NFYB_MOUSE
ID NFYB_MOUSE Reviewed; 207 AA.
AC P63139; P22569; Q3UK54;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 143.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 51-69; 137-140 AND
RP 194-206.
RX PubMed=1698608;
RA Hooft van Huijsduijnen R., Li X.-Y., Black D., Matthes H., Benoist C.,
RA Mathis D.;
RT "Co-evolution from yeast to mouse: cDNA cloning of the two NF-Y (CP-1/CBF)
RT subunits.";
RL EMBO J. 9:3119-3127(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1549471; DOI=10.1093/nar/20.5.1087;
RA Li X.-Y., Mantovani R., Hooft van Huijsduijnen R., Andre I., Benoist C.,
RA Mathis D.;
RT "Evolutionary variation of the CCAAT-binding transcription factor NF-Y.";
RL Nucleic Acids Res. 20:1087-1091(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RX PubMed=1577736; DOI=10.1016/s0021-9258(19)50377-5;
RA Li X.-Y., Hooft van Huijsduijnen R., Mantovani R., Benoist C.O., Mathis D.;
RT "Intron-exon organization of the NF-Y genes. Tissue-specific splicing
RT modifies an activation domain.";
RL J. Biol. Chem. 267:8984-8990(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, and C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=3 isoforms may be produced.;
CC Name=1;
CC IsoId=P63139-1, P22569-1;
CC Sequence=Displayed;
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; X55316; CAA39024.1; -; mRNA.
DR EMBL; AK010762; BAB27166.1; -; mRNA.
DR EMBL; AK146168; BAE26948.1; -; mRNA.
DR EMBL; BC010719; AAH10719.1; -; mRNA.
DR CCDS; CCDS48654.1; -.
DR PIR; F38245; F38245.
DR RefSeq; NP_035044.1; NM_010914.2. [P63139-1]
DR RefSeq; XP_011241681.1; XM_011243379.2. [P63139-1]
DR AlphaFoldDB; P63139; -.
DR SMR; P63139; -.
DR BioGRID; 201761; 8.
DR ComplexPortal; CPX-89; CCAAT-binding factor complex.
DR STRING; 10090.ENSMUSP00000122403; -.
DR PhosphoSitePlus; P63139; -.
DR EPD; P63139; -.
DR MaxQB; P63139; -.
DR PaxDb; P63139; -.
DR PRIDE; P63139; -.
DR ProteomicsDB; 252887; -.
DR Antibodypedia; 3780; 278 antibodies from 32 providers.
DR DNASU; 18045; -.
DR Ensembl; ENSMUST00000130911; ENSMUSP00000122403; ENSMUSG00000020248. [P63139-1]
DR GeneID; 18045; -.
DR KEGG; mmu:18045; -.
DR UCSC; uc007gjv.1; mouse.
DR CTD; 4801; -.
DR MGI; MGI:97317; Nfyb.
DR VEuPathDB; HostDB:ENSMUSG00000020248; -.
DR eggNOG; KOG0869; Eukaryota.
DR GeneTree; ENSGT00940000154917; -.
DR InParanoid; P63139; -.
DR OMA; PRWDWFL; -.
DR PhylomeDB; P63139; -.
DR TreeFam; TF314521; -.
DR BioGRID-ORCS; 18045; 25 hits in 74 CRISPR screens.
DR ChiTaRS; Nfyb; mouse.
DR PRO; PR:P63139; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P63139; protein.
DR Bgee; ENSMUSG00000020248; Expressed in cortical plate and 264 other tissues.
DR ExpressionAtlas; P63139; baseline and differential.
DR Genevisible; P63139; MM.
DR GO; GO:0016602; C:CCAAT-binding factor complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0032993; C:protein-DNA complex; ISO:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IC:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
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:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IGI:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:MGI.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0035065; P:regulation of histone acetylation; ISO:MGI.
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:MGI.
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; Alternative splicing; Direct protein sequencing; DNA-binding;
KW Isopeptide bond; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..207
FT /note="Nuclear transcription factor Y subunit beta"
FT /id="PRO_0000204610"
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
