DYRK2

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

Cofactorⁱ

Protein has several cofactor binding sites:

Activity 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 key	Position(s)	DescriptionActions	Graphical view	Length
Binding siteⁱ	251	ATPCurated		1
Active siteⁱ	348	Proton acceptorPROSITE-ProRule annotation		1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	228 – 236	ATPCurated		9
Nucleotide bindingⁱ	301 – 304	ATPCurated		4

GO - Molecular functionⁱ

ATP binding
Source: UniProtKB
Inferred from direct assayⁱ
- 11311121
magnesium ion binding
Source: UniProtKB
Inferred from direct assayⁱ
- 9748265
manganese ion binding
Source: UniProtKB
Inferred from direct assayⁱ
- 9748265
protein serine/threonine/tyrosine kinase activity Source: UniProtKB-EC
protein serine/threonine kinase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 11311121
protein tyrosine kinase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 9748265

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cellular response to DNA damage stimulus
Source: UniProtKB
Inferred from expression patternⁱ
- 19965871
intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator
Source: UniProtKB
Inferred from direct assayⁱ
- 17349958
negative regulation of calcineurin-NFAT signaling cascade
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 16511445
positive regulation of glycogen biosynthetic process
Source: UniProtKB
Inferred from direct assayⁱ
- 11311121
protein phosphorylation
Source: UniProtKB
Inferred from direct assayⁱ
- 11311121
regulation of signal transduction by p53 class mediator Source: Reactome
smoothened signaling pathway
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 18455992

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Kinase, Serine/threonine-protein kinase, Transferase, Tyrosine-protein kinase
Biological process	Apoptosis, Ubl conjugation pathway
Ligand	ATP-binding, Magnesium, Manganese, Nucleotide-binding

Enzyme and pathway databases

BRENDAⁱ	2.7.12.1 2681
Reactomeⁱ	R-HSA-6804756 Regulation of TP53 Activity through Phosphorylation
SignaLinkⁱ	Q92630
SIGNORⁱ	Q92630

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Dual specificity tyrosine-phosphorylation-regulated kinase 2 (EC:2.7.12.1)
Gene namesⁱ	Name:DYRK2
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 12

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000127334.10
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:3093 DYRK2
MIMⁱ	603496 gene
neXtProtⁱ	NX_Q92630

Keywords - Cellular componentⁱ

Cytoplasm, Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	106	T → A: Impaired ATM-mediated phosphorylation, reduced affinity with MDM2 and altered MDM2-triggered ubiquitination. 1 Publication	1
Mutagenesisⁱ	189 – 191	KKR → NNN: Impaired nuclear translocation. 1 Publication	3
Mutagenesisⁱ	251	K → R: Abolishes protein serine/threonine kinase activity. 1 Publication	1
Mutagenesisⁱ	442	S → A: Impaired ATM-mediated phosphorylation, reduced affinity with MDM2 and altered MDM2-triggered ubiquitination. 1 Publication	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	8445
Open Targets More...OpenTargetsⁱ	ENSG00000127334
PharmGKBⁱ	PA27550

Chemistry databases

ChEMBLⁱ	CHEMBL4376
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYⁱ	2011

Polymorphism and mutation databases

BioMutaⁱ	DYRK2
DMDMⁱ	148887370

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000085936	1 – 601	Dual specificity tyrosine-phosphorylation-regulated kinase 2Add BLAST		601

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	30	PhosphoserineCombined sources	1
Modified residueⁱ	106	Phosphothreonine; by ATM1 Publication	1
Modified residueⁱ	381	Phosphothreonine; by MAP3K101 Publication	1
Modified residueⁱ	382	Phosphotyrosine; by autocatalysis1 Publication	1
Modified residueⁱ	442	Phosphoserine; by ATM1 Publication	1
Modified residueⁱ	449	Phosphoserine; by MAP3K101 Publication	1

