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Q9VP22

- CDK12_DROME

UniProt

Q9VP22 - CDK12_DROME

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
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    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. protein phosphorylation Source: FlyBase
    5. regulation of cell cycle Source: GOC

    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

    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 795-1143.
    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.
    GeneTreeiENSGT00740000114964.
    InParanoidiQ8T9E1.
    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_dom.
    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

    MHASSAAATA LVEYSDVSSE DFSDQEAGDL DADAGKGAGN IKKPKPAPDN     50
    QFSKGRLDAK PDKEGYDNYR SRRAEDSSDP VAAGSRQTSS SEATNPREEP 100
    SQASNTSKDE LWGREIYMSS DSIDTDELEA EMKRQKRKKQ KKEKHKHKSK 150
    KKSKKRKKKR AKSYSSIDSM SDNDINALLD RRYTPPTAPS KSNERTVSAA 200
    PSSFTPHNLK ESSSPATPPP VRRPNTNSNY YGESSLETAN SALGSNLQVT 250
    VTNKQSISNR LRSPPPSSRS SGNGPRFGNS PRTPPPSHYS SSGGGGVGSG 300
    SVVRDSRSSR YVNSPHKEDV SAHHRSSHDH GYQGRYSGAG SSSHDTRKVK 350
    RLSPELDRYN HQPSTPPHKR RKFSDGREVG LGNFEHSRHH SGKYERYSRD 400
    RYSRRSSRSP SVQHSRSRQS PSGGLSSGSN AFRHGGSHKH KYGTTVSSTP 450
    SHTTRTSKRA SGTGTSGDRY SRSPRTSSRY MESSPPSPVG ASGSHHYHHR 500
    RSPRMRQRTR GDSRRRSPSS ASSESSASRS RSPTSRDLKH KREEYIKKIS 550
    ETSLFAELVK DRHKRQKALK EIIERQEENS NSNSNGALTI NDNSSSVDGN 600
    TPNAADGRSA PGSGTPAAAS TTSNGLQALG SKPDLDLNNI PMPNKQNDSV 650
    VSNPASNADV PDSVAQLKQP LLVPPFSASK NNIKPKSLTS LPLPPGMNVL 700
    DLAGARSPSP GQKKESDEKN VTSSGSANKS VLNLPMPPVI PGSEELSGDD 750
    DVIDSPEDFD APAVGTVHGH GGGPGTTRQR PVILNRRDSR NNVRDWGERC 800
    VDVFEMIAQI GEGTYGQVYK ARDHHTNDMV ALKKVRLEHE KEGFPITAVR 850
    EIKILRQLNH RNIVNLHEIV TDKQDAVEFR KDKGSFYLVF EYMDHDLMGL 900
    LESGMVDFNE ENNASIMKQL LDGLNYCHKK NFLHRDIKCS NILMNNRGKV 950
    KLADFGLARL YNADDRERPY TNKVITLWYR PPELLLGEER YGPSIDVWSC 1000
    GCILGELFVK RPLFQANAEM AQLETISKIC GSPVPAVWPN VIKLPLFHTL 1050
    KQKKTHRRRL REDFEFMPAP ALDLLDKMLD LDPDKRITAE DALRSPWLRK 1100
    INPDEMPTPQ LPTWQDCHEL WSKKRRRQMR EQQESLPPTV IASTKYQQHG 1150
    ATMVGDA 1157
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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_141068.3.
    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:
    EMBL
    GenBank
    DDBJ
    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_141068.3.
    NP_730643.1. NM_168912.2.
    UniGenei Dm.1943.

    3D structure databases

    ProteinModelPortali Q9VP22.
    SMRi Q9VP22. Positions 795-1143.
    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 ENSGT00740000114964.
    InParanoidi Q8T9E1.
    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_dom.
    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

    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: October 1, 2014
    This is version 119 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