NC2B_HUMAN
ID NC2B_HUMAN Reviewed; 176 AA.
AC Q01658;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 198.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 of
RT 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 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., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., 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., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., 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., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, AND INTERACTION WITH DRAP1.
RX PubMed=8670811; DOI=10.1002/j.1460-2075.1996.tb00673.x;
RA Goppelt A.R., Stelzer G., Lottspeich F., Meisterernst M.;
RT "A mechanism for repression of class II gene transcription through specific
RT binding of NC2 to TBP-promoter complexes via heterodimeric histone fold
RT 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 E4BP4
RT 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT 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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT 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., Buerckstuemmer T.,
RA 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., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105 AND SER-106, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.62 ANGSTROMS) IN COMPLEX WITH DRAP1; TBP AND 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 results
CC in a functional repression of both activated and basal transcription of
CC class II genes. This interaction precludes the formation of a
CC transcription-competent complex by inhibiting the association of TFIIA
CC and/or TFIIB with TBP. Can bind to DNA on its own. Component of the
CC ATAC complex, a complex with histone acetyltransferase activity on
CC histones H3 and H4. {ECO:0000269|PubMed:19103755,
CC ECO:0000269|PubMed:8670811}.
CC -!- SUBUNIT: Heterodimer with DRAP1. DR1 exists in solution as a
CC homotetramer that dissociates during interaction with TBP and then,
CC after complexing with TBP, reassociates at a slow rate, to reconstitute
CC the tetramer. Interacts with NFIL3. Component of the ADA2A-containing
CC complex (ATAC), composed of KAT14, KAT2A, TADA2L, TADA3L, ZZ3, MBIP,
CC WDR5, YEATS2, CCDC101 and DR1. {ECO:0000269|PubMed:11461703,
CC ECO:0000269|PubMed:19103755, ECO:0000269|PubMed:8670811,
CC ECO:0000269|PubMed:8836190}.
CC -!- INTERACTION:
CC Q01658; P13928: ANXA8; NbExp=3; IntAct=EBI-750300, EBI-2556915;
CC Q01658; P05067: APP; NbExp=3; IntAct=EBI-750300, EBI-77613;
CC Q01658; Q6XD76: ASCL4; NbExp=3; IntAct=EBI-750300, EBI-10254793;
CC Q01658; Q9H7T9: AUNIP; NbExp=3; IntAct=EBI-750300, EBI-10693257;
CC Q01658; P46379-2: BAG6; NbExp=3; IntAct=EBI-750300, EBI-10988864;
CC Q01658; Q8TBE0: BAHD1; NbExp=3; IntAct=EBI-750300, EBI-742750;
