Full text data of DR1
DR1
[Confidence: low (only semi-automatic identification from reviews)]
Protein Dr1 (Down-regulator of transcription 1; Negative cofactor 2-beta; NC2-beta; TATA-binding protein-associated phosphoprotein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Protein Dr1 (Down-regulator of transcription 1; Negative cofactor 2-beta; NC2-beta; TATA-binding protein-associated phosphoprotein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q01658
ID NC2B_HUMAN Reviewed; 176 AA.
AC Q01658;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUL-1993, sequence version 1.
DT 22-JAN-2014, entry version 128.
DE RecName: Full=Protein Dr1;
DE AltName: Full=Down-regulator of transcription 1;
DE AltName: Full=Negative cofactor 2-beta;
DE Short=NC2-beta;
DE AltName: Full=TATA-binding protein-associated phosphoprotein;
GN Name=DR1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1339312; DOI=10.1016/0092-8674(92)90172-9;
RA Inostroza J.A., Mermelstein F.H., Ha I., Lane W.S., Reinberg D.;
RT "Dr1, a TATA-binding protein-associated phosphoprotein and inhibitor
RT of class II gene transcription.";
RL Cell 70:477-489(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph, Testis, and Uterus;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, AND INTERACTION WITH DRAP1.
RX PubMed=8670811;
RA Goppelt A.R., Stelzer G., Lottspeich F., Meisterernst M.;
RT "A mechanism for repression of class II gene transcription through
RT specific binding of NC2 to TBP-promoter complexes via heterodimeric
RT histone fold domains.";
RL EMBO J. 15:3105-3116(1996).
RN [6]
RP INTERACTION WITH NFIL3.
RX PubMed=8836190; DOI=10.1093/nar/24.18.3607;
RA Cowell I.G., Hurst H.C.;
RT "Protein-protein interaction between the transcriptional repressor
RT E4BP4 and the TBP-binding protein Dr1.";
RL Nucleic Acids Res. 24:3607-3613(1996).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166 AND SER-167, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP FUNCTION, AND IDENTIFICATION IN ATAC COMPLEX.
RX PubMed=19103755; DOI=10.1128/MCB.01599-08;
RA Guelman S., Kozuka K., Mao Y., Pham V., Solloway M.J., Wang J., Wu J.,
RA Lill J.R., Zha J.;
RT "The double-histone-acetyltransferase complex ATAC is essential for
RT mammalian development.";
RL Mol. Cell. Biol. 29:1176-1188(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.62 ANGSTROMS) IN COMPLEX WITH DRAP1; TBP AND
RP DNA.
RX PubMed=11461703; DOI=10.1016/S0092-8674(01)00417-2;
RA Kamada K., Shu F., Chen H., Malik S., Stelzer G., Roeder R.G.,
RA Meisterernst M., Burley S.K.;
RT "Crystal structure of negative cofactor 2 recognizing the TBP-DNA
RT transcription complex.";
RL Cell 106:71-81(2001).
CC -!- FUNCTION: The association of the DR1/DRAP1 heterodimer with TBP
CC results in a functional repression of both activated and basal
CC transcription of class II genes. This interaction precludes the
CC formation of a transcription-competent complex by inhibiting the
CC association of TFIIA and/or TFIIB with TBP. Can bind to DNA on its
CC own. Component of the ATAC complex, a complex with histone
CC acetyltransferase activity on histones H3 and H4.
CC -!- SUBUNIT: Heterodimer with DRAP1. DR1 exists in solution as a
CC homotetramer that dissociates during interaction with TBP and
CC then, after complexing with TBP, reassociates at a slow rate, to
CC reconstitute the tetramer. Interacts with NFIL3. Component of the
CC ADA2A-containing complex (ATAC), composed of CSRP2BP, KAT2A,
CC TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- PTM: Phosphorylation regulates its interaction with TBP. Not
CC phosphorylated when bound to DRAP1.
CC -!- SIMILARITY: Belongs to the NC2 beta/DR1 family.
CC -!- SIMILARITY: Contains 1 histone-fold domain.
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DR EMBL; M97388; AAA58442.1; -; mRNA.
DR EMBL; BT006972; AAP35618.1; -; mRNA.
DR EMBL; AL137159; CAC17578.1; -; Genomic_DNA.
DR EMBL; BC002809; AAH02809.1; -; mRNA.
DR EMBL; BC035507; AAH35507.1; -; mRNA.
DR EMBL; BC068553; AAH68553.1; -; mRNA.
DR PIR; A43320; A43320.
