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P39073 (SSN3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Meiotic mRNA stability protein kinase SSN3

EC=2.7.11.22
EC=2.7.11.23
Alternative name(s):
Cyclin-dependent kinase 8
Suppressor of RNA polymerase B SRB10
Gene names
Name:SSN3
Synonyms:ARE1, CDK8, GIG2, SRB10, UME5
Ordered Locus Names:YPL042C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length555 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the SRB8-11 complex. The SRB8-11 complex is a regulatory module of the Mediator complex which is itself involved in regulation of basal and activated RNA polymerase II-dependent transcription. The SRB8-11 complex may be involved in the transcriptional repression of a subset of genes regulated by Mediator. It may inhibit the association of the Mediator complex with RNA polymerase II to form the holoenzyme complex. The SRB8-11 complex phosphorylates the C-terminal domain (CTD) of the largest subunit of RNA polymerase II RPB1 at serines 2 and 5. The SSN3/SRB10 and SSN8/SRB11 kinase-cyclin pair may also positively and negatively regulate numerous transcriptional activators in response to changes in nutritional and physiological conditions. Phosphorylates GCN4, promoting its ubiquitin-mediated degradation, and MSN2, promoting its nuclear exclusion. Phosphorylates STE12, thereby promoting its degradation and inhibition of filamentous growth. Phosphorylates GAL4, and this phosphorylation is required for efficient galactose-inducible transcription. Also phosphorylates BDF1 and the TAF2 subunit of the TFIID complex. Ref.2 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.6 Ref.7 Ref.8 Ref.11 Ref.12 Ref.14 Ref.21

ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate. Ref.6 Ref.7 Ref.8 Ref.11 Ref.12 Ref.14 Ref.21

Subunit structure

Component of the SRB8-11 complex which consists of SRB8, SSN2/SRB9, SSN3/SRB10 and SSN8/SRB11. The SRB8-11 complex associates with the Mediator complex. The SSN3/SRB10 and SSN8/SRB11 kinase-cyclin pair also associate with the RNA polymerase II holoenzyme. Interacts with TUP1. Ref.2 Ref.6 Ref.9 Ref.10 Ref.11 Ref.14

Subcellular location

Nucleus Probable.

Induction

Protein level and kinase activity are reduced during nitrogen starvation. Ref.5 Ref.12

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 AAC13785.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processMeiosis
Transcription
Transcription regulation
   Cellular componentNucleus
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionActivator
Kinase
Repressor
Serine/threonine-protein kinase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmeiotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of filamentous growth

Inferred from mutant phenotype Ref.12. Source: SGD

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype Ref.19. Source: SGD

nuclear-transcribed mRNA catabolic process, non-stop decay

Inferred from mutant phenotype PubMed 17660569. Source: SGD

phosphorylation of RNA polymerase II C-terminal domain

Inferred from direct assay Ref.6. Source: SGD

positive regulation of transcription from RNA polymerase II promoter by galactose

Inferred from mutant phenotype Ref.20. Source: SGD

protein destabilization

Inferred from mutant phenotype Ref.12. Source: SGD

protein phosphorylation

Inferred from mutant phenotype Ref.19. Source: SGD

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentmediator complex

Inferred from direct assay PubMed 11383511Ref.11. Source: SGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA polymerase II carboxy-terminal domain kinase activity

Inferred from direct assay Ref.6. Source: SGD

cyclin-dependent protein serine/threonine kinase activity

Inferred from direct assay Ref.8. Source: SGD

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 555555Meiotic mRNA stability protein kinase SSN3
PRO_0000086784

Regions

Domain75 – 463389Protein kinase
Nucleotide binding81 – 899ATP By similarity

Sites

Active site2861Proton acceptor By similarity
Binding site1831ATP Probable

Experimental info

Mutagenesis1831K → R in UME5-4; loss of activity. Ref.1
Mutagenesis3041D → A: Abrogates kinase activity and transcriptional repression. Ref.6 Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.15

Sequences

Sequence LengthMass (Da)Tools
P39073 [UniParc].

Last modified September 5, 2006. Version 3.
Checksum: C7B6DDC868CCD61E

FASTA55562,847
        10         20         30         40         50         60 
MYNGKDRAQN SYQPMYQRPM QVQGQQQAQS FVGKKNTIGS VHGKAPMLMA NNDVFTIGPY 

        70         80         90        100        110        120 
RARKDRMRVS VLEKYEVIGY IAAGTYGKVY KAKRQINSGT NSANGSSLNG TNAKIPQFDS 

       130        140        150        160        170        180 
TQPKSSSSMD MQANTNALRR NLLKDEGVTP GRIRTTREDV SPHYNSQKQT LIKKPLTVFY 

       190        200        210        220        230        240 
AIKKFKTEKD GVEQLHYTGI SQSACREMAL CRELHNKHLT TLVEIFLERK CVHMVYEYAE 

