Search Results

Overview

Uniprot IDQ9NYV4
Protein NameCyclin-dependent kinase 12
Gene NameCDK12
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
1064 VEEPPPSKTSRKETT
1068 PPSKTSRKETTSGTS
1372 SLVQTLVKNRTFSGS
139 KSQEVSSKSGSMKDR
163 EETDDYGKAQVAKSS
168 YGKAQVAKSSSKESR
414 AAAAAAAKMDGKESK
421 KMDGKESKGSPVFLP
438 ENSSVEAKDSGLESK
445 KDSGLESKKLPRSVK
455 PRSVKLEKSAPDTEL
493 NSEKHLVKDLKAQGT
496 KHLVKDLKAQGTRDS

Function

Cyclin-dependent kinase that phosphorylates the C-terminal domain (CTD) of the large subunit of RNA polymerase II (POLR2A), thereby acting as a key regulator of transcription elongation. Regulates the expression of genes involved in DNA repair and is required for the maintenance of genomic stability. Preferentially phosphorylates 'Ser-5' in CTD repeats that are already phosphorylated at 'Ser-7', but can also phosphorylate 'Ser-2'. Required for RNA splicing, possibly by phosphorylating SRSF1/SF2. Involved in regulation of MAP kinase activity, possibly leading to affect the response to estrogen inhibitors

Protein Sequence

10 MPNSERHGGK 20 KDGSGGASGT 30 LQPSSGGGSS 40 NSRERHRLVS 50 KHKRHKSKHS 60 KDMGLVTPEA 70 ASLGTVIKPL 80 VEYDDISSDS 90 DTFSDDMAFK 100 LDRRENDERR 110 GSDRSDRLHK 120 HRHHQHRRSR 130 DLLKAKQTEK 140 EKSQEVSSKS 150 GSMKDRISGS 160 SKRSNEETDD 170 YGKAQVAKSS 180 SKESRSSKLH 190 KEKTRKEREL 200 KSGHKDRSKS 210 HRKRETPKSY 220 KTVDSPKRRS 230 RSPHRKWSDS 240 SKQDDSPSGA 250 SYGQDYDLSP 260 SRSHTSSNYD 270 SYKKSPGSTS 280 RRQSVSPPYK 290 EPSAYQSSTR 300 SPSPYSRRQR 310 SVSPYSRRRS 320 SSYERSGSYS 330 GRSPSPYGRR 340 RSSSPFLSKR 350 SLSRSPLPSR 360 KSMKSRSRSP 370 AYSRHSSSHS 380 KKKRSSSRSR 390 HSSISPVRLP 400 LNSSLGAELS 410 RKKKERAAAA 420 AAAKMDGKES 430 KGSPVFLPRK 440 ENSSVEAKDS 450 GLESKKLPRS 460 VKLEKSAPDT 470 ELVNVTHLNT 480 EVKNSSDTGK 490 VKLDENSEKH 500 LVKDLKAQGT 510 RDSKPIALKE 520 EIVTPKETET 530 SEKETPPPLP 540 TIASPPPPLP 550 TTTPPPQTPP 560 LPPLPPIPAL 570 PQQPPLPPSQ 580 PAFSQVPASS 590 TSTLPPSTHS 600 KTSAVSSQAN 610 SQPPVQVSVK 620 TQVSVTAAIP 630 HLKTSTLPPL 640 PLPPLLPGDD 650 DMDSPKETLP 660 SKPVKKEKEQ 670 RTRHLLTDLP 680 LPPELPGGDL 690 SPPDSPEPKA 700 ITPPQQPYKK 710 RPKICCPRYG 720 ERRQTESDWG 730 KRCVDKFDII 740 GIIGEGTYGQ 750 VYKAKDKDTG 760 ELVALKKVRL 770 DNEKEGFPIT 780 AIREIKILRQ 790 LIHRSVVNMK 800 EIVTDKQDAL 810 DFKKDKGAFY 820 LVFEYMDHDL 830 MGLLESGLVH 840 FSEDHIKSFM 850 KQLMEGLEYC 860 HKKNFLHRDI 870 KCSNILLNNS 880 GQIKLADFGL 890 ARLYNSEESR 900 PYTNKVITLW 910 YRPPELLLGE 920 ERYTPAIDVW 930 SCGCILGELF 940 TKKPIFQANL 950 ELAQLELISR 960 LCGSPCPAVW 970 PDVIKLPYFN 980 TMKPKKQYRR 990 RLREEFSFIP 1000 SAALDLLDHM 1010 LTLDPSKRCT 1020 AEQTLQSDFL 1030 KDVELSKMAP 1040 PDLPHWQDCH 1050 ELWSKKRRRQ 1060 RQSGVVVEEP 1070 PPSKTSRKET 1080 TSGTSTEPVK 1090 NSSPAPPQPA 1100 PGKVESGAGD 1110 AIGLADITQQ 1120 LNQSELAVLL 1130 NLLQSQTDLS 1140 IPQMAQLLNI 1150 HSNPEMQQQL 1160 EALNQSISAL 1170 TEATSQQQDS 1180 ETMAPEESLK 1190 EAPSAPVILP 1200 SAEQTTLEAS 1210 STPADMQNIL 1220 AVLLSQLMKT 1230 QEPAGSLEEN 1240 NSDKNSGPQG 1250 PRRTPTMPQE 1260 EAAACPPHIL 1270 PPEKRPPEPP 1280 GPPPPPPPPP 1290 LVEGDLSSAP 1300 QELNPAVTAA 1310 LLQLLSQPEA 1320 EPPGHLPHEH 1330 QALRPMEYST 1340 RPRPNRTYGN 1350 TDGPETGFSA 1360 IDTDERNSGP 1370 ALTESLVQTL 1380 VKNRTFSGSL 1390 SHLGESSSYQ 1400 GTGSVQFPGD 1410 QDLRFARVPL 1420 ALHPVVGQPF 1430 LKAEGSSNSV 1440 VHAETKLQNY 1450 GELGPGTTGA 1460 SSSGAGLHWG 1470 GPTQSSAYGK 1480 LYRGPTRVPP 1490 RGGRGRGVPY

Gene Ontology

Classification GO ID Description
Cellular Component GO:0002944 cyclin K-CDK12 complex
Cellular Component GO:0008024 cyclin/CDK positive transcription elongation factor complex
Cellular Component GO:0019908 nuclear cyclin-dependent protein kinase holoenzyme complex
Cellular Component GO:0016607 nuclear speck
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0030332 cyclin binding
Molecular Function GO:0004693 cyclin-dependent protein serine/threonine kinase activity
Molecular Function GO:0004672 protein kinase activity
Molecular Function GO:0019901 protein kinase binding
Molecular Function GO:0106310 protein serine kinase activity
Molecular Function GO:0008353 RNA polymerase II CTD heptapeptide repeat kinase activity
Biological Process GO:0071391 cellular response to estrogen stimulus
Biological Process GO:0006397 mRNA processing
Biological Process GO:0033147 negative regulation of intracellular estrogen receptor signaling pathway
Biological Process GO:0043409 negative regulation of MAPK cascade
Biological Process GO:0045944 positive regulation of transcription by RNA polymerase II
Biological Process GO:0032968 positive regulation of transcription elongation by RNA polymerase II
Biological Process GO:0043405 regulation of MAP kinase activity
Biological Process GO:0008380 RNA splicing
Biological Process GO:0006366 transcription by RNA polymerase II

Reference

[1] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[2] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[3] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[4] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[5] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.