DR RefSeq; NP_001929.1; NM_001938.2.
DR UniGene; Hs.348418; -.
DR PDB; 1JFI; X-ray; 2.62 A; B=1-176.
DR PDBsum; 1JFI; -.
DR ProteinModelPortal; Q01658; -.
DR SMR; Q01658; 9-143.
DR IntAct; Q01658; 4.
DR MINT; MINT-204839; -.
DR STRING; 9606.ENSP00000359290; -.
DR PhosphoSite; Q01658; -.
DR DMDM; 401162; -.
DR PaxDb; Q01658; -.
DR PeptideAtlas; Q01658; -.
DR PRIDE; Q01658; -.
DR DNASU; 1810; -.
DR Ensembl; ENST00000370267; ENSP00000359290; ENSG00000117505.
DR Ensembl; ENST00000370272; ENSP00000359295; ENSG00000117505.
DR GeneID; 1810; -.
DR KEGG; hsa:1810; -.
DR UCSC; uc001dpu.3; human.
DR CTD; 1810; -.
DR GeneCards; GC01P093811; -.
DR HGNC; HGNC:3017; DR1.
DR HPA; HPA050785; -.
DR HPA; HPA055308; -.
DR MIM; 601482; gene.
DR neXtProt; NX_Q01658; -.
DR PharmGKB; PA27475; -.
DR eggNOG; COG5150; -.
DR HOGENOM; HOG000178641; -.
DR HOVERGEN; HBG002051; -.
DR InParanoid; Q01658; -.
DR OMA; ACDHITK; -.
DR OrthoDB; EOG7T4MMT; -.
DR PhylomeDB; Q01658; -.
DR EvolutionaryTrace; Q01658; -.
DR GeneWiki; DR1_(gene); -.
DR GenomeRNAi; 1810; -.
DR NextBio; 7377; -.
DR PRO; PR:Q01658; -.
DR ArrayExpress; Q01658; -.
DR Bgee; Q01658; -.
DR CleanEx; HS_DR1; -.
DR Genevestigator; Q01658; -.
DR GO; GO:0005671; C:Ada2/Gcn5/Ada3 transcription activator complex; IDA:BHF-UCL.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0017025; F:TBP-class protein binding; IDA:BHF-UCL.
DR GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR003958; CBFA_NFYB_domain.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR003957; Transcrpt_fac_NFYB/HAP3.
DR Pfam; PF00808; CBFD_NFYB_HMF; 1.
DR PRINTS; PR00615; CCAATSUBUNTA.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome;
KW Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein;
KW Polymorphism; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 176 Protein Dr1.
FT /FTId=PRO_0000072440.
FT MOTIF 100 103 Nuclear localization signal (Potential).
FT COMPBIAS 121 168 Ala/Gln-rich.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 166 166 Phosphoserine.
FT MOD_RES 167 167 Phosphoserine.
FT VARIANT 171 171 E -> D (in dbSNP:rs3088371).
FT /FTId=VAR_034506.
FT HELIX 15 25
FT HELIX 33 60
FT STRAND 64 66
FT HELIX 68 78
FT HELIX 81 83
FT HELIX 84 110
FT STRAND 111 113
FT HELIX 115 140
SQ SEQUENCE 176 AA; 19444 MW; 36E7E59F2FD6CAB5 CRC64;
MASSSGNDDD LTIPRAAINK MIKETLPNVR VANDARELVV NCCTEFIHLI SSEANEICNK
SEKKTISPEH VIQALESLGF GSYISEVKEV LQECKTVALK RRKASSRLEN LGIPEEELLR
QQQELFAKAR QQQAELAQQE WLQMQQAAQQ AQLAAASASA SNQAGSSQDE EDDDDI
//
ID NC2B_HUMAN Reviewed; 176 AA.
AC Q01658;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUL-1993, sequence version 1.
DT 22-JAN-2014, entry version 128.
DE RecName: Full=Protein Dr1;
DE AltName: Full=Down-regulator of transcription 1;
DE AltName: Full=Negative cofactor 2-beta;
DE Short=NC2-beta;
DE AltName: Full=TATA-binding protein-associated phosphoprotein;
GN Name=DR1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1339312; DOI=10.1016/0092-8674(92)90172-9;
RA Inostroza J.A., Mermelstein F.H., Ha I., Lane W.S., Reinberg D.;
RT "Dr1, a TATA-binding protein-associated phosphoprotein and inhibitor
RT of class II gene transcription.";
RL Cell 70:477-489(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph, Testis, and Uterus;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, AND INTERACTION WITH DRAP1.
