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Database: UniProt
Entry: Q05195
LinkDB: Q05195
Original site: Q05195 
ID   MAD1_HUMAN              Reviewed;         221 AA.
AC   Q05195; B2R6V8; B7ZLI6; D6W5G2; Q6FI41;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   29-SEP-2021, entry version 190.
DE   RecName: Full=Max dimerization protein 1;
DE            Short=Max dimerizer 1;
DE   AltName: Full=Protein MAD;
GN   Name=MXD1; Synonyms=MAD;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH MAX,
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RC   TISSUE=Lung;
RX   PubMed=8425218; DOI=10.1016/0092-8674(93)90661-9;
RA   Ayer D.E., Kretzner L., Eisenman R.N.;
RT   "Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional
RT   activity.";
RL   Cell 72:211-222(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA   Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA   LaBaer J.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Placenta;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain, and Placenta;
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   [7]
RP   FUNCTION.
RX   PubMed=12837246; DOI=10.1016/s0092-8674(03)00430-6;
RA   Lin S.Y., Elledge S.J.;
RT   "Multiple tumor suppressor pathways negatively regulate telomerase.";
RL   Cell 113:881-889(2003).
RN   [8]
RP   UBIQUITINATION BY BIRC2/C-IAP1.
RX   PubMed=18082613; DOI=10.1016/j.molcel.2007.10.027;
RA   Xu L., Zhu J., Hu X., Zhu H., Kim H.T., LaBaer J., Goldberg A., Yuan J.;
RT   "c-IAP1 cooperates with Myc by acting as a ubiquitin ligase for Mad1.";
RL   Mol. Cell 28:914-922(2007).
CC   -!- FUNCTION: Component of a transcriptional repressor complex together
CC       with MAX (PubMed:8425218). In complex with MAX binds to the core DNA
CC       sequence 5'-CAC[GA]TG-3' (PubMed:8425218). Antagonizes MYC
CC       transcriptional activity by competing with MYC for MAX binding
CC       (PubMed:8425218). Binds to the TERT promoter and represses telomerase
CC       expression, possibly by interfering with MYC binding (PubMed:12837246).
CC       {ECO:0000269|PubMed:12837246, ECO:0000269|PubMed:8425218}.
CC   -!- SUBUNIT: Heterodimer with MAX; the interaction is required for DNA-
CC       binding (PubMed:8425218). DNA binding requires dimerization with
CC       another bHLH protein; does not form homodimers, and does not bind to
CC       DNA in the absence of MAX in vitro (PubMed:8425218). Interacts with
CC       RNF17 (By similarity). {ECO:0000250|UniProtKB:P50538,
CC       ECO:0000269|PubMed:8425218}.
CC   -!- INTERACTION:
CC       Q05195; P61244: MAX; NbExp=3; IntAct=EBI-8833637, EBI-751711;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:8425218}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q05195-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q05195-2; Sequence=VSP_043074;
CC   -!- PTM: Ubiquitinated by BIRC2/c-IAP1, leading to its subsequent
CC       degradation by the proteasome. {ECO:0000269|PubMed:18082613}.
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DR   EMBL; L06895; AAA36194.1; -; mRNA.
DR   EMBL; CR536495; CAG38734.1; -; mRNA.
DR   EMBL; CR541692; CAG46493.1; -; mRNA.
DR   EMBL; AK312734; BAG35605.1; -; mRNA.
DR   EMBL; AC019206; AAY14867.1; -; Genomic_DNA.
DR   EMBL; CH471053; EAW99839.1; -; Genomic_DNA.
DR   EMBL; BC069377; AAH69377.1; -; mRNA.
DR   EMBL; BC069433; AAH69433.1; -; mRNA.
DR   EMBL; BC098396; AAH98396.1; -; mRNA.
DR   EMBL; BC113531; AAI13532.1; -; mRNA.
DR   EMBL; BC117260; AAI17261.1; -; mRNA.
DR   EMBL; BC143831; AAI43832.1; -; mRNA.
DR   CCDS; CCDS1896.1; -. [Q05195-1]
DR   CCDS; CCDS56123.1; -. [Q05195-2]
DR   PIR; A45181; A45181.
DR   RefSeq; NP_001189442.1; NM_001202513.1.
DR   RefSeq; NP_001189443.1; NM_001202514.1. [Q05195-2]
DR   RefSeq; NP_002348.1; NM_002357.3. [Q05195-1]
DR   PDB; 1E91; NMR; -; B=8-20.
DR   PDB; 1G1E; NMR; -; A=6-21.
DR   PDB; 1NLW; X-ray; 2.00 A; A/D=57-136.
DR   PDB; 1PD7; NMR; -; B=5-28.
DR   PDB; 1S5Q; NMR; -; A=6-21.
DR   PDBsum; 1E91; -.
DR   PDBsum; 1G1E; -.
