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Q9VP22

- CDK12_DROME

UniProt

Q9VP22 - CDK12_DROME

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Protein

Cyclin-dependent kinase 12

Gene

Cdk12

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

Functioni

Cyclin-dependent kinase which displays CTD kinase activity: hyperphosphorylates the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit, thereby acting as a key regulator of transcription elongation.1 Publication

Catalytic activityi

ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate.1 Publication
ATP + a protein = ADP + a phosphoprotein.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei833 – 8331ATPPROSITE-ProRule annotation
Active sitei936 – 9361Proton acceptorPROSITE-ProRule annotation
Binding sitei1118 – 11181ATPPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi810 – 8189ATPPROSITE-ProRule annotation
Nucleotide bindingi891 – 8966ATPPROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. neurogenesis Source: FlyBase
  2. phagocytosis Source: FlyBase
  3. phosphorylation of RNA polymerase II C-terminal domain Source: UniProtKB
  4. positive regulation of ERK1 and ERK2 cascade Source: FlyBase
  5. positive regulation of Ras protein signal transduction Source: FlyBase
  6. protein phosphorylation Source: FlyBase
  7. regulation of cell cycle Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

SignaLinkiQ9VP22.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclin-dependent kinase 12 (EC:2.7.11.22, EC:2.7.11.23)
Alternative name(s):
Cell division protein kinase 12
Short name:
dCdk12
Gene namesi
Name:Cdk12
ORF Names:CG7597
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0037093. Cdk12.

Subcellular locationi

Nucleus 1 Publication. Chromosome 1 Publication
Note: Localizes to active genes.

GO - Cellular componenti

  1. nuclear chromosome Source: UniProtKB
  2. nuclear cyclin-dependent protein kinase holoenzyme complex Source: UniProtKB
  3. polytene chromosome Source: FlyBase
  4. polytene chromosome puff Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11571157Cyclin-dependent kinase 12PRO_0000372859Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei106 – 1061Phosphothreonine1 Publication
Modified residuei184 – 1841Phosphothreonine1 Publication
Modified residuei190 – 1901Phosphoserine1 Publication
Modified residuei192 – 1921Phosphoserine1 Publication
Modified residuei217 – 2171Phosphothreonine1 Publication
Modified residuei280 – 2801Phosphoserine1 Publication
Modified residuei283 – 2831Phosphothreonine1 Publication
Modified residuei291 – 2911Phosphoserine1 Publication
Modified residuei301 – 3011Phosphoserine1 Publication
Modified residuei314 – 3141Phosphoserine1 Publication
Modified residuei353 – 3531Phosphoserine1 Publication
Modified residuei365 – 3651Phosphothreonine1 Publication
Modified residuei487 – 4871Phosphoserine1 Publication
Modified residuei492 – 4921Phosphoserine1 Publication
Modified residuei553 – 5531Phosphoserine1 Publication
Modified residuei730 – 7301Phosphoserine1 Publication
Modified residuei743 – 7431Phosphoserine1 Publication
Modified residuei747 – 7471Phosphoserine1 Publication
Modified residuei755 – 7551Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9VP22.
PRIDEiQ9VP22.

Expressioni

Gene expression databases

BgeeiQ9VP22.

Interactioni

Subunit structurei

Interacts with cyclin CycK.1 Publication

Protein-protein interaction databases

BioGridi65630. 1 interaction.
IntActiQ9VP22. 7 interactions.
STRINGi7227.FBpp0078013.

Structurei

3D structure databases

ProteinModelPortaliQ9VP22.
SMRiQ9VP22. Positions 795-1138.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini804 – 1098295Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00770000120511.
InParanoidiQ9VP22.
KOiK08819.
OMAiTISKICG.
OrthoDBiEOG76DTSM.
PhylomeDBiQ9VP22.

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.

Q9VP22-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MHASSAAATA LVEYSDVSSE DFSDQEAGDL DADAGKGAGN IKKPKPAPDN
60 70 80 90 100
QFSKGRLDAK PDKEGYDNYR SRRAEDSSDP VAAGSRQTSS SEATNPREEP
110 120 130 140 150
SQASNTSKDE LWGREIYMSS DSIDTDELEA EMKRQKRKKQ KKEKHKHKSK
160 170 180 190 200
KKSKKRKKKR AKSYSSIDSM SDNDINALLD RRYTPPTAPS KSNERTVSAA
210 220 230 240 250
PSSFTPHNLK ESSSPATPPP VRRPNTNSNY YGESSLETAN SALGSNLQVT
260 270 280 290 300
VTNKQSISNR LRSPPPSSRS SGNGPRFGNS PRTPPPSHYS SSGGGGVGSG
310 320 330 340 350
SVVRDSRSSR YVNSPHKEDV SAHHRSSHDH GYQGRYSGAG SSSHDTRKVK
360 370 380 390 400
RLSPELDRYN HQPSTPPHKR RKFSDGREVG LGNFEHSRHH SGKYERYSRD
410 420 430 440 450
RYSRRSSRSP SVQHSRSRQS PSGGLSSGSN AFRHGGSHKH KYGTTVSSTP
460 470 480 490 500
SHTTRTSKRA SGTGTSGDRY SRSPRTSSRY MESSPPSPVG ASGSHHYHHR
510 520 530 540 550
RSPRMRQRTR GDSRRRSPSS ASSESSASRS RSPTSRDLKH KREEYIKKIS
560 570 580 590 600
ETSLFAELVK DRHKRQKALK EIIERQEENS NSNSNGALTI NDNSSSVDGN
610 620 630 640 650
TPNAADGRSA PGSGTPAAAS TTSNGLQALG SKPDLDLNNI PMPNKQNDSV
660 670 680 690 700
VSNPASNADV PDSVAQLKQP LLVPPFSASK NNIKPKSLTS LPLPPGMNVL
710 720 730 740 750
DLAGARSPSP GQKKESDEKN VTSSGSANKS VLNLPMPPVI PGSEELSGDD
760 770 780 790 800
DVIDSPEDFD APAVGTVHGH GGGPGTTRQR PVILNRRDSR NNVRDWGERC
810 820 830 840 850
VDVFEMIAQI GEGTYGQVYK ARDHHTNDMV ALKKVRLEHE KEGFPITAVR
860 870 880 890 900
EIKILRQLNH RNIVNLHEIV TDKQDAVEFR KDKGSFYLVF EYMDHDLMGL
910 920 930 940 950
LESGMVDFNE ENNASIMKQL LDGLNYCHKK NFLHRDIKCS NILMNNRGKV
960 970 980 990 1000
KLADFGLARL YNADDRERPY TNKVITLWYR PPELLLGEER YGPSIDVWSC
1010 1020 1030 1040 1050
GCILGELFVK RPLFQANAEM AQLETISKIC GSPVPAVWPN VIKLPLFHTL
1060 1070 1080 1090 1100
KQKKTHRRRL REDFEFMPAP ALDLLDKMLD LDPDKRITAE DALRSPWLRK
1110 1120 1130 1140 1150
INPDEMPTPQ LPTWQDCHEL WSKKRRRQMR EQQESLPPTV IASTKYQQHG