RX PubMed=8670811;
RA Goppelt A.R., Stelzer G., Lottspeich F., Meisterernst M.;
RT "A mechanism for repression of class II gene transcription through
RT specific binding of NC2 to TBP-promoter complexes via heterodimeric
RT histone fold domains.";
RL EMBO J. 15:3105-3116(1996).
RN [6]
RP INTERACTION WITH NFIL3.
RX PubMed=8836190; DOI=10.1093/nar/24.18.3607;
RA Cowell I.G., Hurst H.C.;
RT "Protein-protein interaction between the transcriptional repressor
RT E4BP4 and the TBP-binding protein Dr1.";
RL Nucleic Acids Res. 24:3607-3613(1996).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166 AND SER-167, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP FUNCTION, AND IDENTIFICATION IN ATAC COMPLEX.
RX PubMed=19103755; DOI=10.1128/MCB.01599-08;
RA Guelman S., Kozuka K., Mao Y., Pham V., Solloway M.J., Wang J., Wu J.,
RA Lill J.R., Zha J.;
RT "The double-histone-acetyltransferase complex ATAC is essential for
RT mammalian development.";
RL Mol. Cell. Biol. 29:1176-1188(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.62 ANGSTROMS) IN COMPLEX WITH DRAP1; TBP AND
RP DNA.
RX PubMed=11461703; DOI=10.1016/S0092-8674(01)00417-2;
RA Kamada K., Shu F., Chen H., Malik S., Stelzer G., Roeder R.G.,
RA Meisterernst M., Burley S.K.;
RT "Crystal structure of negative cofactor 2 recognizing the TBP-DNA
RT transcription complex.";
RL Cell 106:71-81(2001).
CC -!- FUNCTION: The association of the DR1/DRAP1 heterodimer with TBP
CC results in a functional repression of both activated and basal
CC transcription of class II genes. This interaction precludes the
CC formation of a transcription-competent complex by inhibiting the
CC association of TFIIA and/or TFIIB with TBP. Can bind to DNA on its
CC own. Component of the ATAC complex, a complex with histone
CC acetyltransferase activity on histones H3 and H4.
CC -!- SUBUNIT: Heterodimer with DRAP1. DR1 exists in solution as a
CC homotetramer that dissociates during interaction with TBP and
CC then, after complexing with TBP, reassociates at a slow rate, to
CC reconstitute the tetramer. Interacts with NFIL3. Component of the
CC ADA2A-containing complex (ATAC), composed of CSRP2BP, KAT2A,
CC TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- PTM: Phosphorylation regulates its interaction with TBP. Not
CC phosphorylated when bound to DRAP1.
CC -!- SIMILARITY: Belongs to the NC2 beta/DR1 family.
CC -!- SIMILARITY: Contains 1 histone-fold domain.
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DR EMBL; M97388; AAA58442.1; -; mRNA.
DR EMBL; BT006972; AAP35618.1; -; mRNA.
DR EMBL; AL137159; CAC17578.1; -; Genomic_DNA.
DR EMBL; BC002809; AAH02809.1; -; mRNA.
DR EMBL; BC035507; AAH35507.1; -; mRNA.
DR EMBL; BC068553; AAH68553.1; -; mRNA.
DR PIR; A43320; A43320.
DR RefSeq; NP_001929.1; NM_001938.2.
DR UniGene; Hs.348418; -.
DR PDB; 1JFI; X-ray; 2.62 A; B=1-176.
DR PDBsum; 1JFI; -.
DR ProteinModelPortal; Q01658; -.
DR SMR; Q01658; 9-143.
DR IntAct; Q01658; 4.
DR MINT; MINT-204839; -.
DR STRING; 9606.ENSP00000359290; -.
DR PhosphoSite; Q01658; -.
DR DMDM; 401162; -.
DR PaxDb; Q01658; -.
DR PeptideAtlas; Q01658; -.
DR PRIDE; Q01658; -.
DR DNASU; 1810; -.
DR Ensembl; ENST00000370267; ENSP00000359290; ENSG00000117505.
DR Ensembl; ENST00000370272; ENSP00000359295; ENSG00000117505.
DR GeneID; 1810; -.
DR KEGG; hsa:1810; -.
DR UCSC; uc001dpu.3; human.
DR CTD; 1810; -.
DR GeneCards; GC01P093811; -.
DR HGNC; HGNC:3017; DR1.
DR HPA; HPA050785; -.
