MED11_SCHPO
ID MED11_SCHPO Reviewed; 112 AA.
AC Q9P6Q0;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 11;
DE AltName: Full=Mediator complex subunit 11;
GN Name=med11; ORFNames=SPAC644.10;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP IDENTIFICATION, REVISION OF GENE MODEL, AND INTERACTION WITH MED22 AND
RP MED17.
RX PubMed=21498544; DOI=10.1093/nar/gkr229;
RA Seizl M., Lariviere L., Pfaffeneder T., Wenzeck L., Cramer P.;
RT "Mediator head subcomplex Med11/22 contains a common helix bundle building
RT block with a specific function in transcription initiation complex
RT stabilization.";
RL Nucleic Acids Res. 39:6291-6304(2011).
CC -!- FUNCTION: Component of the Mediator complex, a coactivator involved in
CC the regulated transcription of nearly all RNA polymerase II-dependent
CC genes. Mediator functions as a bridge to convey information from gene-
CC specific regulatory proteins to the basal RNA polymerase II
CC transcription machinery. Mediator is recruited to promoters by direct
CC interactions with regulatory proteins and serves as a scaffold for the
CC assembly of a functional preinitiation complex (PIC) with RNA
CC polymerase II and the general transcription factors. The essential
CC med11/22 heterodimer specifically functions in promoting stable PIC
CC formation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the Mediator complex, which is composed of at
CC least 21 subunits that form three structurally distinct submodules. The
CC Mediator head module, the middle module, and the tail module. The head
CC and the middle modules interact directly with RNA polymerase II,
CC whereas the elongated tail module interacts with gene-specific
CC regulatory proteins (By similarity). Med11 is part of the head module.
CC Forms a heterodimer with med22. The med11/22 heterodimer binds to and
CC stabilizes the central head subunit med17. {ECO:0000250,
CC ECO:0000269|PubMed:21498544}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 11 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB90137.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CU329670; CAB90137.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_593878.1; NM_001019308.2.
DR PDB; 4H63; X-ray; 3.40 A; K=1-112.
DR PDB; 5N9J; X-ray; 3.40 A; V=1-112.
DR PDB; 5U0P; EM; 4.40 A; K=1-111.
DR PDB; 5U0S; EM; 7.80 A; K=1-111.
DR PDBsum; 4H63; -.
DR PDBsum; 5N9J; -.
DR PDBsum; 5U0P; -.
DR PDBsum; 5U0S; -.
DR AlphaFoldDB; Q9P6Q0; -.
DR SMR; Q9P6Q0; -.
DR DIP; DIP-60134N; -.
DR IntAct; Q9P6Q0; 7.
DR STRING; 4896.SPAC644.10.1; -.
DR iPTMnet; Q9P6Q0; -.
DR MaxQB; Q9P6Q0; -.
DR PaxDb; Q9P6Q0; -.
DR PRIDE; Q9P6Q0; -.
DR GeneID; 2543656; -.
DR KEGG; spo:SPAC644.10; -.
DR PomBase; SPAC644.10; med11.
DR HOGENOM; CLU_2147321_0_0_1; -.
DR PRO; PR:Q9P6Q0; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0016592; C:mediator complex; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:PomBase.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IC:PomBase.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Nucleus; Reference proteome.
FT CHAIN 1..112
FT /note="Mediator of RNA polymerase II transcription subunit
FT 11"
FT /id="PRO_0000304078"
FT HELIX 17..30
FT /evidence="ECO:0007829|PDB:4H63"
FT HELIX 33..46
FT /evidence="ECO:0007829|PDB:4H63"
FT HELIX 51..81
FT /evidence="ECO:0007829|PDB:4H63"
FT HELIX 98..110
FT /evidence="ECO:0007829|PDB:4H63"
SQ SEQUENCE 112 AA; 12631 MW; 8D2077ECDFE8E3DD CRC64;
MTNSDDDLFS EKSTSSDTQQ VQNILELEAK IPDILSSAGK CIEAIQLNNS LEDFRKYSKE
FLETVEFIST GLRRQALELE KAEVPVVSLQ PKKRYASTPL SNLIFDQSSK LM