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Q3MJK5

- CDK12_RAT

UniProt

Q3MJK5 - CDK12_RAT

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Protein

Cyclin-dependent kinase 12

Gene
Cdk12, Crk7, Crkrs, Pksc
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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'. Involved in regulation of MAP kinase activity, possibly leading to affect the response to estrogen inhibitors By similarity. Required for RNA splicing, possibly by phosphorylating SRSF1/SF2.1 Publication

Catalytic activityi

ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate.
ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei752 – 7521ATP By similarity
Active sitei855 – 8551Proton acceptor By similarity
Binding sitei1036 – 10361ATP By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi729 – 7379ATP By similarity
Nucleotide bindingi810 – 8156ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cyclin binding Source: UniProtKB
  3. cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB-EC
  4. RNA polymerase II carboxy-terminal domain kinase activity Source: UniProtKB

GO - Biological processi

  1. mRNA processing Source: UniProtKB-KW
  2. phosphorylation of RNA polymerase II C-terminal domain Source: UniProtKB
  3. protein autophosphorylation Source: Ensembl
  4. regulation of MAP kinase activity Source: UniProtKB
  5. RNA splicing Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclin-dependent kinase 12 (EC:2.7.11.22, EC:2.7.11.23)
Alternative name(s):
Cdc2-related kinase, arginine/serine-rich
Short name:
CrkRS
Cell division cycle 2-related protein kinase 7
Short name:
CDC2-related protein kinase 7
Cell division protein kinase 12
Protein kinase for splicing component
Gene namesi
Name:Cdk12
Synonyms:Crk7, Crkrs, Pksc
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 10

Organism-specific databases

RGDi621111. Cdk12.

Subcellular locationi

Nucleus. Nucleus speckle
Note: Colocalized with nuclear speckles throughout interphase.1 Publication

GO - Cellular componenti

  1. cyclin K-CDK12 complex Source: Ensembl
  2. nuclear cyclin-dependent protein kinase holoenzyme complex Source: UniProtKB
  3. nuclear speck Source: UniProtKB
  4. nucleolus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14841484Cyclin-dependent kinase 12PRO_0000314471Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei57 – 571Phosphothreonine By similarity
Modified residuei73 – 731Phosphotyrosine By similarity
Modified residuei235 – 2351Phosphoserine By similarity
Modified residuei248 – 2481Phosphoserine By similarity
Modified residuei273 – 2731Phosphoserine By similarity
Modified residuei275 – 2751Phosphoserine By similarity
Modified residuei300 – 3001Phosphoserine By similarity
Modified residuei302 – 3021Phosphoserine By similarity
Modified residuei309 – 3091Phosphoserine By similarity
Modified residuei311 – 3111Phosphoserine By similarity
Modified residuei317 – 3171Phosphoserine By similarity
Modified residuei322 – 3221Phosphoserine By similarity
Modified residuei324 – 3241Phosphoserine By similarity
Modified residuei331 – 3311Phosphoserine By similarity
Modified residuei332 – 3321Phosphoserine By similarity
Modified residuei333 – 3331Phosphoserine By similarity
Modified residuei337 – 3371Phosphoserine By similarity
Modified residuei344 – 3441Phosphoserine By similarity
Modified residuei382 – 3821Phosphoserine By similarity
Modified residuei384 – 3841Phosphoserine By similarity
Modified residuei399 – 3991Phosphoserine By similarity
Modified residuei419 – 4191Phosphoserine By similarity
Modified residuei422 – 4221Phosphoserine By similarity
Modified residuei511 – 5111Phosphothreonine By similarity
Modified residuei677 – 6771Phosphoserine By similarity
Modified residuei681 – 6811Phosphoserine By similarity
Modified residuei688 – 6881Phosphothreonine By similarity
Modified residuei889 – 8891Phosphothreonine By similarity
Modified residuei1049 – 10491Phosphoserine By similarity
Modified residuei1079 – 10791Phosphoserine By similarity
Modified residuei1240 – 12401Phosphothreonine By similarity

Post-translational modificationi

Phosphorylation at Thr-889 increases kinase activity By similarity.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ3MJK5.
PRIDEiQ3MJK5.