DR HPA; HPA055308; -.
DR MIM; 601482; gene.
DR neXtProt; NX_Q01658; -.
DR PharmGKB; PA27475; -.
DR eggNOG; COG5150; -.
DR HOGENOM; HOG000178641; -.
DR HOVERGEN; HBG002051; -.
DR InParanoid; Q01658; -.
DR OMA; ACDHITK; -.
DR OrthoDB; EOG7T4MMT; -.
DR PhylomeDB; Q01658; -.
DR EvolutionaryTrace; Q01658; -.
DR GeneWiki; DR1_(gene); -.
DR GenomeRNAi; 1810; -.
DR NextBio; 7377; -.
DR PRO; PR:Q01658; -.
DR ArrayExpress; Q01658; -.
DR Bgee; Q01658; -.
DR CleanEx; HS_DR1; -.
DR Genevestigator; Q01658; -.
DR GO; GO:0005671; C:Ada2/Gcn5/Ada3 transcription activator complex; IDA:BHF-UCL.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0017025; F:TBP-class protein binding; IDA:BHF-UCL.
DR GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR003958; CBFA_NFYB_domain.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR003957; Transcrpt_fac_NFYB/HAP3.
DR Pfam; PF00808; CBFD_NFYB_HMF; 1.
DR PRINTS; PR00615; CCAATSUBUNTA.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome;
KW Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein;
KW Polymorphism; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 176 Protein Dr1.
FT /FTId=PRO_0000072440.
FT MOTIF 100 103 Nuclear localization signal (Potential).
FT COMPBIAS 121 168 Ala/Gln-rich.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 166 166 Phosphoserine.
FT MOD_RES 167 167 Phosphoserine.
FT VARIANT 171 171 E -> D (in dbSNP:rs3088371).
FT /FTId=VAR_034506.
FT HELIX 15 25
FT HELIX 33 60
FT STRAND 64 66
FT HELIX 68 78
FT HELIX 81 83
FT HELIX 84 110
FT STRAND 111 113
FT HELIX 115 140
SQ SEQUENCE 176 AA; 19444 MW; 36E7E59F2FD6CAB5 CRC64;
MASSSGNDDD LTIPRAAINK MIKETLPNVR VANDARELVV NCCTEFIHLI SSEANEICNK
SEKKTISPEH VIQALESLGF GSYISEVKEV LQECKTVALK RRKASSRLEN LGIPEEELLR
QQQELFAKAR QQQAELAQQE WLQMQQAAQQ AQLAAASASA SNQAGSSQDE EDDDDI
//
MIM
601482
*RECORD*
*FIELD* NO
601482
*FIELD* TI
*601482 DOWNREGULATOR OF TRANSCRIPTION 1, TBP-BINDING; DR1
;;TATA BOX-BINDING PROTEIN-ASSOCIATED PHOSPHOPROTEIN DR1;;
read moreNEGATIVE COFACTOR 2-BETA;;
NC2-BETA
*FIELD* TX
CLONING
Several phosphoproteins interact with TBP, the TATA box-binding protein
(600075). Among them, DR1 is a TBP-associated phosphoprotein that
represses both basal and activated levels of transcription. Inostroza et
al. (1992) biochemically characterized DR1 purified from HeLa cells and
cloned the human gene from a HeLa cell cDNA library. The gene encodes a
176-amino acid polypeptide of 19 kD. They showed that DR1 is
phosphorylated in vivo and that phosphorylation of DR1 affected its
interaction with TBP.
Using Northern blot analysis, Inostroza et al. (1992) and Mermelstein et
al. (1996) detected varying levels of 1.5- and 3.4-kb DR1 transcripts in
all tissues examined. By Northern blot analysis of rat tissues, Purello
et al. (1996) detected a 3.6 kb mRNA in all tested tissues, with a
second 1.8 kb message in testis. The highest level of expression was
seen in testis.
GENE FUNCTION
Mermelstein et al. (1996) identified DR1-associated protein-1 (DRAP1;
602289), a corepressor of DR1 that enhances DR1-mediated repression of
transcription. Mermelstein et al. (1996) immunodetected DR1 protein in
all cell populations of the developing rat brain: actively dividing stem
cells, nondividing migratory neurons, and nondividing, highly
differentiated neurons. Based on the differential expression of DR1 and
DRAP1 proteins in the developing rat brain, Mermelstein et al. (1996)
suggested that DR1-mediated repression of transcription is higher in
nondividing, highly differentiated cells than in actively dividing
cells.
