CDK9_SCHPO
ID CDK9_SCHPO Reviewed; 591 AA.
AC Q96WV9; O13607;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Probable cyclin-dependent kinase 9;
DE EC=2.7.11.22;
DE EC=2.7.11.23;
DE AltName: Full=Cell division protein kinase 9;
GN Name=cdk9; ORFNames=pi014, SPBC32H8.10;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=10620777;
RX DOI=10.1002/(sici)1097-0061(20000115)16:1<71::aid-yea505>3.0.co;2-5;
RA Machida M., Yamazaki S., Kunihiro S., Tanaka T., Kushida N., Jinno K.,
RA Haikawa Y., Yamazaki J., Yamamoto S., Sekine M., Oguchi A., Nagai Y.,
RA Sakai M., Aoki K., Ogura K., Kudoh Y., Kikuchi H., Zhang M.Q., Yanagida M.;
RT "A 38 kb segment containing the cdc2 gene from the left arm of fission
RT yeast chromosome II: sequence analysis and characterization of the genomic
RT DNA and cDNAs encoded on the segment.";
RL Yeast 16:71-80(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP FUNCTION, INTERACTION WITH PCH1 AND PCT1, AND MUTAGENESIS OF LYS-65;
RP GLU-83; ASP-184 AND THR-212.
RX PubMed=12475973; DOI=10.1074/jbc.m211713200;
RA Pei Y., Schwer B., Shuman S.;
RT "Interactions between fission yeast Cdk9, its cyclin partner Pch1, and mRNA
RT capping enzyme Pct1 suggest an elongation checkpoint for mRNA quality
RT control.";
RL J. Biol. Chem. 278:7180-7188(2003).
RN [4]
RP INTERACTION WITH PCM1.
RX PubMed=16428435; DOI=10.1128/mcb.26.3.777-788.2006;
RA Pei Y., Du H., Singer J., Saint Amour C., Granitto S., Shuman S.,
RA Fisher R.P.;
RT "Cyclin-dependent kinase 9 (Cdk9) of fission yeast is activated by the CDK-
RT activating kinase Csk1, overlaps functionally with the TFIIH-associated
RT kinase Mcs6, and associates with the mRNA cap methyltransferase Pcm1 in
RT vivo.";
RL Mol. Cell. Biol. 26:777-788(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-211; THR-212; THR-565 AND
RP SER-577, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Component of the positive transcription elongation factor b
CC (P-TEFb) which consists of cdk9 and pch1, and which phosphorylates the
CC C-terminal domain (CTD) of RNA polymerase II and spt5.
CC {ECO:0000269|PubMed:12475973}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.22;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-
CC [DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA-
CC COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546,
CC ChEBI:CHEBI:456216; EC=2.7.11.23;
CC -!- ACTIVITY REGULATION: May be activated by autophosphorylation or
CC phosphorylation by a separate activating kinase.
CC -!- SUBUNIT: Interacts with pch1 cyclin via its N-terminal domain. Via its
CC C-terminal domain, interacts with RNA triphosphatase pct1 which is
CC involved in mRNA capping. Interacts also with pcm1.
CC {ECO:0000269|PubMed:12475973, ECO:0000269|PubMed:16428435}.
CC -!- INTERACTION:
CC Q96WV9; O74627: pch1; NbExp=2; IntAct=EBI-443557, EBI-443575;
CC Q96WV9; Q9P6Q6: pct1; NbExp=2; IntAct=EBI-443557, EBI-443547;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA21391.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB004534; BAA21391.2; ALT_INIT; Genomic_DNA.
DR EMBL; CU329671; CAC37500.1; -; Genomic_DNA.
DR RefSeq; NP_595616.1; NM_001021511.2.
DR AlphaFoldDB; Q96WV9; -.
DR SMR; Q96WV9; -.
DR BioGRID; 276771; 30.
DR IntAct; Q96WV9; 2.
DR MINT; Q96WV9; -.
DR STRING; 4896.SPBC32H8.10.1; -.
DR iPTMnet; Q96WV9; -.
DR MaxQB; Q96WV9; -.
DR PaxDb; Q96WV9; -.
DR PRIDE; Q96WV9; -.
DR EnsemblFungi; SPBC32H8.10.1; SPBC32H8.10.1:pep; SPBC32H8.10.
DR GeneID; 2540239; -.
DR KEGG; spo:SPBC32H8.10; -.
DR PomBase; SPBC32H8.10; cdk9.
DR VEuPathDB; FungiDB:SPBC32H8.10; -.
DR eggNOG; KOG0600; Eukaryota.
DR HOGENOM; CLU_000288_181_21_1; -.
DR InParanoid; Q96WV9; -.
DR OMA; YLAPPCQ; -.
DR PhylomeDB; Q96WV9; -.
DR BRENDA; 2.7.11.23; 5613.
DR PRO; PR:Q96WV9; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IPI:PomBase.
DR GO; GO:0008024; C:cyclin/CDK positive transcription elongation factor complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0070691; C:P-TEFb complex; IPI:PomBase.
DR GO; GO:0070693; C:P-TEFb-cap methyltransferase complex; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0030332; F:cyclin binding; IBA:GO_Central.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IDA:PomBase.
DR GO; GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IBA:GO_Central.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IMP:PomBase.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0023052; P:signaling; NAS:PomBase.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..591
FT /note="Probable cyclin-dependent kinase 9"
FT /id="PRO_0000085808"
FT DOMAIN 36..339
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..385
FT /note="Interaction with pch1"
FT REGION 341..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..523
FT /note="Binds to pct1"
FT REGION 549..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..486
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 166
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 42..50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 211
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 212
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 565
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 577
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MUTAGEN 65
FT /note="K->A: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:12475973"
FT MUTAGEN 83
FT /note="E->A: Defective kinase activity."
FT /evidence="ECO:0000269|PubMed:12475973"
FT MUTAGEN 184
FT /note="D->N: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:12475973"
FT MUTAGEN 212
FT /note="T->A: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:12475973"
SQ SEQUENCE 591 AA; 68029 MW; 28DFF6032388E16A CRC64;
MKRSSSVSVE DEKSARRKLD VVPKLHFVGC SHLTDYHLME KLGEGTFGEV YKSQRRKDGK
VYALKRILMH TEKEGFPITA IREIKILKSI KHENIIPLSD MTVVRADKKH RRRGSIYMVT
PYMDHDLSGL LENPSVKFTE PQIKCYMKQL FAGTKYLHDQ LILHRDLKAA NLLIDNHGIL
KIADFGLARV ITEESYANKN PGLPPPNRRE YTGCVVTRWY RSPELLLGER RYTTAIDMWS
VGCIMAEMYK GRPILQGSSD LDQLDKIFRL CGSPTQATMP NWEKLPGCEG VRSFPSHPRT
LETAFFTFGK EMTSLCGAIL TLNPDERLSA SMALEHEYFT TPPYPANPSE LQSYSASHEY
DKRRKREQRD ANSHAFEQTA NGKRQFRFMT RGPSDPWYGI RRPNYNSQPQ YQRGSYNREG
GNMDRSRNVN YQPKRQQNFK PLTSDLPQKN SEFSETNAMN QTSNHSHADG QRYYRPEQDR
SQRLRNPSDY GRQGRQSSQS QQPAWNVSSR YQNNSKVQTT SRASENADTN KTQHNIKYID
SYVPEYSIAR QSANQKTNEQ HPSSTSLHQQ STSDLKSPSF HENSNVDDTP K
