MED1_PONAB
ID MED1_PONAB Reviewed; 1581 AA.
AC Q5RES4;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 1;
DE AltName: Full=Mediator complex subunit 1;
DE AltName: Full=Peroxisome proliferator-activated receptor-binding protein;
DE Short=PBP;
DE Short=PPAR-binding protein;
GN Name=MED1; Synonyms=PPARBP, TRAP220;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. Acts as a coactivator for GATA1-
CC mediated transcriptional activation during erythroid differentiation of
CC K562 erythroleukemia cells (By similarity).
CC {ECO:0000250|UniProtKB:Q15648}.
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. This subunit specifically
CC interacts with a number of nuclear receptors in a ligand-dependent
CC fashion including AR, ESR1, ESR2, PPARA, PPARG, RORA, RXRA, RXRG, THRA,
CC THRB and VDR. Interacts with CTNNB1, GABPA, GLI3, PPARGC1A and TP53.
CC Interacts with GATA1 and YWHAH. Interacts with CLOCK; this interaction
CC requires the presence of THRAP3. Interacts with CCAR1. Interacts with
CC NR4A3 (By similarity). Interacts (via IBM motif) with PSIP1 (via IBD
CC domain); phosphorylation increases its affinity for PSIP1 (By
CC similarity). {ECO:0000250|UniProtKB:Q15648,
CC ECO:0000250|UniProtKB:Q925J9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=A subset of the
CC protein may enter the nucleolus subsequent to phosphorylation by MAPK1
CC or MAPK3. {ECO:0000250}.
CC -!- PTM: Phosphorylated by MAPK1 or MAPK3 during G2/M phase which may
CC enhance protein stability and promote entry into the nucleolus (By
CC similarity). Phosphorylation increases its interaction with PSIP1 (By
CC similarity). {ECO:0000250|UniProtKB:Q15648}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 1 family.
CC {ECO:0000305}.
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DR EMBL; CR857442; CAH89733.1; -; mRNA.
DR AlphaFoldDB; Q5RES4; -.
DR SMR; Q5RES4; -.
DR STRING; 9601.ENSPPYP00000009539; -.
DR eggNOG; ENOG502QPZ7; Eukaryota.
DR InParanoid; Q5RES4; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0016592; C:mediator complex; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:UniProt.
DR InterPro; IPR019680; Mediator_Med1.
DR Pfam; PF10744; Med1; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Activator; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..1581
FT /note="Mediator of RNA polymerase II transcription subunit
FT 1"
FT /id="PRO_0000302019"
FT REGION 1..670
FT /note="Interaction with the Mediator complex and THRA"
FT /evidence="ECO:0000250"
FT REGION 16..590
FT /note="Interaction with ESR1"
FT /evidence="ECO:0000250|UniProtKB:Q15648"
FT REGION 108..212
FT /note="Interaction with the Mediator complex"
FT /evidence="ECO:0000250"
FT REGION 215..390
FT /note="Interaction with the Mediator complex"
FT /evidence="ECO:0000250"
FT REGION 405..644
FT /note="Interaction with THRA"
FT /evidence="ECO:0000250"
FT REGION 542..788
FT /note="Interaction with VDR"
FT /evidence="ECO:0000250"
FT REGION 609..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..701
FT /note="Interaction with PPARGC1A and THRA"
FT /evidence="ECO:0000250"
FT REGION 656..1065
FT /note="Interaction with ESR1"
FT /evidence="ECO:0000250"
FT REGION 681..715
FT /note="Interaction with GATA1"
FT /evidence="ECO:0000250|UniProtKB:Q15648"
FT REGION 791..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..1566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1249..1421
FT /note="Interaction with TP53"
FT /evidence="ECO:0000250"
FT MOTIF 604..608
FT /note="LXXLL motif 1"
FT MOTIF 645..649
FT /note="LXXLL motif 2"
FT MOTIF 874..901
FT /note="Integrase domain-binding motif (IBM)"
FT /evidence="ECO:0000250|UniProtKB:Q15648"
FT COMPBIAS 652..682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..705
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..819
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..884
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1019
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1052