The DR1 protein contains 3 domains: a histone fold motif at the N
terminus, a TBP-binding domain, and a glutamine- and alanine-rich
region. Mermelstein et al. (1996) showed that the histone fold motif of
DR1 is required for DR1-DRAP1 interaction. Both the TBP-binding domain
and the glutamine- and alanine-rich region are required for DR1-mediated
repression of transcription. Yeung et al. (1997) demonstrated that the
TBP-binding domain has 2 functions: it tethers the DR1 repressor complex
to the promoter by interacting with TBP, and it is required for the
corepression activity of DRAP1, although it is not required for
DR1-DRAP1 interaction. Yeung et al. (1997) determined that the
glutamine- and alanine-rich region is the repressor domain of DR1 and
that this domain interacts with TBP. Goppelt et al. (1996) proposed that
binding of DR1 repressor complexes to TBP-promoter complexes establishes
a mechanism in which an altered DNA conformation, together with the
formation of higher order complexes, inhibits the assembly of the
preinitiation complex and controls the rate of RNA polymerase II
transcription.
Willy et al. (2000) identified an activity that was required for
transcription of downstream promoter element (DPE)-containing core
promoters in vitro. The purified factor was found to be the Drosophila
homolog of the NC2 transcriptional repressor, also known as DR1-DRAP1.
Drosophila Nc2 is composed of a 43-kD subunit homologous to DRAP1
(NC2-alpha) and a 22-kD subunit homologous to DR1 (NC2-beta). Purified
recombinant Drosophila Nc2 activated DPE-driven promoters and repressed
TATA-driven promoters. A mutant version of Drosophila Nc2 could activate
DPE promoters but was unable to repress TATA promoters. Thus, the
activation and repression functions are distinct. Willy et al. (2000)
concluded that NC2 is a bifunctional basal transcription factor that
differentially regulates gene transcription through DPE or TATA box
motifs.
Using mass spectrometry, Wang et al. (2008) identified NC2-beta as a
component of the ADA2A (TADA2A; 602276)-containing (ATAC) histone
acetyltransferase complex in HeLa cells.
GENE STRUCTURE
Rozet et al. (1996) determined that the DR1 gene contains 3 exons and
spans 15 kb of genomic DNA.
BIOCHEMICAL FEATURES
Kamada et al. (2001) determined the x-ray structure of a ternary complex
of NC2, TBP, and DNA at 2.6-angstrom resolution. The N termini of
NC2-alpha and -beta resemble histones H2A (see 613499) and H2B (see
609904), respectively, and form a heterodimer that binds to the bent DNA
double helix on the underside of the preformed TBP-DNA complex via
electrostatic interactions. NC2-beta contributes to inhibition of
TATA-dependent transcription through interactions of its C-terminal
alpha helix with a conserved hydrophobic feature on the upper surface of
TBP, which in turn positions the penultimate alpha helix of NC2-beta to
block recognition of the TBP-DNA complex by transcription factor IIB
(189963).
MAPPING
By fluorescence in situ hybridization, Rozet et al. (1996) mapped the
DR1 gene to 1p22.1. Purello et al. (1996) used somatic cell genetics and
fluorescence in situ hybridization to map the DR1 gene to human
chromosome region 1p21-p13. Southern blot analysis showed that the gene
is present as a single copy in the genomes of all eukaryotes examined.
Kaplan et al. (1993) mapped an expressed sequence tag (EST) of the DR1
gene to the YAC contig encompassing the Stargardt disease locus (STGD;
248200) on 1p. Using SSCP analysis of genomic DNA amplified with
specific primers in 10 controls and 35 unrelated patients with either
Stargardt disease (26 patients) or late-onset fundus flavimaculatus, a
condition allelic to STGD (9 patients), Rozet et al. (1996) found no
mutation in the DR1 gene. Rozet et al. (1996) were not able to study the
promoter of the gene, but the findings suggested that DR1 is not
involved in Stargardt disease.
*FIELD* RF
1. Goppelt, A.; Stelzer, G.; Lottspeich, F.; Meisterernst, M.: A
mechanism for repression of class II gene transcription through specific
binding of NC2 to TBP-promoter complexes via heterodimeric histone
fold domains. EMBO J. 15: 3105-3116, 1996.
2. Inostroza, J. A.; Mermeistein, F. H.; Ha, I.; Lane, W. S.; Reinberg,
D.: Dr1, a TATA-binding protein-associated phosphoprotein and inhibitor
of class II gene transcription. Cell 70: 477-489, 1992.
