GenomeNet

Database: UniProt
Entry: A0A0G2KA28_RAT
LinkDB: A0A0G2KA28_RAT
Original site: A0A0G2KA28_RAT 
ID   A0A0G2KA28_RAT          Unreviewed;       140 AA.
AC   A0A0G2KA28;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   05-JUN-2019, entry version 20.
DE   RecName: Full=Mediator of RNA polymerase II transcription subunit 9 {ECO:0000256|RuleBase:RU364145};
DE   AltName: Full=Mediator complex subunit 9 {ECO:0000256|RuleBase:RU364145};
GN   Name=Med9 {ECO:0000313|Ensembl:ENSRNOP00000075235,
GN   ECO:0000313|RGD:1563669};
GN   Synonyms=MED9 {ECO:0000256|RuleBase:RU364145};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000075235, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000075235, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000075235,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
RA   Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
RA   Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
RA   Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
RA   Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
RA   Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
RA   Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
RA   Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
RA   Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
RA   D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
RA   Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
RA   Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
RA   Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
RA   Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
RA   Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
RA   Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
RA   Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
RA   Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
RA   Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
RA   Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
RA   Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
RA   Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
RA   Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
RA   Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
RA   Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
RA   Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
RA   Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
RA   Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
RA   Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
RA   Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
RA   Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
RA   Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
RA   Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
RA   Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
RA   Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into
RT   mammalian evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000075235}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000075235};
RG   Ensembl;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- FUNCTION: Component of the Mediator complex, a coactivator
CC       involved in the regulated transcription of nearly all RNA
CC       polymerase II-dependent genes. Mediator functions as a bridge to
CC       convey information from gene-specific regulatory proteins to the
CC       basal RNA polymerase II transcription machinery. Mediator is
CC       recruited to promoters by direct interactions with regulatory
CC       proteins and serves as a scaffold for the assembly of a functional
CC       preinitiation complex with RNA polymerase II and the general
CC       transcription factors. {ECO:0000256|RuleBase:RU364145}.
CC   -!- SUBUNIT: Component of the Mediator complex, which is composed of
CC       MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13,
CC       MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21,
CC       MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31,
CC       CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8
CC       subunits form a distinct module termed the CDK8 module. Mediator
CC       containing the CDK8 module is less active than Mediator lacking
CC       this module in supporting transcriptional activation. Individual
CC       preparations of the Mediator complex lacking one or more distinct
CC       subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and
CC       TRAP. {ECO:0000256|RuleBase:RU364145}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU364145,
CC       ECO:0000256|SAAS:SAAS00869478}.
CC   -!- SIMILARITY: Belongs to the Mediator complex subunit 9 family.
CC       {ECO:0000256|RuleBase:RU364145}.
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DR   EMBL; AC122995; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSRNOT00000089724; ENSRNOP00000075235; ENSRNOG00000053961.
DR   RGD; 1563669; Med9.
DR   GeneTree; ENSGT00390000017379; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000053961; Expressed in 10 organ(s), highest expression level in testis.
DR   ExpressionAtlas; A0A0G2KA28; baseline and differential.
DR   GO; GO:0016592; C:mediator complex; IBA:GO_Central.
DR   GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   InterPro; IPR037212; Med7/Med21-like.
DR   InterPro; IPR011425; Med9.
DR   InterPro; IPR039242; MED9_metazoa.
DR   PANTHER; PTHR20844; PTHR20844; 1.
DR   Pfam; PF07544; Med9; 1.
DR   SUPFAM; SSF140718; SSF140718; 1.
PE   3: Inferred from homology;
KW   Activator {ECO:0000256|RuleBase:RU364145};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002494};
KW   Nucleus {ECO:0000256|RuleBase:RU364145,
KW   ECO:0000256|SAAS:SAAS00869474};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Transcription {ECO:0000256|RuleBase:RU364145,
KW   ECO:0000256|SAAS:SAAS00869482};
KW   Transcription regulation {ECO:0000256|RuleBase:RU364145,
KW   ECO:0000256|SAAS:SAAS00869473}.
FT   REGION        1     52       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0G2KA28}.
FT   COILED      112    132       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS     19     47       Pro-rich. {ECO:0000256|MobiDB-lite:
FT                                A0A0G2KA28}.
SQ   SEQUENCE   140 AA;  15567 MW;  B169DCD017C527AF CRC64;
     SSGVAGGRQA EDTLQPPPEL LPESKPPPPP QPLPVAALPP PAAPRPQSPA GVKEENYSFL
     PLVHNVIKCM DKDSPDLHQD LNALKTKFQE MRKLIGTMPG IHVSPEQQQQ QLHSLREQVR
     TKNELLQKYK SLCMFEIPKE
//
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