MED12_PONPY
ID MED12_PONPY Reviewed; 2181 AA.
AC Q5RCU2; Q7YQK7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 25-MAY-2022, entry version 64.
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 Pongo pygmaeus (Bornean orangutan).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9600;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 154-2181 (ISOFORM 1).
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 regulated gene 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 pathways (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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5RCU2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5RCU2-2; Sequence=VSP_029981;
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 12 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH90415.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CR858176; CAH90415.1; ALT_FRAME; mRNA.
DR EMBL; AB102670; BAC81139.1; -; mRNA.
DR AlphaFoldDB; Q5RCU2; -.
DR GO; GO:0016592; C:mediator complex; IEA:InterPro.
DR GO; GO:0008013; F:beta-catenin binding; IEA:InterPro.
DR GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR InterPro; IPR019035; Mediator_Med12.
DR InterPro; IPR021989; Mediator_Med12_catenin-bd.
DR InterPro; IPR021990; Mediator_Med12_LCEWAV.
DR Pfam; PF09497; Med12; 1.
DR Pfam; PF12145; Med12-LCEWAV; 1.
DR Pfam; PF12144; Med12-PQL; 1.
DR SMART; SM01281; Med12; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Activator; Alternative splicing; Methylation; Nucleus;
KW Phosphoprotein; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..2181
FT /note="Mediator of RNA polymerase II transcription subunit
FT 12"
FT /id="PRO_0000312959"
FT REGION 12..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1241..1266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1394..1415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1450..1474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1616..2054
FT /note="Interaction with CTNNB1 and GLI3"
FT /evidence="ECO:0000250"
FT REGION 1738..1829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1958..2003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2119..2153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2162..2181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..654
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..716
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1450..1471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1738..1760
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2138..2153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 80
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:A2AGH6"
FT MOD_RES 166
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q93074"
FT MOD_RES 635
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q93074"
FT MOD_RES 665
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q93074"
FT MOD_RES 698
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q93074"
FT MOD_RES 700
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q93074"
FT MOD_RES 1258
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q93074"
FT MOD_RES 1269
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q93074"
FT MOD_RES 1798
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:A2AGH6"
FT MOD_RES 1899
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:A2AGH6"
FT MOD_RES 1899