3. Kamada, K.; Shu, F.; Chen, H.; Malik, S.; Stelzer, G.; Roeder,
R. G.; Meisterernst, M.; Burley, S. K.: Crystal structure of negative
cofactor 2 recognizing the TBP-DNA transcription complex. Cell 106:
71-81, 2001.
4. Kaplan, J.; Gerber, S.; Larget-Piet, D.; Rozet, J.-M.; Dollfus,
H.; Dufier, J.-L.; Odent, S.; Postel-Vinay, A.; Janin, N.; Briard,
M.-L.; Frezal, J.; Munnich, A.: A gene for Stargardt's disease (fundus
flavimaculatus) maps to the short arm of chromosome 1. Nature Genet. 5:
308-311, 1993. Note: Erratum: Nature Genet. 6: 214 only, 1994.
5. Mermelstein, F.; Yeung, K.; Cao, J.; Inostroza, J. A.; Erdjument-Bromage,
H.; Eagelson, K.; Landsman, D.; Levitt, P.; Tempst, P.; Reinberg,
D.: Requirement of a corepressor for Dr1-mediated repression of transcription. Genes
Dev. 10: 1033-1048, 1996.
6. Purello, M.; Di Pietro, C.; Rapisarda, A.; Viola, A.; Corsaro,
C.; Motta, S.; Grzeschik, K.-H.; Sichel, G.: Genomic localization
of the human gene encoding Dr1, a negative modulator of transcription
of class II and class III genes. Cytogenet. Cell Genet. 75: 186-189,
1996.
7. Rozet, J.-M.; Gerber, S.; Perrault, I.; Camuzat, A.; Calvas, P.;
Viegas-Pequignot, E.; Molina-Gomes, D.; Le Paslier, D.; Chumakov,
I.; Munnich, A.; Kaplan, J.: Structure and physical mapping of DR1,
a TATA-binding protein-associated phosphoprotein gene, to chromosome
1p22.1 and its exclusion in Stargardt disease (STGD). Genomics 36:
554-556, 1996.
8. Wang, Y.-L.; Faiola, F.; Xu, M.; Pan, S.; Martinez, E.: Human
ATAC is a GCN5/PCAF-containing acetylase complex with a novel NC2-like
histone fold module that interacts with the TATA-binding protein. J.
Biol. Chem. 283: 33808-33815, 2008.
9. Willy, P. J.; Kobayashi, R.; Kadonaga, J. T.: A basal transcription
factor that activates or represses transcription. Science 290: 982-984,
2000.
10. Yeung, K.; Kim, S.; Reinberg, D.: Functional dissection of a
human Dr1-DRAP1 repressor complex. Molec. Cell. Biol. 17: 36-45,
1997.
*FIELD* CN
Patricia A. Hartz - updated: 4/20/2010
Stylianos E. Antonarakis - updated: 8/2/2001
Ada Hamosh - updated: 11/16/2000
Jennifer P. Macke - updated: 5/1/1998
Patti M. Sherman - updated: 1/28/1998
Mark H. Paalman - updated: 10/25/1996
*FIELD* CD
Victor A. McKusick: 10/24/1996
*FIELD* ED
mgross: 01/29/2013
mgross: 1/11/2013
terry: 12/20/2012
mgross: 4/20/2010
terry: 4/20/2010
alopez: 4/13/2009
carol: 8/13/2001
mgross: 8/2/2001
mgross: 11/16/2000
terry: 4/29/1999
alopez: 5/1/1998
dholmes: 1/28/1998
mark: 10/25/1996
mark: 10/24/1996
*RECORD*
*FIELD* NO
601482
*FIELD* TI
*601482 DOWNREGULATOR OF TRANSCRIPTION 1, TBP-BINDING; DR1
;;TATA BOX-BINDING PROTEIN-ASSOCIATED PHOSPHOPROTEIN DR1;;
read moreNEGATIVE COFACTOR 2-BETA;;
NC2-BETA
*FIELD* TX
CLONING
Several phosphoproteins interact with TBP, the TATA box-binding protein
(600075). Among them, DR1 is a TBP-associated phosphoprotein that
represses both basal and activated levels of transcription. Inostroza et
al. (1992) biochemically characterized DR1 purified from HeLa cells and
cloned the human gene from a HeLa cell cDNA library. The gene encodes a
176-amino acid polypeptide of 19 kD. They showed that DR1 is
phosphorylated in vivo and that phosphorylation of DR1 affected its
interaction with TBP.
