MED12_PANTR
ID MED12_PANTR Reviewed; 2027 AA.
AC Q7YQK8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 12;
DE AltName: Full=Mediator complex subunit 12;
DE AltName: Full=Trinucleotide repeat-containing gene 11 protein;
GN Name=MED12; Synonyms=TNRC11;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12777533; DOI=10.1093/molbev/msg134;
RA Kitano T., Schwarz C., Nickel B., Paeaebo S.;
RT "Gene diversity patterns at 10 X-chromosomal loci in humans and
RT chimpanzees.";
RL Mol. Biol. Evol. 20:1281-1289(2003).
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. This subunit may specifically
CC regulate transcription of targets of the Wnt signaling pathway and SHH
CC signaling pathway (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. Also interacts with CTNNB1
CC and GLI3 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 12 family.
CC {ECO:0000305}.
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DR EMBL; AB102669; BAC81138.1; -; mRNA.
DR RefSeq; NP_001009019.1; NM_001009019.1.
DR AlphaFoldDB; Q7YQK8; -.
DR STRING; 9598.ENSPTRP00000047374; -.
DR PaxDb; Q7YQK8; -.
DR GeneID; 449626; -.
DR KEGG; ptr:449626; -.
DR CTD; 9968; -.
DR eggNOG; KOG3598; Eukaryota.
DR InParanoid; Q7YQK8; -.
DR OrthoDB; 15873at2759; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0016592; C:mediator complex; IBA:GO_Central.
DR GO; GO:0008013; F:beta-catenin binding; IEA:InterPro.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR021989; Mediator_Med12_catenin-bd.
DR InterPro; IPR021990; Mediator_Med12_LCEWAV.
DR Pfam; PF12145; Med12-LCEWAV; 1.
DR Pfam; PF12144; Med12-PQL; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Activator; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..2027
FT /note="Mediator of RNA polymerase II transcription subunit
FT 12"
FT /id="PRO_0000312958"
FT REGION 170..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1088..1113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1241..1262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1297..1321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1463..1901
FT /note="Interaction with CTNNB1 and GLI3"
FT /evidence="ECO:0000250"
FT REGION 1585..1676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1805..1850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1965..1999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2008..2027
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..501
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..563
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1297..1318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1585..1607
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1984..1999
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q93074"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q93074"
FT MOD_RES 512
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q93074"
FT MOD_RES 545
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q93074"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q93074"
