Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cyclin-dependent kinase 5 homolog

Gene

Cdk5

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei33 – 331ATPPROSITE-ProRule annotation
Active sitei126 – 1261Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 189ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • cyclin-dependent protein serine/threonine kinase activity Source: FlyBase
  • protein serine/threonine kinase activity Source: FlyBase

GO - Biological processi

  • adult locomotory behavior Source: FlyBase
  • axonogenesis Source: FlyBase
  • cell division Source: UniProtKB-KW
  • centrosome localization Source: FlyBase
  • determination of adult lifespan Source: FlyBase
  • flight behavior Source: FlyBase
  • intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: FlyBase
  • melanotic encapsulation of foreign target Source: FlyBase
  • mitotic cell cycle Source: FlyBase
  • motor neuron axon guidance Source: FlyBase
  • protein phosphorylation Source: FlyBase
  • regulation of cell cycle Source: GOC
  • regulation of synaptic growth at neuromuscular junction Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, Cell division

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.22. 1994.
ReactomeiREACT_287092. Factors involved in megakaryocyte development and platelet production.
REACT_319268. CRMPs in Sema3A signaling.
SignaLinkiP48609.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclin-dependent kinase 5 homolog (EC:2.7.11.22)
Alternative name(s):
Cell division protein kinase 5
Gene namesi
Name:Cdk5
ORF Names:CG8203
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0013762. Cdk5.

Subcellular locationi

GO - Cellular componenti

  • cyclin-dependent protein kinase 5 holoenzyme complex Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 294294Cyclin-dependent kinase 5 homologPRO_0000085788Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei14 – 141PhosphothreonineBy similarity
Modified residuei15 – 151PhosphotyrosineBy similarity
Modified residuei159 – 1591PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP48609.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiP48609.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CycCP250084EBI-94216,EBI-195485

Protein-protein interaction databases

BioGridi62461. 42 interactions.
DIPiDIP-22131N.
IntActiP48609. 41 interactions.
MINTiMINT-775083.

Structurei

3D structure databases

ProteinModelPortaliP48609.
SMRiP48609. Positions 1-288.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 286283Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00790000122973.
InParanoidiP48609.
KOiK02090.
OMAiFPPITSW.
OrthoDBiEOG7966H8.
PhylomeDBiP48609.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P48609-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQKYDKMEKI GEGTYGTVFK GRNRDTMEIV ALKRVRLDED DEGVPSSALR
60 70 80 90 100
EICLLKELKH KNIVRLIDVL HSDKKLTLVF EHCDQDLKKY FDSLNGEIDM
110 120 130 140 150
AVCRSFMLQL LRGLAFCHSH NVLHRDLKPQ NLLINKNGEL KLADFGLARA
160 170 180 190 200
FGIPVKCYSA EVVTLWYRPP DVLFGAKLYT TSIDMWSAGC ILAELADAGR
210 220 230 240 250
PLFPGSDVLD QLMKIFRVLG TPNEDSWPGV SHLSDYVALP SFPAITSWSQ
260 270 280 290
LVPRLNSKGR DLLQKLLICR PNQRISAEAA MQHPYFTDSS SSGH
Length:294
Mass (Da):33,180
Last modified:December 1, 2000 - v2
Checksum:iE6B7B37B2410AA23
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251D → A in AAA63754 (PubMed:7805863).Curated
Sequence conflicti166 – 1661W → L in AAA63754 (PubMed:7805863).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U21552 Genomic DNA. Translation: AAA63754.1.
X99511 mRNA. Translation: CAA67861.1.
AE013599 Genomic DNA. Translation: AAF58119.1.
AY061049 mRNA. Translation: AAL28597.1.
PIRiS51008.
RefSeqiNP_477080.1. NM_057732.4.
UniGeneiDm.640.

Genome annotation databases

EnsemblMetazoaiFBtr0087350; FBpp0086483; FBgn0013762.
GeneIDi36727.
KEGGidme:Dmel_CG8203.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U21552 Genomic DNA. Translation: AAA63754.1.
X99511 mRNA. Translation: CAA67861.1.
AE013599 Genomic DNA. Translation: AAF58119.1.
AY061049 mRNA. Translation: AAL28597.1.
PIRiS51008.
RefSeqiNP_477080.1. NM_057732.4.
UniGeneiDm.640.

3D structure databases

ProteinModelPortaliP48609.
SMRiP48609. Positions 1-288.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi62461. 42 interactions.
DIPiDIP-22131N.
IntActiP48609. 41 interactions.
MINTiMINT-775083.

Proteomic databases

PaxDbiP48609.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0087350; FBpp0086483; FBgn0013762.
GeneIDi36727.
KEGGidme:Dmel_CG8203.

Organism-specific databases

CTDi1020.
FlyBaseiFBgn0013762. Cdk5.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00790000122973.
InParanoidiP48609.
KOiK02090.
OMAiFPPITSW.
OrthoDBiEOG7966H8.
PhylomeDBiP48609.

Enzyme and pathway databases

BRENDAi2.7.11.22. 1994.
ReactomeiREACT_287092. Factors involved in megakaryocyte development and platelet production.
REACT_319268. CRMPs in Sema3A signaling.
SignaLinkiP48609.

Miscellaneous databases

GenomeRNAii36727.
NextBioi800081.
PROiP48609.

Gene expression databases

BgeeiP48609.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.

Entry informationi

Entry nameiCDK5_DROME
AccessioniPrimary (citable) accession number: P48609
Secondary accession number(s): Q94878, Q9V7D8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: December 1, 2000
Last modified: May 27, 2015
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.