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

EPDⁱ	Q92630
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q92630
PaxDbⁱ	Q92630
PeptideAtlas More...PeptideAtlasⁱ	Q92630
PRIDEⁱ	Q92630
ProteomicsDBⁱ	75387 75388 [Q92630-2]

PTM databases

iPTMnetⁱ	Q92630
PhosphoSitePlusⁱ	Q92630

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

Bgeeⁱ	ENSG00000127334 Expressed in 235 organ(s), highest expression level in neocortex
CleanExⁱ	HS_DYRK2
ExpressionAtlasⁱ	Q92630 baseline and differential
Genevisibleⁱ	Q92630 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA027230 HPA056902

HPAⁱ

HPA027230
HPA056902

Interactionⁱ

Subunit structureⁱ

Component of an E3 ligase complex containing DYRK2, EDD/UBR5, DDB1 and DCAF1 (EDVP complex). Interacts directly with EDD/UBR5, DDB1 and DCAF1. Interacts with SIAH2 and MDM2. Interacts with MAP3K10 and NFATC1. May also interact with CCNL2.6 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
DYRK4	Q9NR20	3	EBI-749432,EBI-3914009
IKZF1	Q13422	3	EBI-749432,EBI-745305
KXD1	Q9BQD3	3	EBI-749432,EBI-739657
LZTS2	Q9BRK4	3	EBI-749432,EBI-741037
SP100	P23497	3	EBI-749432,EBI-751145
WDR62	O43379	3	EBI-749432,EBI-714790
ZBTB9	Q96C00	3	EBI-749432,EBI-395708

Protein-protein interaction databases

BioGridⁱ	114023, 63 interactors
CORUMⁱ	Q92630
IntActⁱ	Q92630, 13 interactors
STRINGⁱ	9606.ENSP00000342105

Chemistry databases

BindingDBⁱ

Q92630

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	149 – 152	Combined sources	4
Helixⁱ	156 – 163	Combined sources	8
Helixⁱ	164 – 166	Combined sources	3
Helixⁱ	169 – 174	Combined sources	6
Helixⁱ	175 – 177	Combined sources	3
Beta strandⁱ	179 – 181	Combined sources	3
Helixⁱ	198 – 202	Combined sources	5
Beta strandⁱ	206 – 208	Combined sources	3
Turnⁱ	219 – 221	Combined sources	3
Beta strandⁱ	222 – 231	Combined sources	10
Beta strandⁱ	234 – 241	Combined sources	8
Turnⁱ	242 – 245	Combined sources	4
Beta strandⁱ	246 – 253	Combined sources	8
Helixⁱ	257 – 274	Combined sources	18
Beta strandⁱ	287 – 292	Combined sources	6
Beta strandⁱ	297 – 301	Combined sources	5
Helixⁱ	308 – 314	Combined sources	7
Turnⁱ	315 – 317	Combined sources	3
Helixⁱ	322 – 341	Combined sources	20
Helixⁱ	351 – 353	Combined sources	3
Beta strandⁱ	354 – 358	Combined sources	5
Beta strandⁱ	364 – 366	Combined sources	3
Helixⁱ	375 – 377	Combined sources	3
Helixⁱ	386 – 388	Combined sources	3
Helixⁱ	391 – 395	Combined sources	5
Helixⁱ	402 – 417	Combined sources	16
Helixⁱ	427 – 438	Combined sources	12
Helixⁱ	443 – 447	Combined sources	5
Helixⁱ	452 – 455	Combined sources	4
Beta strandⁱ	465 – 469	Combined sources	5
Beta strandⁱ	471 – 473	Combined sources	3
Beta strandⁱ	475 – 478	Combined sources	4
Helixⁱ	496 – 499	Combined sources	4
Turnⁱ	500 – 502	Combined sources	3
Helixⁱ	506 – 515	Combined sources	10
Turnⁱ	520 – 522	Combined sources	3
Helixⁱ	526 – 529	Combined sources	4
Helixⁱ	533 – 535	Combined sources	3

