Reviewed, UniProtKB/Swiss-Prot P23573 (CDC2C_DROME)

Names and origin

Protein names

Recommended name:
    Cell division control protein 2 cognate
    EC=2.7.11.22
    EC=2.7.11.23

Gene names

Name:	cdc2c
ORF Names:	CG10498

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

General annotation (Comments)

Function	Like cdc2, could play a key role in the control of the eukaryotic cell cycle.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate.
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	JAK-STAT cascade Inferred from physical interaction. Source: FlyBase cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW protein amino acid phosphorylation Non-traceable author statement. Source: FlyBase
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA polymerase subunit kinase activity Inferred from electronic annotation. Source: EC cyclin-dependent protein kinase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Cks85A	Q9VHN1	2	EBI-95916,EBI-122930
CycH	O17144	2	EBI-95916,EBI-466327
CycJ	Q24159	4	EBI-95916,EBI-455799
CycJ	Q9VZP3	2	EBI-95916,EBI-187073
CycK	Q961D1	5	EBI-95916,EBI-130995
dap	P91668	2	EBI-95916,EBI-466504

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 314	314	Cell division control protein 2 cognate		PRO_0000085744
Regions
	Domain	8 – 287	280	Protein kinase
	Nucleotide binding	14 – 22	9	ATP By similarity
Sites
	Active site	130	1	Proton acceptor By similarity
	Binding site	37	1	ATP By similarity
Amino acid modifications
	Modified residue	18	1	Phosphothreonine By similarity
	Modified residue	19	1	Phosphotyrosine By similarity
	Modified residue	162	1	Phosphotyrosine Ref.6
	Modified residue	163	1	Phosphothreonine Ref.6
Experimental info
	Sequence conflict	27	1	S → T Ref.5
	Sequence conflict	119	1	G → A Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P23573-1 [UniParc]. Last modified November 1, 1991. Version 1. Checksum: 576A88767F9D35C0	FASTA	314	35,888
	10 20 30 40 50 60 MTTILDNFQR AEKIGEGTYG IVYKARSNST GQDVALKKIR LEGETEGVPS TAIREISLLK 70 80 90 100 110 120 NLKHPNVVQL FDVVISGNNL YMIFEYLNMD LKKLMDKKKD VFTPQLIKSY MHQILDAVGF 130 140 150 160 170 180 CHTNRILHRD LKPQNLLVDT AGKIKLADFG LARAFNVPMR AYTHEVVTLW YRAPEILLGT 190 200 210 220 230 240 KFYSTGVDIW SLGCIFSEMI MRRSLFPGDS EIDQLYRIFR TLSTPDETNW PGVTQLPDFK 250 260 270 280 290 300 TKFPRWEGTN MPQPITEHEA HELIMSMLCY DPNLRISAKD ALQHAYFRNV QHVDHVALPV 310 DPNAGSASRL TRLV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Drosophila cdc2 homologs: a functional homolog is coexpressed with a cognate variant." Lehner C.F., O'Farrell P.H. EMBO J. 9:3573-3581(1990) [PubMed: 2120045] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Oregon-R. Tissue: Embryo.
[2]	"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.
[3]	"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.
[4]	"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.
[5]	"Primary structure, expression, and signal-dependent tyrosine phosphorylation of a Drosophila homolog of extracellular signal-regulated kinase." Biggs W.H. III, Zipursky S.L. Proc. Natl. Acad. Sci. U.S.A. 89:6295-6299(1992) [PubMed: 1378625] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 21-167. Tissue: Imaginal disk.
[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: 18327897] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-162 AND THR-163, MASS SPECTROMETRY. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X57486 mRNA. Translation: CAA40724.1. AE014297 Genomic DNA. Translation: AAN14363.1. AY051671 mRNA. Translation: AAK93095.1.
PIR	E46036.
RefSeq	NP_524420.1. NP_732544.1.
UniGene	Dm.2392
3D structure databases
HSSP	HSSP built from PDB template 1BI8 based on UniProtKB Q00534.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:648N.
IntAct	P23573. 82 interactions.
Proteomic databases
PRIDE	P23573.
Genome annotation databases
Ensembl	FBgn0004107. Drosophila melanogaster. [Contig view]
GeneID	42453.
KEGG	dme:Dmel_CG10498.
Organism-specific databases
FlyBase	FBgn0004107. cdc2c.
Phylogenomic databases
HOGENOM	P23573.
OMA	P23573. YMIFEYL.
Enzyme and pathway databases
BioCyc	DMEL-XXX-02:DMEL-XXX-02-012530-MON. DMEL-XXX-02:DMEL-XXX-02-012531-MON.
BRENDA	2.7.11.22. 48. 2.7.11.23. 48.
Gene expression databases
ArrayExpress	P23573.
GermOnline	CG10498. 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	828859.

Entry information

Entry name

CDC2C_DROME

Accession

Primary (citable) accession number: P23573
Secondary accession number(s): Q0KI40, Q9TXB2, Q9VDJ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	November 1, 1991
Last modified:	June 16, 2009
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project