Reviewed, UniProtKB/Swiss-Prot Q9V3D5 (DYRK2_DROME)

Names and origin

Protein names

Recommended name:
    Dual specificity tyrosine-phosphorylation-regulated kinase 2
    EC=2.7.12.1
Alternative name(s):
    dDyrk2
    Protein smell impaired at 35A

Gene names

Name:	smi35A
Synonyms:	Dyrk2
ORF Names:	CG4551

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	722 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	In vitro; can phosphorylate exogenous substrates on Ser and Thr residues. May have a physiological role in development being involved in cellular growth and differentiation. Ref.1
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. Ref.1
Cofactor	Magnesium. Ref.1
Enzyme regulation	Autophosphorylates on Tyr-356 and Tyr-358. Ref.1
Subcellular location	Cytoplasm. Ref.1
Developmental stage	Highly expressed and active during embryogenesis and pupation and at lower levels in larva and adult. Ref.1
Post-translational modification	Phosphorylated on serine/threonine residues. Ref.1 Ref.7
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MNB/DYRK subfamily. Contains 1 protein kinase domain.
Sequence caution	The sequence AAL39328.1 differs from that shown. Reason: Miscellaneous discrepancy. Deletion within an exon that does not correspond to an intron.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	ATP-binding Magnesium Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	olfactory behavior Inferred from mutant phenotype. Source: FlyBase protein amino acid phosphorylation Ref.1 Inferred from direct assay. Source: UniProtKB
Cellular component	cytosol Ref.1 Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Ref.1 Inferred from direct assay. Source: UniProtKB magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Ref.1 Inferred from direct assay. Source: UniProtKB protein tyrosine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 722	722	Dual specificity tyrosine-phosphorylation-regulated kinase 2		PRO_0000085937
Regions
	Domain	198 – 494	297	Protein kinase
	Nucleotide binding	204 – 212	9	ATP By similarity UniProtKB Q92630
Sites
	Active site	324	1	Proton acceptor By similarity UniProtKB Q92630
	Binding site	227	1	ATP By similarity UniProtKB Q92630
Amino acid modifications
	Modified residue	25	1	Phosphoserine Ref.7
	Modified residue	356	1	Phosphotyrosine; by autocatalysis Ref.1
	Modified residue	358	1	Phosphotyrosine; by autocatalysis Ref.1
Experimental info
	Mutagenesis	356	1	Y → D or F: Blocks tyrosine phosphorylation. Ref.1
	Mutagenesis	358	1	Y → D or F: Blocks tyrosine phosphorylation. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9V3D5-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: E431C03DDFE81F4E	FASTA	722	79,609
	10 20 30 40 50 60 MLDRCEMPIQ LDNEKLRRDV RLSGSRLDLP QLCNGSRRLD GHNNHVAANE NTVTTTSLNG 70 80 90 100 110 120 NGNGNGNSNS NNNNNIGSPV SSSTTNSSNG GNERGSSTKS NSSSGSGSSG NSASSTGSGE 130 140 150 160 170 180 LKCNTPMTPS ELVKKFRNYL TDLEFEELKV YKEVWYFGQH ASKNYNKPAP TANTTNLGYD 190 200 210 220 230 240 DDNGNYKIIE HDHIAFRYEI LEVIGKGSFG QVIRALDHKT NTHVAIKIIR NKKRFLNQAV 250 260 270 280 290 300 VELNILDELR EKDADGSHNV IHMLDYTYFR KHLCITFELM SLNLYELIKK NNYNGFSMSL 310 320 330 340 350 360 IRRFCNSIVK CLRLLYKENI IHCDLKPENI LLKQRGSSSI KVIDFGSSCY VDRKIYTYIQ 370 380 390 400 410 420 SRFYRSPEVI LGLQYGTAID MWSLGCILAE LYTGFPLFPG ENEVEQLACI MEVLGLPPKV 430 440 450 460 470 480 LISVARRRRL FFDSRDAPRC ITNTKGRKRS PGSKSLAHIL HCQDRYFIDF LQRCLEWDPA 490 500 510 520 530 540 ERMTPDEAAH HEFLQPSASS RHRSCRMSSS SSSSGLNSVS QKSSCYSFSE ISPGTNGPVV 550 560 570 580 590 600 ASITSTTAVH NAAIATTTKS