NC2B_RAT
ID NC2B_RAT Reviewed; 176 AA.
AC Q5XI68;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 122.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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).
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. Component of the ADA2A-containing complex (ATAC),
CC composed of KAT14, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2,
CC 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; BC083822; AAH83822.1; -; mRNA.
DR RefSeq; NP_001011914.1; NM_001011914.1.
DR RefSeq; XP_003751365.1; XM_003751317.4.
DR RefSeq; XP_017460226.1; XM_017604737.1.
DR AlphaFoldDB; Q5XI68; -.
DR SMR; Q5XI68; -.
DR STRING; 10116.ENSRNOP00000000080; -.
DR iPTMnet; Q5XI68; -.
DR PhosphoSitePlus; Q5XI68; -.
DR jPOST; Q5XI68; -.
DR PaxDb; Q5XI68; -.
DR PRIDE; Q5XI68; -.
DR GeneID; 289881; -.
DR KEGG; rno:289881; -.
DR UCSC; RGD:1305201; rat.
DR CTD; 1810; -.
DR RGD; 1305201; Dr1.
DR VEuPathDB; HostDB:ENSRNOG00000000070; -.
DR eggNOG; KOG0871; Eukaryota.
DR HOGENOM; CLU_066247_11_1_1; -.
DR InParanoid; Q5XI68; -.
DR OMA; KTIAPDH; -.
DR OrthoDB; 1465912at2759; -.
DR PhylomeDB; Q5XI68; -.
DR TreeFam; TF317588; -.
DR PRO; PR:Q5XI68; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000000070; Expressed in thymus and 18 other tissues.
DR Genevisible; Q5XI68; RN.
DR GO; GO:0140672; C:ATAC complex; ISO:RGD.
DR GO; GO:0017054; C:negative cofactor 2 complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD.
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:RGD.
DR GO; GO:0017025; F:TBP-class protein binding; ISO:RGD.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0043966; P:histone H3 acetylation; ISO:RGD.
DR GO; GO:0044154; P:histone H3-K14 acetylation; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0051302; P:regulation of cell division; ISO:RGD.
DR GO; GO:0045995; P:regulation of embryonic development; ISO:RGD.
DR GO; GO:0031063; P:regulation of histone deacetylation; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0090043; P:regulation of tubulin deacetylation; ISO:RGD.
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 2: Evidence at transcript 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_0000072442"
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:0000250|UniProtKB:Q01658"
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; 19430 MW; 36E7E59F2FD77AB5 CRC64;
MASSSGNDDD LTIPRAAINK MIKETLPNVR VANDARELVV NCCTEFIHLI SSEANEICNK
SEKKTISPEH VIQALESLGF GSYISEVKEV LQECKTVALK RRKASSRLEN LGIPEEELLR
QQQELFAKAR QQQAELAQQE WLQMQQAAQQ AQLAAASASA SNQAGSSQDE DDDDDI
