Tag | Content |
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CPLM ID | CPLM-012964 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Cyclin-dependent kinase 12 |
Protein Synonyms/Alias | Cdc2-related kinase, arginine/serine-rich; CrkRS; Cell division cycle 2-related protein kinase 7; CDC2-related protein kinase 7; Cell division protein kinase 12; Protein kinase for splicing component |
Gene Name | Cdk12 |
Gene Synonyms/Alias | Crk7; Crkrs; Pksc |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
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501 | AQGTKDTKPVALKEV | acetylation | [1] | 1464 | GPAQSFGKPYRGAAR | acetylation | [1] |
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Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
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. Involved in regulation of MAP kinase activity, possibly leading to affect the response to estrogn inhibitors (By similarity). Required for RNA splicing, possibly by phosphorylating SRSF1/SF2. |
Sequence Annotation | DOMAIN 723 1016 Protein kinase. NP_BIND 729 737 ATP (By similarity). ACT_SITE 855 855 Proton acceptor (By similarity). BINDING 752 752 ATP (By similarity). MOD_RES 57 57 Phosphothreonine (By similarity). MOD_RES 73 73 Phosphotyrosine (By similarity). MOD_RES 235 235 Phosphoserine (By similarity). MOD_RES 248 248 Phosphoserine (By similarity). MOD_RES 273 273 Phosphoserine (By similarity). MOD_RES 275 275 Phosphoserine (By similarity). MOD_RES 278 278 Phosphotyrosine (By similarity). MOD_RES 300 300 Phosphoserine (By similarity). MOD_RES 302 302 Phosphoserine (By similarity). MOD_RES 309 309 Phosphoserine (By similarity). MOD_RES 311 311 Phosphoserine (By similarity). MOD_RES 317 317 Phosphoserine (By similarity). MOD_RES 318 318 Phosphotyrosine (By similarity). MOD_RES 322 322 Phosphoserine (By similarity). MOD_RES 324 324 Phosphoserine (By similarity). MOD_RES 331 331 Phosphoserine (By similarity). MOD_RES 332 332 Phosphoserine (By similarity). MOD_RES 333 333 Phosphoserine (By similarity). MOD_RES 337 337 Phosphoserine (By similarity). MOD_RES 344 344 Phosphoserine (By similarity). MOD_RES 382 382 Phosphoserine (By similarity). MOD_RES 384 384 Phosphoserine (By similarity). MOD_RES 399 399 Phosphoserine (By similarity). MOD_RES 419 419 Phosphoserine (By similarity). MOD_RES 422 422 Phosphoserine (By similarity). MOD_RES 511 511 Phosphothreonine (By similarity). MOD_RES 677 677 Phosphoserine (By similarity). MOD_RES 681 681 Phosphoserine (By similarity). MOD_RES 688 688 Phosphothreonine (By similarity). MOD_RES 889 889 Phosphothreonine (By similarity). MOD_RES 1049 1049 Phosphoserine (By similarity). MOD_RES 1079 1079 Phosphoserine (By similarity). MOD_RES 1240 1240 Phosphothreonine (By similarity). |
