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Q9VP22 (CDK12_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cyclin-dependent kinase 12

EC=2.7.11.22
EC=2.7.11.23
Alternative name(s):
Cell division protein kinase 12
Short name=dCdk12
Gene names
Name:Cdk12
ORF Names:CG7597
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length1157 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cyclin-dependent kinase which displays CTD kinase activity: hyperphosphorylates the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit, thereby acting as a key regulator of transcription elongation. Ref.7

Catalytic activity

ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate. Ref.7

ATP + a protein = ADP + a phosphoprotein. Ref.7

Subunit structure

Interacts with cyclin CycK. Ref.7

Subcellular location

Nucleus. Chromosome. Note: Localizes to active genes. Ref.7

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.

Contains 1 protein kinase domain.

Sequence caution

The sequence AAL28383.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11571157Cyclin-dependent kinase 12
PRO_0000372859

Regions

Domain804 – 1098295Protein kinase
Nucleotide binding810 – 8189ATP By similarity
Nucleotide binding891 – 8966ATP By similarity

Sites

Active site9361Proton acceptor By similarity
Binding site8331ATP By similarity
Binding site11181ATP By similarity

Amino acid modifications

Modified residue1061Phosphothreonine Ref.5
Modified residue1841Phosphothreonine Ref.5
Modified residue1901Phosphoserine Ref.5
Modified residue1921Phosphoserine Ref.5
Modified residue2171Phosphothreonine Ref.5
Modified residue2801Phosphoserine Ref.5
Modified residue2831Phosphothreonine Ref.5
Modified residue2911Phosphoserine Ref.5
Modified residue3011Phosphoserine Ref.5
Modified residue3141Phosphoserine Ref.5
Modified residue3531Phosphoserine Ref.5
Modified residue3651Phosphothreonine Ref.5
Modified residue4871Phosphoserine Ref.5
Modified residue4921Phosphoserine Ref.5
Modified residue5531Phosphoserine Ref.6
Modified residue7301Phosphoserine Ref.5
Modified residue7431Phosphoserine Ref.5
Modified residue7471Phosphoserine Ref.5
Modified residue7551Phosphoserine Ref.5

Experimental info

Sequence conflict1881A → V in AAL39951. Ref.3
Sequence conflict10991R → K in AAL28383. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9VP22 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: B37ADCFBCAB4E9F3

FASTA1,157128,333
        10         20         30         40         50         60 
MHASSAAATA LVEYSDVSSE DFSDQEAGDL DADAGKGAGN IKKPKPAPDN QFSKGRLDAK 

        70         80         90        100        110        120 
PDKEGYDNYR SRRAEDSSDP VAAGSRQTSS SEATNPREEP SQASNTSKDE LWGREIYMSS 

       130        140        150        160        170        180 
DSIDTDELEA EMKRQKRKKQ KKEKHKHKSK KKSKKRKKKR AKSYSSIDSM SDNDINALLD 

       190        200        210        220        230        240 
RRYTPPTAPS KSNERTVSAA PSSFTPHNLK ESSSPATPPP VRRPNTNSNY YGESSLETAN 

       250        260        270        280        290        300 
SALGSNLQVT VTNKQSISNR LRSPPPSSRS SGNGPRFGNS PRTPPPSHYS SSGGGGVGSG 

       310        320        330        340        350        360 
SVVRDSRSSR YVNSPHKEDV SAHHRSSHDH GYQGRYSGAG SSSHDTRKVK RLSPELDRYN 

       370        380        390        400        410        420 
HQPSTPPHKR RKFSDGREVG LGNFEHSRHH SGKYERYSRD RYSRRSSRSP SVQHSRSRQS 

       430        440        450        460        470        480 
PSGGLSSGSN AFRHGGSHKH KYGTTVSSTP SHTTRTSKRA SGTGTSGDRY SRSPRTSSRY 

       490        500        510        520        530        540 
MESSPPSPVG ASGSHHYHHR RSPRMRQRTR GDSRRRSPSS ASSESSASRS RSPTSRDLKH 

       550        560        570        580        590        600 
KREEYIKKIS ETSLFAELVK DRHKRQKALK EIIERQEENS NSNSNGALTI NDNSSSVDGN 

       610        620        630        640        650        660 
TPNAADGRSA PGSGTPAAAS TTSNGLQALG SKPDLDLNNI PMPNKQNDSV VSNPASNADV 