CC Q01658; Q9H972-2: C14orf93; NbExp=3; IntAct=EBI-750300, EBI-11524174;
CC Q01658; Q96LL4: C8orf48; NbExp=3; IntAct=EBI-750300, EBI-751596;
CC Q01658; Q13191: CBLB; NbExp=3; IntAct=EBI-750300, EBI-744027;
CC Q01658; Q494V2-2: CFAP100; NbExp=3; IntAct=EBI-750300, EBI-11953200;
CC Q01658; P48730-2: CSNK1D; NbExp=3; IntAct=EBI-750300, EBI-9087876;
CC Q01658; Q5TAQ9-2: DCAF8; NbExp=3; IntAct=EBI-750300, EBI-25842815;
CC Q01658; Q92782-2: DPF1; NbExp=3; IntAct=EBI-750300, EBI-23669343;
CC Q01658; Q86TI2-2: DPP9; NbExp=3; IntAct=EBI-750300, EBI-21529239;
CC Q01658; Q14919: DRAP1; NbExp=32; IntAct=EBI-750300, EBI-712941;
CC Q01658; Q9Y6C2-2: EMILIN1; NbExp=3; IntAct=EBI-750300, EBI-11748557;
CC Q01658; Q6P1L5: FAM117B; NbExp=3; IntAct=EBI-750300, EBI-3893327;
CC Q01658; Q17RN3: FAM98C; NbExp=3; IntAct=EBI-750300, EBI-5461838;
CC Q01658; Q8IZU1: FAM9A; NbExp=3; IntAct=EBI-750300, EBI-8468186;
CC Q01658; Q96IJ6: GMPPA; NbExp=3; IntAct=EBI-750300, EBI-750953;
CC Q01658; Q9HBQ8: GOLGA2P5; NbExp=3; IntAct=EBI-750300, EBI-22000587;
CC Q01658; Q9Y4H4: GPSM3; NbExp=3; IntAct=EBI-750300, EBI-347538;
CC Q01658; Q6NXT2: H3-5; NbExp=3; IntAct=EBI-750300, EBI-2868501;
CC Q01658; Q9HCC6: HES4; NbExp=3; IntAct=EBI-750300, EBI-2680288;
CC Q01658; Q13123: IK; NbExp=3; IntAct=EBI-750300, EBI-713456;
CC Q01658; Q92613: JADE3; NbExp=3; IntAct=EBI-750300, EBI-10278909;
CC Q01658; Q9UIH9: KLF15; NbExp=3; IntAct=EBI-750300, EBI-2796400;
CC Q01658; Q92615: LARP4B; NbExp=3; IntAct=EBI-750300, EBI-1052558;
CC Q01658; A2RU56: LOC401296; NbExp=3; IntAct=EBI-750300, EBI-9088215;
CC Q01658; Q14693: LPIN1; NbExp=3; IntAct=EBI-750300, EBI-5278370;
CC Q01658; Q8TD91-2: MAGEC3; NbExp=3; IntAct=EBI-750300, EBI-10694180;
CC Q01658; Q9H000: MKRN2; NbExp=3; IntAct=EBI-750300, EBI-2341005;
CC Q01658; Q15049: MLC1; NbExp=3; IntAct=EBI-750300, EBI-8475277;
CC Q01658; O95563: MPC2; NbExp=3; IntAct=EBI-750300, EBI-719403;
CC Q01658; P01106: MYC; NbExp=3; IntAct=EBI-750300, EBI-447544;
CC Q01658; Q13952-2: NFYC; NbExp=3; IntAct=EBI-750300, EBI-11956831;
CC Q01658; O15381-5: NVL; NbExp=3; IntAct=EBI-750300, EBI-18577082;
CC Q01658; Q9BYU1: PBX4; NbExp=3; IntAct=EBI-750300, EBI-10302990;
CC Q01658; Q5T6S3: PHF19; NbExp=3; IntAct=EBI-750300, EBI-2339674;
CC Q01658; Q9NRF9: POLE3; NbExp=7; IntAct=EBI-750300, EBI-744901;
CC Q01658; P19388: POLR2E; NbExp=3; IntAct=EBI-750300, EBI-395189;
CC Q01658; Q99873-2: PRMT1; NbExp=3; IntAct=EBI-750300, EBI-16399024;
CC Q01658; Q9Y5P3: RAI2; NbExp=3; IntAct=EBI-750300, EBI-746228;
CC Q01658; Q96D59: RNF183; NbExp=3; IntAct=EBI-750300, EBI-743938;
CC Q01658; Q969K3: RNF34; NbExp=3; IntAct=EBI-750300, EBI-2340642;
CC Q01658; Q9BUL9: RPP25; NbExp=3; IntAct=EBI-750300, EBI-366570;
CC Q01658; P62701: RPS4X; NbExp=3; IntAct=EBI-750300, EBI-354303;
CC Q01658; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-750300, EBI-6257312;