PTM databases

PhosphoSiteiQ3MJK5.

Expressioni

Tissue specificityi

Expressed in embryonic tissues such as brain, spinal cord, heart, lung, liver, gut and limb. Levels are lower in adult tissues.1 Publication

Developmental stagei

Expressed at E10.5 and E14.5.1 Publication

Gene expression databases

GenevestigatoriQ3MJK5.

Interactioni

Subunit structurei

Interacts with CCNL1 and CCNL2.1 Publication

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000008256.

Structurei

3D structure databases

ProteinModelPortaliQ3MJK5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini723 – 1016294Protein kinaseAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi137 – 393257Ser-richAdd
BLAST
Compositional biasi406 – 4127Poly-Ala
Compositional biasi524 – 703180Pro-richAdd
BLAST
Compositional biasi1234 – 127643Pro-richAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00740000114964.
HOGENOMiHOG000049118.
HOVERGENiHBG050852.
InParanoidiQ3MJK5.
KOiK08819.
OMAiYSTRSHP.
OrthoDBiEOG76DTSM.
PhylomeDBiQ3MJK5.
TreeFamiTF101060.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q3MJK5-1) [UniParc]FASTAAdd to Basket

Also known as: CDK12(L)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MPNSERHGGK KDGSGGASGT SQPSSGGGSS NSRERHRLVS KHKRHKSKHS     50
KDMGLVTPEA ASLGTIIKPL VEYDDISSDS DTFSDDMAFK SDRRENDERR 100
GTDRSDRLHR HRHHQHRRSR DLLKTKQTEK EKNQEVSKSG SMKDRLSGSS 150
KRSVEGNDDY GKAQLSKSSS KESRSSKMHK EKTRKERELK SGHKDRSKSH 200
RKRETPKSYK TVDSPKRRSR SPHRKWSDSS KQDDSPSGAS YGQDYDLSPP 250
RSHTSSNYDS YKKSPGSTSR RQSISPPYKE PSAYQSSTRS PSPYSRRQRS 300
VSPYSRRRSS SYERSGSYSG RSPSPYGRRR SSSPFLSKRS LSRSPISSRK 350
SMKSRSRSPA YSRHSSSHSK KKRSGSRSRH SSISPVRLPL NSSLGAELSR 400
KKKERAAAAA AAKLDGKESK GSPIILPKKE KFEVKESGLE SKKLPRGIKS 450
EKSTPDTELV NVAHSNTEVK NCLDTGKVKL DENLQKHPVK DLKAQGTKDT 500
KPVALKEVIV TSKETETSEK EALPPLPTIT SPPPLPSTTP PPQTPPLPPL 550
PPLPAVPLQP PLPPPQPPFS QVPVSNTSTL PSSPHPRTST LSSQTNSQPL 600
VQVSMKTQLS VTAAIPHLKT STLPPLPLPP LLPGDDDMDS PKEMLPSKPA 650
KKEKEQRTRH LLTDLPLPPE LPGGDPSPPD SPEPKAITPP QQPYKKRPKI 700
CCPRYGERRQ TESDWGKRCV DKFDIIGIIG EGTYGQVYKA KDKDTGELVA 750
LKKVRLDNEK EGFPITAIRE IKILRQLVHQ SVVNMKEIVT DKQDALDFKK 800
DKGAFYLVFE YMDHDLMGLL ESGLVHFSED HIKSFMKQLM EGLDYCHKKN 850
FLHRDIKCSN ILLNNSGQIK LADFGLARLY NSEESRPYTN KVITLWYRPP 900
ELLLGEERYT PAIDVWSCGC ILGELFTKKP IFQANLELAQ LELISRLCGS 950
PCPAVWPDVI KLPYFNTMKP KKQYRRRLRE EFSFIPSAAL DLLDHMLTLD 1000
PSKRCTAEQT LQSDFLKDVE LSKMAPPDLP HWQDCHELWS KKRRRQRQSG 1050
IVIEEQPPSK ASRKETTSGT AAEPVKNSSP APPQPAPVKA EPGPGDAVGL 1100
GDITQQLNQS ELAVLLNLLQ SQTDLSIPQM AQLLNIHSNP EMQQQLEALN 1150
QSISALTEAS SQQQDSESIA PEESLKEVPS VSVVLPPAEQ TTPEASNTPA 1200
DMQNMLAVLL SQLMKTQEPA GNLEENTSDK NSGPQGPRRT PTMPQEEAAA 1250
CPPHILPPEK RPPEPPGPPP PPPPPPLVEG DLSSAPQELN PAVTAALLQL 1300
LSQPEAEPPG HLPHEHQALR PMEYSTRSHP NRTYGNTDGP ETGFSATDTD 1350
ERSSGPALTE SLVQTLVKNR TFSGSVSHLG ESNSYQGTGS VQFPGDQDLR 1400
FTRVPLALHS VVGQPFLKSE GNSNSVVHAE TKLQNYGELG PGTTGANSSG 1450
TTLQWGGPAQ SFGKPYRGAA RVPPRGGRGR GVPY 1484
Length:1,484
Mass (Da):163,790
Last modified:October 25, 2005 - v1
Checksum:iE3B346EA6A587D7B
GO
Isoform 2 (identifier: Q3MJK5-2) [UniParc]FASTAAdd to Basket

