ID   BANP_BOVIN              Reviewed;         503 AA.
AC   Q0VCW3;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Protein BANP;
GN   Name=BANP;
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Controls V(D)J recombination during T-cell development by
CC       repressing T-cell receptor (TCR) beta enhancer function. Binds to
CC       scaffold/matrix attachment region beta (S/MARbeta), an ATC-rich DNA
CC       sequence located upstream of the TCR beta enhancer. Represses cyclin D1
CC       transcription by recruiting HDAC1 to its promoter, thereby diminishing
CC       H3K9ac, H3S10ph and H4K8ac levels. Promotes TP53 activation, which
CC       causes cell cycle arrest (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:Q8VBU8}.
CC   -!- SUBUNIT: Interacts with TP53 (By similarity). Interacts with CUX1/CDP
CC       (By similarity). Interacts with HDAC1 (By similarity). Part of a
CC       corepressor complex containing BANP, HDAC1, SIN3A, SIN3B, RBL1 and RBL2
CC       (By similarity). {ECO:0000250|UniProtKB:Q8N9N5,
CC       ECO:0000250|UniProtKB:Q8VBU8}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the BANP/SMAR1 family. {ECO:0000305}.
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DR   EMBL; BC119967; AAI19968.1; -; mRNA.
DR   RefSeq; NP_001069088.1; NM_001075620.1.
DR   AlphaFoldDB; Q0VCW3; -.
DR   SMR; Q0VCW3; -.
DR   STRING; 9913.ENSBTAP00000032458; -.
DR   PRIDE; Q0VCW3; -.
DR   GeneID; 513446; -.
DR   KEGG; bta:513446; -.
DR   CTD; 54971; -.
DR   eggNOG; ENOG502QRIF; Eukaryota.
DR   InParanoid; Q0VCW3; -.
DR   OrthoDB; 1401911at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0042177; P:negative regulation of protein catabolic process; IBA:GO_Central.
DR   GO; GO:0034504; P:protein localization to nucleus; IBA:GO_Central.
DR   InterPro; IPR042343; BANP.
DR   InterPro; IPR018379; BEN_domain.
DR   PANTHER; PTHR16243; PTHR16243; 1.
DR   Pfam; PF10523; BEN; 1.
DR   SMART; SM01025; BEN; 1.
DR   PROSITE; PS51457; BEN; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cell cycle; Chromatin regulator; Coiled coil;
KW   Developmental protein; DNA-binding; Isopeptide bond; Nucleus;
KW   Phosphoprotein; Reference proteome; Repressor; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN           1..503
FT                   /note="Protein BANP"
FT                   /id="PRO_0000297909"
FT   DOMAIN          234..330
FT                   /note="BEN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00784"
FT   REGION          160..350
FT                   /note="Interaction with CUX1 and HDAC1"
FT                   /evidence="ECO:0000250"
FT   REGION          174..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          335..371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          350..399
FT                   /note="DNA-binding"
FT                   /evidence="ECO:0000250"
FT   COILED          65..98
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        189..203
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        335..363
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         19
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N9N5"
FT   MOD_RES         98
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N9N5"
FT   MOD_RES         108
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N9N5"
FT   MOD_RES         283
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VBU8"
FT   MOD_RES         347
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VBU8"
FT   CROSSLNK        141
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N9N5"
SQ   SEQUENCE   503 AA;  54820 MW;  3F3E7AB0E09316EA CRC64;
     MMSEQDLADV VQIAVEELSP GHPVVLENHV VTDEDEPALK RQRLEINCQD PSIKSFLYSI
     NQTICLRLDS IEAKLQALEA TCKSLEEKLD LVTNKQHSPI QVPMVAGSPL GATQTCNKVR
     CVVPQTTVIL NSDRQNAVVA KMEDPLSGRA PEPLENVISN AVPGRRQNTI VVKVPGQEDS
     HNEDGESGSE ASDSVSNCGQ SGSQNIGNNV TLITLNSEED YPNGTWLGDE NNPEMRVRCA
     IIPSDMLHIS TNCRTAEKMA LTLLDYLFHR EVQAVSNLSG QGKHGKKQLD PLTIYGIRCH
     LFYKFGITES DWYRIKQSID SKCRTAWRRK QRGQSLAVKS FSRRTPSSSS YGASETMMST
     PPPSSELQQP PPQALHYALA NAQQVQIHQI GEDGQVQVGH LHIAQVPQGE QVQITQDSEG
     NLQIHHVGQD GQVLQGAQLI AVASSDPAAT GVDGSPLQGS DIQVQYVQLA PVTDHTAAAQ
     AADALQPTLQ PEMQLEHGAI QIQ