SDGSVVLNGG RSRRGKLRGP PESREWGNAL
510 520 530 540 550
KGCDDPLFLD FLKQCLEWDP AVRMTPGQAL RHPWLRRRLP KPPTGEKTSV
560 570 580 590 600
KRITESTGAI TSISKLPPPS SSASKLRTNL AQMTDANGNI QQRTVLPKLV

S
Length:601
Mass (Da):66,652
Last modified:June 12, 2007 - v3
Checksum:iA7BEE25CDF944436
GO
Isoform 2 (identifier: Q92630-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-73: Missing.

Show »
Length:528
Mass (Da):59,715
Checksum:iAF2C6822ED9522D7
GO

Sequence cautioni

The sequence CAA73885.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti37 – 371A → P in CAA73885. (PubMed:9748265)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti98 – 981S → G.1 Publication
Corresponds to variant rs35139851 [ dbSNP | Ensembl ].
VAR_040458
Natural varianti198 – 1981P → L in a glioblastoma multiforme sample; somatic mutation. 1 Publication
VAR_040459
Natural varianti245 – 2451H → N.1 Publication
Corresponds to variant rs34166200 [ dbSNP | Ensembl ].
VAR_040460
Natural varianti295 – 2951N → S.1 Publication
Corresponds to variant rs56293072 [ dbSNP | Ensembl ].
VAR_040461
Natural varianti451 – 4511R → Q.1 Publication
Corresponds to variant rs35688869 [ dbSNP | Ensembl ].
VAR_040462
Natural varianti455 – 4551F → Y.1 Publication
Corresponds to variant rs55774594 [ dbSNP | Ensembl ].
VAR_040463

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7373Missing in isoform 2. 1 PublicationVSP_026115Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y13493 mRNA. Translation: CAA73885.1. Different initiation.
AK313937 mRNA. Translation: BAG36656.1.
CH471054 Genomic DNA. Translation: EAW97176.1.
BC005809 mRNA. Translation: AAH05809.1.
BC006375 mRNA. Translation: AAH06375.1.
Y09216 mRNA. Translation: CAA70418.1.
CCDSiCCDS8978.1. [Q92630-1]
CCDS8979.1. [Q92630-2]
RefSeqiNP_003574.1. NM_003583.3. [Q92630-2]
NP_006473.2. NM_006482.2. [Q92630-1]
UniGeneiHs.173135.

Genome annotation databases

EnsembliENST00000344096; ENSP00000342105; ENSG00000127334. [Q92630-1]
ENST00000393555; ENSP00000377186; ENSG00000127334. [Q92630-2]
GeneIDi8445.
KEGGihsa:8445.
UCSCiuc001str.4. human. [Q92630-1]

Polymorphism databases

DMDMi148887370.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y13493 mRNA. Translation: CAA73885.1 . Different initiation.
AK313937 mRNA. Translation: BAG36656.1 .
CH471054 Genomic DNA. Translation: EAW97176.1 .
BC005809 mRNA. Translation: AAH05809.1 .
BC006375 mRNA. Translation: AAH06375.1 .
Y09216 mRNA. Translation: CAA70418.1 .
CCDSi CCDS8978.1. [Q92630-1 ]
CCDS8979.1. [Q92630-2 ]
RefSeqi NP_003574.1. NM_003583.3. [Q92630-2 ]
NP_006473.2. NM_006482.2. [Q92630-1 ]
UniGenei Hs.173135.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3K2L X-ray 2.36 A 146-552 [» ]
3KVW X-ray 2.28 A 146-552 [» ]
4AZF X-ray 2.55 A 146-540 [» ]
ProteinModelPortali Q92630.
SMRi Q92630. Positions 146-543.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114023. 45 interactions.
IntActi Q92630. 5 interactions.
MINTi MINT-1469581.
STRINGi 9606.ENSP00000342105.

Chemistry

BindingDBi Q92630.
ChEMBLi CHEMBL4376.
GuidetoPHARMACOLOGYi 2011.

PTM databases

PhosphoSitei Q92630.

Polymorphism databases

DMDMi 148887370.

Proteomic databases

PaxDbi Q92630.
PRIDEi Q92630.