Keyword | Alternative splicing; ATP-binding; Complete proteome; Kinase; mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Serine/threonine-protein kinase; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1484 AA |
Protein Sequence | MPNSERHGGK KDGSGGASGT SQPSSGGGSS NSRERHRLVS KHKRHKSKHS KDMGLVTPEA 60 ASLGTIIKPL VEYDDISSDS DTFSDDMAFK SDRRENDERR GTDRSDRLHR HRHHQHRRSR 120 DLLKTKQTEK EKNQEVSKSG SMKDRLSGSS KRSVEGNDDY GKAQLSKSSS KESRSSKMHK 180 EKTRKERELK SGHKDRSKSH RKRETPKSYK TVDSPKRRSR SPHRKWSDSS KQDDSPSGAS 240 YGQDYDLSPP RSHTSSNYDS YKKSPGSTSR RQSISPPYKE PSAYQSSTRS PSPYSRRQRS 300 VSPYSRRRSS SYERSGSYSG RSPSPYGRRR SSSPFLSKRS LSRSPISSRK SMKSRSRSPA 360 YSRHSSSHSK KKRSGSRSRH SSISPVRLPL NSSLGAELSR KKKERAAAAA AAKLDGKESK 420 GSPIILPKKE KFEVKESGLE SKKLPRGIKS EKSTPDTELV NVAHSNTEVK NCLDTGKVKL 480 DENLQKHPVK DLKAQGTKDT KPVALKEVIV TSKETETSEK EALPPLPTIT SPPPLPSTTP 540 PPQTPPLPPL PPLPAVPLQP PLPPPQPPFS QVPVSNTSTL PSSPHPRTST LSSQTNSQPL 600 VQVSMKTQLS VTAAIPHLKT STLPPLPLPP LLPGDDDMDS PKEMLPSKPA KKEKEQRTRH 660 LLTDLPLPPE LPGGDPSPPD SPEPKAITPP QQPYKKRPKI CCPRYGERRQ TESDWGKRCV 720 DKFDIIGIIG EGTYGQVYKA KDKDTGELVA LKKVRLDNEK EGFPITAIRE IKILRQLVHQ 780 SVVNMKEIVT DKQDALDFKK DKGAFYLVFE YMDHDLMGLL ESGLVHFSED HIKSFMKQLM 840 EGLDYCHKKN FLHRDIKCSN ILLNNSGQIK LADFGLARLY NSEESRPYTN KVITLWYRPP 900 ELLLGEERYT PAIDVWSCGC ILGELFTKKP IFQANLELAQ LELISRLCGS PCPAVWPDVI 960 KLPYFNTMKP KKQYRRRLRE EFSFIPSAAL DLLDHMLTLD PSKRCTAEQT LQSDFLKDVE 1020 LSKMAPPDLP HWQDCHELWS KKRRRQRQSG IVIEEQPPSK ASRKETTSGT AAEPVKNSSP 1080 APPQPAPVKA EPGPGDAVGL GDITQQLNQS ELAVLLNLLQ SQTDLSIPQM AQLLNIHSNP 1140 EMQQQLEALN QSISALTEAS SQQQDSESIA PEESLKEVPS VSVVLPPAEQ TTPEASNTPA 1200 DMQNMLAVLL SQLMKTQEPA GNLEENTSDK NSGPQGPRRT PTMPQEEAAA CPPHILPPEK 1260 RPPEPPGPPP PPPPPPLVEG DLSSAPQELN PAVTAALLQL LSQPEAEPPG HLPHEHQALR 1320 PMEYSTRSHP NRTYGNTDGP ETGFSATDTD ERSSGPALTE SLVQTLVKNR TFSGSVSHLG 1380 ESNSYQGTGS VQFPGDQDLR FTRVPLALHS VVGQPFLKSE GNSNSVVHAE TKLQNYGELG 1440 PGTTGANSSG TTLQWGGPAQ SFGKPYRGAA RVPPRGGRGR GVPY 1484 |
Gene Ontology | GO:0002944; C:cyclin K-CDK12 complex; IEA:Compara. GO:0019908; C:nuclear cyclin-dependent protein kinase holoenzyme complex; IDA:UniProtKB. GO:0016607; C:nuclear speck; IDA:UniProtKB. GO:0005730; C:nucleolus; IEA:Compara. 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; ISS:UniProtKB. GO:0006397; P:mRNA processing; IEA:UniProtKB-KW. GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; ISS:UniProtKB. GO:0046777; P:protein autophosphorylation; IEA:Compara. GO:0043405; P:regulation of MAP kinase activity; ISS:UniProtKB. GO:0008380; P:RNA splicing; IMP:UniProtKB. |
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