ID A0A384DA31_URSMA Unreviewed; 207 AA.
AC A0A384DA31;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Nuclear transcription factor Y subunit beta {ECO:0000256|ARBA:ARBA00015277};
DE AltName: Full=CAAT box DNA-binding protein subunit B {ECO:0000256|ARBA:ARBA00029965};
DE AltName: Full=Nuclear transcription factor Y subunit B {ECO:0000256|ARBA:ARBA00031126};
GN Name=NFYB {ECO:0000313|Ensembl:ENSUMAP00000025694,
GN ECO:0000313|RefSeq:XP_008703897.1, ECO:0000313|RefSeq:XP_008703898.1,
GN ECO:0000313|RefSeq:XP_040493329.1};
OS Ursus maritimus (Polar bear) (Thalarctos maritimus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=29073 {ECO:0000313|Proteomes:UP000261680, ECO:0000313|RefSeq:XP_008703897.1};
RN [1] {ECO:0000313|Ensembl:ENSUMAP00000025694}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_008703897.1, ECO:0000313|RefSeq:XP_008703898.1}
RP IDENTIFICATION.
RC TISSUE=Whole blood {ECO:0000313|RefSeq:XP_008703897.1,
RC ECO:0000313|RefSeq:XP_008703898.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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. {ECO:0000256|ARBA:ARBA00025263}.
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 {ECO:0000256|ARBA:ARBA00025891}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the NFYB/HAP3 subunit family.
CC {ECO:0000256|ARBA:ARBA00009053}.
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DR RefSeq; XP_008703897.1; XM_008705675.2.
DR RefSeq; XP_008703898.1; XM_008705676.2.
DR RefSeq; XP_040493329.1; XM_040637395.1.
DR STRING; 29073.ENSUMAP00000025694; -.
DR Ensembl; ENSUMAT00000030432.1; ENSUMAP00000025694.1; ENSUMAG00000018728.1.
DR GeneID; 103676483; -.
DR KEGG; umr:103676483; -.
DR CTD; 4801; -.
DR OMA; GVQPIQF; -.
DR OrthoDB; 24067at2759; -.
DR Proteomes; UP000261680; Unplaced.
DR GO; GO:0016602; C:CCAAT-binding factor complex; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0032993; C:protein-DNA complex; IEA:Ensembl.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0035065; P:regulation of histone acetylation; IEA:Ensembl.
DR Gene3D; 1.10.20.10; Histone, subunit A; 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; CCAAT-BINDING TRANSCRIPTION FACTOR-RELATED; 1.
DR PANTHER; PTHR11064:SF9; NUCLEAR TRANSCRIPTION FACTOR Y SUBUNIT BETA; 1.
DR Pfam; PF00808; CBFD_NFYB_HMF; 1.
DR PRINTS; PR00615; CCAATSUBUNTA.
DR SUPFAM; SSF47113; Histone-fold; 1.
DR PROSITE; PS00685; NFYB_HAP3; 1.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Reference proteome {ECO:0000313|Proteomes:UP000261680};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 58..122
FT /note="Transcription factor CBF/NF-Y/archaeal histone"
FT /evidence="ECO:0000259|Pfam:PF00808"
FT REGION 27..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 207 AA; 22815 MW; E2F8715C371C5FA6 CRC64;
MTMDGDSATT DASQLGISAD YIGGSHYVIQ PHDDTEDSMN DHEDTNGSKE SFREQDIYLP
IANVARIMKN AIPQTGKIAK DAKECVQECV SEFISFITSE ASERCHQEKR KTINGEDILF
AMSTLGFDSY VEPLKLYLQK FREAMKGEKG IGGTVTATDG LSEELTEEAF TNQLPAGLIT
ADGQQQNVMV YTTSYQQISG VQQIQFS
//