Protocols and materials databases

DNASUi 8445.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000344096 ; ENSP00000342105 ; ENSG00000127334 . [Q92630-1 ]
ENST00000393555 ; ENSP00000377186 ; ENSG00000127334 . [Q92630-2 ]
GeneIDi 8445.
KEGGi hsa:8445.
UCSCi uc001str.4. human. [Q92630-1 ]

Organism-specific databases

CTDi 8445.
GeneCardsi GC12P068042.
HGNCi HGNC:3093. DYRK2.
HPAi HPA027230.
HPA056902.
MIMi 603496. gene.
neXtProti NX_Q92630.
PharmGKBi PA27550.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000119032.
HOGENOMi HOG000220863.
HOVERGENi HBG051426.
InParanoidi Q92630.
KOi K08825.
OMAi HTIGGSK.
OrthoDBi EOG77127N.
PhylomeDBi Q92630.
TreeFami TF314624.

Enzyme and pathway databases

BRENDAi 2.7.12.1. 2681.
SignaLinki Q92630.

Miscellaneous databases

EvolutionaryTracei Q92630.
GeneWikii DYRK2.
GenomeRNAii 8445.
NextBioi 31596.
PROi Q92630.
SOURCEi Search...

Gene expression databases

Bgeei Q92630.
CleanExi HS_DYRK2.
ExpressionAtlasi Q92630. baseline and differential.
Genevestigatori Q92630.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence characteristics, subcellular localization, and substrate specificity of DYRK-related kinases, a novel family of dual specificity protein kinases."
    Becker W., Weber Y., Wetzel K., Eirmbter K., Tejedor F.J., Joost H.-G.
    J. Biol. Chem. 273:25893-25902(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, COFACTOR, PHOSPHORYLATION, TISSUE SPECIFICITY.
    Tissue: Fetal brain.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Muscle and Skin.
  5. Becker W., Joost H.-G.
    Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 320-528 (ISOFORMS 1/2).
    Tissue: Placenta.
  6. "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."
    Woods Y.L., Cohen P., Becker W., Jakes R., Goedert M., Wang X., Proud C.G.
    Biochem. J. 355:609-615(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Amplification and overexpression of the dual-specificity tyrosine-(Y)-phosphorylation regulated kinase 2 (DYRK2) gene in esophageal and lung adenocarcinomas."
    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.
    Cancer Res. 63:4136-4143(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION IN CANCER.
  8. "The C terminus of initiation factor 4E-binding protein 1 contains multiple regulatory features that influence its function and phosphorylation."
    Wang X., Li W., Parra J.L., Beugnet A., Proud C.G.
    Mol. Cell. Biol. 23:1546-1557(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Phosphorylation of Ser640 in muscle glycogen synthase by DYRK family protein kinases."
    Skurat A.V., Dietrich A.D.
    J. Biol. Chem. 279:2490-2498(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Characterization of cyclin L2, a novel cyclin with an arginine/serine-rich domain: phosphorylation by DYRK1A and colocalization with splicing factors."
    de Graaf K., Hekerman P., Spelten O., Herrmann A., Packman L.C., Bussow K., Muller-Newen G., Becker W.
    J. Biol. Chem. 279:4612-4624(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CCNL2.
  11. "Identification of calcium-regulated heat-stable protein of 24 kDa (CRHSP24) as a physiological substrate for PKB and RSK using KESTREL."
    Auld G.C., Campbell D.G., Morrice N., Cohen P.
    Biochem. J. 389:775-783(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Distinct priming kinases contribute to differential regulation of collapsin response mediator proteins by glycogen synthase kinase-3 in vivo."
    Cole A.R., Causeret F., Yadirgi G., Hastie C.J., McLauchlan H., McManus E.J., Hernandez F., Eickholt B.J., Nikolic M., Sutherland C.
    J. Biol. Chem. 281:16591-16598(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS CRMP4/DPYSL3 KINASE, ENZYME REGULATION BY PURVALANOL.
  13. "A genome-wide Drosophila RNAi screen identifies DYRK-family kinases as regulators of NFAT."
    Gwack Y., Sharma S., Nardone J., Tanasa B., Iuga A., Srikanth S., Okamura H., Bolton D., Feske S., Hogan P.G., Rao A.
    Nature 441:646-650(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NFATC1.
  14. "DYRK2 is targeted to the nucleus and controls p53 via Ser46 phosphorylation in the apoptotic response to DNA damage."
    Taira N., Nihira K., Yamaguchi T., Miki Y., Yoshida K.
    Mol. Cell 25:725-738(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  15. "Role for DYRK family kinases on regulation of apoptosis."
