Primary Information |
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BoMiProt ID | Bomi4957 |
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Protein Name | Cyclin-dependent kinase 13/CDC2-related protein kinase 5/Cell division cycle 2-like protein kinase 5/Cell division protein kinase 13 |
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Organism | Bos taurus |
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Uniprot ID | E1BB52 |
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Milk Fraction | Whey |
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Ref Sequence ID | NP_001192360.1 |
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Aminoacid Length | 1512 |
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Molecular Weight | 164717 |
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FASTA Sequence |
Download |
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Gene Name | CDK13/CDC2L/CDC2L5 |
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Gene ID | 511147 |
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Protein Existence Status | reviewed |
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Secondary Information |
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Protein Function | Ser/Thr protein kinases take part in transcription process.Hyper phosphorylationg CTD domain of Pol-II subunit RPB1.Required for mRNA processing. |
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Biochemical Properties | CTD contains 52 heptapeptide repeats of the consensus sequence YSPTSPS on which serine residues at positions 5 and 2 of the heptapeptide repeat is phosphorylated by this kinase.Interacting cyclin subunit K.CdK 13 contains typical kinase fold consisting of an N-terminal lobe (amino acids 695–794), and a C-terminal lobe (amino acids 795–998) as well as a C-terminal extension segment (amino acids 999–1032).. The catalytic protein kinase domain is 294 amino acids long and extends from position 705 to 998 in the polypeptide chain.Within this domain the lysine residue at position 734 represents the ATP binding site and the aspartate residue at position 837 is the proton acceptor site.The nucleotide-binding site extends from amino acids 711–719 (I-G-E-G-T-Y-G-Q-V). |
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PTMs | Acetylation, Isopeptide bond formation, Phosphorylation, Ubl conjugation |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|E1BB52|CDK13_BOVIN Cyclin-dependent kinase 13 OS=Bos taurus OX=9913 GN=CDK13 PE=3 SV=1
MPSSSDTALGGGGGLSWAEKKLEERRKRRRFLSPQQPPLLLPLLQPQLLQPPPPPPPLLF
LAAPGTAAAAAAAAAASSSCFSPGPPLEVKRLARGKRRAGGRQKRRRGPRAGQEAEKRRV
FSLPQPQQDGGGGASSGGGVTPLVEYEDVSSQSEQGLLLGGASAATAATAAGGTGGSGGS
PASSSGTQRRGEGSERRPRRDRRSSSGRSKDRHREHRRRDGQRGGGEASKSRSRHGHGGE
ERAEAGKSGSSSSSGGRRKSASATSSSSSSRKDRDPKAHRSRTKSSKEPPSAYKEPPKAY
REDKTEPKAYRRRQRS*316LS*318PLGGRDDS*326PVSHRASQSLRNRKS*341PS*343PAGGGSSPYSRRLARS*359PS*361PYSRRRSPSYSRHSSYERGGDVS*384PSPYSSSSWRRS*396RS*398PYS*401PVIRRSAKSRSRSPYSSRH
SRSRSRHRLSRSRSRHSS*438IS*440PSTLTLKSSLAAELNKNKKARAAEAARAAEAAKAAEAAKA
AEAAAKAAKAASTSTPTKGNTETGASASQTNHVKDVKKLKTEHAPS*526PSSGGTLKNDKAKT
KPPLQVTKVDNNLIVDKATKKAVVVGKESKSAATKEEPVSLKEKTKPLT*589PSIGAKEKEQH
VALVTSTLPPLPLPPMLPEDKDADSLRGNISVKAVKKEVEKKLRCLLADLPLPPELPGGD
DLSKSPEEKKTATQLHNKRRPKICGPRFGEIKEKDIDWGKRCVDKFDIIGIIGEGTYGQV
YKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKEDALD
FKKDKGAFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIK
CSNILLNNRGQIKLADFGLARLYSSEESRPYT*872NKVITLWYRPPELLLGEERYTPAIDVWS
CGCILGELFTKKPIFQANQELAQLELISRICGSPCPAVWPDVIKLPYFNTMKPKKQYRRK
LREEFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEFLRDVEPSKMPPPDLPLWQDCHE
LWSKKRRRQKQMGMTDDVSTVKAPRKDLS*1049LGMDDSRTST*1059PQSVLPSSQLKPQGNSNAAPV
KTGPGQQLNHSELAILLNLLQSKTSVNMADFVQVLNIKVNSETQQQLNKINLPAGILATG
EKQTDPSTPQQESSKPLGGIQPSQNMQPKVEPDAAQAAVQSAFAVLLTQLIKAQQSKQKD
VLLEERENGSGHEAPLQLRPPPEPATPASGQDDLIQHQDMRLLELT*1246PEPDRPRILPPDQR
PPEPPEPPPVTEEDLDYRTENQHVPTTSSSLTDPHAGVKAALLQLLAQHQPQDDPKRESG
IDYQAGDTYVPSSDYKDNFGSSSFSSAPYVSNDGLGSASAPPLERRSFMGNSDIQSLDNY
STTSSHSGGPPQPSAFSESFPSSVAGYGDIYLNTGPMLFSGDKDHRFEYSHGPIAVLANS
SDPSTGPESTHPLPAKMHNYNYGGSLQETPGGHGLMHGQTWTSPAQGPGYSQGYRGHIST
SAGRGRGRGLPY
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Predicted Disorder Regions | NA |
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DisProt Annotation | |
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TM Helix Prediction | No TM helices |
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Significance of PTMs | Phosphorylated Thr in the kinase T-loop is imp for transcriptional regulation.The formation of three salt bridges between arginine residues from sequentially distant loop sections of the kinase to the phosphorylated threonine of the T-loop is a hallmark of CDK activation. |
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Additional Comments | Mutations in CDK13 have been identified as a novel cause of syndromic intellectual disability.CDK13 is ubiquitously expressed with highest
expression in the cerebellum, tibial nerve, endocervix, uterus, fallopian tube,and ovary. |
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Bibliography | Lu H, Yu D, Hansen AS, Ganguly S, Liu R, Heckert A, Darzacq X, Zhou Q. Phase-separation mechanism for C-terminal hyperphosphorylation of RNA polymerase II. Nature. 2018 Jun;558(7709):318-323. doi: 10.1038/s41586-018-0174-3. Epub 2018 May 30. PMID: 29849146; PMCID: PMC6475116. 2.Hamilton MJ, Suri M. CDK13-related disorder. Adv Genet. 2019;103:163-182. doi: 10.1016/bs.adgen.2018.11.001. Epub 2018 Dec 11. PMID: 30904094. 3.Greifenberg AK, Hönig D, Pilarova K, Düster R, Bartholomeeusen K, Bösken CA, Anand K, Blazek D, Geyer M. Structural and Functional Analysis of the Cdk13/Cyclin K Complex. Cell Rep. 2016 Jan 12;14(2):320-31. doi: 10.1016/j.celrep.2015.12.025. Epub 2015 Dec 31. PMID: 26748711. |