NC2B_MOUSE
ID NC2B_MOUSE Reviewed; 176 AA.
AC Q91WV0; Q3UT14;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
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 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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Egg, Kidney, Liver, Thymus, and Urinary bladder;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- PTM: Phosphorylation regulates its interaction with TBP. Not
CC phosphorylated when bound to DRAP1 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NC2 beta/DR1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK031057; BAE20474.1; -; mRNA.
DR EMBL; AK075713; BAC35903.1; -; mRNA.
DR EMBL; AK090113; BAC41099.1; -; mRNA.
DR EMBL; AK139866; BAE24166.1; -; mRNA.
DR EMBL; AK146573; BAE27269.1; -; mRNA.
DR EMBL; BC013461; AAH13461.1; -; mRNA.
DR CCDS; CCDS19509.1; -.
DR RefSeq; NP_080382.2; NM_026106.4.
DR AlphaFoldDB; Q91WV0; -.
DR SMR; Q91WV0; -.
DR BioGRID; 199303; 5.
DR ComplexPortal; CPX-1025; GCN5-containing ATAC complex.
DR ComplexPortal; CPX-1029; PCAF-containing ATAC complex.
DR IntAct; Q91WV0; 2.
DR MINT; Q91WV0; -.
DR STRING; 10090.ENSMUSP00000031190; -.
DR iPTMnet; Q91WV0; -.
DR PhosphoSitePlus; Q91WV0; -.
DR EPD; Q91WV0; -.
DR jPOST; Q91WV0; -.
DR MaxQB; Q91WV0; -.
DR PaxDb; Q91WV0; -.
DR PRIDE; Q91WV0; -.
DR ProteomicsDB; 287352; -.
DR Antibodypedia; 19942; 207 antibodies from 31 providers.
DR DNASU; 13486; -.
DR Ensembl; ENSMUST00000031190; ENSMUSP00000031190; ENSMUSG00000029265.
DR GeneID; 13486; -.
DR KEGG; mmu:13486; -.
DR UCSC; uc008ynt.1; mouse.
DR CTD; 1810; -.
DR MGI; MGI:1100515; Dr1.
DR VEuPathDB; HostDB:ENSMUSG00000029265; -.
DR eggNOG; KOG0871; Eukaryota.
DR GeneTree; ENSGT00550000075010; -.
DR HOGENOM; CLU_066247_11_1_1; -.
DR InParanoid; Q91WV0; -.
DR OMA; KTIAPDH; -.
DR OrthoDB; 1465912at2759; -.
DR PhylomeDB; Q91WV0; -.
DR TreeFam; TF317588; -.
DR BioGRID-ORCS; 13486; 21 hits in 76 CRISPR screens.
DR PRO; PR:Q91WV0; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q91WV0; protein.
DR Bgee; ENSMUSG00000029265; Expressed in spermatocyte and 273 other tissues.
DR Genevisible; Q91WV0; MM.
DR GO; GO:0140672; C:ATAC complex; IDA:ComplexPortal.
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; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0017025; F:TBP-class protein binding; ISO:MGI.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0043966; P:histone H3 acetylation; ISO:MGI.
DR GO; GO:0044154; P:histone H3-K14 acetylation; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
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; IDA:ComplexPortal.
DR GO; GO:0031063; P:regulation of histone deacetylation; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0090043; P:regulation of tubulin deacetylation; ISO:MGI.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IBA:GO_Central.
DR Gene3D; 1.10.20.10; -; 1.
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 Acetylation; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q01658"
FT CHAIN 2..176
FT /note="Protein Dr1"
FT /id="PRO_0000072441"
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:0000250|UniProtKB:Q01658"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01658"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01658"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01658"
SQ SEQUENCE 176 AA; 19431 MW; 36E7E59F2FD6D647 CRC64;
MASSSGNDDD LTIPRAAINK MIKETLPNVR VANDARELVV NCCTEFIHLI SSEANEICNK
SEKKTISPEH VIQALESLGF GSYISEVKEV LQECKTVALK RRKASSRLEN LGIPEEELLR
QQQELFAKAR QQQAELAQQE WLQMQQAAQQ AQLAAASASA STQAGSSQDE EDDDDI