DR   PDBsum; 1NLW; -.
DR   PDBsum; 1PD7; -.
DR   PDBsum; 1S5Q; -.
DR   BMRB; Q05195; -.
DR   SMR; Q05195; -.
DR   BioGRID; 110259; 39.
DR   ComplexPortal; CPX-104; Transcriptional repressor Mad-Max complex.
DR   CORUM; Q05195; -.
DR   DIP; DIP-204N; -.
DR   ELM; Q05195; -.
DR   IntAct; Q05195; 15.
DR   MINT; Q05195; -.
DR   STRING; 9606.ENSP00000264444; -.
DR   iPTMnet; Q05195; -.
DR   PhosphoSitePlus; Q05195; -.
DR   BioMuta; MXD1; -.
DR   DMDM; 729978; -.
DR   MassIVE; Q05195; -.
DR   PaxDb; Q05195; -.
DR   PeptideAtlas; Q05195; -.
DR   PRIDE; Q05195; -.
DR   ProteomicsDB; 58314; -. [Q05195-1]
DR   ProteomicsDB; 58315; -. [Q05195-2]
DR   Antibodypedia; 893; 181 antibodies.
DR   DNASU; 4084; -.
DR   Ensembl; ENST00000264444; ENSP00000264444; ENSG00000059728. [Q05195-1]
DR   Ensembl; ENST00000540449; ENSP00000443935; ENSG00000059728. [Q05195-2]
DR   GeneID; 4084; -.
DR   KEGG; hsa:4084; -.
DR   UCSC; uc002sfy.4; human. [Q05195-1]
DR   CTD; 4084; -.
DR   DisGeNET; 4084; -.
DR   GeneCards; MXD1; -.
DR   HGNC; HGNC:6761; MXD1.
DR   HPA; ENSG00000059728; Tissue enhanced (blood, bone marrow, esophagus).
DR   MIM; 600021; gene.
DR   neXtProt; NX_Q05195; -.
DR   OpenTargets; ENSG00000059728; -.
DR   PharmGKB; PA30520; -.
DR   VEuPathDB; HostDB:ENSG00000059728; -.
DR   eggNOG; KOG2483; Eukaryota.
DR   GeneTree; ENSGT00940000159446; -.
DR   HOGENOM; CLU_082604_0_1_1; -.
DR   InParanoid; Q05195; -.
DR   OMA; SSTHNEM; -.
DR   OrthoDB; 1311585at2759; -.
DR   PhylomeDB; Q05195; -.
DR   TreeFam; TF315654; -.
DR   PathwayCommons; Q05195; -.
DR   SIGNOR; Q05195; -.
DR   BioGRID-ORCS; 4084; 3 hits in 1040 CRISPR screens.
DR   ChiTaRS; MXD1; human.
DR   EvolutionaryTrace; Q05195; -.
DR   GeneWiki; MXD1; -.
DR   GenomeRNAi; 4084; -.
DR   Pharos; Q05195; Tbio.
DR   PRO; PR:Q05195; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; Q05195; protein.
DR   Bgee; ENSG00000059728; Expressed in buccal mucosa cell and 220 other tissues.
DR   ExpressionAtlas; Q05195; baseline and differential.
DR   Genevisible; Q05195; HS.
DR   GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
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; IDA:NTNU_SB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 4.10.280.10; -; 1.
DR   IDEAL; IID00165; -.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   InterPro; IPR040157; MXD1.
DR   PANTHER; PTHR11969:SF18; PTHR11969:SF18; 1.
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   3D-structure; Alternative splicing; DNA-binding; Nucleus;
KW   Reference proteome; Repressor; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   CHAIN           1..221
FT                   /note="Max dimerization protein 1"
FT                   /id="PRO_0000127264"
FT   DOMAIN          56..108
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          30..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          173..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           21..49
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         58..67
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_043074"
FT   HELIX           9..19
FT                   /evidence="ECO:0007829|PDB:1E91"
FT   HELIX           58..81
FT                   /evidence="ECO:0007829|PDB:1NLW"
FT   STRAND          87..89
FT                   /evidence="ECO:0007829|PDB:1NLW"
FT   HELIX           95..134
FT                   /evidence="ECO:0007829|PDB:1NLW"
SQ   SEQUENCE   221 AA;  25254 MW;  B39FAEBFD708B6AB CRC64;
     MAAAVRMNIQ MLLEAADYLE RREREAEHGY ASMLPYNNKD RDALKRRNKS KKNNSSSRST
     HNEMEKNRRA HLRLCLEKLK GLVPLGPESS RHTTLSLLTK AKLHIKKLED CDRKAVHQID
     QLQREQRHLK RQLEKLGIER IRMDSIGSTV SSERSDSDRE EIDVDVESTD YLTGDLDWSS
     SSVSDSDERG SMQSLGSDEG YSSTSIKRIK LQDSHKACLG L
//
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