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Q9VP22

- CDK12_DROME

UniProt

Q9VP22 - CDK12_DROME

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Protein

Cyclin-dependent kinase 12

Gene
Cdk12, CG7597
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate.1 Publication
ATP + a protein = ADP + a phosphoprotein.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei833 – 8331ATP By similarity
Active sitei936 – 9361Proton acceptor By similarity
Binding sitei1118 – 11181ATP By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi810 – 8189ATP By similarity
Nucleotide bindingi891 – 8966ATP 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: FlyBase
  4. RNA polymerase II carboxy-terminal domain kinase activity Source: UniProtKB

GO - Biological processi

  1. neurogenesis Source: FlyBase
  2. phagocytosis Source: FlyBase
  3. phosphorylation of RNA polymerase II C-terminal domain Source: UniProtKB
  4. protein phosphorylation Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

SignaLinkiQ9VP22.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Cdk12
ORF Names:CG7597
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0037093. Cdk12.

Subcellular locationi

Nucleus. Chromosome
Note: Localizes to active genes.1 Publication

GO - Cellular componenti

  1. nuclear chromosome Source: UniProtKB
  2. nuclear cyclin-dependent protein kinase holoenzyme complex Source: UniProtKB
  3. polytene chromosome Source: FlyBase
  4. polytene chromosome puff Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11571157Cyclin-dependent kinase 12PRO_0000372859Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei106 – 1061Phosphothreonine1 Publication
Modified residuei184 – 1841Phosphothreonine1 Publication
Modified residuei190 – 1901Phosphoserine1 Publication
Modified residuei192 – 1921Phosphoserine1 Publication
Modified residuei217 – 2171Phosphothreonine1 Publication
Modified residuei280 – 2801Phosphoserine1 Publication
Modified residuei283 – 2831Phosphothreonine1 Publication
Modified residuei291 – 2911Phosphoserine1 Publication
Modified residuei301 – 3011Phosphoserine1 Publication
Modified residuei314 – 3141Phosphoserine1 Publication
Modified residuei353 – 3531Phosphoserine1 Publication
Modified residuei365 – 3651Phosphothreonine1 Publication
Modified residuei487 – 4871Phosphoserine1 Publication
Modified residuei492 – 4921Phosphoserine1 Publication
Modified residuei553 – 5531Phosphoserine1 Publication
Modified residuei730 – 7301Phosphoserine1 Publication
Modified residuei743 – 7431Phosphoserine1 Publication
Modified residuei747 – 7471Phosphoserine1 Publication
Modified residuei755 – 7551Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9VP22.
PRIDEiQ9VP22.

Expressioni

Gene expression databases

BgeeiQ9VP22.

Interactioni

Subunit structurei

Interacts with cyclin CycK.1 Publication

Protein-protein interaction databases

BioGridi65630. 1 interaction.
IntActiQ9VP22. 7 interactions.
STRINGi7227.FBpp0078013.

Structurei

3D structure databases

ProteinModelPortaliQ9VP22.
SMRiQ9VP22. Positions 795-1143.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini804 – 1098295Protein kinaseAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00740000114964.
InParanoidiQ8T9E1.
KOiK08819.
OMAiTISKICG.
OrthoDBiEOG76DTSM.
PhylomeDBiQ9VP22.

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]

Sequencei

Sequence statusi: Complete.

