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Protein

CTD kinase subunit alpha

Gene

lsk1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic subunit of the CTDK-I complex, which hyperphosphorylates the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit. Involved in RNA polymerase II transcriptional elongation and pre-mRNA 3'-end processing (By similarity). Together with ctk2/lsc1, required for the regulation of cytokinesis by phosphorylating 'Ser-2' residues found in the heptad repeats of the CTD. Required for nuclear localization of ctk2/lsc1. Positively regulates the septation initiation network (SIN) and promotes successful completion of cytokinesis in response to perturbation of the actomyosin ring. Acts in parallel to clp1 to promote actomyosin ring stability upon cytokinesis checkpoint activation.By similarity2 Publications

Catalytic activityi

ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei306 – 3061ATPPROSITE-ProRule annotationBy similarity
Active sitei399 – 3991Proton acceptorPROSITE-ProRule annotationBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi283 – 2919ATPPROSITE-ProRule annotationBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • cyclin-dependent protein serine/threonine kinase activity Source: PomBase
  • RNA polymerase II carboxy-terminal domain kinase activity Source: PomBase

GO - Biological processi

  • mRNA processing Source: UniProtKB-KW
  • phosphorylation of RNA polymerase II C-terminal domain serine 2 residues Source: PomBase
  • positive regulation of induction of conjugation with cellular fusion by regulation of transcription from RNA polymerase II promoter Source: PomBase
  • positive regulation of transcription from RNA polymerase II promoter in response to nitrogen starvation Source: PomBase
  • regulation of mitotic actomyosin contractile ring maintenance Source: PomBase
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

mRNA processing, Transcription

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
CTD kinase subunit alpha (EC:2.7.11.23)
Short name:
CTDK-I subunit alpha
Alternative name(s):
CTD kinase subunit 1
Latrunculin sensitive kinase 1
Gene namesi
Name:lsk1Imported
Synonyms:ctk1By similarity
ORF Names:SPAC2F3.15
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC2F3.15.
PomBaseiSPAC2F3.15. lsk1.

Subcellular locationi

GO - Cellular componenti

  • nuclear chromatin Source: PomBase
  • nuclear cyclin-dependent protein kinase holoenzyme complex Source: PomBase
  • nucleolus Source: PomBase
  • nucleus Source: PomBase
  • trimeric positive transcription elongation factor complex b Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Cells display severe cytokinesis defects. They are able to form, but not maintain the integrity of the actomyosin ring and are unable to successfully complete division septum formation upon treatment with low doses (0.3 µM) of actin depolymerizing drug, latrunculin A (LatA). However, deletion mutants are competent to delay nuclear cycle progression after cytokinetic failure upon treatment with LatA. In addition, deletion mutants suppress the lethal, multiseptate phenotype conferred by hyperactivation of the SIN.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi306 – 3061K → R: No kinase activity. No interaction with ctk2/lsc1. Mislocalization of ctk2/lsc1. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 593593CTD kinase subunit alphaPRO_0000338603Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei56 – 561Phosphoserine1 Publication
Modified residuei58 – 581Phosphoserine1 Publication
Modified residuei104 – 1041Phosphoserine1 Publication
Modified residuei109 – 1091Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO14098.

PTM databases

iPTMnetiO14098.
SwissPalmiO14098.

Interactioni

Subunit structurei

CTDK-I consists of three subunits, ctk1/lsk1, ctk2/lsc1 and ctk3 (also called alpha, beta and gamma) (By similarity). Interacts with ctk2/lsc1. This interaction is dependent on kinase activity.By similarity1 Publication

Protein-protein interaction databases

BioGridi278168. 160 interactions.
MINTiMINT-4670463.

Structurei

3D structure databases

ProteinModelPortaliO14098.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini277 – 561285Protein kinasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi44 – 215172Ser-richSequence analysisAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000233024.
InParanoidiO14098.
KOiK00916.
OMAiSPRRGHT.
OrthoDBiEOG7K3TWD.
PhylomeDBiO14098.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
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.

O14098-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSYSKSTIYR RQGTEPNSHF RRTVEEKSQL SGTNEESLGG HTLSSNAFKN
60 70 80 90 100
NSSSISPSSS AKDPREQRKR TFPLNDTHSS RARQHERPFR SRKSRRRKGK
110 120 130 140 150
KAFSPRPGSP PSPSFYRSGS QKRARNLTTK DYFAKRSESS SSASVSPISP
160 170 180 190 200
SANRNDSKRQ ASSFRRSPPS SVHMKPSAFN GRKVSRRPSS SPPPIPSIPH
210 220 230 240 250
ETTSSDTQKK SSVSSGFPEN KHGKFHFHIP NERRSRFDQP PSKRMALTST
260 270 280 290 300
ARESVPAPLP SPPSGPIYTY TYPKPAYEKI DQIGEGTYGK VYKAINTVTG
310 320 330 340 350
DLVALKRIRL EQEKDGFPIT TVREVKILQR LRHKNIVRLL EIMVEKSSVY
360 370 380 390 400
MVFEYMDHDL TGVLLNSQLH FTPGNIKHLS KQIFEALAYL HHRGVLHRDI
410 420 430 440 450
KGSNILLNNN GDLKFADFGL ARFNTSSKSA NYTNRVITLW FRPPELLLGE
460 470 480 490 500
TAYDTAVDIW SAGCIVMELF TGKPFFQGRD EISQLEVIYD MMGTPDVHSW
510 520 530 540 550
PEVKNLPWYE LLKPVEEKKS RFVETFKEIL SPAAIDLCQK LLALNPFCRP
560 570 580 590
SAHETLMHEY FTSESPPPEP AVILKNMQGS WHEWESKKRK SKR
Length:593
Mass (Da):67,366
Last modified:January 1, 1998 - v1
Checksum:iE37DD7AA762F0713
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB16269.1.
PIRiT38547.
RefSeqiNP_594393.1. NM_001019816.2.

Genome annotation databases

EnsemblFungiiSPAC2F3.15.1; SPAC2F3.15.1:pep; SPAC2F3.15.
GeneIDi2541672.
KEGGispo:SPAC2F3.15.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB16269.1.
PIRiT38547.
RefSeqiNP_594393.1. NM_001019816.2.

3D structure databases

ProteinModelPortaliO14098.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278168. 160 interactions.
MINTiMINT-4670463.

PTM databases

iPTMnetiO14098.
SwissPalmiO14098.

Proteomic databases

MaxQBiO14098.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC2F3.15.1; SPAC2F3.15.1:pep; SPAC2F3.15.
GeneIDi2541672.
KEGGispo:SPAC2F3.15.

Organism-specific databases

EuPathDBiFungiDB:SPAC2F3.15.
PomBaseiSPAC2F3.15. lsk1.

Phylogenomic databases

HOGENOMiHOG000233024.
InParanoidiO14098.
KOiK00916.
OMAiSPRRGHT.
OrthoDBiEOG7K3TWD.
PhylomeDBiO14098.

Miscellaneous databases

PROiO14098.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "The nuclear kinase Lsk1p positively regulates the septation initiation network and promotes the successful completion of cytokinesis in response to perturbation of the actomyosin ring in Schizosaccharomyces pombe."
    Karagiannis J., Bimbo A., Rajagopalan S., Liu J., Balasubramanian M.K.
    Mol. Biol. Cell 16:358-371(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
  3. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  4. "A cyclin-dependent kinase that promotes cytokinesis through modulating phosphorylation of the carboxy terminal domain of the RNA Pol II Rpb1p sub-unit."
    Karagiannis J., Balasubramanian M.K.
    PLoS ONE 2:E433-E433(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CTK2, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-306.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56; SER-58; SER-104 AND SER-109, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiCTK1_SCHPO
AccessioniPrimary (citable) accession number: O14098
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: January 1, 1998
Last modified: June 8, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.