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Q9VT57

- CDK8_DROME

UniProt

Q9VT57 - CDK8_DROME

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Protein

Cyclin-dependent kinase 8

Gene

Cdk8

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

Functioni

Component of the Mediator complex, a coactivator involved in regulated gene transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. May phosphorylate the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAp II), which may inhibit the formation of a transcription initiation complex. Required for leg and eye development and macrochaete specification or differentiation.2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.By similarity1 Publication
ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate.

Cofactori

Magnesium.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei52 – 521ATPBy similarityPROSITE-ProRule annotation
Active sitei151 – 1511Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi27 – 359ATPBy similarityPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB-EC
  3. protein serine/threonine kinase activity Source: FlyBase
  4. RNA polymerase II carboxy-terminal domain kinase activity Source: UniProtKB-EC
  5. RNA polymerase II transcription cofactor activity Source: FlyBase

GO - Biological processi

  1. axon guidance Source: FlyBase
  2. chaeta development Source: FlyBase
  3. G1/S transition of mitotic cell cycle Source: UniProtKB
  4. imaginal disc-derived leg segmentation Source: FlyBase
  5. mitotic cell cycle Source: FlyBase
  6. mitotic G2 DNA damage checkpoint Source: FlyBase
  7. protein phosphorylation Source: UniProtKB
  8. regulation of transcription from RNA polymerase II promoter Source: GOC
  9. sex comb development Source: FlyBase
  10. snRNA 3'-end processing Source: FlyBase
  11. transcription initiation from RNA polymerase II promoter Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Activator, Kinase, Repressor, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_180846. PPARA activates gene expression.
REACT_181685. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
SignaLinkiQ9VT57.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclin-dependent kinase 8 (EC:2.7.11.22, EC:2.7.11.23)
Alternative name(s):
Cell division protein kinase 8
Short name:
DmCdk8
Mediator complex subunit Cdk8
Mediator of RNA polymerase II transcription subunit Cdk8
Gene namesi
Name:Cdk8
ORF Names:CG10572
OrganismiDrosophila melanogaster (Fruit fly)Imported
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0015618. Cdk8.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. mediator complex Source: FlyBase
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 454454Cyclin-dependent kinase 8PRO_0000085798Add
BLAST

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9VT57.

Expressioni

Developmental stagei

Expressed both maternally and zygotically during developmental periods of maximal cell division; most abundant in early embryos and low levels in larvae, pupae and adults.1 Publication

Gene expression databases

BgeeiQ9VT57.
ExpressionAtlasiQ9VT57. differential.

Interactioni

Subunit structurei

Component of the Cdk8 module of the Mediator complex, composed of CycC, Cdk8, kto and skd.

Binary interactionsi

WithEntry#Exp.IntActNotes
CycCP250082EBI-163640,EBI-195485

Protein-protein interaction databases

BioGridi64544. 32 interactions.
DIPiDIP-38574N.
IntActiQ9VT57. 3 interactions.
MINTiMINT-4329200.
STRINGi7227.FBpp0076098.

Structurei

3D structure databases

ProteinModelPortaliQ9VT57.
SMRiQ9VT57. Positions 1-359.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 335315Protein kinasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi328 – 451124Gln-richAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00530000064012.
InParanoidiQ9VT57.
KOiK02208.
OMAiNVITLIR.
OrthoDBiEOG76739K.
PhylomeDBiQ9VT57.

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.

Q9VT57-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDYDFKMKTQ IERTKVEDLF NYEGCKVGRG TYGHVYKAKW KETSDGKEYA
60 70 80 90 100
LKQIDGTGLS MSACREIALL RELKHQNVIT LIRVFLSHND RKVFLLIDYA
110 120 130 140 150
EHDLWHIIKF HRAAKATKKQ VVVPRGMVKS LLYQILDGIH YLHSNWVLHR
160 170 180 190 200
DLKPANILVM GDGNERGRVK IADMGFARLF NAPLKPLADL DPVVVTFWYR
210 220 230 240 250
APELLLGARH YTKAIDIWAI GCIFAELLTS EPIFHCRQED IKTSNPYHHD
260 270 280 290 300
QLDRIFNVMG FPQDKDWEDI KKMPEHHTLT KDFKRSTYST CSLAKYMERH
310 320 330 340 350
KIKPDSKAFH LLQKLLLMDP NKRITSEQAM QDQYFQEEPQ PTQDVFAGCP
360 370 380 390 400
IPYPKREFLT DDDQEDKSDN KRQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ
410 420 430 440 450
MNAEPNAKRV RLSGAGNQQD FHHQQQQQQQ QQQQQQQQQQ QMMFNQQQNF

