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Reviewed, UniProtKB/Swiss-Prot P48609 (CDK5_DROME)

Last modified June 16, 2009. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Cell division protein kinase 5 homolog
    EC=2.7.11.22
Alternative name(s):
    Cyclin-dependent kinase 5
Gene names
Name: Cdk5
ORF Names: CG8203
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length294 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Probably involved in the control of the cell cycle. Interacts with D1 and D3-type G1 cyclins. Possible regulator of neuronal differentiation and/or development By similarity.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Tissue specificity

Abundantly expressed in all adult tissues. Lower levels found in larvae and early embryos. Barely detectable in late embryos.

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.

Contains 1 protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 294294Cell division protein kinase 5 homolog
PRO_0000085788

Regions

Domain4 – 286283Protein kinase
Nucleotide binding10 – 189ATP By similarity

Sites

Active site1261Proton acceptor By similarity
Binding site331ATP By similarity

Amino acid modifications

Modified residue141Phosphothreonine By similarity
Modified residue151Phosphotyrosine By similarity
Modified residue1591Phosphoserine By similarity

Experimental info

Sequence conflict251D → A in AAA63754. Ref.1
Sequence conflict1661W → L in AAA63754. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P48609-1 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: E6B7B37B2410AA23

FASTA29433,180
        10         20         30         40         50         60 
MQKYDKMEKI GEGTYGTVFK GRNRDTMEIV ALKRVRLDED DEGVPSSALR EICLLKELKH 

        70         80         90        100        110        120 
KNIVRLIDVL HSDKKLTLVF EHCDQDLKKY FDSLNGEIDM AVCRSFMLQL LRGLAFCHSH 

       130        140        150        160        170        180 
NVLHRDLKPQ NLLINKNGEL KLADFGLARA FGIPVKCYSA EVVTLWYRPP DVLFGAKLYT 

       190        200        210        220        230        240 
TSIDMWSAGC ILAELADAGR PLFPGSDVLD QLMKIFRVLG TPNEDSWPGV SHLSDYVALP 

       250        260        270        280        290 
SFPAITSWSQ LVPRLNSKGR DLLQKLLICR PNQRISAEAA MQHPYFTDSS SSGH 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of the Drosophila melanogaster CDK5 homolog."
Hellmich M.R., Kennison J.A., Hampton L.L., Battey J.F.
FEBS Lett. 356:317-321(1994) [PubMed: 7805863] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Oregon-R.
[2]"Novel members of the cdc2-related kinase family in Drosophila: cdk4/6, cdk5, PFTAIRE, and PITSLRE kinase."
Sauer K., Weigmann K., Sigrist S., Lehner C.F.
Mol. Biol. Cell 7:1759-1769(1996) [PubMed: 8930898] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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. expand/collapse author list , 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. expand/collapse author list , 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]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

U21552 Genomic DNA. Translation: AAA63754.1.
X99511 mRNA. Translation: CAA67861.1.
AE013599 Genomic DNA. Translation: AAF58119.1.
AY061049 mRNA. Translation: AAL28597.1.
PIRS51008.
RefSeqNP_477080.1.
UniGeneDm.640

3D structure databases

HSSPHSSP built from PDB template 1H0W based on UniProtKB P24941.
SMRP48609. Positions 1-288.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:22131N.
IntActP48609. 45 interactions.

Genome annotation databases

EnsemblFBgn0013762. Drosophila melanogaster. [Contig view]
GeneID36727.
KEGGdme:Dmel_CG8203.
NMPDRfig|7227.3.peg.5413.

Organism-specific databases

FlyBaseFBgn0013762. Cdk5.

Phylogenomic databases

HOGENOMP48609.
OMAP48609. YVALKEV.

Enzyme and pathway databases

BioCycDMEL-XXX-02:DMEL-XXX-02-004787-MON.
BRENDA2.7.11.22. 48.

Gene expression databases

ArrayExpressP48609.
GermOnlineCG8203. Drosophila melanogaster.

Family and domain databases

InterProIPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_pkinase-rel.
IPR008271. Ser_thr_pkin_AS.
IPR002290. Ser_thr_pkinase.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
ProDomPD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio800081.

Entry information

Entry nameCDK5_DROME
AccessionPrimary (citable) accession number: P48609
Secondary accession number(s): Q94878, Q9V7D8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: December 1, 2000
Last modified: June 16, 2009
This is version 82 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents