Q8IH24 (MED31_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Mediator of RNA polymerase II transcription subunit 31

Alternative name(s):
Mediator complex subunit 31
Protein SOH1
dSOH1

Gene names

Name:	MED31
Synonyms:	Trap18
ORF Names:	CG1057

Organism

Drosophila melanogaster (Fruit fly)

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	204 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. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. Required for activated transcription of the MtnA gene. Ref.4 Ref.5
Subunit structure	Component of the Mediator complex, which includes at least MED4, MED6, MED14, MED17, MED18, MED20, MED21, MED23, MED24, MED27, MED30 and MED31.
Subcellular location	Nucleus Probable.
Sequence similarities	Belongs to the Mediator complex subunit 31 family.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Molecular function	Activator
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	anterior/posterior axis specification, embryo Inferred from mutant phenotype. Source: FlyBase transcription initiation from RNA polymerase II promoter Inferred from direct assay Ref.4. Source: UniProtKB
Cellular component	mediator complex Inferred from direct assay Ref.4. Source: UniProtKB
Molecular function	RNA polymerase II transcription cofactor activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction Ref.4. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8IH24-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q8IH24-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-71: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 204	204	Mediator of RNA polymerase II transcription subunit 31		PRO_0000212530
Regions
	Compositional bias	127 – 189	63	Gln-rich
Natural variations
	Alternative sequence	1 – 71	71	Missing in isoform 2.		VSP_008708

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 31, 2003. Version 2. Checksum: A387204AD57A9157	FASTA	204	23,531
	10 20 30 40 50 60 MAKMYGKGKT AIESEELQKR RWQIELEFVQ CLSNPNYLNF LAQRGFFKDQ SFINYLKYLQ 70 80 90 100 110 120 YWKEPDYAKY LMYPMCLYFL DLLQYEHFRR EIVNSQCCKF IDDQAILQWQ HYTRKRIKLI 130 140 150 160 170 180 ENVTAAQQQQ QQLQQQQQQA NGMEAATGGE SAAPTPNVNG SASTADSQQT SSALQPVQAQ 190 200 PGNPQQQQQI NGVASGANIK LELN
	Isoform 2 [UniParc]. Checksum: 437723F214FDAA6D	FASTA	133	14,834
	10 20 30 40 50 60 MYPMCLYFLD LLQYEHFRRE IVNSQCCKFI DDQAILQWQH YTRKRIKLIE NVTAAQQQQQ 70 80 90 100 110 120 QLQQQQQQAN GMEAATGGES AAPTPNVNGS ASTADSQQTS SALQPVQAQP GNPQQQQQIN 130 GVASGANIKL ELN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[2]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[3]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Strain: Berkeley. Tissue: Embryo and Ovary.
[4]	"Drosophila Mediator complex is broadly utilized by diverse gene-specific transcription factors at different types of core promoters." Park J.M., Gim B.S., Kim J.M., Yoon J.H., Kim H.-S., Kang J.-G., Kim Y.-J. Mol. Cell. Biol. 21:2312-2323(2001) [PubMed: 11259581] [Abstract] Cited for: FUNCTION OF THE MEDIATOR COMPLEX, IDENTIFICATION IN A COMPLEX WITH CDK8; MED4; MED6; MED14; MED17; MED18; MED20 AND MED21.
[5]	"Coactivator cross-talk specifies transcriptional output." Marr M.T. II, Isogai Y., Wright K.J., Tjian R. Genes Dev. 20:1458-1469(2006) [PubMed: 16751183] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014297 Genomic DNA. Translation: AAF52111.1. AE014297 Genomic DNA. Translation: AAN13286.1. AY061423 mRNA. Translation: AAL28971.1. BT001465 mRNA. Translation: AAN71220.1.
RefSeq	NP_649483.1. NM_141226.3. NP_730861.1. NM_169013.2.
UniGene	Dm.1060.
3D structure databases
ProteinModelPortal	Q8IH24.
SMR	Q8IH24. Positions 17-103.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8IH24. 4 interactions.
MINT	MINT-807354.
STRING	Q8IH24.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0078856; FBpp0078496; FBgn0037262. FBtr0078857; FBpp0078497; FBgn0037262. FBtr0305312; FBpp0293855; FBgn0037262.
GeneID	40577.
KEGG	dme:Dmel_CG1057.
Organism-specific databases
CTD	51003.
FlyBase	FBgn0037262. MED31.
Phylogenomic databases
eggNOG	inNOG10376.
GeneTree	EMGT00050000004782.
InParanoid	Q8IH24.
OMA	NQCCKFI.
OrthoDB	EOG412JNS.
PhylomeDB	Q8IH24.
Gene expression databases
Bgee	Q8IH24.
GermOnline	CG1057. Drosophila melanogaster.
Family and domain databases
InterPro	IPR008831. Mediator_Med31. [Graphical view]
KO	K15153.
PANTHER	PTHR13186. SOH1. 1 hit.
Pfam	PF05669. Med31. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	819475.

Entry information

Entry name

MED31_DROME

Accession

Primary (citable) accession number: Q8IH24
Secondary accession number(s): A4V2E4, Q9VN40

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2003
Last sequence update:	October 31, 2003
Last modified:	January 25, 2012
This is version 74 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project