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MED29_MOUSE
ID   MED29_MOUSE             Reviewed;         199 AA.
AC   Q9DB91;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Mediator of RNA polymerase II transcription subunit 29;
DE   AltName: Full=Intersex-like protein;
DE   AltName: Full=Mediator complex subunit 29;
GN   Name=Med29; Synonyms=Ixl;
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; TISSUE=Cerebellum;
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=C57BL/6J, and FVB/N; TISSUE=Brain, and 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).
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. Associates with the
CC       MED18/MED20 heteromer (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Mediator complex subunit 29 family.
CC       {ECO:0000305}.
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DR   EMBL; AK005112; BAB23826.1; -; mRNA.
DR   EMBL; BC023192; AAH23192.1; -; mRNA.
DR   EMBL; BC083314; AAH83314.1; -; mRNA.
DR   CCDS; CCDS21042.1; -.
DR   RefSeq; NP_080318.2; NM_026042.3.
DR   PDB; 6W1S; EM; 4.02 A; X=52-185.
DR   PDBsum; 6W1S; -.
DR   AlphaFoldDB; Q9DB91; -.
DR   SMR; Q9DB91; -.
DR   BioGRID; 212029; 3.
DR   ComplexPortal; CPX-3264; Core mediator complex.
DR   DIP; DIP-60702N; -.
DR   IntAct; Q9DB91; 3.
DR   STRING; 10090.ENSMUSP00000003536; -.
DR   iPTMnet; Q9DB91; -.
DR   PhosphoSitePlus; Q9DB91; -.
DR   EPD; Q9DB91; -.
DR   MaxQB; Q9DB91; -.
DR   PaxDb; Q9DB91; -.
DR   PeptideAtlas; Q9DB91; -.
DR   PRIDE; Q9DB91; -.
DR   ProteomicsDB; 295921; -.
DR   Antibodypedia; 30311; 63 antibodies from 19 providers.
DR   DNASU; 67224; -.
DR   Ensembl; ENSMUST00000003536; ENSMUSP00000003536; ENSMUSG00000003444.
DR   GeneID; 67224; -.
DR   KEGG; mmu:67224; -.
DR   UCSC; uc009fyt.2; mouse.
DR   CTD; 55588; -.
DR   MGI; MGI:1914474; Med29.
DR   VEuPathDB; HostDB:ENSMUSG00000003444; -.
DR   eggNOG; ENOG502QRNJ; Eukaryota.
DR   GeneTree; ENSGT00390000007540; -.
DR   HOGENOM; CLU_101133_2_0_1; -.
DR   InParanoid; Q9DB91; -.
DR   OMA; MPDNAGP; -.
DR   OrthoDB; 1480686at2759; -.
DR   PhylomeDB; Q9DB91; -.
DR   TreeFam; TF326632; -.
DR   BioGRID-ORCS; 67224; 10 hits in 72 CRISPR screens.
DR   PRO; PR:Q9DB91; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q9DB91; protein.
DR   Bgee; ENSMUSG00000003444; Expressed in dorsal pancreas and 201 other tissues.
DR   Genevisible; Q9DB91; MM.
DR   GO; GO:0070847; C:core mediator complex; ISO:MGI.
DR   GO; GO:0016592; C:mediator complex; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
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; IC:ComplexPortal.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IC:ComplexPortal.
DR   InterPro; IPR021018; Mediator_Med29_met.
DR   PANTHER; PTHR28314; PTHR28314; 1.
DR   Pfam; PF11568; Med29; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Activator; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NX70"
FT   CHAIN           2..199
FT                   /note="Mediator of RNA polymerase II transcription subunit
FT                   29"
FT                   /id="PRO_0000288059"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..47
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NX70"
SQ   SEQUENCE   199 AA;  21011 MW;  60C50BE919D5A2C1 CRC64;
     MAAPQPQAAA VSSASGVSGP GSAGGPGPQQ QPQPTQLVGS AQSGLLQQQQ QDFDPVQRYK
     MLIPQLKESL QTLMKVAAQN LIQNTNIDNG QKSSDAPLQR FDKCLEEFYA LCDQLELCLR
     LAHECLSQSC DSAKHSPTLV PTATKPDAVQ PDSLPYPQYL AVIKAQITCA KDIHTALLDC
     ANKVTGKTTA PSTGPGGSL
 
 
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