Q06213 (MED10_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Mediator of RNA polymerase II transcription subunit 10

Alternative name(s):
Mediator complex subunit 10
Negative regulator of URS2 protein 2

Gene names

Name:	NUT2
Synonyms:	MED10
Ordered Locus Names:	YPR168W
ORF Names:	P9325.2

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	157 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins. Ref.3 Ref.5 Ref.12 Ref.13
Subunit structure	Component of the Mediator complex, which is composed of at least 21 subunits that form three structurally distinct submodules. The Mediator head module contains MED6, MED8, MED11, SRB4/MED17, SRB5/MED18, ROX3/MED19, SRB2/MED20 and SRB6/MED22, the middle module contains MED1, MED4, NUT1/MED5, MED7, CSE2/MED9, NUT2/MED10, SRB7/MED21 and SOH1/MED31, and the tail module contains MED2, PGD1/MED3, RGR1/MED14, GAL11/MED15 and SIN4/MED16. The head and the middle modules interact directly with RNA polymerase II, whereas the elongated tail module interacts with gene-specific regulatory proteins. NUT2/MED10 interacts directly with SRB7/MED21. Ref.5 Ref.10 Ref.14
Subcellular location	Nucleus Ref.6.
Miscellaneous	Present with 1472 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the Mediator complex subunit 10 family.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Molecular function	Activator
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype PubMed 16452140. Source: SGD positive regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype PubMed 9891034. Source: SGD
Cellular_component	core mediator complex Inferred from direct assay PubMed 9891034. Source: SGD mediator complex Inferred from electronic annotation. Source: InterPro
Molecular_function	RNA polymerase II transcription cofactor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
LSM1	P47017	1	EBI-12414,EBI-174
SOH1	P38633	1	EBI-12414,EBI-17658

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 157	157	Mediator of RNA polymerase II transcription subunit 10		PRO_0000096357

Sequences

	Sequence		Length	Mass (Da)
	Q06213 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 0E77A43A5222E862	FASTA	157	17,908
	10 20 30 40 50 60 MNGNSTNNEQ LQQELATTQD QVASIIESFV ELGVSIYDFP GTPEATKGMI TNLQRNVDRL 70 80 90 100 110 120 YKLNVRSNDP QSSLSKVDIP LEVVQYIEDG RNPDIYTREF VEAIRRSNQY QRGKMHGLKQ 130 140 150 LRDSLADKIV DEFPELKEPV EDIIKRTSPI DNVSNTH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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. , 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 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"Nuclear proteins Nut1p and Nut2p cooperate to negatively regulate a Swi4p-dependent lacZ reporter gene in Saccharomyces cerevisiae." Tabtiang R.K., Herskowitz I. Mol. Cell. Biol. 18:4707-4718(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[4]	"Identification of new mediator subunits in the RNA polymerase II holoenzyme from Saccharomyces cerevisiae." Gustafsson C.M., Myers L.C., Beve J., Spaahr H., Lui M., Erdjument-Bromage H., Tempst P., Kornberg R.D. J. Biol. Chem. 273:30851-30854(1998) [PubMed] [Europe PMC] [Abstract] Cited for: COMPONENT OF MEDIATOR COMPLEX.
[5]	"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 SRB7, FUNCTION OF THE MEDIATOR COMPLEX, INTERACTION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE II.
[6]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]	"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. , 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.
[9]	"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.
[10]	"A conserved mediator hinge revealed in the structure of the MED7-MED21 (Med7-Srb7) heterodimer." Baumli S., Hoeppner S., Cramer P. J. Biol. Chem. 280:18171-18178(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SRB7.
[11]	"Preponderance of free mediator in the yeast Saccharomyces cerevisiae." Takagi Y., Chadick J.Z., Davis J.A., Asturias F.J. J. Biol. Chem. 280:31200-31207(2005) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF THE MEDIATOR COMPLEX.
[12]	"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.
[13]	"Mediator as a general transcription factor." Takagi Y., Kornberg R.D. J. Biol. Chem. 281:80-89(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE MEDIATOR COMPLEX.
[14]	"Med19(Rox3) regulates intermodule interactions in the Saccharomyces cerevisiae mediator complex." Baidoobonso S.M., Guidi B.W., Myers L.C. J. Biol. Chem. 282:5551-5559(2007) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF THE MEDIATOR COMPLEX, INTERACTION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE II.
[15]	"Structure of the yeast RNA polymerase II holoenzyme: mediator conformation and polymerase interaction." Davis J.A., Takagi Y., Kornberg R.D., Asturias F.J. Mol. Cell 10:409-415(2002) [PubMed] [Europe PMC] [Abstract] Cited for: ELECTRON MICROSCOPY OF MEDIATOR COMPLEX IN COMPLEX WITH RNA POLYMERASE II.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U25840 Genomic DNA. Translation: AAB68155.1. BK006949 Genomic DNA. Translation: DAA11585.1.
PIR	S59827.
RefSeq	NP_015494.1. NM_001184265.1.
3D structure databases
ProteinModelPortal	Q06213.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-3922N.
IntAct	Q06213. 9 interactions.
MINT	MINT-503239.
STRING	4932.YPR168W.
Proteomic databases
PaxDb	Q06213.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YPR168W; YPR168W; YPR168W.
GeneID	856297.
KEGG	sce:YPR168W.
Organism-specific databases
CYGD	YPR168w.
SGD	S000006372. NUT2.
Phylogenomic databases
eggNOG	NOG245504.
GeneTree	ENSGT00390000014501.
HOGENOM	HOG000001009.
KO	K15151.
OMA	IRRSNQY.
OrthoDB	EOG44TSJC.
Gene expression databases
Genevestigator	Q06213.
GermOnline	YPR168W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR019145. Mediator_Med10. [Graphical view]
Pfam	PF09748. Med10. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	981650.

Entry information

Entry name

MED10_YEAST

Accession

Primary (citable) accession number: Q06213
Secondary accession number(s): D6W4G9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program