MAD3_MOUSE
ID MAD3_MOUSE Reviewed; 206 AA.
AC Q80US8; Q60947;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Max dimerization protein 3;
DE Short=Max dimerizer 3;
DE AltName: Full=Max-associated protein 3;
GN Name=Mxd3; Synonyms=Mad3;
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,
RP SUBCELLULAR LOCATION, AND 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11154258; DOI=10.1128/mcb.21.3.703-712.2001;
RA Queva C., McArthur G.A., Iritani B.M., Eisenman R.N.;
RT "Targeted deletion of the S-phase-specific Myc antagonist Mad3 sensitizes
RT neuronal and lymphoid cells to radiation-induced apoptosis.";
RL Mol. Cell. Biol. 21:703-712(2001).
RN [6]
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 {ECO:0000255|PROSITE-ProRule:PRU00981,
CC ECO:0000269|PubMed:8521822}.
CC -!- TISSUE SPECIFICITY: Expressed only in the proliferating areas of the
CC testis and thymus. {ECO:0000269|PubMed:11154258}.
CC -!- DEVELOPMENTAL STAGE: Expressed during neural and epidermal
CC differentiation. Expression restricted to proliferating cells prior to
CC differentiation. Specifically expressed in the S phase of the cell
CC cycle in neuronal progenitor cells. In the developing embryo, detected
CC from 9.5 to 12.5 dpc especially in the ventricular zone of the
CC neuroepithelia, in the progression zone of the limb buds and in the
CC aortic arches and liver. In the spinal cord at embryonic days 10.5,
CC 11.5 and 12.5 dpc, expressed in the cells at the perimeter of the
CC ventricular zone. In the developing epidermis, expressed only in the
CC uppermost differentiated cell layers underneath the stratum corneum.
CC {ECO:0000269|PubMed:11154258, ECO:0000269|PubMed:8521822}.
CC -!- MISCELLANEOUS: Mice deficient for Mxd3 show increased sensitivity of
CC neuronal and lymphoid cells to gamma-radiation induced apoptosis.
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DR EMBL; U32394; AAB02794.1; -; mRNA.
DR EMBL; AK138742; BAE23764.1; -; mRNA.
DR EMBL; BC051970; AAH51970.1; -; mRNA.
DR CCDS; CCDS26543.1; -.
DR PIR; S60005; S60005.
DR RefSeq; NP_057871.2; NM_016662.4.
DR AlphaFoldDB; Q80US8; -.
DR SMR; Q80US8; -.
DR BioGRID; 201271; 1.
DR DIP; DIP-948N; -.
DR STRING; 10090.ENSMUSP00000021941; -.
DR PhosphoSitePlus; Q80US8; -.
DR EPD; Q80US8; -.
DR PaxDb; Q80US8; -.
DR PRIDE; Q80US8; -.
DR ProteomicsDB; 291999; -.
DR ABCD; Q80US8; 1 sequenced antibody.
DR Antibodypedia; 17372; 233 antibodies from 29 providers.
DR DNASU; 17121; -.
DR Ensembl; ENSMUST00000021941; ENSMUSP00000021941; ENSMUSG00000021485.
DR GeneID; 17121; -.
DR KEGG; mmu:17121; -.
DR UCSC; uc007qqn.1; mouse.
DR CTD; 83463; -.
DR MGI; MGI:104987; Mxd3.
DR VEuPathDB; HostDB:ENSMUSG00000021485; -.
DR eggNOG; KOG2483; Eukaryota.
DR GeneTree; ENSGT00940000161050; -.
DR HOGENOM; CLU_082604_1_0_1; -.
DR InParanoid; Q80US8; -.
DR OMA; IVFDCVD; -.
DR OrthoDB; 1545091at2759; -.
DR PhylomeDB; Q80US8; -.
DR TreeFam; TF315654; -.
DR BioGRID-ORCS; 17121; 3 hits in 76 CRISPR screens.
DR PRO; PR:Q80US8; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q80US8; protein.
DR Bgee; ENSMUSG00000021485; Expressed in lumbar dorsal root ganglion and 202 other tissues.
DR Genevisible; Q80US8; MM.
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..206
FT /note="Max dimerization protein 3"
FT /id="PRO_0000253708"
FT DOMAIN 57..109
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 8..25
FT /note="Interaction with SIN3A and SIN3B"
FT /evidence="ECO:0000269|PubMed:8521822"
FT REGION 29..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 177
FT /note="S -> N (in Ref. 1; AAB02794)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 206 AA; 23635 MW; 17E1149064907085 CRC64;
MEPVASNIQV LLQAAEFLER REREAEHGYA SLCPHHSPGT VCRRRKPPLQ APGALNSGRS
VHNELEKRRR AQLKRCLEQL RQQMPLGVDC TRYTTLSLLR RARVHIQKLE EQEQQARRLK
EKLRSKQQSL QQQLEQLQGL PGARERERLR ADSLDSSGLS SERSDSDQED LEVDVESLVF
GTETELLQSF SAGREHSYSH STCAWL