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1074..1197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1219..1301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1328..1348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1349..1366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1367..1388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1421..1484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1508..1530
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1531..1556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 588
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15648"
FT MOD_RES 664
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15648"
FT MOD_RES 794
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15648"
FT MOD_RES 804
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15648"
FT MOD_RES 886
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15648"
FT MOD_RES 952
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q925J9"
FT MOD_RES 1031
FT /note="Phosphothreonine; by MAPK1 or MAPK3"
FT /evidence="ECO:0000250|UniProtKB:Q15648"
FT MOD_RES 1050
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15648"
FT MOD_RES 1056
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15648"
FT MOD_RES 1156
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15648"
FT MOD_RES 1177
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15648"
FT MOD_RES 1207
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15648"
FT MOD_RES 1215
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15648"
FT MOD_RES 1223
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15648"
FT MOD_RES 1302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15648"
FT MOD_RES 1347
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15648"
FT MOD_RES 1403
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15648"
FT MOD_RES 1433
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15648"
FT MOD_RES 1440
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15648"
FT MOD_RES 1457
FT /note="Phosphothreonine; by MAPK1 or MAPK3"
FT /evidence="ECO:0000250|UniProtKB:Q15648"
FT MOD_RES 1463
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15648"
FT MOD_RES 1465
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q925J9"
FT MOD_RES 1479
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15648"
FT MOD_RES 1481
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15648"
FT MOD_RES 1482
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15648"
FT MOD_RES 1529
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15648"
SQ SEQUENCE 1581 AA; 168583 MW; 31A82CF247C98B45 CRC64;
MKAQGETEES EKLSKMSSLL ERLHAKFNQN RPWSETIKLV RQVMEKRVVM SSGGHQHLVS
CLETLQKALK VTSLPAMTDR LESIARQNGL GSHLSASGTE CYITSDMFYV EVQLDPAGQL
CDVKVAHHGE NPVSCLELVQ QLREKNFDEF SKHLKGLVNL YNLPGDNKLK TKMYLALQSL
EQDLSKMAIM YWKATNAGPL DKILHGSVGY LTPRSGGHLM NLKYYVSPSD LLDDKTASPI
ILHENNVSRS LGMNASVTIE GTSAMYKLPI APLIMGSHPV DNKWTPSFSS ITSANSVDLP
ACFFLKFPQP IPVSRAFVQK LQNCTGIPLF ETQPTYAPLY ELITQFELSK DPDPIPLNHN
MRFYAALPGQ QHCYFLNKDA PLPDGRSLQG TLISKITFQH PGRVPLILNL IRHQVAYNTL
IGSCVKRTIL KEDSPGLLQF EVCPLSESRF SVSFQHPVND SLVCVVMDVQ DSTHVSCKLY
KGLSDALICT DDFIAKVVQR CMSIPVTMRA IRRKAETIQA DTPALSLIAE TVEDMVKKNL
PPASSPGYGM TTGSNPMSGT TTPTNTFPGG PITTLFNMSM SIKDRHESVG HGEDFSKVSQ
NPILTSLLQI TGNGGSTIGS SPTPPHHTPP PVSSMAGNTK NHPMLMNLLK DNPAQDFSTL
YGSSPLERQN SSSGSPRMEI CSGSNKTKKK ESSRLPPEKP KHQTEDDFQR ELFSMDVDSQ
NPIFDVNMTA DTLDTPHITP APSQCSTPTT YPQPVPHPQP SIQRMVRLSS SDSIGPDVTD
ILSDIAEEAS KLPSTSDDCP AIGTPLRDSS SSGHSQSTLF DSDVFQTNNN ENPYTDPADL
IADAAGSPSS DSPTNHFFHD GVDFNPDLSN SQSQSGFGEE YFDESSQSGD NDDFKGFASQ
ALNTLGVPML GGDNGETKFK GNNQADTVDF SIISVAGKAL APADLMEHHS GSQGSLLTTG
DLGKEKTQKR VKEGNGTSNS TLSGPGLDSK PGKRSRTPSN DGKSKDKPPK RKKADTEGKS
PSHSSSNRPF TPPTSTGGSK SPGSSGRSQT PPGVATPPIP KITIQIPKGT VMVGKPSSHS
QYTSSGSVSS SGSKSHHSHS SSSSSSSAST SRKMKSSKSE GSSSSKLSSS MYSSQGSSGS
SQSKNSSQSG GKPGSSPITK HGLSSGSSST KMKPQGKPSS LMNPSLSKPN ISPSHSRPPG
GSDKLASPMK PVPGTPPSSK AKSPISSGSG GSHMSGTSSS SGMKSSSGLG SSGSLSQKTP
PSSNSCTASS SSFSSSGSSM SSSQNQHGSS KGKSPSRNKK PSLTAVIDKL KHGVVTSGPG
GEDPLDGQMG VSTNSSSHPM SSKHNMSGGE FQGKREKSDK DKSKVSTSGS SVDSSKKTSE
SKNVGSTGVA KIIISKHDGG SPSIKAKVTL QKPGESSGEG LRPQMASSKN YGSPLISGST
PKHERGSPSH SKSPAYTPQN LDSESESGSS IAEKSYQNSP SSDDGIRPLP EYSTEKHKKH
KKEKKKVKDK DRDRDRDKDR DKKKSHSIKP ESWSKSPISS DQSLSMTSNT ILSADRPSRL
SPDFMIGEED DDLMDVALIG N
