ID G1P7G3_MYOLU Unreviewed; 1575 AA.
AC G1P7G3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 1 {ECO:0000256|ARBA:ARBA00020612, ECO:0000256|RuleBase:RU364059};
DE AltName: Full=Mediator complex subunit 1 {ECO:0000256|ARBA:ARBA00031254, ECO:0000256|RuleBase:RU364059};
GN Name=MED1 {ECO:0000313|Ensembl:ENSMLUP00000006061.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000006061.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000006061.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000006061.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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. {ECO:0000256|RuleBase:RU364059}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU364059}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 1 family.
CC {ECO:0000256|ARBA:ARBA00006210, ECO:0000256|RuleBase:RU364059}.
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DR EMBL; AAPE02041556; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006100837.1; XM_006100775.2.
DR STRING; 59463.ENSMLUP00000006061; -.
DR Ensembl; ENSMLUT00000006638.2; ENSMLUP00000006061.2; ENSMLUG00000006633.2.
DR GeneID; 102436605; -.
DR KEGG; mlf:102436605; -.
DR CTD; 5469; -.
DR eggNOG; ENOG502QPZ7; Eukaryota.
DR GeneTree; ENSGT00660000095569; -.
DR HOGENOM; CLU_245015_0_0_1; -.
DR InParanoid; G1P7G3; -.
DR OMA; FDDPPRM; -.
DR OrthoDB; 2909825at2759; -.
DR TreeFam; TF324954; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0070847; C:core mediator complex; IEA:Ensembl.
DR GO; GO:0016592; C:mediator complex; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:Ensembl.
DR GO; GO:0050693; F:LBD domain binding; IEA:Ensembl.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; IEA:Ensembl.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; ISS:UniProtKB.
DR GO; GO:0042974; F:nuclear retinoic acid receptor binding; IEA:Ensembl.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; ISS:UniProtKB.
DR GO; GO:0042809; F:nuclear vitamin D receptor binding; IEA:Ensembl.
DR GO; GO:0042975; F:peroxisome proliferator activated receptor binding; IEA:Ensembl.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IEA:Ensembl.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0001223; F:transcription coactivator binding; IEA:Ensembl.
DR GO; GO:0003712; F:transcription coregulator activity; ISS:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR GO; GO:0006702; P:androgen biosynthetic process; ISS:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
DR GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0000902; P:cell morphogenesis; ISS:UniProtKB.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IEA:Ensembl.
DR GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IEA:Ensembl.
DR GO; GO:0035050; P:embryonic heart tube development; IEA:Ensembl.
DR GO; GO:0035162; P:embryonic hemopoiesis; IEA:Ensembl.
DR GO; GO:0035116; P:embryonic hindlimb morphogenesis; IEA:Ensembl.
DR GO; GO:0001892; P:embryonic placenta development; IEA:Ensembl.
DR GO; GO:0048822; P:enucleate erythrocyte development; IEA:Ensembl.
DR GO; GO:0060750; P:epithelial cell proliferation involved in mammary gland duct elongation; IEA:Ensembl.
DR GO; GO:0048821; P:erythrocyte development; ISS:UniProtKB.
DR GO; GO:0045444; P:fat cell differentiation; IEA:Ensembl.
DR GO; GO:0045023; P:G0 to G1 transition; IEA:Ensembl.
DR GO; GO:0060218; P:hematopoietic stem cell differentiation; IEA:Ensembl.
DR GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0030216; P:keratinocyte differentiation; ISS:UniProtKB.
DR GO; GO:0007595; P:lactation; IEA:Ensembl.
DR GO; GO:0002088; P:lens development in camera-type eye; ISS:UniProtKB.
DR GO; GO:0001889; P:liver development; IEA:Ensembl.
DR GO; GO:0060745; P:mammary gland branching involved in pregnancy; IEA:Ensembl.
DR GO; GO:0060744; P:mammary gland branching involved in thelarche; IEA:Ensembl.
DR GO; GO:0035855; P:megakaryocyte development; ISS:UniProtKB.
DR GO; GO:0030224; P:monocyte differentiation; IEA:Ensembl.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0010839; P:negative regulation of keratinocyte proliferation; ISS:UniProtKB.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0035357; P:peroxisome proliferator activated receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IEA:Ensembl.
DR GO; GO:0070318; P:positive regulation of G0 to G1 transition; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
DR GO; GO:2000347; P:positive regulation of hepatocyte proliferation; IEA:Ensembl.
DR GO; GO:0033148; P:positive regulation of intracellular estrogen receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0045618; P:positive regulation of keratinocyte differentiation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0060261; P:positive regulation of transcription initiation by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0060335; P:positive regulation of type II interferon-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0006606; P:protein import into nucleus; IEA:Ensembl.
DR GO; GO:2001141; P:regulation of RNA biosynthetic process; ISS:UniProtKB.
DR GO; GO:0070562; P:regulation of vitamin D receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0003406; P:retinal pigment epithelium development; IEA:Ensembl.
DR GO; GO:0006590; P:thyroid hormone generation; IEA:Ensembl.
