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MED30_MOUSE
ID   MED30_MOUSE             Reviewed;         178 AA.
AC   Q9CQI9;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Mediator of RNA polymerase II transcription subunit 30;
DE   AltName: Full=Mediator complex subunit 30;
DE   AltName: Full=Thyroid hormone receptor-associated protein 6;
DE   AltName: Full=Thyroid hormone receptor-associated protein complex 25 kDa component;
DE            Short=Trap25;
GN   Name=Med30; Synonyms=Thrap6, Trap25;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and DBA/2J; TISSUE=Liver, and Pancreas;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, Lung, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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 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 (By similarity).
CC       {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q9CQI9; Q9R0X0: Med20; NbExp=2; IntAct=EBI-309220, EBI-398698;
CC       Q9CQI9; Q9D7W5: Med8; NbExp=2; IntAct=EBI-309220, EBI-7990252;
CC       Q9CQI9; Q9NVC6: MED17; Xeno; NbExp=2; IntAct=EBI-309220, EBI-394562;
CC       Q9CQI9; Q15528: MED22; Xeno; NbExp=6; IntAct=EBI-309220, EBI-394687;
CC       Q9CQI9; Q6P2C8: MED27; Xeno; NbExp=2; IntAct=EBI-309220, EBI-394603;
CC       Q9CQI9; Q9H204: MED28; Xeno; NbExp=2; IntAct=EBI-309220, EBI-514199;
CC       Q9CQI9; Q9NX70: MED29; Xeno; NbExp=2; IntAct=EBI-309220, EBI-394656;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the Mediator complex subunit 30 family.
CC       {ECO:0000305}.
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DR   EMBL; AK007739; BAB25226.1; -; mRNA.
DR   EMBL; AK011104; BAB27401.1; -; mRNA.
DR   EMBL; AK146250; BAE27012.1; -; mRNA.
DR   EMBL; BC020113; AAH20113.1; -; mRNA.
DR   CCDS; CCDS27465.1; -.
DR   RefSeq; NP_081488.1; NM_027212.2.
DR   PDB; 6W1S; EM; 4.02 A; Y=27-178.
DR   PDBsum; 6W1S; -.
DR   AlphaFoldDB; Q9CQI9; -.
DR   SMR; Q9CQI9; -.
DR   BioGRID; 213682; 3.
DR   ComplexPortal; CPX-3264; Core mediator complex.
DR   IntAct; Q9CQI9; 15.
DR   MINT; Q9CQI9; -.
DR   STRING; 10090.ENSMUSP00000042204; -.
DR   PhosphoSitePlus; Q9CQI9; -.
DR   EPD; Q9CQI9; -.
DR   MaxQB; Q9CQI9; -.
DR   PaxDb; Q9CQI9; -.
DR   PeptideAtlas; Q9CQI9; -.
DR   PRIDE; Q9CQI9; -.
DR   ProteomicsDB; 295871; -.
DR   Antibodypedia; 26728; 202 antibodies from 25 providers.
DR   DNASU; 69790; -.
DR   Ensembl; ENSMUST00000037115; ENSMUSP00000042204; ENSMUSG00000038622.
DR   GeneID; 69790; -.
DR   KEGG; mmu:69790; -.
DR   UCSC; uc007vrg.1; mouse.
DR   CTD; 90390; -.
DR   MGI; MGI:1917040; Med30.
DR   VEuPathDB; HostDB:ENSMUSG00000038622; -.
DR   eggNOG; ENOG502QV3C; Eukaryota.
DR   GeneTree; ENSGT00390000010887; -.
DR   HOGENOM; CLU_074190_1_1_1; -.
DR   InParanoid; Q9CQI9; -.
DR   OMA; KHDDRGV; -.
DR   OrthoDB; 1549016at2759; -.
DR   PhylomeDB; Q9CQI9; -.
DR   TreeFam; TF324588; -.
DR   Reactome; R-MMU-212436; Generic Transcription Pathway.
DR   BioGRID-ORCS; 69790; 18 hits in 74 CRISPR screens.
DR   ChiTaRS; Med30; mouse.
DR   PRO; PR:Q9CQI9; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; Q9CQI9; protein.
DR   Bgee; ENSMUSG00000038622; Expressed in medial ganglionic eminence and 255 other tissues.
DR   Genevisible; Q9CQI9; MM.
DR   GO; GO:0070847; C:core mediator complex; ISO:MGI.
DR   GO; GO:0016592; C:mediator complex; IDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0000151; C:ubiquitin ligase complex; ISO:MGI.
DR   GO; GO:0046966; F:nuclear thyroid hormone receptor binding; ISO:MGI.
DR   GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR   GO; GO:0003712; F:transcription coregulator activity; ISO:MGI.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
DR   GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IC:ComplexPortal.
DR   GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; ISO:MGI.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR   GO; GO:0016567; P:protein ubiquitination; ISO:MGI.
DR   GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IC:ComplexPortal.
DR   GO; GO:0035019; P:somatic stem cell population maintenance; IMP:MGI.
DR   InterPro; IPR021019; Mediator_Med30_met.
DR   PANTHER; PTHR31705; PTHR31705; 1.
DR   Pfam; PF11315; Med30; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Activator; Coiled coil; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q96HR3"
FT   CHAIN           2..178
FT                   /note="Mediator of RNA polymerase II transcription subunit
FT                   30"
FT                   /id="PRO_0000239407"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          134..173
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96HR3"
SQ   SEQUENCE   178 AA;  20358 MW;  8766D3C929C1E98D CRC64;
     MSTPPLAPTG MASGPFGGPQ AQQAAREVNT ATLCRIGQET VQDIVYRTME IFQLLRNMQL
     PNGVTYHTGT YQDRLTKLQD HLRQLSILFR KLRLVYDKCN ENCGGMDPIP VEQLIPYVDE
     DGSKNDDRAG PPRFASEERR EIVEVNKKLK QKNQQLKQIM DQLRNLIWDI NAMLAMRN
 
 
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