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UniProtKB/Swiss-Prot entry P23573


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CDC2C_DROME
Primary accession number P23573
Secondary accession numbers Q0KI40 Q9TXB2 Q9VDJ4
Integrated into Swiss-Prot on November 1, 1991
Sequence was last modified on November 1, 1991 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 85)
Name and origin of the protein
Protein name Cell division control protein 2 cognate
Synonyms EC 2.7.11.22
EC 2.7.11.23
Gene name
Name: cdc2c
ORFNames: CG10498
From
Drosophila melanogaster (Fruit fly) [TaxID: 7227] 
Taxonomy Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Oregon-R;
TISSUE=Embryo;
PubMed=2120045 [NCBI, ExPASy, EBI, Israel, Japan]
Lehner C.F., O'Farrell P.H.;
"Drosophila cdc2 homologs: a functional homolog is coexpressed with a cognate variant.";
EMBO J. 9:3573-3581(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
DOI=10.1126/science.287.5461.2185; PubMed=10731132 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION.
PubMed=12537572 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley;
TISSUE=Embryo;
PubMed=12537569 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5]
NUCLEOTIDE SEQUENCE OF 21-167.
TISSUE=Imaginal disk;
PubMed=1378625 [NCBI, ExPASy, EBI, Israel, Japan]
Biggs W.H. III, Zipursky S.L.;
"Primary structure, expression, and signal-dependent tyrosine phosphorylation of a Drosophila homolog of extracellular signal-regulated kinase.";
Proc. Natl. Acad. Sci. U.S.A. 89:6295-6299(1992).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-162 AND THR-163, AND MASS SPECTROMETRY.
TISSUE=Embryo;
DOI=10.1021/pr700696a; PubMed=18327897 [NCBI, ExPASy, EBI, Israel, Japan]
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X57486; CAA40724.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014297; AAN14363.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY051671; AAK93095.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR E46036; E46036.
RefSeq NP_524420.1; -.
NP_732544.1; -.
UniGene Dm.2392
3D structure databases
HSSP Q00534; 1BI8. [HSSP ENTRY / PDB]
ModBase P23573.
Protein-protein interaction databases
DIP DIP:648N; -.
IntAct P23573; -.
Enzyme and pathway databases
BioCyc DMEL-XXX-02:DMEL-XXX-02-012530-MON; -.
DMEL-XXX-02:DMEL-XXX-02-012531-MON; -.
Organism-specific databases
FlyBase FBgn0004107; cdc2c.
Gene expression databases
ArrayExpress P23573; -.
GermOnline CG10498; Drosophila melanogaster.
Ontologies
GO
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0004693; Molecular function: cyclin-dependent protein kinase activity (inferred from electronic annotation from EC).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0008353; Molecular function: RNA polymerase subunit kinase activity (inferred from electronic annotation from EC).
GO:0051301; Biological process: cell division (inferred from electronic annotation from UniProtKB-KW).
GO:0007259; Biological process: JAK-STAT cascade (inferred from physical interaction from FlyBase).
GO:0007067; Biological process: mitosis (inferred from electronic annotation from UniProtKB-KW).
GO:0006468; Biological process: protein amino acid phosphorylation (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
IPR002290; Ser_thr_pkinase.
Graphical view of domain structure.
Pfam PF00069; Pkinase; 1.
Pfam graphical view of domain structure.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00220; S_TKc; 1.
SMART graphical view of domain structure.
PROSITE PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P23573.
ProtoNet P23573.
Genome annotation databases
Ensembl CG10498; Drosophila melanogaster. [Contig view]
GeneID 42453; -.
KEGG dme:Dmel_CG10498; -.
Phylogenomic databases
HOGENOM P23573; -.
Other
NextBio 828859; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Cell cycle; Cell division; Complete proteome; Kinase; Mitosis; Nucleotide-binding; Phosphoprotein; Serine/threonine-protein kinase; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   314  314     Cell division control protein 2 cognate. PRO_0000085744
DOMAIN   8   287  280     Protein kinase. 
NP_BIND   14    22  9     ATP (By similarity). 
ACT_SITE   130   130        Proton acceptor (By similarity). 
BINDING   37    37        ATP (By similarity). 
MOD_RES   18    18        Phosphothreonine (By similarity). 
MOD_RES   19    19        Phosphotyrosine (By similarity). 
MOD_RES   162   162        Phosphotyrosine. 
MOD_RES   163   163        Phosphothreonine. 
CONFLICT   27    27        S -> T (in Ref. 5). 
CONFLICT   119   119        G -> A (in Ref. 5). 
Sequence information
Length: 314 AA [This is the length of the unprocessed precursor] Molecular weight: 35888 Da [This is the MW of the unprocessed precursor] CRC64: 576A88767F9D35C0 [This is a checksum on the sequence]
        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 

P23573 in FASTA format

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