       670        680        690        700        710        720 
PDSVAQLKQP LLVPPFSASK NNIKPKSLTS LPLPPGMNVL DLAGARSPSP GQKKESDEKN 

       730        740        750        760        770        780 
VTSSGSANKS VLNLPMPPVI PGSEELSGDD DVIDSPEDFD APAVGTVHGH GGGPGTTRQR 

       790        800        810        820        830        840 
PVILNRRDSR NNVRDWGERC VDVFEMIAQI GEGTYGQVYK ARDHHTNDMV ALKKVRLEHE 

       850        860        870        880        890        900 
KEGFPITAVR EIKILRQLNH RNIVNLHEIV TDKQDAVEFR KDKGSFYLVF EYMDHDLMGL 

       910        920        930        940        950        960 
LESGMVDFNE ENNASIMKQL LDGLNYCHKK NFLHRDIKCS NILMNNRGKV KLADFGLARL 

       970        980        990       1000       1010       1020 
YNADDRERPY TNKVITLWYR PPELLLGEER YGPSIDVWSC GCILGELFVK RPLFQANAEM 

      1030       1040       1050       1060       1070       1080 
AQLETISKIC GSPVPAVWPN VIKLPLFHTL KQKKTHRRRL REDFEFMPAP ALDLLDKMLD 

      1090       1100       1110       1120       1130       1140 
LDPDKRITAE DALRSPWLRK INPDEMPTPQ LPTWQDCHEL WSKKRRRQMR EQQESLPPTV 

      1150 
IASTKYQQHG ATMVGDA 

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[2]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[3]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo and Ovary.
[4]Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
[5]"Phosphoproteome analysis of Drosophila melanogaster embryos."
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-106; THR-184; SER-190; SER-192; THR-217; SER-280; THR-283; SER-291; SER-301; SER-314; SER-353; THR-365; SER-487; SER-492; SER-730; SER-743; SER-747 AND SER-755, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryo.
[6]"An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells."
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.
Mol. Biosyst. 3:275-286(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-553, IDENTIFICATION BY MASS SPECTROMETRY.
[7]"CDK12 is a transcription elongation-associated CTD kinase, the metazoan ortholog of yeast Ctk1."
Bartkowiak B., Liu P., Phatnani H.P., Fuda N.J., Cooper J.J., Price D.H., Adelman K., Lis J.T., Greenleaf A.L.
Genes Dev. 24:2303-2316(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH CYCK.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014296 Genomic DNA. Translation: AAF51738.1.
AE014296 Genomic DNA. Translation: AAN12171.1.
AY060835 mRNA. Translation: AAL28383.1. Different initiation.
AY069806 mRNA. Translation: AAL39951.1.
BT058001 mRNA. Translation: ACM16711.1.
RefSeqNP_001262167.1. NM_001275238.1.
NP_649325.2. NM_141068.3.
NP_730643.1. NM_168912.2.
UniGeneDm.1943.

3D structure databases

ProteinModelPortalQ9VP22.
SMRQ9VP22. Positions 795-1143.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid65630. 1 interaction.
IntActQ9VP22. 7 interactions.
STRING7227.FBpp0078013.

Proteomic databases

PaxDbQ9VP22.
PRIDEQ9VP22.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0078357; FBpp0078013; FBgn0037093.
FBtr0078358; FBpp0078014; FBgn0037093.
FBtr0332716; FBpp0304962; FBgn0037093.
GeneID40385.
KEGGdme:Dmel_CG7597.
UCSCCG7597-RA. d. melanogaster.

Organism-specific databases

CTD51755.
FlyBaseFBgn0037093. Cdk12.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00740000114964.
InParanoidQ8T9E1.
KOK08819.
OMATISKICG.
OrthoDBEOG76DTSM.
PhylomeDBQ9VP22.

Enzyme and pathway databases

SignaLinkQ9VP22.

Gene expression databases

BgeeQ9VP22.

Family and domain databases

InterProIPR011009. 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]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi40385.
NextBio818504.
PROQ9VP22.

Entry information

Entry nameCDK12_DROME
AccessionPrimary (citable) accession number: Q9VP22
Secondary accession number(s): Q8T9E1, Q95SE1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 26, 2009
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase