MED26_BOVIN
ID MED26_BOVIN Reviewed; 599 AA.
AC A5PK23;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 26;
DE AltName: Full=Cofactor required for Sp1 transcriptional activation subunit 7;
DE Short=CRSP complex subunit 7;
DE AltName: Full=Mediator complex subunit 26;
GN Name=MED26; Synonyms=CRSP7;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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 pre-initiation complex with RNA polymerase II
CC and the general transcription factors (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the Mediator complex, which is composed of MED1,
CC MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L,
CC MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23,
CC MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and
CC CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct
CC module termed the CDK8 module. Mediator containing the CDK8 module is
CC less active than Mediator lacking this module in supporting
CC transcriptional activation. Individual preparations of the Mediator
CC complex lacking one or more distinct subunits have been variously
CC termed ARC, CRSP, DRIP, PC2, SMCC and TRAP. Interacts with CEBPB (when
CC not methylated) (By similarity). {ECO:0000250|UniProtKB:O95402,
CC ECO:0000250|UniProtKB:Q7TN02}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 26 family.
CC {ECO:0000305}.
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DR EMBL; BC142325; AAI42326.1; -; mRNA.
DR RefSeq; NP_001092358.1; NM_001098888.1.
DR AlphaFoldDB; A5PK23; -.
DR SMR; A5PK23; -.
DR STRING; 9913.ENSBTAP00000006986; -.
DR PaxDb; A5PK23; -.
DR PRIDE; A5PK23; -.
DR GeneID; 506331; -.
DR KEGG; bta:506331; -.
DR CTD; 9441; -.
DR eggNOG; KOG1105; Eukaryota.
DR HOGENOM; CLU_478915_0_0_1; -.
DR InParanoid; A5PK23; -.
DR OrthoDB; 459216at2759; -.
DR TreeFam; TF328436; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0070847; C:core mediator complex; IBA:GO_Central.
DR GO; GO:0016592; C:mediator complex; ISS:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR Gene3D; 1.20.930.10; -; 1.
DR InterPro; IPR042376; MED26.
DR InterPro; IPR031416; Med26_C.
DR InterPro; IPR031417; Med26_Mid.
DR InterPro; IPR003617; TFIIS/CRSP70_N_sub.
DR InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR InterPro; IPR017923; TFIIS_N.
DR PANTHER; PTHR15201; PTHR15201; 1.
DR Pfam; PF08711; Med26; 1.
DR Pfam; PF15693; Med26_C; 1.
DR Pfam; PF15694; Med26_M; 1.
DR SMART; SM00509; TFS2N; 1.
DR SUPFAM; SSF47676; SSF47676; 1.
DR PROSITE; PS51319; TFIIS_N; 1.
PE 2: Evidence at transcript level;
KW Activator; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..599
FT /note="Mediator of RNA polymerase II transcription subunit
FT 26"
FT /id="PRO_0000304958"
FT DOMAIN 10..87
FT /note="TFIIS N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00649"
FT REGION 98..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..222
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95402"
FT MOD_RES 469
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95402"
SQ SEQUENCE 599 AA; 65515 MW; 38592548FB7DEDD9 CRC64;
MTAAPPSPQQ IRDRLLQAID PQSNIRNMVA VQEVISSLEK YPITKEALEE TRLGKLINDV
RKKTKNEELA KRAKKLLRSW QKLIEPVHQN EAALRGLAGA PGSANGGAHN CRPEAGAAGP
PKSVHDLKYR NDMPRLCGQR LDRLGSRKRR GDQRDLGHPG PPPKVSKASH DSLVPNSSPL
PTNGISGSPE SFPSPLDSSG HVGPEGNRLE HGENDKHSGK IPVNAVRPHT SSPGLGKPPG
PCLQTKAVVL QQLDKVDETP GPPHPKGPPR CSLGSRNSRH EGSFARQRSP YTYKGSLPSP
SPRPQSLDAT QVPSPLPLAQ PSTPPVRRLE LLPSAESPVR WLEQPEGHQR LAGLGCKAGL
PPAEPLLPRA GFSPDSSKAD SDAASSGGSD SKKKKRYRPR DYTVNLDGQV AEAGVKPVRL
KERKLTFDPM TRQIKPLTQK EPVRADSPVH TEQPRTELDK PEAKASLQSP FEQTNWKELS
RNEIIQSYLS RQSSLLSSSG AQTPGAHHFM SEYLKQEEST RRGARKPHVL VPHGPPTDFP
GLSREVTRDD LDKIQAHQWP GVNGCQDTQG NWYDWTQCIS LDPHGDDGRL NILPYVCLD
