NC2A_BOVIN
ID NC2A_BOVIN Reviewed; 205 AA.
AC Q2YDP3;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Dr1-associated corepressor;
DE AltName: Full=Dr1-associated protein 1;
DE AltName: Full=Negative cofactor 2-alpha;
DE Short=NC2-alpha;
GN Name=DRAP1 {ECO:0000250|UniProtKB:Q14919};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1] {ECO:0000312|EMBL:AAI10128.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus {ECO:0000312|EMBL:AAI10128.1};
RC TISSUE=Liver {ECO:0000312|EMBL:AAI10128.1};
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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|UniProtKB:Q14919}.
CC -!- SUBUNIT: Heterodimer with DR1. Binds BTAF1 (By similarity).
CC {ECO:0000250|UniProtKB:Q14919}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q14919}.
CC -!- PTM: Phosphorylation reduces DNA binding, but has no effect on
CC heterodimerization and TBP binding. {ECO:0000250|UniProtKB:Q14919}.
CC -!- SIMILARITY: Belongs to the NC2 alpha/DRAP1 family. {ECO:0000305}.
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DR EMBL; BC110127; AAI10128.1; -; mRNA.
DR RefSeq; NP_001069682.1; NM_001076214.1.
DR AlphaFoldDB; Q2YDP3; -.
DR SMR; Q2YDP3; -.
DR STRING; 9913.ENSBTAP00000008142; -.
DR PaxDb; Q2YDP3; -.
DR PRIDE; Q2YDP3; -.
DR Ensembl; ENSBTAT00000008142; ENSBTAP00000008142; ENSBTAG00000006199.
DR GeneID; 540345; -.
DR KEGG; bta:540345; -.
DR CTD; 10589; -.
DR VEuPathDB; HostDB:ENSBTAG00000006199; -.
DR VGNC; VGNC:28203; DRAP1.
DR eggNOG; KOG1659; Eukaryota.
DR GeneTree; ENSGT00390000012424; -.
DR HOGENOM; CLU_045277_10_0_1; -.
DR InParanoid; Q2YDP3; -.
DR OMA; QYMHMGN; -.
DR OrthoDB; 1504101at2759; -.
DR TreeFam; TF313964; -.
DR Proteomes; UP000009136; Chromosome 29.
DR Bgee; ENSBTAG00000006199; Expressed in tongue muscle and 106 other tissues.
DR ExpressionAtlas; Q2YDP3; baseline and differential.
DR GO; GO:0017054; C:negative cofactor 2 complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; 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:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IBA:GO_Central.
DR GO; GO:0001091; F:RNA polymerase II general transcription initiation factor binding; IEA:Ensembl.
DR GO; GO:0017025; F:TBP-class protein binding; IEA:Ensembl.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
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:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR003958; CBFA_NFYB_domain.
DR InterPro; IPR009072; Histone-fold.
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..205
FT /note="Dr1-associated corepressor"
FT /id="PRO_0000311697"
FT DOMAIN 14..77
FT /note="Histone-fold"
FT /evidence="ECO:0000255"
FT REGION 91..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..153
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..193
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 205 AA; 22324 MW; 2B65031FE42437B2 CRC64;
MPSKKKKYNA RFPPARIKKI MQTDEEIGKV AAAVPVIISR ALELFLESLL KKACQVTQSR
NAKTMTTSHL KQCIELEQQF DFLKDLVASV PDMQGDGEDN HMDGDKGPRR GRKSGSSGRK
NGGMGSKGKD KKLSGTDSEQ EDESEDTDSD GEEETPQVPP QASHPPAHFQ SPPTPFMPFT
STLPVPPAPP GASAPDAEEE EDYDS