Reviewed, UniProtKB/Swiss-Prot P83102 (DYRK3_DROME)

Names and origin

Protein names

Recommended name:
    Putative dual specificity tyrosine-phosphorylation-regulated kinase 3 homolog
    EC=2.7.12.1

Gene names

Name:	Dyrk3
ORF Names:	CG40478

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

General annotation (Comments)

Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Post-translational modification	Autophosphorylated on tyrosine residues By similarity.
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 AAD39356.1 differs from that shown. Reason: Miscellaneous discrepancy. Intron retention.

Ontologies

Keywords
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW 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 – 828	828	Putative dual specificity tyrosine-phosphorylation-regulated kinase 3 homolog		PRO_0000085939
Regions
	Domain	276 – 589	314	Protein kinase
	Nucleotide binding	282 – 290	9	ATP By similarity
Sites
	Active site	402	1	Proton acceptor By similarity
	Binding site	305	1	ATP By similarity
Amino acid modifications
	Modified residue	616	1	Phosphoserine Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P83102-1 [UniParc]. Last modified September 19, 2003. Version 3. Checksum: 9A4AFB31AE52F3E1	FASTA	828	92,740
	10 20 30 40 50 60 MVGSQEKKNN HIELSETPAT DKNNLNTTHL ENTQLSKALS PPTSLPQIQI QMINQNLTHT 70 80 90 100 110 120 GIAQNNTEKA NRHQYRDSGL QYLTRCFEPL AMLNDSKEDF PTQPSNNIAN YPGDIQILPI 130 140 150 160 170 180 FDCCEISESI QAISLPNVTS PSKTKDVPGL FLRTISENSK SKSEPECESL ISVKESSVME 190 200 210 220 230 240 NHTFLFHEQI IMSGQQKCEL HEKPKVLVVS PQQVMILYMN KLTPYERTEI LTYPQIYFIG 250 260 270 280 290 300 ANAKKRPGVY GPNNSEYDNE QGAYIHVPHD HVAYRYEMLK IIGKGSFGQV IKAYDHKTHE 310 320 330 340 350 360 HVALKIVRNE KRFHRQAQEE IRILHHLRRH DKYNTMNIIH MFDYFTFRNH TCITFELLSI 370 380 390 400 410 420 NLYELIKKNG FKGFSLQLVR KFAHSLLQCL DALYKNDIIH CDMKPENVLL KQQGRSGIKV 430 440 450 460 470 480 IDFGSSCFEN QRIYTYIQSR FYRAPEVILG GKYGRAIDMW SLGCILAELL SGHALFPGEN 490 500 510 520 530 540 ESDQLACIIE VLGMPNKNIL ASSKRSKSFF SPKGYPRYCT VRTMSDGMVV LIGGQSRRGK 550 560 570 580 590 600 QRGPPCSKSL SKALDGCKDP LFLNFIRGCL EWDADKRLTP SEALKHPWLR RRLPRPPSSS 610 620 630 640 650 660 SGCGGVSGLC SSRNESPVTG QNRNFAAETT ASSTSATSIS LTIKRENSHS SLRLHHGAVP 670 680 690 700 710 720 ETDFKLIKSV PEGSSTATKE PMMNSDILPE SFRQTTVVSP SKHSADSGGM SCLSAVDVGP 730 740 750 760 770 780 SRYYPYMNNN ENNRLFSSSL NSSANSLSHL EQATKLDALG EYSASTTPNL LSKNTGYSFN 790 800 810 820 SGSINIDVAQ ESLVNIASNY ALDKSIDIIG KSNVSLHTNK LKVQSKDM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	"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.
[3]	"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]. Strain: Berkeley. Tissue: Embryo.
[4]	"Telomere swapping alters chromosomal properties." Wallrath L.L., Cryderman D.E., Morris E.J., Pavlova M., Biessmann H., Levis R.W., Elgin S.C.R. Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 76-290.
[5]	"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-616, MASS SPECTROMETRY. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE014135 Genomic DNA. Translation: ABC65837.1. AE014135 Genomic DNA. Translation: ABC65838.1. AE014135 Genomic DNA. Translation: ABC65839.1. AE014135 Genomic DNA. Translation: ABC65840.1. AE014135 Genomic DNA. Translation: ABC65841.1. AY118401 mRNA. Translation: AAM48430.1. AF103941 Genomic DNA. Translation: AAD39356.1. Sequence problems.
RefSeq	NP_001033810.1. NP_001033811.1. NP_001033812.1. NP_001033813.1. NP_001033814.1.
UniGene	Dm.13812
3D structure databases
HSSP	HSSP built from PDB template 1BI8 based on UniProtKB Q00534.
ModBase	Search...
Genome annotation databases
Ensembl	FBtr0100406; FBpp0099820; FBgn0027101; Drosophila melanogaster. [Genome view]
GeneID	3885567.
KEGG	dme:Dmel_CG40478.
UCSC	CG40478-RA. d. melanogaster.
Organism-specific databases
CTD	3885567.
FlyBase	FBgn0027101. Dyrk3.
Enzyme and pathway databases
BRENDA	2.7.12.1. 48.
Gene expression databases
GermOnline	CG40478. 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	854825.

Entry information

Entry name

DYRK3_DROME

Accession

Primary (citable) accession number: P83102
Secondary accession number(s): A4V144 , Q2PDL5, Q5LJP2, Q8MT39, Q9Y1N4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 2, 2001
Last sequence update:	September 19, 2003
Last modified:	September 1, 2009
This is version 70 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project