ID   CDK13_BOVIN             Reviewed;        1512 AA.
AC   E1BB52;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=Cyclin-dependent kinase 13;
DE            EC=2.7.11.22;
DE            EC=2.7.11.23;
DE   AltName: Full=CDC2-related protein kinase 5;
DE   AltName: Full=Cell division cycle 2-like protein kinase 5;
DE   AltName: Full=Cell division protein kinase 13;
GN   Name=CDK13; Synonyms=CDC2L, CDC2L5;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford;
RX   PubMed=19390049; DOI=10.1126/science.1169588;
RG   The bovine genome sequencing and analysis consortium;
RT   "The genome sequence of taurine cattle: a window to ruminant biology and
RT   evolution.";
RL   Science 324:522-528(2009).
CC   -!- FUNCTION: Cyclin-dependent kinase which displays CTD kinase activity
CC       and is required for RNA splicing. Has CTD kinase activity by
CC       hyperphosphorylating the C-terminal heptapeptide repeat domain (CTD) of
CC       the largest RNA polymerase II subunit RPB1, thereby acting as a key
CC       regulator of transcription elongation. Required for RNA splicing,
CC       probably by phosphorylating SRSF1/SF2. Required during hematopoiesis
CC       (By similarity). {ECO:0000250}.
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   -!- 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   -!- SUBUNIT: Interacts with CCNK, CCNL1 and CCNL2. Interacts with C1QBP.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC       protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
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DR   EMBL; AAFC03029660; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAFC03047979; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001192360.1; NM_001205431.1.
DR   AlphaFoldDB; E1BB52; -.
DR   SMR; E1BB52; -.
DR   STRING; 9913.ENSBTAP00000002003; -.
DR   PaxDb; 9913-ENSBTAP00000002003; -.
DR   Ensembl; ENSBTAT00000002003.4; ENSBTAP00000002003.3; ENSBTAG00000001528.4.
DR   GeneID; 511147; -.
DR   KEGG; bta:511147; -.
DR   CTD; 8621; -.
DR   VEuPathDB; HostDB:ENSBTAG00000001528; -.
DR   VGNC; VGNC:27118; CDK13.
DR   eggNOG; KOG0600; Eukaryota.
DR   GeneTree; ENSGT00940000157852; -.
DR   HOGENOM; CLU_004166_3_0_1; -.
DR   InParanoid; E1BB52; -.
DR   OMA; GHMHGQT; -.
DR   TreeFam; TF101060; -.
DR   Reactome; R-BTA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR   Reactome; R-BTA-6798695; Neutrophil degranulation.
DR   Proteomes; UP000009136; Chromosome 4.
DR   Bgee; ENSBTAG00000001528; Expressed in thymus and 109 other cell types or tissues.
DR   GO; GO:0008024; C:cyclin/CDK positive transcription elongation factor complex; IBA:GO_Central.
DR   GO; GO:0019908; C:nuclear cyclin-dependent protein kinase holoenzyme complex; ISS:UniProtKB.
DR   GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0030332; F:cyclin binding; IBA:GO_Central.
DR   GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; ISS:UniProtKB.
DR   GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   GO; GO:0030097; P:hemopoiesis; ISS:UniProtKB.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd07864; STKc_CDK12; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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   PANTHER; PTHR24056; CELL DIVISION PROTEIN KINASE; 1.
DR   PANTHER; PTHR24056:SF459; CYCLIN-DEPENDENT KINASE 13; 1.
DR   Pfam; PF12330; Haspin_kinase; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   Acetylation; ATP-binding; Isopeptide bond; Kinase; mRNA processing;
KW   mRNA splicing; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase;
KW   Ubl conjugation.