Show more details

3D structure databases

ProteinModelPortalⁱ	Q92630
SMRⁱ	Q92630
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	Q92630

EvolutionaryTraceⁱ

Q92630

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	222 – 535	Protein kinasePROSITE-ProRule annotationAdd BLAST		314

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	189 – 191	Nuclear localization signal1 Publication		3

Sequence similaritiesⁱ

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MNB/DYRK subfamily.Curated

Phylogenomic databases

eggNOGⁱ	KOG0667 Eukaryota ENOG410XPET LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00760000119032
HOGENOMⁱ	HOG000220863
HOVERGENⁱ	HBG051426
InParanoidⁱ	Q92630
KEGG Orthology (KO) More...KOⁱ	K18669
OMAⁱ	KLTTFEH
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0Q46
PhylomeDBⁱ	Q92630
TreeFamⁱ	TF314624

Family and domain databases

InterProⁱ	View protein in InterPro IPR011009 Kinase-like_dom_sf IPR000719 Prot_kinase_dom IPR017441 Protein_kinase_ATP_BS IPR008271 Ser/Thr_kinase_AS
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00069 Pkinase, 1 hit
SMARTⁱ	View protein in SMART SM00220 S_TKc, 1 hit
SUPFAMⁱ	SSF56112 SSF56112, 1 hit
PROSITEⁱ	View protein in PROSITE PS00107 PROTEIN_KINASE_ATP, 1 hit PS50011 PROTEIN_KINASE_DOM, 1 hit PS00108 PROTEIN_KINASE_ST, 1 hit

Sequences (2+)ⁱ

Sequence statusⁱ: Complete.

This entry describes 2 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 2 described isoforms and 3 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: Q92630-1) [UniParc]FASTA Add 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]FASTA Add to basket

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

« Hide

        10         20         30         40         50
MNDHLHVGSH AHGQIQVQQL FEDNSNKRTV LTTQPNGLTT VGKTGLPVVP 
        60         70         80         90        100
ERQLDSIHRR QGSSTSLKSM EGMGKVKATP MTPEQAMKQY MQKLTAFEHH 
       110        120        130        140        150
EIFSYPEIYF LGLNAKKRQG MTGGPNNGGY DDDQGSYVQV PHDHVAYRYE 
       160        170        180        190        200
VLKVIGKGSF GQVVKAYDHK VHQHVALKMV RNEKRFHRQA AEEIRILEHL 
       210        220        230        240        250
RKQDKDNTMN VIHMLENFTF RNHICMTFEL LSMNLYELIK KNKFQGFSLP 
       260        270        280        290        300
LVRKFAHSIL QCLDALHKNR IIHCDLKPEN ILLKQQGRSG IKVIDFGSSC 
       310        320        330        340        350
YEHQRVYTYI QSRFYRAPEV ILGARYGMPI DMWSLGCILA ELLTGYPLLP 
       360        370        380        390        400
GEDEGDQLAC MIELLGMPSQ KLLDASKRAK NFVSSKGYPR YCTVTTLSDG 
       410        420        430        440        450
SVVLNGGRSR RGKLRGPPES REWGNALKGC DDPLFLDFLK QCLEWDPAVR 
       460        470        480        490        500
MTPGQALRHP WLRRRLPKPP TGEKTSVKRI TESTGAITSI SKLPPPSSSA 
       510        520 
SKLRTNLAQM TDANGNIQQR TVLPKLVS

Show »