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:A2AGH6"
FT MOD_RES 1910
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:A2AGH6"
FT MOD_RES 1997
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q93074"
FT MOD_RES 2018
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q93074"
FT VAR_SEQ 1964..1988
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_029981"
FT CONFLICT 575
FT /note="D -> G (in Ref. 1; CAH90415)"
FT /evidence="ECO:0000305"
FT CONFLICT 705
FT /note="D -> G (in Ref. 1; CAH90415)"
FT /evidence="ECO:0000305"
FT CONFLICT 1126
FT /note="D -> G (in Ref. 1; CAH90415)"
FT /evidence="ECO:0000305"
FT CONFLICT 1614
FT /note="M -> V (in Ref. 1; CAH90415)"
FT /evidence="ECO:0000305"
FT CONFLICT 1671
FT /note="I -> V (in Ref. 1; CAH90415)"
FT /evidence="ECO:0000305"
FT CONFLICT 1821
FT /note="L -> P (in Ref. 1; CAH90415)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2181 AA; 243522 MW; 03124C9EF8C4D586 CRC64;
MAAFGILSYE HRPLKRPRLG PPDVYPQDPK QKEDELTALN VKQGFNNQPA VSGDEHGSAK
NVSFNPAKIS SNFSSIIAEK LRCNTLPDTG RRKPQVNQKD NFWLVTARSQ SAINTWFTDL
AGTKPLTQLA KKVPIFSKKE EVFGYLAKYT VPVMRAAWLI KMTCAYYAAI SETKVKKRHV
DPFMEWTQII TKYLWEQLQK MAEYYRPGPA GSGGCGSTIG PLPHDVEVAI RQWDYTEKLA
MFMFQDGMLD RHEFLTWVLE CFEKIRPGED ELLKLLLPLL LRYSGEFVQS AYLSRRLAYF
CTRRLALQLD GVSSHSSHVI SAQSTSTLPT TPAPQPPTSS TPSTPFSDLL MCPQHRPLVF
GLSCILQTIL LCCPSALVWH YSLTDSRIKT GSPLDHLPIA PSNLPMPEGN SAFTQQVRAK
LREIEQQIKE RGQAVEVRWS FDKCQEATAG FTIGRVLHTL EVLDSHSFER SDFSNSLDSL
CNRIFGLGPS KDGHEISSDD DAVVSLLCEW AVSCKRSGRH RAMVVAKLLE KRQAEIEAER
CGESEAADEK GSIASGSLSA PSAPIFQDVL LQFLDTQAPM LTDPRSESER VEFFNLVLLF
CELIRHDVFS HNMYTCTLIS RGDLAFGAPG PRPPSPFDDP ADDPEHKEAE GSSSSKLEDP
GLSESMDIDP SSSVLFEDME KPDFSLFSPT MPCEGKGSPS PEKPDVEKEV KPPPKEKIEG
TLGVLYDQPR HVQYATHFPI PQEESCSHEC NQRLVVLFGV GKQRDDARHA IKKITKDILK
VLNRKGTAET DQLAPIVPLN PGDLTFLGGE DGQKRRRNRP EAFPTAEDIF AKFQHLSHYD
QHQVTAQVSR NVLEQITSFA LGMSYHLPLV QHVQFIFDLM EYSLSISGLI DFAIQLLNEL
SVVEAELLLK SSDLVGSYTT SLCLCIVAVL RHYHACLILN QDQMAQVFEG LCGVVKHGMN
RSDGSSAERC ILAYLYDLYT SCSHLKNKFG ELFSDFCSKV KNTIYCNVEP SESNMRWAPE
FMIDTLENPA AHTFTYTGLG KSLSENPANR YSFVCNALMH VCVGHHDPDR VNDIAILCAE
LTGYCKSLSA EWLGVLKALC CSSNNGTCGF NDLLCNVDVS DLSFHDSLAT FVAILIARQC
LLLEDLIRCA AIPSLLNAAC SEQDSEPGAR LTCRILLHLF KTPQLNPCQS DGNKPTVGIR
SSCDRHLLAA SQNRIVDGAV FAVLKAVFVL GDAELKGSGF TVTGGTEELP EEEGGGGSGG
RRQGGRNISV ETASLDVYAK YVLRSICQQE WVGERCLKSL CEDSNDLQDP VLSSAQAQRL
MQLICYPHRL LDNEDGENPQ RQRIKRILQN LDQWTMRQSS LELQLMIKQT PNNEMNSLLE
NIAKATIEVF QQSAETGSSS GSTASNMPSS SKTKPVLSSL ERSGVWLVAP LIAKLPTSVQ
GHVLKAAGEE LEKGQHLGSS SRKERDRQKQ KSMSLLSQQP FLSLVLTCLK GQDEQREGLL
TSLYSQVHQI VNNWRDDQYL DDCKPKQLMH EALKLRLNLV GGMFDTVQRS TQQTTEWAML
LLEIIISGTV DMQSNNELFT TVLDMLSVLI NGTLAADMSS ISQGSMEENK RAYMNLAKKL
QKELGERQSD SLEKVRQLLP LPKQTRDVIT CEPQGSLIDT KGNKIAGFDS IFKKEGLQVS
TKQKISPWDL FEGLKPSAPL SWGWFGTVRV DRRVARGEEQ QRLLLYHTHL RPRPRAYYLE
PLPLPPEDEE PPAPTLLEPE KKAPEPPKTD KPGAAPPSTE ERKKKSTKGK KRSQPATKTE
DYGMGPGRSG PYGVTVPPDL LHHPNPGSIT HLNYRQGSIG LYTQNQPLPA GGPRVDPYRP
VRLPMQKLPT RPTYPGVLPT TMTGVMGLEP SSYKTSVYRQ QQPAVPQGQR LRQQLQAKIQ
SQGMLGQSSV HQMTPSSSYG LQTSQGYTPY VSHVGLQQHT GPAGTMVPPS YSSQPYQSTH
PSTNPTLVDP TRHLQQRPSG YVHQQAPTYG HGLTSTQRFS HQTLQQTPMI STMTPMSAQG
VQAGVRSTAI LPEQQQQQQQ QQQQQQQQQQ QQQQQQQQQY HIRQQQQQQI LRQQQQQQQQ
QQQQQQQQQQ QQQQQQQQQH QQQQQQQAAP PQPQPQSQPQ FQRQGLQQTQ QQQQTAALVR
QLQQQLSNTQ PQPSTNIFGR Y