ATMVGDA
Length:1,157
Mass (Da):128,333
Last modified:May 1, 2000 - v1
Checksum:iB37ADCFBCAB4E9F3
GO

Sequence cautioni

The sequence AAL28383.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti188 – 1881A → V in AAL39951. (PubMed:12537569)Curated
Sequence conflicti1099 – 10991R → K in AAL28383. (PubMed:12537569)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014296 Genomic DNA. Translation: AAF51738.1.
AE014296 Genomic DNA. Translation: AAN12171.1.
AY060835 mRNA. Translation: AAL28383.1. Different initiation.
AY069806 mRNA. Translation: AAL39951.1.
BT058001 mRNA. Translation: ACM16711.1.
RefSeqiNP_001262167.1. NM_001275238.1.
NP_649325.2. NM_141068.4.
NP_730643.1. NM_168912.2.
UniGeneiDm.1943.

Genome annotation databases

EnsemblMetazoaiFBtr0078357; FBpp0078013; FBgn0037093.
FBtr0078358; FBpp0078014; FBgn0037093.
FBtr0332716; FBpp0304962; FBgn0037093.
GeneIDi40385.
KEGGidme:Dmel_CG7597.
UCSCiCG7597-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014296 Genomic DNA. Translation: AAF51738.1 .
AE014296 Genomic DNA. Translation: AAN12171.1 .
AY060835 mRNA. Translation: AAL28383.1 . Different initiation.
AY069806 mRNA. Translation: AAL39951.1 .
BT058001 mRNA. Translation: ACM16711.1 .
RefSeqi NP_001262167.1. NM_001275238.1.
NP_649325.2. NM_141068.4.
NP_730643.1. NM_168912.2.
UniGenei Dm.1943.

3D structure databases

ProteinModelPortali Q9VP22.
SMRi Q9VP22. Positions 795-1138.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 65630. 1 interaction.
IntActi Q9VP22. 7 interactions.
STRINGi 7227.FBpp0078013.

Proteomic databases

PaxDbi Q9VP22.
PRIDEi Q9VP22.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0078357 ; FBpp0078013 ; FBgn0037093 .
FBtr0078358 ; FBpp0078014 ; FBgn0037093 .
FBtr0332716 ; FBpp0304962 ; FBgn0037093 .
GeneIDi 40385.
KEGGi dme:Dmel_CG7597.
UCSCi CG7597-RA. d. melanogaster.

Organism-specific databases

CTDi 51755.
FlyBasei FBgn0037093. Cdk12.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00770000120511.
InParanoidi Q9VP22.
KOi K08819.
OMAi TISKICG.
OrthoDBi EOG76DTSM.
PhylomeDBi Q9VP22.

Enzyme and pathway databases

SignaLinki Q9VP22.

Miscellaneous databases

GenomeRNAii 40385.
NextBioi 818504.
PROi Q9VP22.

Gene expression databases

Bgeei Q9VP22.

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. "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.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo and Ovary.
  4. Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.
    Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
  5. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-106; THR-184; SER-190; SER-192; THR-217; SER-280; THR-283; SER-291; SER-301; SER-314; SER-353; THR-365; SER-487; SER-492; SER-730; SER-743; SER-747 AND SER-755, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.
  6. "An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells."
    Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.
    Mol. Biosyst. 3:275-286(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-553, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "CDK12 is a transcription elongation-associated CTD kinase, the metazoan ortholog of yeast Ctk1."
    Bartkowiak B., Liu P., Phatnani H.P., Fuda N.J., Cooper J.J., Price D.H., Adelman K., Lis J.T., Greenleaf A.L.
    Genes Dev. 24:2303-2316(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH CYCK.

Entry informationi

Entry nameiCDK12_DROME
AccessioniPrimary (citable) accession number: Q9VP22
Secondary accession number(s): Q8T9E1, Q95SE1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 26, 2009
Last sequence update: May 1, 2000
Last modified: November 26, 2014
This is version 121 of the entry and version 1 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