ID   NFYB_HORSE              Reviewed;         207 AA.
AC   Q6RG77;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Nuclear transcription factor Y subunit beta;
DE   AltName: Full=CAAT box DNA-binding protein subunit B;
DE   AltName: Full=Nuclear transcription factor Y subunit B;
DE            Short=NF-YB;
GN   Name=NFYB;
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Takafuji V.A., Woody S.L., Crisman M.V., Howard R.D.;
RT   "Equus caballus nuclear transcription factor-Y beta (NFYb) mRNA.";
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the sequence-specific heterotrimeric
CC       transcription factor (NF-Y) which specifically recognizes a 5'-CCAAT-3'
CC       box motif found in the promoters of its target genes. NF-Y can function
CC       as both an activator and a repressor, depending on its interacting
CC       cofactors (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterotrimeric transcription factor composed of three
CC       components, NF-YA, NF-YB and NF-YC. NF-YB and NF-YC must interact and
CC       dimerize for NF-YA association and DNA binding. Interacts with C1QBP
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- DOMAIN: Can be divided into 3 domains: the weakly conserved A domain,
CC       the highly conserved B domain thought to be involved in subunit
CC       interaction and DNA binding, and the Glu-rich C domain.
CC   -!- PTM: Monoubiquitination at Lys-140 plays an important role in
CC       transcriptional activation by allowing the deposition of histone H3
CC       methylations as well as histone H2B monoubiquitination at 'Lys-121'.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the NFYB/HAP3 subunit family. {ECO:0000305}.
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DR   EMBL; AY499345; AAR91751.1; -; mRNA.
DR   AlphaFoldDB; Q6RG77; -.
DR   SMR; Q6RG77; -.
DR   STRING; 9796.ENSECAP00000007041; -.
DR   PaxDb; Q6RG77; -.
DR   InParanoid; Q6RG77; -.
DR   Proteomes; UP000002281; Unplaced.
DR   GO; GO:0016602; C:CCAAT-binding factor complex; IBA:GO_Central.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0006357; P:regulation of 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   InterPro; IPR027113; Transc_fact_NFYB/HAP3.
DR   InterPro; IPR003956; Transcrpt_fac_NFYB/HAP3_CS.
DR   PANTHER; PTHR11064; PTHR11064; 1.
DR   Pfam; PF00808; CBFD_NFYB_HMF; 1.
DR   SUPFAM; SSF47113; SSF47113; 1.
DR   PROSITE; PS00685; NFYB_HAP3; 1.
PE   2: Evidence at transcript level;
KW   Activator; DNA-binding; Isopeptide bond; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation; Ubl conjugation.
FT   CHAIN           1..207
FT                   /note="Nuclear transcription factor Y subunit beta"
FT                   /id="PRO_0000204608"
FT   DNA_BIND        59..65
FT                   /evidence="ECO:0000250"
FT   REGION          1..52
FT                   /note="A domain"
FT   REGION          27..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          53..142
FT                   /note="B domain"
FT   REGION          86..97
FT                   /note="Subunit association domain (SAD)"
FT                   /evidence="ECO:0000250"
FT   REGION          143..207
FT                   /note="C domain"
FT   COMPBIAS        30..51
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        140
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P25208"
SQ   SEQUENCE   207 AA;  22780 MW;  1ACEB4AA363CF972 CRC64;
     MTMDGDSSTT DASQLGISAD YIGGSHYVIQ PHDDTEDSMN DHEDTNGSKE SFREQDIYLP
     IANVARIMKN AIPQTGKIAK DAKECVQECV SEFISFITSE ASERCHQEKR KTINGEDILF
     AMSTLGFDSY VEPLKLYLQK FREAMKGEKG IGGAVTATDG LSEELAEEAF TNQLPAGLIT
     ADGQQQNVMV YTTSYHQISG VQQIQFS