QRFN
Length:454
Mass (Da):53,682
Last modified:March 1, 2001 - v2
Checksum:iD73F6219E2A03C98
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91T → A in AAB38385. (PubMed:8730095)Curated
Sequence conflicti15 – 151K → N in AAB38385. (PubMed:8730095)Curated
Sequence conflicti37 – 371K → R in AAB38385. (PubMed:8730095)Curated
Sequence conflicti40 – 401W → R in AAB38385. (PubMed:8730095)Curated
Sequence conflicti70 – 701L → W in AAB38385. (PubMed:8730095)Curated
Sequence conflicti185 – 1851K → R in AAM50971. (PubMed:12537569)Curated
Sequence conflicti321 – 3211N → I in AAB38385. (PubMed:8730095)Curated
Sequence conflicti336 – 3361Q → R in AAB38385. (PubMed:8730095)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U33015 mRNA. Translation: AAB38385.1.
AE014296 Genomic DNA. Translation: AAF50197.2.
AY119111 mRNA. Translation: AAM50971.1.
RefSeqiNP_536735.2. NM_080487.4.

Genome annotation databases

EnsemblMetazoaiFBtr0076369; FBpp0076098; FBgn0015618.
GeneIDi39157.
KEGGidme:Dmel_CG10572.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U33015 mRNA. Translation: AAB38385.1 .
AE014296 Genomic DNA. Translation: AAF50197.2 .
AY119111 mRNA. Translation: AAM50971.1 .
RefSeqi NP_536735.2. NM_080487.4.

3D structure databases

ProteinModelPortali Q9VT57.
SMRi Q9VT57. Positions 1-359.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 64544. 32 interactions.
DIPi DIP-38574N.
IntActi Q9VT57. 3 interactions.
MINTi MINT-4329200.
STRINGi 7227.FBpp0076098.

Proteomic databases

PaxDbi Q9VT57.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0076369 ; FBpp0076098 ; FBgn0015618 .
GeneIDi 39157.
KEGGi dme:Dmel_CG10572.

Organism-specific databases

CTDi 1024.
FlyBasei FBgn0015618. Cdk8.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00530000064012.
InParanoidi Q9VT57.
KOi K02208.
OMAi NVITLIR.
OrthoDBi EOG76739K.
PhylomeDBi Q9VT57.

Enzyme and pathway databases

Reactomei REACT_180846. PPARA activates gene expression.
REACT_181685. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
SignaLinki Q9VT57.

Miscellaneous databases

GenomeRNAii 39157.
NextBioi 812240.
PROi Q9VT57.

Gene expression databases

Bgeei Q9VT57.
ExpressionAtlasi Q9VT57. differential.

Family and domain databases

InterProi IPR011009. 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 ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Drosophila Cdk8, a kinase partner of cyclin C that interacts with the large subunit of RNA polymerase II."
    Leclerc V., Tassan J.-P., O'Farrell P.H., Nigg E.A., Leopold P.
    Mol. Biol. Cell 7:505-513(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
    Tissue: Embryo1 Publication.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley1 Publication.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley1 Publication.
    Tissue: Embryo1 Publication.
  5. "Distinct roles for Mediator Cdk8 module subunits in Drosophila development."
    Loncle N., Boube M., Joulia L., Boschiero C., Werner M., Cribbs D.L., Bourbon H.-M.
    EMBO J. 26:1045-1054(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CYCC; KTO AND SKD.

Entry informationi

Entry nameiCDK8_DROME
AccessioniPrimary (citable) accession number: Q9VT57
Secondary accession number(s): P91642, Q8MS41
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 2, 2004
Last sequence update: March 1, 2001
Last modified: October 29, 2014
This is version 115 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