CC Q01658; Q8N488: RYBP; NbExp=3; IntAct=EBI-750300, EBI-752324;
CC Q01658; O75446: SAP30; NbExp=3; IntAct=EBI-750300, EBI-632609;
CC Q01658; P60896: SEM1; NbExp=3; IntAct=EBI-750300, EBI-79819;
CC Q01658; Q8NHS9: SPATA22; NbExp=3; IntAct=EBI-750300, EBI-7067260;
CC Q01658; Q8TCT7-2: SPPL2B; NbExp=3; IntAct=EBI-750300, EBI-8345366;
CC Q01658; Q9NRL3: STRN4; NbExp=3; IntAct=EBI-750300, EBI-717245;
CC Q01658; O60506-4: SYNCRIP; NbExp=3; IntAct=EBI-750300, EBI-11123832;
CC Q01658; Q9BSH4: TACO1; NbExp=3; IntAct=EBI-750300, EBI-747797;
CC Q01658; Q32MN6: TBP; NbExp=3; IntAct=EBI-750300, EBI-10239991;
CC Q01658; Q9P2T0: THEG; NbExp=3; IntAct=EBI-750300, EBI-751020;
CC Q01658; O43615: TIMM44; NbExp=3; IntAct=EBI-750300, EBI-861737;
CC Q01658; O75604-3: USP2; NbExp=3; IntAct=EBI-750300, EBI-10696113;
CC Q01658; P40337-2: VHL; NbExp=3; IntAct=EBI-750300, EBI-12157263;
CC Q01658; P58304: VSX2; NbExp=3; IntAct=EBI-750300, EBI-6427899;
CC Q01658; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-750300, EBI-14104088;
CC Q01658; Q9P2Y4: ZNF219; NbExp=3; IntAct=EBI-750300, EBI-3937106;
CC Q01658; Q96MN9-2: ZNF488; NbExp=3; IntAct=EBI-750300, EBI-25831733;
CC Q01658; Q9P0T4: ZNF581; NbExp=3; IntAct=EBI-750300, EBI-745520;
CC Q01658; Q3KNS6-3: ZNF829; NbExp=3; IntAct=EBI-750300, EBI-18036029;
CC Q01658; Q8NBB4-2: ZSCAN1; NbExp=3; IntAct=EBI-750300, EBI-12021938;
CC Q01658; P10073: ZSCAN22; NbExp=3; IntAct=EBI-750300, EBI-10178224;
CC Q01658; A0A384ME25; NbExp=3; IntAct=EBI-750300, EBI-10211777;
CC Q01658; Q9H669; NbExp=3; IntAct=EBI-750300, EBI-10307430;
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. {ECO:0000305}.
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DR EMBL; M97388; AAA58442.1; -; mRNA.
DR EMBL; BT006972; AAP35618.1; -; mRNA.
DR EMBL; AL137159; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002809; AAH02809.1; -; mRNA.
DR EMBL; BC035507; AAH35507.1; -; mRNA.
DR EMBL; BC068553; AAH68553.1; -; mRNA.
DR CCDS; CCDS744.1; -.
DR PIR; A43320; A43320.
DR RefSeq; NP_001929.1; NM_001938.2.
DR PDB; 1JFI; X-ray; 2.62 A; B=1-176.
DR PDBsum; 1JFI; -.
DR AlphaFoldDB; Q01658; -.
DR SMR; Q01658; -.
DR BioGRID; 108144; 68.
DR ComplexPortal; CPX-1004; PCAF-containing ATAC complex.
DR ComplexPortal; CPX-997; GCN5-containing ATAC complex.
DR CORUM; Q01658; -.
DR IntAct; Q01658; 84.
DR MINT; Q01658; -.
DR STRING; 9606.ENSP00000359295; -.
DR GlyGen; Q01658; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q01658; -.
DR PhosphoSitePlus; Q01658; -.
DR BioMuta; DR1; -.
DR DMDM; 401162; -.
DR EPD; Q01658; -.
DR jPOST; Q01658; -.
DR MassIVE; Q01658; -.
DR PaxDb; Q01658; -.
DR PeptideAtlas; Q01658; -.
DR PRIDE; Q01658; -.
DR ProteomicsDB; 57979; -.
DR Antibodypedia; 19942; 207 antibodies from 31 providers.
DR DNASU; 1810; -.
DR Ensembl; ENST00000370267.1; ENSP00000359290.1; ENSG00000117505.13.