Length:528

Mass (Da):59,715

Checksum:ⁱAF2C6822ED9522D7

GO

Computationally mapped potential isoform sequencesⁱ

There are 3 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

F5H5L5	F5H5L5_HUMAN	Dual-specificity tyrosine-phosphory... Dual-specificity tyrosine-phosphorylation-regulated kinase 2	DYRK2	167	Annotation score:
F5GXG1	F5GXG1_HUMAN	Dual-specificity tyrosine-phosphory... Dual-specificity tyrosine-phosphorylation-regulated kinase 2	DYRK2	156	Annotation score:
A0A0A0MR56	A0A0A0MR56_HUMAN	Dual-specificity tyrosine-phosphory... Dual-specificity tyrosine-phosphorylation-regulated kinase 2	DYRK2	93	Annotation score:

Sequence cautionⁱ

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

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	37	A → P in CAA73885 (PubMed:9748265).Curated		1

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_040458	98	S → G1 PublicationCorresponds to variant dbSNP:rs35139851Ensembl.	1
Natural variantⁱVAR_040459	198	P → L in a glioblastoma multiforme sample; somatic mutation. 1 Publication	1
Natural variantⁱVAR_040460	245	H → N1 PublicationCorresponds to variant dbSNP:rs34166200Ensembl.	1
Natural variantⁱVAR_040461	295	N → S1 PublicationCorresponds to variant dbSNP:rs56293072Ensembl.	1
Natural variantⁱVAR_040462	451	R → Q1 PublicationCorresponds to variant dbSNP:rs35688869Ensembl.	1
Natural variantⁱVAR_040463	455	F → Y1 PublicationCorresponds to variant dbSNP:rs55774594Ensembl.	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_026115	1 – 73	Missing in isoform 2. 1 PublicationAdd BLAST		73

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ 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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS8978.1 [Q92630-1] CCDS8979.1 [Q92630-2]
NCBI Reference Sequences More...RefSeqⁱ	NP_003574.1, NM_003583.3 [Q92630-2] NP_006473.2, NM_006482.2 [Q92630-1] XP_016875521.1, XM_017020032.1 [Q92630-2]
UniGeneⁱ	Hs.173135

Genome annotation databases

Ensemblⁱ	ENST00000344096; ENSP00000342105; ENSG00000127334 [Q92630-1] ENST00000393555; ENSP00000377186; ENSG00000127334 [Q92630-2]
GeneIDⁱ	8445
KEGGⁱ	hsa:8445
UCSC genome browser More...UCSCⁱ	uc001str.5 human [Q92630-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q92630	DYRK2 isoform 1		PANTR		601	UniRef100_Q92630
Q92630-2	Dual specificity tyrosine phosphorylation regulated kinase 2		PANPA		609	UniRef100_A0A2R9CSN8
Uncharacterized protein		NOMLE		584
DYRK2 isoform 5 (Fragment)		PANTR		94
Dual-specificity tyrosine-phosphorylation-regulated kinase 2 (Fragment)		HUMAN		156
DYRK2 isoform 4 (Fragment)		PANTR		156
+2

Protein	Similar proteins		Species	Score	Length	Source
Q92630	Dual specificity tyrosine-phosphorylation-regulated kinase 2		MOUSE		599	UniRef90_Q92630
DYRK2 isoform 1		PANTR		601
Dual specificity tyrosine phosphorylation regulated kinase 2		PANPA		609
Uncharacterized protein		NOMLE		584
Dual-specificity tyrosine-phosphorylation-regulated kinase 2 (Fragment)		HUMAN		156
+188

Protein	Similar proteins		Species	Score	Length	Source
Q92630	Dual specificity tyrosine-phosphorylation-regulated kinase 2		MOUSE		599	UniRef50_Q92630
DYRK2 isoform 1		PANTR		601
Dual specificity tyrosine phosphorylation regulated kinase 2		PANPA		609
Uncharacterized protein		NOMLE		584
Dual-specificity tyrosine-phosphorylation-regulated kinase 2 (Fragment)		HUMAN		156
+332

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ 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] XP_016875521.1, XM_017020032.1 [Q92630-2]
UniGeneⁱ	Hs.173135

