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Protein

Probable cyclin-dependent kinase 9

Gene

cdk9

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

Component of the positive transcription elongation factor b (P-TEFb) which consists of cdk9 and pch1, and which phosphorylates the C-terminal domain (CTD) of RNA polymerase II and spt5.1 Publication

Catalytic activityi

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

Enzyme regulationi

May be activated by autophosphorylation or phosphorylation by a separate activating kinase.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei65ATPPROSITE-ProRule annotation1
Active sitei166Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi42 – 50ATPPROSITE-ProRule annotation9

GO - Molecular functioni

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

GO - Biological processi

  • peptidyl-serine autophosphorylation Source: PomBase
  • peptidyl-serine phosphorylation Source: PomBase
  • peptidyl-threonine autophosphorylation Source: PomBase
  • peptidyl-threonine phosphorylation Source: PomBase
  • peptidyl-tyrosine autophosphorylation Source: PomBase
  • phosphorylation of RNA polymerase II C-terminal domain serine 2 residues involved in positive regulation of transcription elongation from RNA polymerase II promoter Source: PomBase
  • phosphorylation of RNA polymerase II C-terminal domain serine 5 residues Source: PomBase
  • protein phosphorylation Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Probable cyclin-dependent kinase 9 (EC:2.7.11.22, EC:2.7.11.23)
Alternative name(s):
Cell division protein kinase 9
Gene namesi
Name:cdk9
ORF Names:pi014, SPBC32H8.10
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC32H8.10.
PomBaseiSPBC32H8.10. cdk9.

Subcellular locationi

GO - Cellular componenti

  • cyclin-dependent protein kinase holoenzyme complex Source: PomBase
  • nuclear chromatin Source: PomBase
  • nucleus Source: PomBase
  • P-TEFb-cap methyltransferase complex Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi65K → A: Abolishes activity. 1 Publication1
Mutagenesisi83E → A: Defective kinase activity. 1 Publication1
Mutagenesisi184D → N: Abolishes activity. 1 Publication1
Mutagenesisi212T → A: Abolishes activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000858081 – 591Probable cyclin-dependent kinase 9Add BLAST591

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei211Phosphotyrosine1 Publication1
Modified residuei212Phosphothreonine1 Publication1
Modified residuei565Phosphothreonine1 Publication1
Modified residuei577Phosphoserine1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ96WV9.
PRIDEiQ96WV9.

PTM databases

iPTMnetiQ96WV9.

Interactioni

Subunit structurei

Interacts with pch1 cyclin via its N-terminal domain. Via its C-terminal domain, interacts with RNA triphosphatase pct1 which is involved in mRNA capping. Interacts also with pcm1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
pch1O746272EBI-443557,EBI-443575
pct1Q9P6Q62EBI-443557,EBI-443547

Protein-protein interaction databases

BioGridi276771. 21 interactors.
IntActiQ96WV9. 2 interactors.
MINTiMINT-253408.

Structurei

3D structure databases

ProteinModelPortaliQ96WV9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini36 – 339Protein kinasePROSITE-ProRule annotationAdd BLAST304

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 385Interaction with pch1Add BLAST385
Regioni442 – 523Binds to pct1Add BLAST82

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

InParanoidiQ96WV9.
KOiK15562.
OMAiYSASHEY.
OrthoDBiEOG092C2FL8.
PhylomeDBiQ96WV9.

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.

Q96WV9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRSSSVSVE DEKSARRKLD VVPKLHFVGC SHLTDYHLME KLGEGTFGEV
60 70 80 90 100
YKSQRRKDGK VYALKRILMH TEKEGFPITA IREIKILKSI KHENIIPLSD
110 120 130 140 150
MTVVRADKKH RRRGSIYMVT PYMDHDLSGL LENPSVKFTE PQIKCYMKQL
160 170 180 190 200
FAGTKYLHDQ LILHRDLKAA NLLIDNHGIL KIADFGLARV ITEESYANKN
210 220 230 240 250
PGLPPPNRRE YTGCVVTRWY RSPELLLGER RYTTAIDMWS VGCIMAEMYK
260 270 280 290 300
GRPILQGSSD LDQLDKIFRL CGSPTQATMP NWEKLPGCEG VRSFPSHPRT
310 320 330 340 350
LETAFFTFGK EMTSLCGAIL TLNPDERLSA SMALEHEYFT TPPYPANPSE
360 370 380 390 400
LQSYSASHEY DKRRKREQRD ANSHAFEQTA NGKRQFRFMT RGPSDPWYGI
410 420 430 440 450
RRPNYNSQPQ YQRGSYNREG GNMDRSRNVN YQPKRQQNFK PLTSDLPQKN
460 470 480 490 500
SEFSETNAMN QTSNHSHADG QRYYRPEQDR SQRLRNPSDY GRQGRQSSQS
510 520 530 540 550
QQPAWNVSSR YQNNSKVQTT SRASENADTN KTQHNIKYID SYVPEYSIAR
560 570 580 590
QSANQKTNEQ HPSSTSLHQQ STSDLKSPSF HENSNVDDTP K
Length:591
Mass (Da):68,029
Last modified:December 1, 2001 - v1
Checksum:i28DFF6032388E16A
GO

Sequence cautioni

The sequence BAA21391 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB004534 Genomic DNA. Translation: BAA21391.2. Different initiation.
CU329671 Genomic DNA. Translation: CAC37500.1.
RefSeqiNP_595616.1. NM_001021511.2.

Genome annotation databases

EnsemblFungiiSPBC32H8.10.1; SPBC32H8.10.1:pep; SPBC32H8.10.
GeneIDi2540239.
KEGGispo:SPBC32H8.10.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB004534 Genomic DNA. Translation: BAA21391.2. Different initiation.
CU329671 Genomic DNA. Translation: CAC37500.1.
RefSeqiNP_595616.1. NM_001021511.2.

3D structure databases

ProteinModelPortaliQ96WV9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276771. 21 interactors.
IntActiQ96WV9. 2 interactors.
MINTiMINT-253408.

PTM databases

iPTMnetiQ96WV9.

Proteomic databases

MaxQBiQ96WV9.
PRIDEiQ96WV9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC32H8.10.1; SPBC32H8.10.1:pep; SPBC32H8.10.
GeneIDi2540239.
KEGGispo:SPBC32H8.10.

Organism-specific databases

EuPathDBiFungiDB:SPBC32H8.10.
PomBaseiSPBC32H8.10. cdk9.

Phylogenomic databases

InParanoidiQ96WV9.
KOiK15562.
OMAiYSASHEY.
OrthoDBiEOG092C2FL8.
PhylomeDBiQ96WV9.

Miscellaneous databases

PROiQ96WV9.

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...

Entry informationi

Entry nameiCDK9_SCHPO
AccessioniPrimary (citable) accession number: Q96WV9
Secondary accession number(s): O13607
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2003
Last sequence update: December 1, 2001
Last modified: November 2, 2016
This is version 123 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.