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Q96WV9

- CDK9_SCHPO

UniProt

Q96WV9 - CDK9_SCHPO

Protein

Probable cyclin-dependent kinase 9

Gene

cdk9

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

    Component of the positive transcription elongation factor b (P-TEFb) which consists of cdk9 and pch1, and which phosphorylates the C-terminal domain (CTD) of RNA polymerase II and spt5.1 Publication

    Catalytic activityi

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

    Enzyme regulationi

    May be activated by autophosphorylation or phosphorylation by a separate activating kinase.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei65 – 651ATPPROSITE-ProRule annotation
    Active sitei166 – 1661Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi42 – 509ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. phosphorylation of RNA polymerase II C-terminal domain Source: PomBase
    2. protein phosphorylation Source: UniProtKB
    3. regulation of cell cycle Source: GOC
    4. regulation of transcription elongation from RNA polymerase II promoter Source: PomBase
    5. transcription from RNA polymerase I promoter Source: PomBase

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable cyclin-dependent kinase 9 (EC:2.7.11.22, EC:2.7.11.23)
    Alternative name(s):
    Cell division protein kinase 9
    Gene namesi
    Name:cdk9
    ORF Names:pi014, SPBC32H8.10
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome II

    Organism-specific databases

    PomBaseiSPBC32H8.10.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleus Source: PomBase
    2. positive transcription elongation factor complex b Source: PomBase
    3. P-TEFb-cap methyltransferase complex Source: PomBase

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi65 – 651K → A: Abolishes activity. 1 Publication
    Mutagenesisi83 – 831E → A: Defective kinase activity. 1 Publication
    Mutagenesisi184 – 1841D → N: Abolishes activity. 1 Publication
    Mutagenesisi212 – 2121T → A: Abolishes activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 591591Probable cyclin-dependent kinase 9PRO_0000085808Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei211 – 2111Phosphotyrosine1 Publication
    Modified residuei212 – 2121Phosphothreonine1 Publication
    Modified residuei565 – 5651Phosphothreonine1 Publication
    Modified residuei577 – 5771Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ96WV9.
    PRIDEiQ96WV9.

    Interactioni

    Subunit structurei

    Interacts with pch1 cyclin via its N-terminal domain. Via its C-terminal domain, interacts with RNA triphosphatase pct1 which is involved in mRNA capping. Interacts also with pcm1.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    pch1O746272EBI-443557,EBI-443575
    pct1Q9P6Q62EBI-443557,EBI-443547

    Protein-protein interaction databases

    BioGridi276771. 18 interactions.
    IntActiQ96WV9. 2 interactions.
    MINTiMINT-253408.
    STRINGi4896.SPBC32H8.10-1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ96WV9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini36 – 339304Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 385385Interacts with pch1Add
    BLAST
    Regioni442 – 52382Binds to pct1Add
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    KOiK15562.
    OMAiCHSNERM.
    OrthoDBiEOG7K3TWD.
    PhylomeDBiQ96WV9.

    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.

    Q96WV9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKRSSSVSVE DEKSARRKLD VVPKLHFVGC SHLTDYHLME KLGEGTFGEV    50
    YKSQRRKDGK VYALKRILMH TEKEGFPITA IREIKILKSI KHENIIPLSD 100
    MTVVRADKKH RRRGSIYMVT PYMDHDLSGL LENPSVKFTE PQIKCYMKQL 150
    FAGTKYLHDQ LILHRDLKAA NLLIDNHGIL KIADFGLARV ITEESYANKN 200
    PGLPPPNRRE YTGCVVTRWY RSPELLLGER RYTTAIDMWS VGCIMAEMYK 250
    GRPILQGSSD LDQLDKIFRL CGSPTQATMP NWEKLPGCEG VRSFPSHPRT 300
    LETAFFTFGK EMTSLCGAIL TLNPDERLSA SMALEHEYFT TPPYPANPSE 350
    LQSYSASHEY DKRRKREQRD ANSHAFEQTA NGKRQFRFMT RGPSDPWYGI 400
    RRPNYNSQPQ YQRGSYNREG GNMDRSRNVN YQPKRQQNFK PLTSDLPQKN 450
    SEFSETNAMN QTSNHSHADG QRYYRPEQDR SQRLRNPSDY GRQGRQSSQS 500
    QQPAWNVSSR YQNNSKVQTT SRASENADTN KTQHNIKYID SYVPEYSIAR 550
    QSANQKTNEQ HPSSTSLHQQ STSDLKSPSF HENSNVDDTP K 591
    Length:591
    Mass (Da):68,029
    Last modified:December 1, 2001 - v1
    Checksum:i28DFF6032388E16A
    GO