Using Northern blot analysis, Inostroza et al. (1992) and Mermelstein et
al. (1996) detected varying levels of 1.5- and 3.4-kb DR1 transcripts in
all tissues examined. By Northern blot analysis of rat tissues, Purello
et al. (1996) detected a 3.6 kb mRNA in all tested tissues, with a
second 1.8 kb message in testis. The highest level of expression was
seen in testis.
GENE FUNCTION
Mermelstein et al. (1996) identified DR1-associated protein-1 (DRAP1;
602289), a corepressor of DR1 that enhances DR1-mediated repression of
transcription. Mermelstein et al. (1996) immunodetected DR1 protein in
all cell populations of the developing rat brain: actively dividing stem
cells, nondividing migratory neurons, and nondividing, highly
differentiated neurons. Based on the differential expression of DR1 and
DRAP1 proteins in the developing rat brain, Mermelstein et al. (1996)
suggested that DR1-mediated repression of transcription is higher in
nondividing, highly differentiated cells than in actively dividing
cells.
The DR1 protein contains 3 domains: a histone fold motif at the N
terminus, a TBP-binding domain, and a glutamine- and alanine-rich
region. Mermelstein et al. (1996) showed that the histone fold motif of
DR1 is required for DR1-DRAP1 interaction. Both the TBP-binding domain
and the glutamine- and alanine-rich region are required for DR1-mediated
repression of transcription. Yeung et al. (1997) demonstrated that the
TBP-binding domain has 2 functions: it tethers the DR1 repressor complex
to the promoter by interacting with TBP, and it is required for the
corepression activity of DRAP1, although it is not required for
DR1-DRAP1 interaction. Yeung et al. (1997) determined that the
glutamine- and alanine-rich region is the repressor domain of DR1 and
that this domain interacts with TBP. Goppelt et al. (1996) proposed that
binding of DR1 repressor complexes to TBP-promoter complexes establishes
a mechanism in which an altered DNA conformation, together with the
formation of higher order complexes, inhibits the assembly of the
preinitiation complex and controls the rate of RNA polymerase II
transcription.
Willy et al. (2000) identified an activity that was required for
transcription of downstream promoter element (DPE)-containing core
promoters in vitro. The purified factor was found to be the Drosophila
homolog of the NC2 transcriptional repressor, also known as DR1-DRAP1.
Drosophila Nc2 is composed of a 43-kD subunit homologous to DRAP1
(NC2-alpha) and a 22-kD subunit homologous to DR1 (NC2-beta). Purified
recombinant Drosophila Nc2 activated DPE-driven promoters and repressed
TATA-driven promoters. A mutant version of Drosophila Nc2 could activate
DPE promoters but was unable to repress TATA promoters. Thus, the
activation and repression functions are distinct. Willy et al. (2000)
concluded that NC2 is a bifunctional basal transcription factor that
differentially regulates gene transcription through DPE or TATA box
motifs.
Using mass spectrometry, Wang et al. (2008) identified NC2-beta as a
component of the ADA2A (TADA2A; 602276)-containing (ATAC) histone
acetyltransferase complex in HeLa cells.
GENE STRUCTURE
Rozet et al. (1996) determined that the DR1 gene contains 3 exons and
spans 15 kb of genomic DNA.
BIOCHEMICAL FEATURES
Kamada et al. (2001) determined the x-ray structure of a ternary complex
of NC2, TBP, and DNA at 2.6-angstrom resolution. The N termini of
NC2-alpha and -beta resemble histones H2A (see 613499) and H2B (see
609904), respectively, and form a heterodimer that binds to the bent DNA
double helix on the underside of the preformed TBP-DNA complex via
electrostatic interactions. NC2-beta contributes to inhibition of
TATA-dependent transcription through interactions of its C-terminal
alpha helix with a conserved hydrophobic feature on the upper surface of
TBP, which in turn positions the penultimate alpha helix of NC2-beta to
block recognition of the TBP-DNA complex by transcription factor IIB
(189963).
MAPPING
By fluorescence in situ hybridization, Rozet et al. (1996) mapped the
DR1 gene to 1p22.1. Purello et al. (1996) used somatic cell genetics and
fluorescence in situ hybridization to map the DR1 gene to human
chromosome region 1p21-p13. Southern blot analysis showed that the gene
is present as a single copy in the genomes of all eukaryotes examined.