       250        260        270        280        290        300 
HDLLQIIHFH SHPEKRMIPP RMVRSIMWQL LDGVSYLHQN WVLHRDLKPA NIMVTIDGCV 

       310        320        330        340        350        360 
KIGDLGLARK FHNMLQTLYT GDKVVVTIWY RAPELLLGAR HYTPAVDLWS VGCIFAELIG 

       370        380        390        400        410        420 
LQPIFKGEEA KLDSKKTVPF QVNQLQRILE VLGTPDQKIW PYLEKYPEYD QITKFPKYRD 

       430        440        450        460        470        480 
NLATWYHSAG GRDKHALSLL YHLLNYDPIK RIDAFNALEH KYFTESDIPV SENVFEGLTY 

       490        500        510        520        530        540 
KYPARRIHTN DNDIMNLGSR TKNNTQASGI TAGAAANALG GLGVNRRILA AAAAAAAAVS 

       550 
GNNASDEPSR KKNRR 

« Hide

References

« Hide 'large scale' references
[1]"The yeast UME5 gene regulates the stability of meiotic mRNAs in response to glucose."
Surosky R.T., Strich R., Esposito R.E.
Mol. Cell. Biol. 14:3446-3458(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF LYS-183.
[2]"A kinase-cyclin pair in the RNA polymerase II holoenzyme."
Liao S.-M., Zhang J., Jeffery D.A., Koleske A.J., Thompson C.M., Chao D.M., Viljoen M., van Vuuren H.J.J., Young R.A.
Nature 374:193-196(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH SSN8.
Strain: ATCC 204508 / S288c.
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. expand/collapse author list , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Dissecting the regulatory circuitry of a eukaryotic genome."
Holstege F.C.P., Jennings E.G., Wyrick J.J., Lee T.I., Hengartner C.J., Green M.R., Golub T.R., Lander E.S., Young R.A.
Cell 95:717-728(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
[6]"Temporal regulation of RNA polymerase II by Srb10 and Kin28 cyclin-dependent kinases."
Hengartner C.J., Myer V.E., Liao S.-M., Wilson C.J., Koh S.S., Young R.A.
Mol. Cell 2:43-53(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH SSN8 AND THE RNA POLYMERASE II HOLOENZYME, MUTAGENESIS OF ASP-304.
[7]"GAL4 is regulated by the RNA polymerase II holoenzyme-associated cyclin-dependent protein kinase SRB10/CDK8."
Hirst M., Kobor M.S., Kuriakose N., Greenblatt J., Sadowski I.
Mol. Cell 3:673-678(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-304.
[8]"Negative regulation of Gcn4 and Msn2 transcription factors by Srb10 cyclin-dependent kinase."
Chi Y., Huddleston M.J., Zhang X., Young R.A., Annan R.S., Carr S.A., Deshaies R.J.
Genes Dev. 15:1078-1092(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-304.
[9]"The structural and functional organization of the yeast mediator complex."
Kang J.S., Kim S.H., Hwang M.S., Han S.J., Lee Y.C., Kim Y.-J.
J. Biol. Chem. 276:42003-42010(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MED1 AND MED4, FUNCTION OF THE MEDIATOR COMPLEX, INTERACTION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE II.
[10]"Interaction of a transcriptional repressor with the RNA polymerase II holoenzyme plays a crucial role in repression."
Zaman Z., Ansari A.Z., Koh S.S., Young R., Ptashne M.
Proc. Natl. Acad. Sci. U.S.A. 98:2550-2554(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SSN8 AND TUP1, MUTAGENESIS OF ASP-304.
[11]"A complex of the Srb8, -9, -10, and -11 transcriptional regulatory proteins from yeast."
Borggrefe T., Davis R., Erdjument-Bromage H., Tempst P., Kornberg R.D.
J. Biol. Chem. 277:44202-44207(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE SRB8-11 COMPLEX, FUNCTION OF THE SRB8-11 COMPLEX, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-304.
[12]"Srb10/Cdk8 regulates yeast filamentous growth by phosphorylating the transcription factor Ste12."
Nelson C., Goto S., Lund K., Hung W., Sadowski I.
Nature 421:187-190(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, INDUCTION, MUTAGENESIS OF ASP-304.
[13]"A unified nomenclature for protein subunits of mediator complexes linking transcriptional regulators to RNA polymerase II."
Bourbon H.-M., Aguilera A., Ansari A.Z., Asturias F.J., Berk A.J., Bjoerklund S., Blackwell T.K., Borggrefe T., Carey M., Carlson M., Conaway J.W., Conaway R.C., Emmons S.W., Fondell J.D., Freedman L.P., Fukasawa T., Gustafsson C.M., Han M. expand/collapse author list , He X., Herman P.K., Hinnebusch A.G., Holmberg S., Holstege F.C.P., Jaehning J.A., Kim Y.-J., Kuras L., Leutz A., Lis J.T., Meisterernest M., Naeaer A.M., Nasmyth K., Parvin J.D., Ptashne M., Reinberg D., Ronne H., Sadowski I., Sakurai H., Sipiczki M., Sternberg P.W., Stillman D.J., Strich R., Struhl K., Svejstrup J.Q., Tuck S., Winston F., Roeder R.G., Kornberg R.D.
