CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012230
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cyclin-dependent kinase 13 
Protein Synonyms/Alias
 CDC2-related protein kinase 5; Cell division cycle 2-like protein kinase 5; Cell division protein kinase 13; hCDK13; Cholinesterase-related cell division controller 
Gene Name
 CDK13 
Gene Synonyms/Alias
 CDC2L; CDC2L5; CHED; KIAA1791 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
556ENNLIVDKATKKAVIacetylation[1]
943AVWPDVIKLPYFNTMubiquitination[2]
1199KAQQSKQKDVLLEERubiquitination[3]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961] 
Functional Description
 Cyclin-dependent kinase which displays CTD kinase activity and is required for RNA splicing. Has CTD kinase activity by hyperphosphorylating the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit RPB1, thereby acting as a key regulator of transcription elongation. Required for RNA splicing, probably by phosphorylating SRSF1/SF2. Required during hematopoiesis. In case of infection by HIV-1 virus, interacts with HIV-1 Tat protein acetylated at 'Lys-50' and 'Lys- 51', thereby increasing HIV-1 mRNA splicing and promoting the production of the doubly spliced HIV-1 protein Nef. 
Sequence Annotation
 DOMAIN 705 998 Protein kinase.
 NP_BIND 711 719 ATP (By similarity).
 ACT_SITE 837 837 Proton acceptor (By similarity).
 BINDING 734 734 ATP (By similarity).
 MOD_RES 315 315 Phosphoserine.
 MOD_RES 317 317 Phosphoserine.
 MOD_RES 325 325 Phosphoserine.
 MOD_RES 340 340 Phosphoserine.
 MOD_RES 342 342 Phosphoserine.
 MOD_RES 383 383 Phosphoserine.
 MOD_RES 395 395 Phosphoserine.
 MOD_RES 397 397 Phosphoserine.
 MOD_RES 400 400 Phosphoserine.
 MOD_RES 409 409 Phosphoserine (By similarity).
 MOD_RES 436 436 Phosphoserine (By similarity).
 MOD_RES 437 437 Phosphoserine.
 MOD_RES 439 439 Phosphoserine.
 MOD_RES 525 525 Phosphoserine.
 MOD_RES 556 556 N6-acetyllysine.
 MOD_RES 871 871 Phosphothreonine.
 MOD_RES 1048 1048 Phosphoserine.
 MOD_RES 1246 1246 Phosphothreonine.  
Keyword
 Acetylation; Alternative splicing; ATP-binding; Complete proteome; Host-virus interaction; Kinase; mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; RNA editing; Serine/threonine-protein kinase; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1512 AA 
Protein Sequence
MPSSSDTALG GGGGLSWAEK KLEERRKRRR FLSPQQPPLL LPLLQPQLLQ PPPPPPPLLF 60
LAAPGTAAAA AAAAAASSSC FSPGPPLEVK RLARGKRRAG GRQKRRRGPR AGQEAEKRRV 120
FSLPQPQQDG GGGASSGGGV TPLVEYEDVS SQSEQGLLLG GASAATAATA AGGTGGSGGS 180
PASSSGTQRR GEGSERRPRR DRRSSSGRSK ERHREHRRRD GQRGGSEASK SRSRHSHSGE 240
ERAEVAKSGS SSSSGGRRKS ASATSSSSSS RKDRDSKAHR SRTKSSKEPP SAYKEPPKAY 300
REDKTEPKAY RRRRSLSPLG GRDDSPVSHR ASQSLRSRKS PSPAGGGSSP YSRRLPRSPS 360
PYSRRRSPSY SRHSSYERGG DVSPSPYSSS SWRRSRSPYS PVLRRSGKSR SRSPYSSRHS 420
RSRSRHRLSR SRSRHSSISP STLTLKSSLA AELNKNKKAR AAEAARAAEA AKAAEATKAA 480
EAAAKAAKAS NTSTPTKGNT ETSASASQTN HVKDVKKIKI EHAPSPSSGG TLKNDKAKTK 540
PPLQVTKVEN NLIVDKATKK AVIVGKESKS AATKEESVSL KEKTKPLTPS IGAKEKEQHV 600
ALVTSTLPPL PLPPMLPEDK EADSLRGNIS VKAVKKEVEK KLRCLLADLP LPPELPGGDD 660
LSKSPEEKKT ATQLHSKRRP KICGPRYGET KEKDIDWGKR CVDKFDIIGI IGEGTYGQVY 720
KARDKDTGEM VALKKVRLDN EKEGFPITAI REIKILRQLT HQSIINMKEI VTDKEDALDF 780
KKDKGAFYLV FEYMDHDLMG LLESGLVHFN ENHIKSFMRQ LMEGLDYCHK KNFLHRDIKC 840
SNILLNNRGQ IKLADFGLAR LYSSEESRPY TNKVITLWYR PPELLLGEER YTPAIDVWSC 900
GCILGELFTK KPIFQANQEL AQLELISRIC GSPCPAVWPD VIKLPYFNTM KPKKQYRRKL 960
REEFVFIPAA ALDLFDYMLA LDPSKRCTAE QALQCEFLRD VEPSKMPPPD LPLWQDCHEL 1020
WSKKRRRQKQ MGMTDDVSTI KAPRKDLSLG LDDSRTNTPQ GVLPSSQLKS QGSSNVAPVK 1080
TGPGQHLNHS ELAILLNLLQ SKTSVNMADF VQVLNIKVNS ETQQQLNKIN LPAGILATGE 1140
KQTDPSTPQQ ESSKPLGGIQ PSSQTIQPKV ETDAAQAAVQ SAFAVLLTQL IKAQQSKQKD 1200
VLLEERENGS GHEASLQLRP PPEPSTPVSG QDDLIQHQDM RILELTPEPD RPRILPPDQR 1260
PPEPPEPPPV TEEDLDYRTE NQHVPTTSSS LTDPHAGVKA ALLQLLAQHQ PQDDPKREGG 1320
IDYQAGDTYV STSDYKDNFG SSSFSSAPYV SNDGLGSSSA PPLERRSFIG NSDIQSLDNY 1380
STASSHSGGP PQPSAFSESF PSSVAGYGDI YLNAGPMLFS GDKDHRFEYS HGPIAVLANS 1440
SDPSTGPEST HPLPAKMHNY NYGGNLQENP SGPSLMHGQT WTSPAQGPGY SQGYRGHIST 1500
STGRGRGRGL PY 1512 
Gene Ontology
 GO:0002945; C:cyclin K-CDK13 complex; IPI:MGI.
 GO:0019908; C:nuclear cyclin-dependent protein kinase holoenzyme complex; ISS:UniProtKB.
 GO:0016607; C:nuclear speck; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IEA:EC.
 GO:0008353; F:RNA polymerase II carboxy-terminal domain kinase activity; IDA:UniProtKB.
 GO:0000380; P:alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
 GO:0030097; P:hemopoiesis; IMP:UniProtKB.
 GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IDA:UniProtKB.
 GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
 GO:0007088; P:regulation of mitosis; TAS:ProtInc.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
Interpro
 IPR011009; Kinase-like_dom.
 IPR000719; Prot_kinase_cat_dom.
 IPR017441; Protein_kinase_ATP_BS.
 IPR002290; Ser/Thr_dual-sp_kinase_dom.
 IPR008271; Ser/Thr_kinase_AS. 
Pfam
 PF00069; Pkinase 
SMART
 SM00220; S_TKc 
PROSITE
 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM
 PS00108; PROTEIN_KINASE_ST 
PRINTS