| Tag | Content |
|---|
| CPLM ID | CPLM-022405 |
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; hCDK12 |
Gene Name | CDK12 |
Gene Synonyms/Alias | CRK7; CRKRS; KIAA0904 |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 504 | AQGTRDSKPIALKEE | acetylation | [1] | | 1021 | TLQSDFLKDVELSKM | ubiquitination | [2] |
|
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] 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, possibly by phosphorylating SRSF1/SF2. Involved in regulation of MAP kinase activity, possibly leading to affect the response to estrogn inhibitors. |
Sequence Annotation | DOMAIN 727 1020 Protein kinase.
NP_BIND 733 741 ATP (By similarity).
ACT_SITE 859 859 Proton acceptor (By similarity).
BINDING 756 756 ATP (By similarity).
MOD_RES 57 57 Phosphothreonine.
MOD_RES 73 73 Phosphotyrosine.
MOD_RES 236 236 Phosphoserine.
MOD_RES 249 249 Phosphoserine.
MOD_RES 274 274 Phosphoserine.
MOD_RES 276 276 Phosphoserine.
MOD_RES 279 279 Phosphotyrosine (By similarity).
MOD_RES 301 301 Phosphoserine.
MOD_RES 303 303 Phosphoserine.
MOD_RES 310 310 Phosphoserine.
MOD_RES 312 312 Phosphoserine.
MOD_RES 318 318 Phosphoserine.
MOD_RES 319 319 Phosphotyrosine (By similarity).
MOD_RES 323 323 Phosphoserine.
MOD_RES 325 325 Phosphoserine.
MOD_RES 332 332 Phosphoserine.
MOD_RES 333 333 Phosphoserine.
MOD_RES 334 334 Phosphoserine.
MOD_RES 338 338 Phosphoserine.
MOD_RES 345 345 Phosphoserine.
MOD_RES 383 383 Phosphoserine.
MOD_RES 385 385 Phosphoserine.
MOD_RES 400 400 Phosphoserine.
MOD_RES 420 420 Phosphoserine.
MOD_RES 423 423 Phosphoserine.
MOD_RES 514 514 Phosphothreonine.
MOD_RES 681 681 Phosphoserine.
MOD_RES 685 685 Phosphoserine.
MOD_RES 692 692 Phosphothreonine.
MOD_RES 893 893 Phosphothreonine.
MOD_RES 1053 1053 Phosphoserine.
MOD_RES 1083 1083 Phosphoserine.
MOD_RES 1244 1244 Phosphothreonine. |
Keyword | Alternative splicing; ATP-binding; Chromosomal rearrangement; Complete proteome; Kinase; mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Serine/threonine-protein kinase; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1490 AA |
Protein Sequence | MPNSERHGGK KDGSGGASGT LQPSSGGGSS NSRERHRLVS KHKRHKSKHS KDMGLVTPEA 60
ASLGTVIKPL VEYDDISSDS DTFSDDMAFK LDRRENDERR GSDRSDRLHK HRHHQHRRSR 120
DLLKAKQTEK EKSQEVSSKS GSMKDRISGS SKRSNEETDD YGKAQVAKSS SKESRSSKLH 180
KEKTRKEREL KSGHKDRSKS HRKRETPKSY KTVDSPKRRS RSPHRKWSDS SKQDDSPSGA 240
SYGQDYDLSP SRSHTSSNYD SYKKSPGSTS RRQSVSPPYK EPSAYQSSTR SPSPYSRRQR 300
SVSPYSRRRS SSYERSGSYS GRSPSPYGRR RSSSPFLSKR SLSRSPLPSR KSMKSRSRSP 360
AYSRHSSSHS KKKRSSSRSR HSSISPVRLP LNSSLGAELS RKKKERAAAA AAAKMDGKES 420
KGSPVFLPRK ENSSVEAKDS GLESKKLPRS VKLEKSAPDT ELVNVTHLNT EVKNSSDTGK 480
VKLDENSEKH LVKDLKAQGT RDSKPIALKE EIVTPKETET SEKETPPPLP TIASPPPPLP 540
TTTPPPQTPP LPPLPPIPAL PQQPPLPPSQ PAFSQVPASS TSTLPPSTHS KTSAVSSQAN 600
SQPPVQVSVK TQVSVTAAIP HLKTSTLPPL PLPPLLPGDD DMDSPKETLP SKPVKKEKEQ 660
RTRHLLTDLP LPPELPGGDL SPPDSPEPKA ITPPQQPYKK RPKICCPRYG ERRQTESDWG 720
KRCVDKFDII GIIGEGTYGQ VYKAKDKDTG ELVALKKVRL DNEKEGFPIT AIREIKILRQ 780
LIHRSVVNMK EIVTDKQDAL DFKKDKGAFY LVFEYMDHDL MGLLESGLVH FSEDHIKSFM 840
KQLMEGLEYC HKKNFLHRDI KCSNILLNNS GQIKLADFGL ARLYNSEESR PYTNKVITLW 900
YRPPELLLGE ERYTPAIDVW SCGCILGELF TKKPIFQANL ELAQLELISR LCGSPCPAVW 960
PDVIKLPYFN TMKPKKQYRR RLREEFSFIP SAALDLLDHM LTLDPSKRCT AEQTLQSDFL 1020
KDVELSKMAP PDLPHWQDCH ELWSKKRRRQ RQSGVVVEEP PPSKTSRKET TSGTSTEPVK 1080
NSSPAPPQPA PGKVESGAGD AIGLADITQQ LNQSELAVLL NLLQSQTDLS IPQMAQLLNI 1140
HSNPEMQQQL EALNQSISAL TEATSQQQDS ETMAPEESLK EAPSAPVILP SAEQTTLEAS 1200
STPADMQNIL AVLLSQLMKT QEPAGSLEEN NSDKNSGPQG PRRTPTMPQE EAAACPPHIL 1260
PPEKRPPEPP GPPPPPPPPP LVEGDLSSAP QELNPAVTAA LLQLLSQPEA EPPGHLPHEH 1320
QALRPMEYST RPRPNRTYGN TDGPETGFSA IDTDERNSGP ALTESLVQTL VKNRTFSGSL 1380
SHLGESSSYQ GTGSVQFPGD QDLRFARVPL ALHPVVGQPF LKAEGSSNSV VHAETKLQNY 1440
GELGPGTTGA SSSGAGLHWG GPTQSSAYGK LYRGPTRVPP RGGRGRGVPY 1490 |
Gene Ontology | GO:0002944; C:cyclin K-CDK12 complex; IPI:MGI. GO:0019908; C:nuclear cyclin-dependent protein kinase holoenzyme complex; ISS:UniProtKB. GO:0016607; C:nuclear speck; IDA:UniProtKB. GO:0005730; C:nucleolus; IDA:HPA. 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; IMP:UniProtKB. GO:0006397; P:mRNA processing; IEA:UniProtKB-KW. GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IMP:UniProtKB. GO:0046777; P:protein autophosphorylation; IDA:HGNC. GO:0043405; P:regulation of MAP kinase activity; IMP:UniProtKB. GO:0008380; P:RNA splicing; ISS:UniProtKB. |
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SMART | |
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PRINTS | |