RQQPPSQSHG HAQSNGHLPD IKLSASDKYN SMQKVAVRSK 610 620 630 640 650 660 ITSSVSDLES VQQYSLHRIY GGVGSGSTHH VSSAATRKHL PGTGSGIVGA MSSKYGSSTL 670 680 690 700 710 720 AHNHHNVTHH NASTATIATT THHHHHHGGQ QQQQSSSGAS TMAMSHSQST GDVSDRAIFG RA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"dDYRK2: a novel dual-specificity tyrosine-phosphorylation-regulated kinase in Drosophila." Lochhead P.A., Sibbet G., Kinstrie R., Cleghon T., Rylatt M., Morrison D.K., Cleghon V. Biochem. J. 374:381-391(2003) [PubMed: 12786602] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, COFACTOR, ENZYME REGULATION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, PHOSPHORYLATION AT TYR-356 AND TYR-358, MUTAGENESIS OF TYR-356 AND TYR-358. Strain: Oregon-R. Tissue: Embryo.
[2]	"An exploration of the sequence of a 2.9-Mb region of the genome of Drosophila melanogaster: the Adh region." Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T., Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., Harvey D.A., Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., Moshrefi A.R. , Palazzolo M., Reese M.G., Spradling A.C., Tsang G., Wan K.H., Whitelaw K., Celniker S.E., Rubin G.M. Genetics 153:179-219(1999) [PubMed: 10471707] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[4]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[5]	Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D.E., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A. , Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E. Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[6]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 381-722. Strain: Berkeley. Tissue: Head.
[7]	"Phosphoproteome analysis of Drosophila melanogaster embryos." Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P. J. Proteome Res. 7:1675-1682(2008) [PubMed: 18327897] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, MASS SPECTROMETRY. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF168467 mRNA. Translation: AAD47290.1. AE014134 Genomic DNA. Translation: AAF53380.1. AE014134 Genomic DNA. Translation: AAS64705.1. AE014134 Genomic DNA. Translation: AAS64706.1. AE014134 Genomic DNA. Translation: ABC65900.1. AE014134 Genomic DNA. Translation: ABC65901.1. BT010088 mRNA. Translation: AAQ22557.1. AY069183 mRNA. Translation: AAL39328.1. Sequence problems.
RefSeq	NP_001033906.1. NP_001033907.1. NP_523564.1. NP_995710.1. NP_995711.1.
UniGene	Dm.2597
3D structure databases
HSSP	HSSP built from PDB template 1HOW based on UniProtKB Q03656.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9V3D5.
Proteomic databases
PRIDE	Q9V3D5.
Genome annotation databases
Ensembl	FBtr0100448; FBpp0099870; FBgn0016930; Drosophila melanogaster. [Genome view]
GeneID	34831.
KEGG	dme:Dmel_CG4551.
Organism-specific databases
CTD	34831.
FlyBase	FBgn0016930. smi35A.
Phylogenomic databases
HOGENOM	Q9V3D5.
OMA	ANGCIAS.
Enzyme and pathway databases
BioCyc	DMEL-XXX-02:DMEL-XXX-02-008925-MON.
BRENDA	2.7.12.1. 48.
Gene expression databases
ArrayExpress	Q9V3D5.
GermOnline	CG4551. Drosophila melanogaster.
Family and domain databases
InterPro	IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. IPR002290. Ser_thr_pkinase. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	790436.

Entry information

Entry name

DYRK2_DROME

Accession

Primary (citable) accession number: Q9V3D5
Secondary accession number(s): A4V0P7, Q8T0L9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2004
Last sequence update:	May 1, 2000
Last modified:	November 3, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project