Reviewed, UniProtKB/Swiss-Prot P38633 (MED31_YEAST)

Names and origin

Protein names

Recommended name:
    Mediator of RNA polymerase II transcription subunit 31
Alternative name(s):
    Mediator complex subunit 31
    Hpr1 suppressor protein 1

Gene names

Name:	SOH1
Synonyms:	MED31
Ordered Locus Names:	YGL127C
ORF Names:	G2864

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	127 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.11 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.
Subcellular location	Nucleus Ref.5.
Miscellaneous	Present with 468 molecules/cell in log phase SD medium. Ref.6
Sequence similarities	Belongs to the Mediator complex subunit 31 family.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Molecular function	Activator
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	DNA repair Inferred from physical interaction. Source: SGD meiotic gene conversion Inferred from mutant phenotype. Source: SGD meiotic sister chromatid segregation Inferred from mutant phenotype. Source: SGD negative regulation of transposition, RNA-mediated Inferred from mutant phenotype. Source: SGD regulation of transcription Inferred from electronic annotation. Source: UniProtKB-KW transcription from RNA polymerase II promoter Inferred from direct assay. Source: SGD
Cellular component	mediator complex Ref.7 Inferred from direct assay. Source: SGD
Molecular function	RNA polymerase II transcription mediator activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ADE2	P21264	1	EBI-17658,EBI-14252
ATG17	Q06410	1	EBI-17658,EBI-30856
MED4	Q12343	1	EBI-17658,EBI-31503
MED7	Q08278	1	EBI-17658,EBI-10674
MED8	P38304	1	EBI-17658,EBI-20932
NUT2	Q06213	1	EBI-17658,EBI-12414
SRB7	P47822	1	EBI-17658,EBI-18046
STD1	Q02794	1	EBI-17658,EBI-18344
TVP23	P38962	1	EBI-17658,EBI-22146

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 127

127

Mediator of RNA polymerase II transcription subunit 31

PRO_0000212534

Secondary structure

1

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127

Helix Strand Turn

Details...

Helix

22 – 32

11

Helix

36 – 43

8

Helix

47 – 49

3

Helix

53 – 60

8

Helix

61 – 65

5

Helix

69 – 72

4

Helix

77 – 85

9

Turn

89 – 91

3

Sequences

	Sequence		Length	Mass (Da)
	P38633-1 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: A2FE3B62ADC14011	FASTA	127	14,741
	10 20 30 40 50 60 MSSTNGNAPA TPSSDQNPLP TRFEVELEFI QSLANIQYVT YLLTQQQIWK SPNFKNYLKY 70 80 90 100 110 120 LEYWCNPPYS QCIVYPNCLF ILKLLNGFME SAIVNEDGLL EGLDELPKII QLQGPQWMNE MVERWAN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of mutations that suppress the temperature-sensitive growth of the hpr1 delta mutant of Saccharomyces cerevisiae." Fan H.-Y., Klein H.L. Genetics 137:945-956(1994) [PubMed: 7982575] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 200060 / W303.
[2]	"Sequence analysis of a 10 kb DNA fragment from yeast chromosome VII reveals a novel member of the DnaJ family." Rodriguez-Belmonte E., Rodriguez Torres A.M., Tizon B., Cadahia J.L., Gonzalez-Siso I., Ramil E., Becerra M., Gonzalez-Dominguez M., Cerdan E. Yeast 12:145-148(1996) [PubMed: 8686378] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K. Nature 387:81-84(1997) [PubMed: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[4]	"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.
[5]	"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].
[6]	"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].
[7]	"The Soh1/MED31 protein is an ancient component of Schizosaccharomyces pombe and Saccharomyces cerevisiae Mediator." Linder T., Gustafsson C.M. J. Biol. Chem. 279:49455-49459(2004) [PubMed: 15356001] [Abstract] Cited for: COMPONENT OF MEDIATOR COMPLEX.
[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: 15175151] [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: 15477388] [Abstract] Cited for: TOPOLOGY OF THE MEDIATOR COMPLEX.
[10]	"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.
[11]	"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.
[12]	"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: 16109375] [Abstract] Cited for: FUNCTION.
[13]	"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.
[14]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L31921 Genomic DNA. Translation: AAA35066.1.
X87252 Genomic DNA. Translation: CAA60704.1.
Z72649 Genomic DNA. Translation: CAA96836.1.
AY693006 Genomic DNA. Translation: AAT93025.1.

PIR

S47895.

RefSeq

NP_011388.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3FBI	X-ray	2.80	B/D	1-127	[»]
3FBN	X-ray	3.01	B/D	1-127	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1179N.

IntAct

P38633. 89 interactions.

STRING

P38633.

Genome annotation databases

Ensembl

YGL127C; YGL127C; YGL127C; Saccharomyces cerevisiae. [Genome view]

GeneID

852750.

KEGG

sce:YGL127C.

NMPDR

fig|4932.3.peg.2492.

Organism-specific databases

CYGD

YGL127c.

SGD

S000003095. SOH1.

Phylogenomic databases

HOGENOM

HBG628910.

OMA

NEMVERW.

OrthoDB

EOG9VT7F5.

Gene expression databases

ArrayExpress

P38633.

Genevestigator

P38633.

GermOnline

YGL127C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR008831. Mediator_Med31.
[Graphical view]

PANTHER

PTHR13186. SOH1. 1 hit.

Pfam

PF05669. SOH1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

972180.

Entry information

Entry name

MED31_YEAST

Accession

Primary (citable) accession number: P38633

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	December 15, 2009
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)