DR GO; GO:0002154; P:thyroid hormone mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; IEA:Ensembl.
DR InterPro; IPR019680; Mediator_Med1.
DR PANTHER; PTHR12881; MEDIATOR OF RNA POLYMERASE II TRANSCRIPTION SUBUNIT 1; 1.
DR PANTHER; PTHR12881:SF10; MEDIATOR OF RNA POLYMERASE II TRANSCRIPTION SUBUNIT 1; 1.
DR Pfam; PF10744; Med1; 1.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|ARBA:ARBA00023159, ECO:0000256|RuleBase:RU364059};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU364059};
KW Reference proteome {ECO:0000313|Proteomes:UP000001074};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU364059};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|RuleBase:RU364059}.
FT DOMAIN 60..426
FT /note="Mediator complex subunit Med1"
FT /evidence="ECO:0000259|Pfam:PF10744"
FT REGION 614..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..1561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..836
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..885
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1020
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1021..1051
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1073..1194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1209..1296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1323..1342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1343..1360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1361..1382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1415..1476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1502..1524
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1525..1551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1575 AA; 167942 MW; AF072E98D4563A09 CRC64;
MKAQGETEES EKLSKMSSLL ERLHAKFNQN RPWSETIKLV RQVMEKRVVM SSGGHQHLVS
CLETLQKALK VTSLPAMTDR LESIARQNGL GSHLSASGTE CYITSDMFYV EVQLDPAGQL
CDVKVAHHGE NPMSCPELVQ QLREKNFEEF SKHLKGLVNL YNLPGDNKLK TKMYLALQSL
EQDLSKMAVM YWKATNAGPL DKILHGSVGY LTPRSGGHLM NLKYYASPSD LLDDKTTSPI
ILHENNVPRS LGMNASVTIE GTSAMYKLPI APLIMGSHPV DNKWTPSFSS ITSANSVDLP
ACFFLKFPQP IPVSRAFVQK LQNCTGIPLF ETPPTYIPLY ELITQFELSK DPDPIPLKHN
MRFYAALPGQ QHCYFLNKDA PLPDGRSLQG TLVSKITFQH PGRVPLILNL IRHQVAYNTL
IGSCVKRTIL KEDSPGLLQF EVCPLSESRF SVSFQHPVND SLVCVVMDVQ DSTHVSCKLY
KGLSDALICT DDFIAKVVQR CMSIPVTMRA IRRKAETIQA DTPALSLIAE TVEDMVKKNL
PPASSPGYGM TTGNNPMSGT TTPTNTFPGG PITTLFNMSM SIKDRHESVG HGEDFSKVSQ
NPILTSLLQI TGNGGSTIGS SPTPPHHTPP PVSSMAGNTK NHPMLMNLLK DNPAQDFSTL
YGCSPLERQN SSSGSPRMEM CSGSNKTKKK KSSRLLPEKP KHQTEDDFQR ELFSMDVDSQ
NPIFDVNMTA DTLDTPHITP APSQCSTPPT TYPQPVPHPQ PSIQRMVRLS SSDSIGPDVT
DILSDIAEEA SKLPSTSDDC PPIGTPVRDS SSSGHSQSAL FDPDVFQANN NENPYTDPAD
LIADAAGSPS SDSPSNHFFP DGVDFNPDLL NSQSQSGFGE EYFDESSQSG DNDDFKGFTS
QALNTLGVPM LGGDNGETKF KGNSQADTVD FSIIAVAGKA LGSADLMEHH SGSQSPLLTT
GDLGKDKAQK RVKEGNGTSN SLTGPGLDSK PGKRSRTPSN DGKSKDKPPK RKKADTEGKS
PSHSSNRPFT PPTSTGGSKS PGSSGRSQTP PGVATPPIPK ITIQIPKGTV MVGKPSSHSQ
YTSSGSVSSS GSKSHHSHSS SSSSSASNSG KMKSSKSEGS SSKLSSSIYS SQGSSGSSQS
KNSSQSGGKP GSSPITKHGL SSGSSGTKMK LQGKPSSLMN PSLSKPNISP SHSRPPGGSD
KLASPMKSVP GTPPSSKAKS PISSGSSGSH MSGTGSSTGM KSSSGLGSSG SLKTPPSSNS
CTASSSSFSS SGSSMSSSQN QHGSSKGKSP SRNKKPSLTA VIDKLKHGVV TSGPGGEDPM
DGQVGVSTNS SHPMSSKHNM SGGEFQGKRE KSDKDKSKVS TSGGSVDSSK KTSESKNVGS
TGVAKIIISK HDGGSPSIKA KVTLQKPGES SGEGLRPQMA SSKNYGSPLI SGSTPKHERG
SPSHSKSPAY TPQNLDSESE SGSSIAEKSY QNSPCSDDGI RLLPEYSTEK HKKHKKEKKK
VKDKDRDRDR DKDRDKKKSH SIKPESWSKS PISSDQSLSM TSNTILSTDR PSRLSPDFMI
GEEDDDLMDV ALIGN
//