Mol. Cell 14:553-557(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NOMENCLATURE.
[14]"Two cyclin-dependent kinases promote RNA polymerase II transcription and formation of the scaffold complex."
Liu Y., Kung C., Fishburn J., Ansari A.Z., Shokat K.M., Hahn S.
Mol. Cell. Biol. 24:1721-1735(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH RNA POLYMERASE II.
[15]"Promoter-dependent roles for the Srb10 cyclin-dependent kinase and the Hda1 deacetylase in Tup1-mediated repression in Saccharomyces cerevisiae."
Green S.R., Johnson A.D.
Mol. Biol. Cell 15:4191-4202(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ASP-304.
[16]"A high resolution protein interaction map of the yeast Mediator complex."
Guglielmi B., van Berkum N.L., Klapholz B., Bijma T., Boube M., Boschiero C., Bourbon H.-M., Holstege F.C.P., Werner M.
Nucleic Acids Res. 32:5379-5391(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: TOPOLOGY OF THE MEDIATOR COMPLEX.
[17]"Site-specific Srb10-dependent phosphorylation of the yeast Mediator subunit Med2 regulates gene expression from the 2-micrometer plasmid."
Hallberg M., Polozkov G.V., Hu G.-Z., Beve J., Gustafsson C.M., Ronne H., Bjoerklund S.
Proc. Natl. Acad. Sci. U.S.A. 101:3370-3375(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[18]"Mediator and TFIIH govern carboxyl-terminal domain-dependent transcription in yeast extracts."
Nair D., Kim Y., Myers L.C.
J. Biol. Chem. 280:33739-33748(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE MEDIATOR COMPLEX.
[19]"Mediator expression profiling epistasis reveals a signal transduction pathway with antagonistic submodules and highly specific downstream targets."
van de Peppel J., Kettelarij N., van Bakel H., Kockelkorn T.T.J.P., van Leenen D., Holstege F.C.P.
Mol. Cell 19:511-522(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[20]"The Saccharomyces cerevisiae Srb8-Srb11 complex functions with the SAGA complex during Gal4-activated transcription."
Larschan E., Winston F.
Mol. Cell. Biol. 25:114-123(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE SRB8-11 COMPLEX.
[21]"Transcriptional activating regions target attached substrates to a cyclin-dependent kinase."
Ansari A.Z., Ogirala A., Ptashne M.
Proc. Natl. Acad. Sci. U.S.A. 102:2346-2349(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
[22]"Genome-wide location of the coactivator mediator: binding without activation and transient Cdk8 interaction on DNA."
Andrau J.-C., van de Pasch L., Lijnzaad P., Bijma T., Koerkamp M.G., van de Peppel J., Werner M., Holstege F.C.P.
Mol. Cell 22:179-192(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L27151 Genomic DNA. Translation: AAA35193.1.
U20222 Genomic DNA. Translation: AAC13785.1. Different initiation.
U44030 Genomic DNA. Translation: AAB68178.1.
BK006949 Genomic DNA. Translation: DAA11387.1.
PIRS50157.
RefSeqNP_015283.1. NM_001183856.1.

3D structure databases

ProteinModelPortalP39073.
SMRP39073. Positions 153-515.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36137. 263 interactions.
DIPDIP-2574N.
IntActP39073. 24 interactions.
MINTMINT-420230.
STRING4932.YPL042C.

Chemistry

BindingDBP39073.
ChEMBLCHEMBL5395.

Proteomic databases

PaxDbP39073.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYPL042C; YPL042C; YPL042C.
GeneID856065.
KEGGsce:YPL042C.

Organism-specific databases

CYGDYPL042c.
SGDS000005963. SSN3.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00530000064012.
HOGENOMHOG000233024.
KOK02208.
OMARRVTHED.
OrthoDBEOG7K3TWD.

Enzyme and pathway databases

BioCycYEAST:G3O-33956-MONOMER.
BRENDA2.7.11.22. 984.

Gene expression databases

GenevestigatorP39073.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
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. 2 hits.
PROSITEPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio981047.
PROP39073.

Entry information

Entry nameSSN3_YEAST
AccessionPrimary (citable) accession number: P39073
Secondary accession number(s): D6W3X1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: September 5, 2006
Last modified: April 16, 2014
This is version 142 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XVI

Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families