    Yoshida K.
    Biochem. Pharmacol. 76:1389-1394(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN APOPTOSIS AS P53/TP53 KINASE, SUBCELLULAR LOCATION, PHOSPHORYLATION BY ATM, GENE FAMILY.
  16. "Application of active and kinase-deficient kinome collection for identification of kinases regulating hedgehog signaling."
    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.
    Cell 133:537-548(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT THR-381 AND SER-449.
  17. "Nuclear trafficking of pro-apoptotic kinases in response to DNA damage."
    Yoshida K.
    Trends Mol. Med. 14:305-313(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  18. "Harmine specifically inhibits protein kinase DYRK1A and interferes with neurite formation."
    Goeckler N., Jofre G., Papadopoulos C., Soppa U., Tejedor F.J., Becker W.
    FEBS J. 276:6324-6337(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION BY HARMINE.
  19. "Protein kinase DYRK2 is a scaffold that facilitates assembly of an E3 ligase."
    Maddika S., Chen J.
    Nat. Cell Biol. 11:409-419(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN E3 LIGASE REGULATION, FUNCTION AS KATNA1 KINASE, INTERACTION WITH EDVP COMPLEX.
  20. "Structure-activity relationship study of acridine analogs as haspin and DYRK2 kinase inhibitors."
    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.
    Bioorg. Med. Chem. Lett. 20:3491-3494(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION BY ACRIDINE ANALOGS.
  21. "ATM augments nuclear stabilization of DYRK2 by inhibiting MDM2 in the apoptotic response to DNA damage."
    Taira N., Yamamoto H., Yamaguchi T., Miki Y., Yoshida K.
    J. Biol. Chem. 285:4909-4919(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-106 AND SER-442 BY ATM, UBIQUITINATION BY MDM2, INTERACTION WITH MDM2, MUTAGENESIS OF THR-106; SER-442 AND 189-LYS--ARG-191, NUCLEAR LOCALIZATION SIGNAL, INDUCTION BY DNA DAMAGE.
  22. "DYRK2 priming phosphorylation of c-Jun and c-Myc modulates cell cycle progression in human cancer cells."
    Taira N., Mimoto R., Kurata M., Yamaguchi T., Kitagawa M., Miki Y., Yoshida K.
    J. Clin. Invest. 122:859-872(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  23. "Mutual regulation between SIAH2 and DYRK2 controls hypoxic and genotoxic signaling pathways."
    Perez M., Garcia-Limones C., Zapico I., Marina A., Schmitz M.L., Munoz E., Calzado M.A.
    J. Mol. Cell Biol. 4:316-330(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, UBIQUITINATION BY SIAH2.
  24. "Dyrk2-associated EDD-DDB1-VprBP E3 ligase inhibits telomerase by TERT degradation."
    Jung H.Y., Wang X., Jun S., Park J.I.
    J. Biol. Chem. 288:7252-7262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF LYS-251.
  25. "Crystal structure of dual-specificity tyrosine phosphorylation regulated kinase 2 (DYRK2) in complex with an indirubin ligand."
    Structural genomics consortium (SGC)
    Submitted (JAN-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 146-552 IN COMPLEX WITH INDIRUBIN.
  26. "Selectivity, cocrystal structures, and neuroprotective properties of leucettines, a family of protein kinase inhibitors derived from the marine sponge alkaloid leucettamine B."
    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.
    J. Med. Chem. 55:9312-9330(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 146-540 IN COMPLEX WITH LEUCETTAMINE DERIVATIVE, PHOSPHORYLATION AT TYR-382, AUTOPHOSPHORYLATION, ENZYME REGULATION, CATALYTIC ACTIVITY.
  27. "Structures of Down syndrome kinases, DYRKs, reveal mechanisms of kinase activation and substrate recognition."
    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.
    Structure 21:986-996(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.36 ANGSTROMS) OF 146-552.
  28. "Patterns of somatic mutation in human cancer genomes."
    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.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLY-98; LEU-198; ASN-245; SER-295; GLN-451 AND TYR-455.

Entry informationi

Entry nameiDYRK2_HUMAN
AccessioniPrimary (citable) accession number: Q92630
Secondary accession number(s): B2R9V9, Q9BRB5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: June 12, 2007
Last modified: October 29, 2014
This is version 152 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3