Reviewed, UniProtKB/Swiss-Prot P32569 (MED17_YEAST)

Names and origin

Protein names

Recommended name:
    Mediator of RNA polymerase II transcription subunit 17
Alternative name(s):
    Mediator complex subunit 17
    Suppressor of RNA polymerase B 4

Gene names

Name:	SRB4
Synonyms:	MED17
Ordered Locus Names:	YER022W

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	687 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.6 Ref.9 Ref.16 Ref.18 Ref.25
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. The head module may also interact with the TFIIF complex. SRB4/MED17 interacts directly with MED6, MED11, ROX3/MED19, SRB2/MED20 and SRB6/MED22. Interacts directly with the activator GAL4. Ref.9 Ref.25 Ref.7 Ref.8 Ref.14 Ref.21
Subcellular location	Nucleus Ref.10 Ref.19.
Miscellaneous	Present with 1720 molecules/cell in log phase SD medium. Ref.11
Sequence similarities	Belongs to the Mediator complex subunit 17 family.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Molecular function	Activator
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: InterPro transcription from RNA polymerase II promoter Inferred from direct assay. Source: SGD
Cellular component	mediator complex Ref.25 Inferred from direct assay. Source: SGD
Molecular function	RNA polymerase II transcription mediator activity Inferred from direct assay. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AHC2	P25649	1	EBI-18025,EBI-21993
CAF40	P53829	1	EBI-18025,EBI-28306
MED6	P38782	1	EBI-18025,EBI-10667
MED8	P38304	1	EBI-18025,EBI-20932
YAP1	P19880	1	EBI-18025,EBI-31265

