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MED24_RAT
ID   MED24_RAT               Reviewed;         987 AA.
AC   Q4V8B3;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Mediator of RNA polymerase II transcription subunit 24;
DE   AltName: Full=Mediator complex subunit 24;
DE   AltName: Full=Thyroid hormone receptor-associated protein 4;
GN   Name=Med24; Synonyms=Thrap4;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-860 AND SER-871, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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. Interacts with AR (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the Mediator complex subunit 24 family.
CC       {ECO:0000305}.
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DR   EMBL; BC097461; AAH97461.1; -; mRNA.
DR   RefSeq; NP_001029251.1; NM_001034079.1.
DR   AlphaFoldDB; Q4V8B3; -.
DR   SMR; Q4V8B3; -.
DR   STRING; 10116.ENSRNOP00000011947; -.
DR   iPTMnet; Q4V8B3; -.
DR   PhosphoSitePlus; Q4V8B3; -.
DR   jPOST; Q4V8B3; -.
DR   PaxDb; Q4V8B3; -.
DR   PRIDE; Q4V8B3; -.
DR   GeneID; 619436; -.
DR   KEGG; rno:619436; -.
DR   UCSC; RGD:1564565; rat.
DR   CTD; 9862; -.
DR   RGD; 1564565; Med24.
DR   VEuPathDB; HostDB:ENSRNOG00000008711; -.
DR   eggNOG; ENOG502QPJD; Eukaryota.
DR   HOGENOM; CLU_007484_0_0_1; -.
DR   InParanoid; Q4V8B3; -.
DR   OMA; TWQDICL; -.
DR   OrthoDB; 739187at2759; -.
DR   PRO; PR:Q4V8B3; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000008711; Expressed in skeletal muscle tissue and 20 other tissues.
DR   Genevisible; Q4V8B3; RN.
DR   GO; GO:0070847; C:core mediator complex; ISO:RGD.
DR   GO; GO:0016592; C:mediator complex; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; IDA:RGD.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IDA:RGD.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IDA:RGD.
DR   GO; GO:0046966; F:nuclear thyroid hormone receptor binding; ISO:RGD.
DR   GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR   GO; GO:0003713; F:transcription coactivator activity; IDA:RGD.
DR   GO; GO:0003712; F:transcription coregulator activity; ISO:RGD.
DR   GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; ISO:RGD.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR   GO; GO:0016567; P:protein ubiquitination; IDA:RGD.
DR   GO; GO:0019827; P:stem cell population maintenance; ISO:RGD.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; ISO:RGD.
DR   InterPro; IPR021429; Mediator_Med24.
DR   PANTHER; PTHR12898; PTHR12898; 1.
DR   Pfam; PF11277; Med24_N; 1.
PE   1: Evidence at protein level;
KW   Activator; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..987
FT                   /note="Mediator of RNA polymerase II transcription subunit
FT                   24"
FT                   /id="PRO_0000305913"
FT   MOTIF           128..132
FT                   /note="LXXLL motif 1"
FT   MOTIF           344..348
FT                   /note="LXXLL motif 2"
FT   MOTIF           446..450
FT                   /note="LXXLL motif 3"
FT   MOTIF           555..559
FT                   /note="LXXLL motif 4"
FT   MOTIF           786..790
FT                   /note="LXXLL motif 5"
FT   MOTIF           855..859
FT                   /note="LXXLL motif 6"
FT   MOD_RES         860
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         871
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   987 AA;  110081 MW;  0456BD64D5245E56 CRC64;
     MKVVNLKQAI LQAWKERWSD YQWAINMKKF FPKGATWDIL NLAEALLEQA MIGPSPNPLI
     LSYLKYAISS QMVSYSSVLT AISKFDDFSR DLCVQALLDI MDMFCDRLSC HGKAEECIGL
     CRALLSALHW LLRCTAASAE RLQEGLEAGS AVTGEKQLAL CLQCLEKTLS STKNRALLHI
     AKLEEASSWT AIEHCLLKLG EILANLSNPQ LRSQAEHCGT LIRSIPTMLS VHSEQLHKTG
     FPTIHALILL EGTMNLTGEM QPLVEQLMMV KRMQHIPTPL FVLEIWKACF VGLIESPEGT
     QELKWTAFTY LKIPQVLVKL KKYFHGDKDF TEDVNCAFEF LLKLTPLLDK ADQRCNCDCT
     NFLLQECNKQ GLLSEASFAS LVSKRTADRD PQLKSSENAN IQPNPGLILR AEPTVTNILK
     TMDADHSKSP EGLLGVLGHM LSGKSLDLLL AAAAATGKLK SFARKFINLN EFTTHGSGES
     TKTASVRALL FDISFLMLCH VAQTYGSEVI LSESSSGEEV PFFETWMQTC MPEEGKILNP
     DHPCFRPDST KVESLVALLN NSSEMKLVQM KWHEACLSIS AAILEILNAW ENGVLAFESI
     QKITDNIKGK VCSLAVCAVA WLVAHVRMLG LDEREKSLQM IRQLAGPLYS ENTLQFYNER
     VVIMNSILEH MCADVLQQTA TQIKFPSTGV DTMPYWNLLP PKRPIKEVLT DIFAKVLEKG
     WVDSRSIHIL DTLLHMGGVY WFCNNLIKEL LKETRKEHTL RAVQLLYSIF CLDMQQVTLV
     LLGHILPGLL TDSSKWHSLM DPPGTALAKL AVWCALSSYS SHKGQASSRQ KKRHREDIED
     YISLFPVEDM QPSKLMRLLS SNEDDASILS SPTDRSMNSS LSASQLHTVN MRDPLNRVLA
     NLFLLISSVL GSRTAGPHTQ FVQWFMEECV DCLEQDSRGS ILQFMPFTTV SELVKVSAMS
     SPKVVLAITD LSLPLGRQVA AKAIAAL
 
 
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