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB 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	[»]
	5LXC	X-ray	2.15	A/B	146-552	[»]
	5LXD	X-ray	2.58	A/B	146-552	[»]
	5ZTN	X-ray	2.50	A/B	146-552	[»]
ProteinModelPortalⁱ	Q92630
SMRⁱ	Q92630
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	114023, 63 interactors
CORUMⁱ	Q92630
IntActⁱ	Q92630, 13 interactors
STRINGⁱ	9606.ENSP00000342105

Chemistry databases

BindingDBⁱ	Q92630
ChEMBLⁱ	CHEMBL4376
GuidetoPHARMACOLOGYⁱ	2011

PTM databases

iPTMnetⁱ	Q92630
PhosphoSitePlusⁱ	Q92630

Polymorphism and mutation databases

BioMutaⁱ	DYRK2
DMDMⁱ	148887370

Proteomic databases

EPDⁱ	Q92630
MaxQBⁱ	Q92630
PaxDbⁱ	Q92630
PeptideAtlasⁱ	Q92630
PRIDEⁱ	Q92630
ProteomicsDBⁱ	75387 75388 [Q92630-2]

Protocols and materials databases

The DNASU plasmid repository More...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.5 human [Q92630-1]

Organism-specific databases

CTDⁱ	8445
DisGeNETⁱ	8445
EuPathDBⁱ	HostDB:ENSG00000127334.10
GeneCardsⁱ	DYRK2
HGNCⁱ	HGNC:3093 DYRK2
HPAⁱ	HPA027230 HPA056902
MIMⁱ	603496 gene
neXtProtⁱ	NX_Q92630
OpenTargetsⁱ	ENSG00000127334
PharmGKBⁱ	PA27550
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG0667 Eukaryota ENOG410XPET LUCA
GeneTreeⁱ	ENSGT00760000119032
HOGENOMⁱ	HOG000220863
HOVERGENⁱ	HBG051426
InParanoidⁱ	Q92630
KOⁱ	K18669
OMAⁱ	KLTTFEH
OrthoDBⁱ	EOG091G0Q46
PhylomeDBⁱ	Q92630
TreeFamⁱ	TF314624

Enzyme and pathway databases

BRENDAⁱ	2.7.12.1 2681
Reactomeⁱ	R-HSA-6804756 Regulation of TP53 Activity through Phosphorylation
SignaLinkⁱ	Q92630
SIGNORⁱ	Q92630

Miscellaneous databases

ChiTaRSⁱ	DYRK2 human
EvolutionaryTraceⁱ	Q92630
GeneWikiⁱ	DYRK2
GenomeRNAiⁱ	8445
Protein Ontology More...PROⁱ	PR:Q92630
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000127334 Expressed in 235 organ(s), highest expression level in neocortex
CleanExⁱ	HS_DYRK2
ExpressionAtlasⁱ	Q92630 baseline and differential
Genevisibleⁱ	Q92630 HS

Family and domain databases

InterProⁱ	View protein in InterPro IPR011009 Kinase-like_dom_sf IPR000719 Prot_kinase_dom IPR017441 Protein_kinase_ATP_BS IPR008271 Ser/Thr_kinase_AS
Pfamⁱ	View protein in Pfam PF00069 Pkinase, 1 hit
SMARTⁱ	View protein in SMART SM00220 S_TKc, 1 hit
SUPFAMⁱ	SSF56112 SSF56112, 1 hit
PROSITEⁱ	View protein in PROSITE PS00107 PROTEIN_KINASE_ATP, 1 hit PS50011 PROTEIN_KINASE_DOM, 1 hit PS00108 PROTEIN_KINASE_ST, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	DYRK2_HUMAN
Accessionⁱ	Q92630Primary (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 10, 2018
	This is version 191 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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

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

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q92630 (DYRK2_HUMAN)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

Dual specificity tyrosine-phosphorylation-regulated kinase 2

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Nucleus

Other locations

Cytosol

Nucleus

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Motif

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Your basket is currently empty. ⁱ

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequence cautionⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