Q9VP22-1 [UniParc]FASTAAdd to Basket

« Hide

MHASSAAATA LVEYSDVSSE DFSDQEAGDL DADAGKGAGN IKKPKPAPDN     50
QFSKGRLDAK PDKEGYDNYR SRRAEDSSDP VAAGSRQTSS SEATNPREEP 100
SQASNTSKDE LWGREIYMSS DSIDTDELEA EMKRQKRKKQ KKEKHKHKSK 150
KKSKKRKKKR AKSYSSIDSM SDNDINALLD RRYTPPTAPS KSNERTVSAA 200
PSSFTPHNLK ESSSPATPPP VRRPNTNSNY YGESSLETAN SALGSNLQVT 250
VTNKQSISNR LRSPPPSSRS SGNGPRFGNS PRTPPPSHYS SSGGGGVGSG 300
SVVRDSRSSR YVNSPHKEDV SAHHRSSHDH GYQGRYSGAG SSSHDTRKVK 350
RLSPELDRYN HQPSTPPHKR RKFSDGREVG LGNFEHSRHH SGKYERYSRD 400
RYSRRSSRSP SVQHSRSRQS PSGGLSSGSN AFRHGGSHKH KYGTTVSSTP 450
SHTTRTSKRA SGTGTSGDRY SRSPRTSSRY MESSPPSPVG ASGSHHYHHR 500
RSPRMRQRTR GDSRRRSPSS ASSESSASRS RSPTSRDLKH KREEYIKKIS 550
ETSLFAELVK DRHKRQKALK EIIERQEENS NSNSNGALTI NDNSSSVDGN 600
TPNAADGRSA PGSGTPAAAS TTSNGLQALG SKPDLDLNNI PMPNKQNDSV 650
VSNPASNADV PDSVAQLKQP LLVPPFSASK NNIKPKSLTS LPLPPGMNVL 700
DLAGARSPSP GQKKESDEKN VTSSGSANKS VLNLPMPPVI PGSEELSGDD 750
DVIDSPEDFD APAVGTVHGH GGGPGTTRQR PVILNRRDSR NNVRDWGERC 800
VDVFEMIAQI GEGTYGQVYK ARDHHTNDMV ALKKVRLEHE KEGFPITAVR 850
EIKILRQLNH RNIVNLHEIV TDKQDAVEFR KDKGSFYLVF EYMDHDLMGL 900
LESGMVDFNE ENNASIMKQL LDGLNYCHKK NFLHRDIKCS NILMNNRGKV 950
KLADFGLARL YNADDRERPY TNKVITLWYR PPELLLGEER YGPSIDVWSC 1000
GCILGELFVK RPLFQANAEM AQLETISKIC GSPVPAVWPN VIKLPLFHTL 1050
KQKKTHRRRL REDFEFMPAP ALDLLDKMLD LDPDKRITAE DALRSPWLRK 1100
INPDEMPTPQ LPTWQDCHEL WSKKRRRQMR EQQESLPPTV IASTKYQQHG 1150
ATMVGDA 1157
Length:1,157
Mass (Da):128,333
Last modified:May 1, 2000 - v1
Checksum:iB37ADCFBCAB4E9F3
GO

Sequence cautioni

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti188 – 1881A → V in AAL39951. 1 Publication
Sequence conflicti1099 – 10991R → K in AAL28383. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
RefSeqiNP_001262167.1. NM_001275238.1.
NP_649325.2. NM_141068.3.
NP_730643.1. NM_168912.2.
UniGeneiDm.1943.

Genome annotation databases

EnsemblMetazoaiFBtr0078357; FBpp0078013; FBgn0037093.
FBtr0078358; FBpp0078014; FBgn0037093.
FBtr0332716; FBpp0304962; FBgn0037093.
GeneIDi40385.
KEGGidme:Dmel_CG7597.
UCSCiCG7597-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
RefSeqi NP_001262167.1. NM_001275238.1.
NP_649325.2. NM_141068.3.
NP_730643.1. NM_168912.2.
UniGenei Dm.1943.

3D structure databases

ProteinModelPortali Q9VP22.
SMRi Q9VP22. Positions 795-1143.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 65630. 1 interaction.
IntActi Q9VP22. 7 interactions.
STRINGi 7227.FBpp0078013.

Proteomic databases

PaxDbi Q9VP22.
PRIDEi Q9VP22.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0078357 ; FBpp0078013 ; FBgn0037093 .
FBtr0078358 ; FBpp0078014 ; FBgn0037093 .
FBtr0332716 ; FBpp0304962 ; FBgn0037093 .
GeneIDi 40385.
KEGGi dme:Dmel_CG7597.
UCSCi CG7597-RA. d. melanogaster.

Organism-specific databases

CTDi 51755.
FlyBasei FBgn0037093. Cdk12.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00740000114964.
InParanoidi Q8T9E1.
KOi K08819.
OMAi TISKICG.
OrthoDBi EOG76DTSM.
PhylomeDBi Q9VP22.

Enzyme and pathway databases

SignaLinki Q9VP22.

Miscellaneous databases

GenomeRNAii 40385.
NextBioi 818504.
PROi Q9VP22.

Gene expression databases

Bgeei Q9VP22.

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

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. 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.

Entry informationi

Entry nameiCDK12_DROME
AccessioniPrimary (citable) accession number: Q9VP22
Secondary accession number(s): Q8T9E1, Q95SE1
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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