FT   CHAIN           1..1512
FT                   /note="Cyclin-dependent kinase 13"
FT                   /id="PRO_0000406956"
FT   DOMAIN          706..999
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          75..547
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          567..597
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          655..677
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1026..1085
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1139..1173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1201..1231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1245..1273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1309..1334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1353..1400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1483..1512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..60
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        190..205
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        218..244
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        246..269
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        270..319
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        328..348
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        363..411
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        412..434
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        435..452
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        490..512
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        570..593
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1053..1085
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1141..1170
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1369..1400
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1483..1498
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        838
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         712..720
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         735
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         316
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14004"
FT   MOD_RES         318
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14004"
FT   MOD_RES         326
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14004"
FT   MOD_RES         341
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14004"
FT   MOD_RES         343
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14004"
FT   MOD_RES         359
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14004"
FT   MOD_RES         361
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14004"
FT   MOD_RES         384
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14004"
FT   MOD_RES         396
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14004"
FT   MOD_RES         398
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14004"
FT   MOD_RES         401
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14004"
FT   MOD_RES         438
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14004"
FT   MOD_RES         440
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14004"
FT   MOD_RES         526
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14004"
FT   MOD_RES         557
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14004"
FT   MOD_RES         589
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14004"
FT   MOD_RES         872
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14004"
FT   MOD_RES         1049
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14004"
FT   MOD_RES         1059
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q69ZA1"
FT   MOD_RES         1246
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14004"
FT   CROSSLNK        520
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q14004"
FT   CROSSLNK        548
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q14004"
SQ   SEQUENCE   1512 AA;  164717 MW;  1DADA7AB73EA471B CRC64;
     MPSSSDTALG GGGGLSWAEK KLEERRKRRR FLSPQQPPLL LPLLQPQLLQ PPPPPPPLLF
     LAAPGTAAAA AAAAAASSSC FSPGPPLEVK RLARGKRRAG GRQKRRRGPR AGQEAEKRRV
     FSLPQPQQDG GGGASSGGGV TPLVEYEDVS SQSEQGLLLG GASAATAATA AGGTGGSGGS
     PASSSGTQRR GEGSERRPRR DRRSSSGRSK DRHREHRRRD GQRGGGEASK SRSRHGHGGE
     ERAEAGKSGS SSSSGGRRKS ASATSSSSSS RKDRDPKAHR SRTKSSKEPP SAYKEPPKAY
     REDKTEPKAY RRRQRSLSPL GGRDDSPVSH RASQSLRNRK SPSPAGGGSS PYSRRLARSP
     SPYSRRRSPS YSRHSSYERG GDVSPSPYSS SSWRRSRSPY SPVIRRSAKS RSRSPYSSRH
     SRSRSRHRLS RSRSRHSSIS PSTLTLKSSL AAELNKNKKA RAAEAARAAE AAKAAEAAKA
     AEAAAKAAKA ASTSTPTKGN TETGASASQT NHVKDVKKLK TEHAPSPSSG GTLKNDKAKT
     KPPLQVTKVD NNLIVDKATK KAVVVGKESK SAATKEEPVS LKEKTKPLTP SIGAKEKEQH
     VALVTSTLPP LPLPPMLPED KDADSLRGNI SVKAVKKEVE KKLRCLLADL PLPPELPGGD
     DLSKSPEEKK TATQLHNKRR PKICGPRFGE IKEKDIDWGK RCVDKFDIIG IIGEGTYGQV
     YKARDKDTGE MVALKKVRLD NEKEGFPITA IREIKILRQL THQSIINMKE IVTDKEDALD
     FKKDKGAFYL VFEYMDHDLM GLLESGLVHF NENHIKSFMR QLMEGLDYCH KKNFLHRDIK
     CSNILLNNRG QIKLADFGLA RLYSSEESRP YTNKVITLWY RPPELLLGEE RYTPAIDVWS
     CGCILGELFT KKPIFQANQE LAQLELISRI CGSPCPAVWP DVIKLPYFNT MKPKKQYRRK
     LREEFVFIPA AALDLFDYML ALDPSKRCTA EQALQCEFLR DVEPSKMPPP DLPLWQDCHE
     LWSKKRRRQK QMGMTDDVST VKAPRKDLSL GMDDSRTSTP QSVLPSSQLK PQGNSNAAPV
     KTGPGQQLNH SELAILLNLL QSKTSVNMAD FVQVLNIKVN SETQQQLNKI NLPAGILATG
     EKQTDPSTPQ QESSKPLGGI QPSQNMQPKV EPDAAQAAVQ SAFAVLLTQL IKAQQSKQKD
     VLLEERENGS GHEAPLQLRP PPEPATPASG QDDLIQHQDM RLLELTPEPD RPRILPPDQR
     PPEPPEPPPV TEEDLDYRTE NQHVPTTSSS LTDPHAGVKA ALLQLLAQHQ PQDDPKRESG
     IDYQAGDTYV PSSDYKDNFG SSSFSSAPYV SNDGLGSASA PPLERRSFMG NSDIQSLDNY
     STTSSHSGGP PQPSAFSESF PSSVAGYGDI YLNTGPMLFS GDKDHRFEYS HGPIAVLANS
     SDPSTGPEST HPLPAKMHNY NYGGSLQETP GGHGLMHGQT WTSPAQGPGY SQGYRGHIST
     SAGRGRGRGL PY
//