Also known as: CDK12(S)

The sequence of this isoform differs from the canonical sequence as follows:
     1250-1258: ACPPHILPP → GKQTGHESQ
     1259-1484: Missing.

Show »
Length:1,258
Mass (Da):139,985
Checksum:i9CF659A276E67FAE
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1250 – 12589ACPPHILPP → GKQTGHESQ in isoform 2. VSP_030288
Alternative sequencei1259 – 1484226Missing in isoform 2. VSP_030289Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY072294 mRNA. Translation: AAL69525.1.
AY962568 mRNA. Translation: AAY41734.1.
RefSeqiNP_001029039.1. NM_001033867.1. [Q3MJK5-1]
NP_620271.1. NM_138916.2. [Q3MJK5-2]
UniGeneiRn.48817.

Genome annotation databases

EnsembliENSRNOT00000008256; ENSRNOP00000008256; ENSRNOG00000006000. [Q3MJK5-1]
GeneIDi192350.
KEGGirno:192350.
UCSCiRGD:621111. rat. [Q3MJK5-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY072294 mRNA. Translation: AAL69525.1 .
AY962568 mRNA. Translation: AAY41734.1 .
RefSeqi NP_001029039.1. NM_001033867.1. [Q3MJK5-1 ]
NP_620271.1. NM_138916.2. [Q3MJK5-2 ]
UniGenei Rn.48817.

3D structure databases

ProteinModelPortali Q3MJK5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000008256.

PTM databases

PhosphoSitei Q3MJK5.

Proteomic databases

PaxDbi Q3MJK5.
PRIDEi Q3MJK5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000008256 ; ENSRNOP00000008256 ; ENSRNOG00000006000 . [Q3MJK5-1 ]
GeneIDi 192350.
KEGGi rno:192350.
UCSCi RGD:621111. rat. [Q3MJK5-1 ]

Organism-specific databases

CTDi 51755.
RGDi 621111. Cdk12.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00740000114964.
HOGENOMi HOG000049118.
HOVERGENi HBG050852.
InParanoidi Q3MJK5.
KOi K08819.
OMAi YSTRSHP.
OrthoDBi EOG76DTSM.
PhylomeDBi Q3MJK5.
TreeFami TF101060.

Miscellaneous databases

NextBioi 623019.
PROi Q3MJK5.

Gene expression databases

Genevestigatori Q3MJK5.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Identification and characterization of the CDK12/cyclin L1 complex involved in alternative splicing regulation."
    Chen H.-H., Wang Y.-C., Fann M.-J.
    Mol. Cell. Biol. 26:2736-2745(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INTERACTION WITH CCNL1 AND CCNL2, SUBCELLULAR LOCATION, FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
    Strain: Sprague-Dawley.

Entry informationi

Entry nameiCDK12_RAT
AccessioniPrimary (citable) accession number: Q3MJK5
Secondary accession number(s): Q8R458
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 25, 2005
Last modified: June 11, 2014
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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