Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P48609 (CDK5_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cyclin-dependent kinase 5 homolog

EC=2.7.11.22
Alternative name(s):
Cell division protein kinase 5
Gene names
Name:Cdk5
ORF Names:CG8203
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length294 AA.
Sequence statusComplete.
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.

Ontologies

Keywords
   Biological processCell cycle
Cell division
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadult locomotory behavior

Inferred from mutant phenotype PubMed 19263480. Source: FlyBase

axonogenesis

Inferred from mutant phenotype PubMed 10837225. Source: FlyBase

cell division

Inferred from electronic annotation. Source: UniProtKB-KW

centrosome localization

Inferred from mutant phenotype PubMed 23720047. Source: FlyBase

determination of adult lifespan

Inferred from mutant phenotype PubMed 17368005. Source: FlyBase

flight behavior

Inferred from mutant phenotype PubMed 19263480. Source: FlyBase

intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress

Inferred from genetic interaction PubMed 22388889. Source: FlyBase

melanotic encapsulation of foreign target

Inferred from mutant phenotype PubMed 21947570. Source: FlyBase

mitotic cell cycle

Inferred from mutant phenotype PubMed 14527345. Source: FlyBase

motor neuron axon guidance

Inferred from mutant phenotype PubMed 17368005. Source: FlyBase

protein phosphorylation

Inferred from direct assay PubMed 10837225. Source: FlyBase

regulation of synaptic growth at neuromuscular junction

Inferred from mutant phenotype PubMed 19263480. Source: FlyBase

   Cellular_componentcyclin-dependent protein kinase 5 holoenzyme complex

Inferred from physical interaction PubMed 10837225. Source: FlyBase

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

cyclin-dependent protein serine/threonine kinase activity

Inferred from direct assay PubMed 10837225. Source: FlyBase

protein serine/threonine kinase activity

Inferred from direct assay PubMed 22388889. Source: FlyBase

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CycCP250084EBI-94216,EBI-195485

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 294294Cyclin-dependent 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 [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] [Europe PMC] [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] [Europe PMC] [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] [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. 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] [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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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. NM_057732.3.
UniGeneDm.640.

3D structure databases

ProteinModelPortalP48609.
SMRP48609. Positions 1-288.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid62461. 42 interactions.
DIPDIP-22131N.
IntActP48609. 41 interactions.
MINTMINT-775083.

Proteomic databases

PaxDbP48609.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0087350; FBpp0086483; FBgn0013762.
GeneID36727.
KEGGdme:Dmel_CG8203.

Organism-specific databases

CTD1020.
FlyBaseFBgn0013762. Cdk5.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00600000083998.
InParanoidP48609.
KOK02090.
OMAFPAITSW.
OrthoDBEOG7966H8.
PhylomeDBP48609.

Enzyme and pathway databases

BRENDA2.7.11.22. 1994.
SignaLinkP48609.

Gene expression databases

BgeeP48609.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi36727.
NextBio800081.
PROP48609.

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: April 16, 2014
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

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