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 687	687	Mediator of RNA polymerase II transcription subunit 17		PRO_0000096366
Amino acid modifications
	Modified residue	36	1	Phosphoserine Ref.23
	Modified residue	37	1	Phosphoserine Ref.22
	Modified residue	40	1	Phosphoserine Ref.23 Ref.22 Ref.17
	Modified residue	42	1	Phosphothreonine Ref.23
	Modified residue	43	1	Phosphoserine Ref.23
	Modified residue	57	1	Phosphoserine Ref.23 Ref.22
Experimental info
	Mutagenesis	353	1	G → C in SRB4-1; suppresses the phenotypic defects of a RNA polymerase II CTD truncation. Ref.1
	Sequence conflict	430 – 431	2	QL → PI in CAA40613. Ref.4
	Sequence conflict	647	1	I → T in AAT93185. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P32569-1 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: D25B2993A1BADFD6	FASTA	687	78,476
	10 20 30 40 50 60 MTTEDPDSNH LSSETGIKLA LDPNLITLAL SSNPNSSLHS PTSDEPVPES AGKADTSIRL 70 80 90 100 110 120 EGDELENKTK KDNDKNLKFL KNKDSLVSNP HEIYGSMPLE QLIPIILRQR GPGFKFVDLN 130 140 150 160 170 180 EKELQNEIKQ LGSDSSDGHN SEKKDTDGAD ENVQIGEDFM EVDYEDKDNP VDSRNETDHK 190 200 210 220 230 240 TNENGETDDN IETVMTQEQF VKRRRDMLEH INLAMNESSL ALEFVSLLLS SVKESTGMSS 250 260 270 280 290 300 MSPFLRKVVK PSSLNSDKIP YVAPTKKEYI ELDILNKGWK LQSLNESKDL LRASFNKLSS 310 320 330 340 350 360 ILQNEHDYWN KIMQSISNKD VIFKIRDRTS GQKLLAIKYG YEDSGSTYKH DRGIANIRNN 370 380 390 400 410 420 IESQNLDLIP HSSSVFKGTD FVHSVKKFLR VRIFTKIESE DDYILSGESV MDRDSESEEA 430 440 450 460 470 480 ETKDIRKQIQ LLKKIIFEKE LMYQIKKECA LLISYGVSIE NENKVIIELP NEKFEIELLS 490 500 510 520 530 540 LDDDSIVNHE QDLPKINDKR ANLMLVMLRL LLVVIFKKTL RSRISSPHGL INLNVDDDIL 550 560 570 580 590 600 IIRPILGKVR FANYKLLLKK IIKDYVLDIV PGSSITETEV EREQPQENKN IDDENITKLN 610 620 630 640 650 660 KEIRAFDKLL NIPRRELKIN LPLTEHKSPN LSLMLESPNY CNALIHIKFS AGTEANAVSF 670 680 DTTFSDFKEV EDFLHFIVAE YIQQKKV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A multisubunit complex associated with the RNA polymerase II CTD and TATA-binding protein in yeast." Thompson C.M., Koleske A.J., Chao D.M., Young R.A. Cell 73:1361-1375(1993) [PubMed: 8324825] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF GLY-353. Strain: Z28.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome V." Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W. Nature 387:78-81(1997) [PubMed: 9169868] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"ore2, a mutation affecting proline biosynthesis in the yeast Saccharomyces cerevisiae, leads to a cdc phenotype." Neuville P., Aigle M. Mol. Gen. Genet. 234:193-200(1992) [PubMed: 1508147] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 430-687. Strain: ATCC 44827 / SKQ2N.
[5]	"A multiprotein mediator of transcriptional activation and its interaction with the C-terminal repeat domain of RNA polymerase II." Kim Y.-J., Bjoerklund S., Li Y., Sayre M.H., Kornberg R.D. Cell 77:599-608(1994) [PubMed: 8187178] [Abstract] Cited for: COMPONENT OF MEDIATOR COMPLEX.
[6]	"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: 9845373] [Abstract] Cited for: FUNCTION.
[7]	"An activator target in the RNA polymerase II holoenzyme." Koh S.S., Ansari A.Z., Ptashne M., Young R.A. Mol. Cell 1:895-904(1998) [PubMed: 9660972] [Abstract] Cited for: INTERACTION WITH GAL4; SRB2 AND SRB6.
[8]	"Interplay of positive and negative regulators in transcription initiation by RNA polymerase II holoenzyme." Lee T.I., Wyrick J.J., Koh S.S., Jennings E.G., Gadbois E.L., Young R.A. Mol. Cell. Biol. 18:4455-4462(1998) [PubMed: 9671455] [Abstract] Cited for: INTERACTION WITH MED6 AND SRB6.
[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: 11555651] [Abstract] Cited for: INTERACTION WITH MED11 AND ROX3, FUNCTION OF THE MEDIATOR COMPLEX, INTERACTION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE II.
[10]	"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: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[11]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[12]	"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: 15175151] [Abstract] Cited for: NOMENCLATURE.
[13]	"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: 15477388] [Abstract] Cited for: TOPOLOGY OF THE MEDIATOR COMPLEX.
[14]	"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: 15710619] [Abstract] Cited for: INTERACTION WITH MED6.
[15]	"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: 16002404] [Abstract] Cited for: CHARACTERIZATION OF THE MEDIATOR COMPLEX.
[16]	"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: 16076843] [Abstract] Cited for: FUNCTION OF THE MEDIATOR COMPLEX.
[17]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40, MASS SPECTROMETRY.
[18]	"Mediator as a general transcription factor." Takagi Y., Kornberg R.D. J. Biol. Chem. 281:80-89(2006) [PubMed: 16263706] [Abstract] Cited for: FUNCTION OF THE MEDIATOR COMPLEX.
[19]	"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: 16630888] [Abstract] Cited for: SUBCELLULAR LOCATION.
[20]	"Activator-specific recruitment of Mediator in vivo." Fan X., Chou D.M., Struhl K. Nat. Struct. Mol. Biol. 13:117-120(2006) [PubMed: 16429153] [Abstract] Cited for: ASSOCIATION WITH PROMOTER REGIONS.
[21]	"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: 17192271] [Abstract] Cited for: CHARACTERIZATION OF THE MEDIATOR COMPLEX, INTERACTION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE II.
[22]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-40 AND SER-57, MASS SPECTROMETRY.
[23]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-40; THR-42; SER-43 AND SER-57, MASS SPECTROMETRY.
[24]	"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: 12191485] [Abstract] Cited for: ELECTRON MICROSCOPY OF MEDIATOR COMPLEX IN COMPLEX WITH RNA POLYMERASE II.
[25]	"Head module control of mediator interactions." Takagi Y., Calero G., Komori H., Brown J.A., Ehrensberger A.H., Hudmon A., Asturias F.J., Kornberg R.D. Mol. Cell 23:355-364(2006) [PubMed: 16885025] [Abstract] Cited for: ELECTRON MICROSCOPY OF THE MEDIATOR COMPLEX HEAD MODULE, FUNCTION OF THE MEDIATOR COMPLEX HEAD MODULE, INTERACTION OF THE MEDIATOR COMPLEX HEAD MODULE WITH RNA POLYMERASE II AND TFIIF, INTERACTION WITH MED6; MED8; MED11; SRB2; SRB5 AND SRB6.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L12026 Unassigned DNA. Translation: AAA02632.1. U18778 Genomic DNA. Translation: AAB64555.1. AY693166 Genomic DNA. Translation: AAT93185.1. X57338 Genomic DNA. Translation: CAA40613.1.
PIR	A40711.
RefSeq	NP_010939.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-152N.
IntAct	P32569. 116 interactions.
STRING	P32569.
Proteomic databases
PeptideAtlas	P32569.
Genome annotation databases
Ensembl	YER022W; YER022W; YER022W; Saccharomyces cerevisiae. [Genome view]
GeneID	856743.
KEGG	sce:YER022W.
NMPDR	fig|4932.3.peg.1999.
Organism-specific databases
CYGD	YER022w.
SGD	S000000824. SRB4.
Phylogenomic databases
eggNOG	fuNOG04616.
HOGENOM	HBG203745.
OMA	YILSGES.
OrthoDB	EOG905TH9.
PhylomeDB	P32569.
Gene expression databases
ArrayExpress	P32569.
Genevestigator	P32569.
GermOnline	YER022W. Saccharomyces cerevisiae.
Family and domain databases
ProtoNet	Search...
Other Resources
NextBio	982879.

Entry information

Entry name

MED17_YEAST

Accession

Primary (citable) accession number: P32569
Secondary accession number(s): Q06790, Q6B1B4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	February 9, 2010
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)