P54350 (WEE1_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Wee1-like protein kinase
Short name=Dwee1
EC=2.7.10.2

Gene names

Name:	wee
ORF Names:	CG4488

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	609 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Could act as a negative regulator of entry into mitosis (G2 to M transition). This kinase specifically phosphorylates and inactivates cyclin B1-complexed CDC2. Ref.1
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Cofactor	Binds 2 magnesium ions per subunit By similarity.
Enzyme regulation	Negatively regulated by phosphorylation in the M-phase.
Subcellular location	Nucleus By similarity.
Tissue specificity	Expressed in embryos; expression remains high in the proliferating cells of the central nervous system well after cells in the rest of the embryo have ceased dividing. Ref.1
Developmental stage	Expressed both maternally and zygotically during postblastoderm divisions of embryogenesis. Ref.1
Post-translational modification	Phosphorylated during M and G1 phases By similarity.
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. WEE1 subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Nucleus
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW centrosome localization Inferred from mutant phenotype PubMed 16139207. Source: FlyBase centrosome separation Inferred from mutant phenotype PubMed 16139207. Source: FlyBase embryonic development via the syncytial blastoderm Traceable author statement PubMed 14616073. Source: FlyBase mitosis Inferred from electronic annotation. Source: UniProtKB-KW mitotic cell cycle checkpoint Inferred from direct assay Ref.1. Source: FlyBase negative regulation of cyclin-dependent protein serine/threonine kinase activity Inferred from direct assay Ref.1. Source: FlyBase spindle assembly Inferred from mutant phenotype PubMed 16139207. Source: FlyBase
Cellular_component	microtubule associated complex Inferred from direct assay PubMed 18433294. Source: FlyBase nucleus Inferred from direct assay Ref.1. Source: FlyBase
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: InterPro non-membrane spanning protein tyrosine kinase activity Inferred from electronic annotation. Source: EC protein tyrosine kinase activity Inferred from direct assay PubMed 19800237Ref.1. Source: FlyBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 609	609	Wee1-like protein kinase		PRO_0000086814
Regions
	Domain	239 – 517	279	Protein kinase
	Nucleotide binding	245 – 253	9	ATP By similarity
	Compositional bias	122 – 126	5	Poly-Ala
Sites
	Active site	361	1	Proton acceptor By similarity
	Metal binding	366	1	Magnesium; via carbonyl oxygen By similarity
	Metal binding	412	1	Magnesium; via carbonyl oxygen By similarity
	Binding site	268	1	ATP By similarity
Amino acid modifications
	Modified residue	23	1	Phosphoserine Ref.6
	Modified residue	25	1	Phosphoserine Ref.6
	Modified residue	27	1	Phosphoserine Ref.6
	Modified residue	47	1	Phosphothreonine Ref.6
	Modified residue	52	1	Phosphoserine Ref.6
	Modified residue	165	1	Phosphothreonine Ref.6
	Modified residue	168	1	Phosphoserine Ref.6
Experimental info
	Sequence conflict	35 – 36	2	KL → NV in AAC46913. Ref.1
	Sequence conflict	72	1	D → G in AAC46913. Ref.1
	Sequence conflict	275	1	A → R in AAC46913. Ref.1
	Sequence conflict	567	1	N → K in AAC46913. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P54350 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: 7E371EFDA2A5CD96	FASTA	609	68,809
	10 20 30 40 50 60 MAFRQSEHEM SVTSLDSSVE LRSRSPSPQV FNPRKLRFAD DDFDKDTPEG ASPQHPLQQR 70 80 90 100 110 120 PKLSSGEEQQ LDSKIGKEGG DGDVSMSPPC QKVRALRLFS TPATPKTILQ KSTTQCSNHL 130 140 150 160 170 180 SAAAAAVNAS RRSDDLFRLS ERPRSLPLHN RKLPTQDTAN VNPFTPDSLM AHNKKRCRTQ 190 200 210 220 230 240 FGRENLNLNV NAMQKYLLSD ACDDDVTEEA GDSMREIHQQ APKRLALHDT NISRFKREFM 250 260 270 280 290 300 QVNVIGVGEF GVVFQCVNRL DGCIYAIKKS KKPVAGSSFE KRALNEVWAH AVLGKHDNVV 310 320 330 340 350 360 RYYSAWAEDD HMLIQNEFCD GGSLHARIQD HCLGEAELKI VLMHVIEGLR YIHSNDLVHM 370 380 390 400 410 420 DLKPENIFST MNPNAHKLVE VQPQQTKDDD GMDSVYEELR HSENLVTYKI GDLGHVTSVK 430 440 450 460 470 480 EPYVEEGDCR YLPKEILHED YSNLFKADIF SLGITLFEAA GGGPLPKNGP EWHNLRDGKV 490 500 510 520 530 540 PILPSLSRDF NELIAQMMHP YPDKRPTSQS IFSHPILSAV DSKSKLQLGL ELTVEKRKNE 550 560 570 580 590 600 ILMNKLREAK KQIKLLEQRV NLLAVTNNPD SLDGQRCLRS FTRRMRTPFS SHGKFDSISD RNKNVITNI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Drosophila Wee1 kinase rescues fission yeast from mitotic catastrophe and phosphorylates Drosophila Cdc2 in vitro." Campbell S.D., Sprenger F., Edgar B.A., O'Farrell P.H. Mol. Biol. Cell 6:1333-1347(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[2]	Campbell S.D. Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO C-TERMINUS.
[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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[5]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[6]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-25; SER-27; THR-47; SER-52; THR-165 AND SER-168, MASS SPECTROMETRY. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U17223 mRNA. Translation: AAC46913.2. AE014134 Genomic DNA. Translation: AAF52453.2. AY118942 mRNA. Translation: AAM50802.1.
RefSeq	NP_001260167.1. NM_001273238.1. NP_477035.1. NM_057687.4.
UniGene	Dm.3106.
3D structure databases
ProteinModelPortal	P54350.
SMR	P54350. Positions 214-587.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-23536N.
IntAct	P54350. 2 interactions.
MINT	MINT-885153.
STRING	7227.FBpp0078999.
Proteomic databases
PaxDb	P54350.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0079371; FBpp0078999; FBgn0011737. FBtr0332329; FBpp0304607; FBgn0011737.
GeneID	33965.
KEGG	dme:Dmel_CG4488.
Organism-specific databases
CTD	33965.
FlyBase	FBgn0011737. wee.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00530000063230.
InParanoid	P54350.
KO	K06632.
OMA	CIYAIKK.
OrthoDB	EOG4QRFK4.
PhylomeDB	P54350.
Enzyme and pathway databases
BRENDA	2.7.10.2. 1994.
Gene expression databases
Bgee	P54350.
GermOnline	CG4488. Drosophila melanogaster.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017164. Wee1-like_protein_kinase. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
PIRSF	PIRSF037281. Wee1-like_protein_kinase. 1 hit.
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. False negative. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	33965.
NextBio	786174.

Entry information

Entry name

WEE1_DROME

Accession

Primary (citable) accession number: P54350
Secondary accession number(s): Q9VM70

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	December 1, 2000
Last modified:	May 1, 2013
This is version 119 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project