DR Ensembl; ENST00000370272.9; ENSP00000359295.3; ENSG00000117505.13.
DR GeneID; 1810; -.
DR KEGG; hsa:1810; -.
DR MANE-Select; ENST00000370272.9; ENSP00000359295.3; NM_001938.3; NP_001929.1.
DR CTD; 1810; -.
DR DisGeNET; 1810; -.
DR GeneCards; DR1; -.
DR HGNC; HGNC:3017; DR1.
DR HPA; ENSG00000117505; Low tissue specificity.
DR MIM; 601482; gene.
DR neXtProt; NX_Q01658; -.
DR OpenTargets; ENSG00000117505; -.
DR PharmGKB; PA27475; -.
DR VEuPathDB; HostDB:ENSG00000117505; -.
DR eggNOG; KOG0871; Eukaryota.
DR GeneTree; ENSGT00550000075010; -.
DR HOGENOM; CLU_066247_11_1_1; -.
DR InParanoid; Q01658; -.
DR OMA; KTIAPDH; -.
DR OrthoDB; 1465912at2759; -.
DR PhylomeDB; Q01658; -.
DR TreeFam; TF317588; -.
DR PathwayCommons; Q01658; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR SignaLink; Q01658; -.
DR SIGNOR; Q01658; -.
DR BioGRID-ORCS; 1810; 573 hits in 1105 CRISPR screens.
DR ChiTaRS; DR1; human.
DR EvolutionaryTrace; Q01658; -.
DR GeneWiki; DR1_(gene); -.
DR GenomeRNAi; 1810; -.
DR Pharos; Q01658; Tbio.
DR PRO; PR:Q01658; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q01658; protein.
DR Bgee; ENSG00000117505; Expressed in choroid plexus epithelium and 216 other tissues.
DR ExpressionAtlas; Q01658; baseline and differential.
DR Genevisible; Q01658; HS.
DR GO; GO:0140672; C:ATAC complex; IDA:BHF-UCL.
DR GO; GO:0072686; C:mitotic spindle; IC:ComplexPortal.
DR GO; GO:0017054; C:negative cofactor 2 complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:ARUK-UCL.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IDA:ARUK-UCL.
DR GO; GO:0017025; F:TBP-class protein binding; IDA:BHF-UCL.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:BHF-UCL.
DR GO; GO:0044154; P:histone H3-K14 acetylation; IDA:ComplexPortal.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:ARUK-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:ComplexPortal.
DR GO; GO:0051302; P:regulation of cell division; IDA:ComplexPortal.
DR GO; GO:0045995; P:regulation of embryonic development; IC:ComplexPortal.
DR GO; GO:0031063; P:regulation of histone deacetylation; IMP:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:ComplexPortal.
DR GO; GO:0090043; P:regulation of tubulin deacetylation; IMP:ComplexPortal.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IBA:GO_Central.
DR Gene3D; 1.10.20.10; -; 1.
DR IDEAL; IID00206; -.
DR InterPro; IPR003958; CBFA_NFYB_domain.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR042225; Ncb2.
DR PANTHER; PTHR46138; PTHR46138; 1.
DR Pfam; PF00808; CBFD_NFYB_HMF; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..176
FT /note="Protein Dr1"
FT /id="PRO_0000072440"
FT DOMAIN 12..75
FT /note="Histone-fold"
FT /evidence="ECO:0000255"
FT REGION 152..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 100..103
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 152..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VARIANT 171
FT /note="E -> D (in dbSNP:rs3088371)"
FT /id="VAR_034506"
FT HELIX 15..25
FT /evidence="ECO:0007829|PDB:1JFI"
FT HELIX 33..60
FT /evidence="ECO:0007829|PDB:1JFI"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:1JFI"
FT HELIX 68..78
FT /evidence="ECO:0007829|PDB:1JFI"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:1JFI"
FT HELIX 84..110
FT /evidence="ECO:0007829|PDB:1JFI"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:1JFI"
FT HELIX 115..140
FT /evidence="ECO:0007829|PDB:1JFI"
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
