CDK13_BOVIN
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 03-AUG-2022, entry version 78.
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}.
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; 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; E1BB52; -.
DR PRIDE; E1BB52; -.
DR Ensembl; ENSBTAT00000002003; ENSBTAP00000002003; ENSBTAG00000001528.
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; REAPQAY; -.
DR OrthoDB; 925637at2759; -.
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 tissues.
DR GO; GO:0002945; C:cyclin K-CDK13 complex; IEA:Ensembl.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR GO; GO:0008024; C:cyclin/CDK positive transcription elongation factor complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
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; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
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:2000737; P:negative regulation of stem cell differentiation; IEA:Ensembl.
DR GO; GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; ISS:UniProtKB.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0009966; P:regulation of signal transduction; IEA:Ensembl.
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 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
