MAD4_MOUSE
ID MAD4_MOUSE Reviewed; 209 AA.
AC Q60948;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Max dimerization protein 4;
DE Short=Max dimerizer 4;
DE AltName: Full=Max-associated protein 4;
DE AltName: Full=Max-interacting transcriptional repressor MAD4;
GN Name=Mxd4; Synonyms=Mad4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, SUBUNIT, AND
RP INTERACTION WITH SIN3A AND SIN3B.
RC STRAIN=AB1; TISSUE=Embryonic stem cell;
RX PubMed=8521822; DOI=10.1002/j.1460-2075.1995.tb00252.x;
RA Hurlin P.J., Queva C., Koskinen P.J., Steingrimsson E., Ayer D.E.,
RA Copeland N.G., Jenkins N.A., Eisenman R.N.;
RT "Mad3 and Mad4: novel Max-interacting transcriptional repressors that
RT suppress c-myc dependent transformation and are expressed during neural and
RT epidermal differentiation.";
RL EMBO J. 14:5646-5659(1995).
RN [2]
RP ERRATUM OF PUBMED:8521822.
RX PubMed=8617250; DOI=10.1002/j.1460-2075.1996.tb00555.x;
RA Hurlin P.J., Queva C., Koskinen P.J., Steingrimsson E., Ayer D.E.,
RA Copeland N.G., Jenkins N.A., Eisenman R.N.;
RL EMBO J. 15:2030-2030(1996).
RN [3]
RP INTERACTION WITH RNF17.
RX PubMed=10597267; DOI=10.1038/sj.onc.1203097;
RA Yin X.-Y., Gupta K., Prochownik E.V.;
RT "Mmip-2, a novel RING finger protein that interacts with mad members of the
RT Myc oncoprotein network.";
RL Oncogene 18:6621-6634(1999).
CC -!- FUNCTION: Transcriptional repressor. Binds with MAX to form a sequence-
CC specific DNA-binding protein complex which recognizes the core sequence
CC 5'-CAC[GA]TG-3'. Antagonizes MYC transcriptional activity by competing
CC for MAX and suppresses MYC dependent cell transformation.
CC {ECO:0000269|PubMed:8521822}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. Binds DNA as a heterodimer with MAX. Interacts with SIN3A AND
CC SIN3B. Interacts with RNF17. {ECO:0000269|PubMed:10597267,
CC ECO:0000269|PubMed:8521822}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DEVELOPMENTAL STAGE: Expressed during neural and epidermal
CC differentiation. Primarily expressed in growth-arrested differentiating
CC cells. In the spinal cord at embryonic day 10.5, a strong expression
CC seen in the differentiating cells of the intermediate zone at the
CC ventral part of the neural tube and weakly in the ventricular zone. At
CC 11.5 and 12.5 dpc, highly expressed in the intermediate zone and at
CC reduced levels in the ventricular zone that mostly persists in the
CC dorsal part of the neural tube. At 14.5 dpc, expressed throughout the
CC spinal cord. In the developing epidermis, expressed in the dermis, hair
CC follicles and in some differentiating cells in the upper layers of the
CC epidermis. {ECO:0000269|PubMed:8521822}.
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DR EMBL; U32395; AAB02795.1; -; mRNA.
DR CCDS; CCDS19212.1; -.
DR AlphaFoldDB; Q60948; -.
DR SMR; Q60948; -.
DR STRING; 10090.ENSMUSP00000039071; -.
DR PhosphoSitePlus; Q60948; -.
DR MaxQB; Q60948; -.
DR PaxDb; Q60948; -.
DR PRIDE; Q60948; -.
DR ProteomicsDB; 295760; -.
DR MGI; MGI:104991; Mxd4.
DR eggNOG; KOG2483; Eukaryota.
DR InParanoid; Q60948; -.
DR ChiTaRS; Mxd4; mouse.
DR PRO; PR:Q60948; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q60948; protein.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IMP:NTNU_SB.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IGI:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..209
FT /note="Max dimerization protein 4"
FT /id="PRO_0000127267"
FT DOMAIN 53..105
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 6..23
FT /note="Interaction with SIN3A and SIN3B"
FT /evidence="ECO:0000269|PubMed:8521822"
FT REGION 136..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 209 AA; 23590 MW; C8FB5A56AFE3B27C CRC64;
MELNSLLLLL EAAEYLERRD REAEHGYASM LPFDGDFARK KTKTAGLVRK GPNNRSSHNE
LEKHRRAKLR LYLEQLKQLG PLGPDSTRHT TLSLLKRAKM HIKKLEEQDR RALSIKEQLQ
REHRFLKRRL EQLSVQSVER VRTDSTGSAV STDDSEQEVD IEGMEFGPGE LDSAGSSSDA
DDHYSLQSSG CSDSSYGHPC RRPGCPGLS
