NFYB_RAT
ID NFYB_RAT Reviewed; 207 AA.
AC P63140; P22569; Q5FVT0;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Nuclear transcription factor Y subunit beta;
DE AltName: Full=CAAT box DNA-binding protein subunit B;
DE AltName: Full=CCAAT-binding transcription factor subunit B;
DE Short=CBF-B;
DE AltName: Full=Nuclear transcription factor Y subunit B;
DE Short=NF-YB;
GN Name=Nfyb;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 78-97; 82-103; 136-140
RP AND 141-150.
RX PubMed=2266139; DOI=10.1016/s0021-9258(18)45730-4;
RA Vuorio T., Maity S.N., de Crombrugghe B.;
RT "Purification and molecular cloning of the 'A' chain of a rat heteromeric
RT CCAAT-binding protein. Sequence identity with the yeast HAP3 transcription
RT factor.";
RL J. Biol. Chem. 265:22480-22486(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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.
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.
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; M55045; AAA40887.1; -; mRNA.
DR EMBL; BC089791; AAH89791.1; -; mRNA.
DR PIR; A23692; A23692.
DR RefSeq; NP_113741.1; NM_031553.2.
DR RefSeq; XP_006241258.1; XM_006241196.3.
DR AlphaFoldDB; P63140; -.
DR SMR; P63140; -.
DR DIP; DIP-2660N; -.
DR STRING; 10116.ENSRNOP00000061405; -.
DR PaxDb; P63140; -.
DR PRIDE; P63140; -.
DR Ensembl; ENSRNOT00000066143; ENSRNOP00000061405; ENSRNOG00000010309.
DR GeneID; 25336; -.
DR KEGG; rno:25336; -.
DR UCSC; RGD:3172; rat.
DR CTD; 4801; -.
DR RGD; 3172; Nfyb.
DR eggNOG; KOG0869; Eukaryota.
DR GeneTree; ENSGT00940000154917; -.
DR HOGENOM; CLU_066247_9_2_1; -.
DR InParanoid; P63140; -.
DR OMA; PRWDWFL; -.
DR PhylomeDB; P63140; -.
DR TreeFam; TF314521; -.
DR PRO; PR:P63140; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000010309; Expressed in thymus and 19 other tissues.
DR ExpressionAtlas; P63140; baseline and differential.
DR Genevisible; P63140; RN.
DR GO; GO:0016602; C:CCAAT-binding factor complex; IDA:RGD.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0032993; C:protein-DNA complex; ISO:RGD.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:RGD.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; ISO:RGD.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0035065; P:regulation of histone acetylation; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IC:RGD.
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 1: Evidence at protein level;
KW Activator; Direct protein sequencing; DNA-binding; Isopeptide bond;
KW Nucleus; Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..207
FT /note="Nuclear transcription factor Y subunit beta"
FT /id="PRO_0000204611"
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; 22787 MW; 1ADFB4B04A3CFC22 CRC64;
MTMDGDSSTT DASQLGISAD YIGGSHYVIQ PHDDTEDSMN DHEDTNGSKE SFREQDIYLP
IANVARIMKN AIPQTGKIAK DAKECVQECV SEFISFITSE ASERCHQEKR KTINGEDILF
AMSTLGFDSY VEPLKLYLQK FREAMKGEKG IGGAVSATDG LSEELTEEAF TNQLPAGLIT
ADGQQQNVMV YTTSYQQISG VQQIQFS