Kaplan et al. (1993) mapped an expressed sequence tag (EST) of the DR1
gene to the YAC contig encompassing the Stargardt disease locus (STGD;
248200) on 1p. Using SSCP analysis of genomic DNA amplified with
specific primers in 10 controls and 35 unrelated patients with either
Stargardt disease (26 patients) or late-onset fundus flavimaculatus, a
condition allelic to STGD (9 patients), Rozet et al. (1996) found no
mutation in the DR1 gene. Rozet et al. (1996) were not able to study the
promoter of the gene, but the findings suggested that DR1 is not
involved in Stargardt disease.
*FIELD* RF
1. Goppelt, A.; Stelzer, G.; Lottspeich, F.; Meisterernst, M.: A
mechanism for repression of class II gene transcription through specific
binding of NC2 to TBP-promoter complexes via heterodimeric histone
fold domains. EMBO J. 15: 3105-3116, 1996.
2. Inostroza, J. A.; Mermeistein, F. H.; Ha, I.; Lane, W. S.; Reinberg,
D.: Dr1, a TATA-binding protein-associated phosphoprotein and inhibitor
of class II gene transcription. Cell 70: 477-489, 1992.
3. Kamada, K.; Shu, F.; Chen, H.; Malik, S.; Stelzer, G.; Roeder,
R. G.; Meisterernst, M.; Burley, S. K.: Crystal structure of negative
cofactor 2 recognizing the TBP-DNA transcription complex. Cell 106:
71-81, 2001.
4. Kaplan, J.; Gerber, S.; Larget-Piet, D.; Rozet, J.-M.; Dollfus,
H.; Dufier, J.-L.; Odent, S.; Postel-Vinay, A.; Janin, N.; Briard,
M.-L.; Frezal, J.; Munnich, A.: A gene for Stargardt's disease (fundus
flavimaculatus) maps to the short arm of chromosome 1. Nature Genet. 5:
308-311, 1993. Note: Erratum: Nature Genet. 6: 214 only, 1994.
5. Mermelstein, F.; Yeung, K.; Cao, J.; Inostroza, J. A.; Erdjument-Bromage,
H.; Eagelson, K.; Landsman, D.; Levitt, P.; Tempst, P.; Reinberg,
D.: Requirement of a corepressor for Dr1-mediated repression of transcription. Genes
Dev. 10: 1033-1048, 1996.
6. Purello, M.; Di Pietro, C.; Rapisarda, A.; Viola, A.; Corsaro,
C.; Motta, S.; Grzeschik, K.-H.; Sichel, G.: Genomic localization
of the human gene encoding Dr1, a negative modulator of transcription
of class II and class III genes. Cytogenet. Cell Genet. 75: 186-189,
1996.
7. Rozet, J.-M.; Gerber, S.; Perrault, I.; Camuzat, A.; Calvas, P.;
Viegas-Pequignot, E.; Molina-Gomes, D.; Le Paslier, D.; Chumakov,
I.; Munnich, A.; Kaplan, J.: Structure and physical mapping of DR1,
a TATA-binding protein-associated phosphoprotein gene, to chromosome
1p22.1 and its exclusion in Stargardt disease (STGD). Genomics 36:
554-556, 1996.
8. Wang, Y.-L.; Faiola, F.; Xu, M.; Pan, S.; Martinez, E.: Human
ATAC is a GCN5/PCAF-containing acetylase complex with a novel NC2-like
histone fold module that interacts with the TATA-binding protein. J.
Biol. Chem. 283: 33808-33815, 2008.
9. Willy, P. J.; Kobayashi, R.; Kadonaga, J. T.: A basal transcription
factor that activates or represses transcription. Science 290: 982-984,
2000.
10. Yeung, K.; Kim, S.; Reinberg, D.: Functional dissection of a
human Dr1-DRAP1 repressor complex. Molec. Cell. Biol. 17: 36-45,
1997.
*FIELD* CN
Patricia A. Hartz - updated: 4/20/2010
Stylianos E. Antonarakis - updated: 8/2/2001
Ada Hamosh - updated: 11/16/2000
Jennifer P. Macke - updated: 5/1/1998
Patti M. Sherman - updated: 1/28/1998
Mark H. Paalman - updated: 10/25/1996
*FIELD* CD
Victor A. McKusick: 10/24/1996
*FIELD* ED
mgross: 01/29/2013
mgross: 1/11/2013
terry: 12/20/2012
mgross: 4/20/2010
terry: 4/20/2010
alopez: 4/13/2009
carol: 8/13/2001
mgross: 8/2/2001
mgross: 11/16/2000
terry: 4/29/1999
alopez: 5/1/1998
dholmes: 1/28/1998
mark: 10/25/1996
mark: 10/24/1996