FT MOD_RES 1105
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q93074"
FT MOD_RES 1116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q93074"
FT MOD_RES 1645
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:A2AGH6"
FT MOD_RES 1746
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:A2AGH6"
FT MOD_RES 1746
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:A2AGH6"
FT MOD_RES 1757
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:A2AGH6"
FT MOD_RES 1844
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q93074"
FT MOD_RES 1865
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q93074"
SQ SEQUENCE 2027 AA; 226338 MW; D598B3534ED56057 CRC64;
MRAAWLIKMT CAYYAAISET KVKKRHVDPF MEWTQIITKY LWEQLQKMAE YYRPGPAGSG
GCGSTIGPLP HDVEVAIRQW DYTEKLAMFM FQDGMLDRHE FLTWVLECFE KIRPGEDELL
KLLLPLLLRY SGEFVQSAYL SRRLAYFCTR RLALQLDGVS SHSSHVISAQ STSTLPTTPA
PQPPTSSTPS TPFSDLLMCP QHRPLVFGLS CILQTILLCC PSALVWHYSL TDSRIKTGSP
LDHLPIAPSN LPMPEGNSAF TQQVRAKLRE IEQQIKERGQ AVEVRWSFDK CQEATAGFTI
GRVLHTLEVL DSHSFERSDF SNSLDSLCNR IFGLGPSKDG HEISSDDDAV VSLLCEWAVS
CKRSGRHRAM VVAKLLEKRQ AEIEAERCGE SEAADEKGSI ASGSLSAPSA PIFQDVLLQF
LDTQAPMLTD PRSENERVEF FNLVLLFCEL IRHDVFSHNM YTCTLISRGD LAFGAPGPRP
PSPFDDPADD AEHKEAEGSS SSKLEDPGLS ESMDIDPSSS VLFEDMEKPD FSLFSPTMPC
EGKGSPSPEK PDVEKEVKPP PKEKIEGTLG ILYDQPRHVQ YATHFPIPQE ESCSHECNQR
LVVLFGVGKQ RDDARHAIKK ITKDILKVLN RKGTAETDQL APIVPLNPGD LTFLGGEDGQ
KRRRNRPEAF PTAEDIFAKF QHLSHYDQHQ VTAQVSRNVL EQITSFALGM SYHLPLVQHV
QFIFDLMEYS LSISGLIDFA IQLLNELSVV EAELLLKSSD LVGSYTTSLC LCIVAVLRHY
HACLILNQDQ MAQVFEGLCG VVKHGMNRSD GSSAERCILA YLYDLYTSCS HLKNKFGELF
SDFCSKVKNT IYCNVEPSES NMRWAPEFMI DTLENPAAHT FTYTGLGKSL SENPANRYSF
VCNALMHVCV GHHDPDRVND IAILCAELTG YCKSLSAEWL GVLKALCCSS NNGTCGFNDL
LCNVDVSDLS FHDSLATFVA ILIARQCLLL EDLIRCAAIP SLLNAACSEQ DSEPGARLTC
RILLHLFKTP QLNPCQSDGN KPTVGIRSSC DRHLLAASQN RIVDGAVFAV LKAVFVLGDA
ELKGSGFTVT GGTEELPEEE GGGGSGGRRQ GGRNISVETA SLDVYAKYVL RSICQQEWVG
ERCLKSLCED SNDLQDPVLS SAQAQRLMQL ICYPHRLLDN EDGENPQRQR IKRILQNLDQ
WTMRQSSLEL QLMIKQTPNN EMNSLLENIA KATIEVFQQS AETGSSSGST ASNMPSSSKT
KPVLSSLERS GVWLVAPLIA KLPTSVQGHV LKAAGEELEK GQHLGSSSRK ERDRQKQKSM
SLLSQQPFLS LVLTCLKGQD EQREGLLTSL YSQVHQIVNN WRDDQYLDDC KPKQLMHEAL
KLRLNLVGGM FDTVQRSTQQ TTEWAMLLLE IIISGTVDMQ SNNELFTTVL DMLSVLINGT
LAADMSSISQ GSMEENKRAY MNLAKKLQKE LGERQSDSLE KVRQLLPLPK QTRDVITCEP
QGSLIDTKGN KIAGFDSIFK KEGLQVSTKQ KISPWDLFEG LKPSAPLSWG WFGTVRVDRR
VARGEEQQRL LLYHTHLRPR PRAYYLEPLP LPPEDEEPPA PTLLEPEKKA PEPPKTDKPG
AAPPSTEERK KKSTKGKKRS QPATKTEDYG MGPGRSGPYG VTVPPDLLHH PNPGSITHLN
YRQGSIGLYT QNQPLPAGGP RVDPYRPVRL PMQKLPTRPT YPGVLPTTMT GVMGLEPSSY
KTSVYRQQQP AVPQGQRLRQ QLQAKIQSQG MLGQSSVHQM TPSSSYGLQT SQGYTPYVSH
VGLQQHTGPA GTMVPPSYSS QPYQSTHPST NPTLVDPTRH LQQRPSGYVH QQAPTYGHGL
TSTQRFSHQT LQQTPMISTM TPMSAQGVQA GVRSTAILPE QQQQQQQQQQ QQQQQQQQQQ
QQQQQQYHIR QQQQQQILRQ QQQQQQQQQQ QQQQQQQQQQ QQQQQHQQQQ QQQAAPPQPQ
PQSQPQFQRQ GLQQTQQQQQ TAALVRQLQQ QLSNTQPQPS TNIFGRY
