NC2B_CHICK
ID NC2B_CHICK Reviewed; 176 AA.
AC Q5ZMV3;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
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; ORFNames=RCJMB04_1b9;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer with DRAP1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NC2 beta/DR1 family. {ECO:0000305}.
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DR EMBL; AJ719281; CAG30940.1; -; mRNA.
DR RefSeq; NP_001008478.1; NM_001008478.1.
DR AlphaFoldDB; Q5ZMV3; -.
DR SMR; Q5ZMV3; -.
DR STRING; 9031.ENSGALP00000009403; -.
DR PaxDb; Q5ZMV3; -.
DR Ensembl; ENSGALT00000009417; ENSGALP00000009403; ENSGALG00000005858.
DR GeneID; 424496; -.
DR KEGG; gga:424496; -.
DR CTD; 1810; -.
DR VEuPathDB; HostDB:geneid_424496; -.
DR eggNOG; KOG0871; Eukaryota.
DR GeneTree; ENSGT00550000075010; -.
DR HOGENOM; CLU_066247_11_1_1; -.
DR InParanoid; Q5ZMV3; -.
DR OMA; KTIAPDH; -.
DR OrthoDB; 1465912at2759; -.
DR PhylomeDB; Q5ZMV3; -.
DR TreeFam; TF317588; -.
DR PRO; PR:Q5ZMV3; -.
DR Proteomes; UP000000539; Chromosome 8.
DR Bgee; ENSGALG00000005858; Expressed in spermatid and 13 other tissues.
DR GO; GO:0140672; C:ATAC complex; IEA:Ensembl.
DR GO; GO:0017054; C:negative cofactor 2 complex; IBA:GO_Central.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0017025; F:TBP-class protein binding; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0044154; P:histone H3-K14 acetylation; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
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; IEA:Ensembl.
DR GO; GO:0051302; P:regulation of cell division; IEA:Ensembl.
DR GO; GO:0045995; P:regulation of embryonic development; IEA:Ensembl.
DR GO; GO:0031063; P:regulation of histone deacetylation; IEA:Ensembl.
DR GO; GO:0090043; P:regulation of tubulin deacetylation; IEA:Ensembl.
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 DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..176
FT /note="Protein Dr1"
FT /id="PRO_0000072439"
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"
SQ SEQUENCE 176 AA; 19444 MW; 36E7E59E9FD77AB5 CRC64;
MASSSGNDDD LTIPRAAINK MIKETLPNVR VANDARELVV NCCTEFIHLI SSEANEICNK
SEKKTISPEH VIQALESLGF GSYISEVKEV LQECKTVALK RRKASSRLEN LGIPEEELLR
QQQELFAKAR QQQAELAQQE WLQMQQAAQQ AQLAAASASA SNQAGSSQDE DDEDDI