    Sequence cautioni

    The sequence BAA21391.2 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB004534 Genomic DNA. Translation: BAA21391.2. Different initiation.
    CU329671 Genomic DNA. Translation: CAC37500.1.
    RefSeqiNP_595616.1. NM_001021511.2.

    Genome annotation databases

    EnsemblFungiiSPBC32H8.10.1; SPBC32H8.10.1:pep; SPBC32H8.10.
    GeneIDi2540239.
    KEGGispo:SPBC32H8.10.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB004534 Genomic DNA. Translation: BAA21391.2 . Different initiation.
    CU329671 Genomic DNA. Translation: CAC37500.1 .
    RefSeqi NP_595616.1. NM_001021511.2.

    3D structure databases

    ProteinModelPortali Q96WV9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 276771. 18 interactions.
    IntActi Q96WV9. 2 interactions.
    MINTi MINT-253408.
    STRINGi 4896.SPBC32H8.10-1.

    Proteomic databases

    MaxQBi Q96WV9.
    PRIDEi Q96WV9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPBC32H8.10.1 ; SPBC32H8.10.1:pep ; SPBC32H8.10 .
    GeneIDi 2540239.
    KEGGi spo:SPBC32H8.10.

    Organism-specific databases

    PomBasei SPBC32H8.10.

    Phylogenomic databases

    eggNOGi COG0515.
    KOi K15562.
    OMAi CHSNERM.
    OrthoDBi EOG7K3TWD.
    PhylomeDBi Q96WV9.

    Miscellaneous databases

    NextBioi 20801370.

    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. "A 38 kb segment containing the cdc2 gene from the left arm of fission yeast chromosome II: sequence analysis and characterization of the genomic DNA and cDNAs encoded on the segment."
      Machida M., Yamazaki S., Kunihiro S., Tanaka T., Kushida N., Jinno K., Haikawa Y., Yamazaki J., Yamamoto S., Sekine M., Oguchi A., Nagai Y., Sakai M., Aoki K., Ogura K., Kudoh Y., Kikuchi H., Zhang M.Q., Yanagida M.
      Yeast 16:71-80(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 972 / ATCC 24843.
    2. "The genome sequence of Schizosaccharomyces pombe."
      Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
      , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
      Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 972 / ATCC 24843.
    3. "Interactions between fission yeast Cdk9, its cyclin partner Pch1, and mRNA capping enzyme Pct1 suggest an elongation checkpoint for mRNA quality control."
      Pei Y., Schwer B., Shuman S.
      J. Biol. Chem. 278:7180-7188(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PCH1 AND PCT1, MUTAGENESIS OF LYS-65; GLU-83; ASP-184 AND THR-212.
    4. "Cyclin-dependent kinase 9 (Cdk9) of fission yeast is activated by the CDK-activating kinase Csk1, overlaps functionally with the TFIIH-associated kinase Mcs6, and associates with the mRNA cap methyltransferase Pcm1 in vivo."
      Pei Y., Du H., Singer J., Saint Amour C., Granitto S., Shuman S., Fisher R.P.
      Mol. Cell. Biol. 26:777-788(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PCM1.
    5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-211; THR-212; THR-565 AND SER-577, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiCDK9_SCHPO
    AccessioniPrimary (citable) accession number: Q96WV9
    Secondary accession number(s): O13607
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 27, 2003
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 105 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Schizosaccharomyces pombe
      Schizosaccharomyces pombe: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3