NFYB_HUMAN
ID NFYB_HUMAN Reviewed; 207 AA.
AC P25208; A8K7B9; Q96IY8;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 2.
DT 03-AUG-2022, entry version 209.
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; Synonyms=HAP3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Badley Clarke J., Ting J.P.Y.;
RT "Sequence of human NF-YB, a transcriptional regulatory protein of MHC class
RT II genes.";
RL Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Urinary bladder;
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).
RN [7]
RP INTERACTION WITH C1QBP.
RX PubMed=15243141; DOI=10.1093/nar/gkh692;
RA Chattopadhyay C., Hawke D., Kobayashi R., Maity S.N.;
RT "Human p32, interacts with B subunit of the CCAAT-binding factor, CBF/NF-Y,
RT and inhibits CBF-mediated transcription activation in vitro.";
RL Nucleic Acids Res. 32:3632-3641(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 51-143.
RX PubMed=12401788; DOI=10.1074/jbc.m209635200;
RA Romier C., Cocchiarella F., Mantovani R., Moras D.;
RT "The NF-YB/NF-YC structure gives insight into DNA binding and transcription
RT regulation by CCAAT factor NF-Y.";
RL J. Biol. Chem. 278:1336-1345(2003).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (3.08 ANGSTROMS) OF 51-143 IN COMPLEX WITH NYFA; NYFC
RP AND PROMOTER DNA, SUBUNIT, AND UBIQUITINATION AT LYS-140.
RX PubMed=23332751; DOI=10.1016/j.cell.2012.11.047;
RA Nardini M., Gnesutta N., Donati G., Gatta R., Forni C., Fossati A.,
RA Vonrhein C., Moras D., Romier C., Bolognesi M., Mantovani R.;
RT "Sequence-specific transcription factor NF-Y displays histone-like DNA
RT binding and H2B-like ubiquitination.";
RL Cell 152:132-143(2013).
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 {ECO:0000269|PubMed:15243141, ECO:0000269|PubMed:23332751}.
CC -!- INTERACTION:
CC P25208; Q6RW13: AGTRAP; NbExp=3; IntAct=EBI-389728, EBI-741181;
CC P25208; P06307: CCK; NbExp=3; IntAct=EBI-389728, EBI-6624398;
CC P25208; Q14919: DRAP1; NbExp=4; IntAct=EBI-389728, EBI-712941;
CC P25208; P13473-2: LAMP2; NbExp=3; IntAct=EBI-389728, EBI-21591415;
CC P25208; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-389728, EBI-16439278;
CC P25208; P23511: NFYA; NbExp=8; IntAct=EBI-389728, EBI-389739;
CC P25208; P23511-2: NFYA; NbExp=6; IntAct=EBI-389728, EBI-11061759;
CC P25208; Q13952: NFYC; NbExp=6; IntAct=EBI-389728, EBI-389755;
CC P25208; Q13952-2: NFYC; NbExp=6; IntAct=EBI-389728, EBI-11956831;
CC P25208; Q9NR33: POLE4; NbExp=12; IntAct=EBI-389728, EBI-867034;
CC P25208; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-389728, EBI-2623095;
CC P25208; P04637: TP53; NbExp=6; IntAct=EBI-389728, EBI-366083;
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 -!- SIMILARITY: Belongs to the NFYB/HAP3 subunit family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA42230.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L06145; AAA59930.1; -; mRNA.
DR EMBL; X59710; CAA42230.1; ALT_INIT; mRNA.
DR EMBL; AK291934; BAF84623.1; -; mRNA.
DR EMBL; CH471054; EAW97740.1; -; Genomic_DNA.
DR EMBL; BC005316; AAH05316.1; -; mRNA.
DR EMBL; BC005317; AAH05317.1; -; mRNA.
DR EMBL; BC007035; AAH07035.1; -; mRNA.
DR CCDS; CCDS9098.1; -.
DR PIR; S22817; S22817.
DR RefSeq; NP_006157.1; NM_006166.3.
DR PDB; 1N1J; X-ray; 1.67 A; A=51-143.
DR PDB; 4AWL; X-ray; 3.08 A; B=51-143.
DR PDB; 4CSR; X-ray; 1.50 A; A=51-143.
DR PDB; 6QMP; X-ray; 2.00 A; B=51-143.
DR PDB; 6QMQ; X-ray; 2.50 A; B=51-143.
DR PDB; 6QMS; X-ray; 1.80 A; B=51-143.
DR PDB; 7AH8; X-ray; 2.70 A; A/C=54-142.
DR PDBsum; 1N1J; -.
DR PDBsum; 4AWL; -.
DR PDBsum; 4CSR; -.
DR PDBsum; 6QMP; -.
DR PDBsum; 6QMQ; -.
DR PDBsum; 6QMS; -.
DR PDBsum; 7AH8; -.
DR AlphaFoldDB; P25208; -.
DR SASBDB; P25208; -.
DR SMR; P25208; -.
DR BioGRID; 110867; 40.
DR ComplexPortal; CPX-1956; CCAAT-binding factor complex.
DR CORUM; P25208; -.
DR IntAct; P25208; 13.
DR STRING; 9606.ENSP00000240055; -.
DR iPTMnet; P25208; -.
DR PhosphoSitePlus; P25208; -.
DR BioMuta; NFYB; -.
DR DMDM; 399193; -.
DR EPD; P25208; -.
DR jPOST; P25208; -.
DR MassIVE; P25208; -.
DR MaxQB; P25208; -.
DR PaxDb; P25208; -.
DR PeptideAtlas; P25208; -.
DR PRIDE; P25208; -.
DR ProteomicsDB; 54266; -.
DR Antibodypedia; 3780; 278 antibodies from 32 providers.
DR DNASU; 4801; -.
DR Ensembl; ENST00000240055.8; ENSP00000240055.3; ENSG00000120837.8.
DR Ensembl; ENST00000551727.5; ENSP00000447486.1; ENSG00000120837.8.
DR GeneID; 4801; -.
DR KEGG; hsa:4801; -.
DR MANE-Select; ENST00000240055.8; ENSP00000240055.3; NM_006166.4; NP_006157.1.
DR UCSC; uc001tkl.2; human.
DR CTD; 4801; -.
DR DisGeNET; 4801; -.
DR GeneCards; NFYB; -.
DR HGNC; HGNC:7805; NFYB.
DR HPA; ENSG00000120837; Low tissue specificity.
DR MIM; 189904; gene.
DR neXtProt; NX_P25208; -.
DR OpenTargets; ENSG00000120837; -.
DR PharmGKB; PA31610; -.
DR VEuPathDB; HostDB:ENSG00000120837; -.
DR eggNOG; KOG0869; Eukaryota.
DR GeneTree; ENSGT00940000154917; -.
DR InParanoid; P25208; -.
DR OMA; PRWDWFL; -.
DR OrthoDB; 1529111at2759; -.
DR PhylomeDB; P25208; -.
DR TreeFam; TF314521; -.
DR PathwayCommons; P25208; -.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
DR Reactome; R-HSA-380994; ATF4 activates genes in response to endoplasmic reticulum stress.
DR Reactome; R-HSA-381183; ATF6 (ATF6-alpha) activates chaperone genes.
DR Reactome; R-HSA-9614657; FOXO-mediated transcription of cell death genes.
DR SignaLink; P25208; -.
DR SIGNOR; P25208; -.
DR BioGRID-ORCS; 4801; 552 hits in 1070 CRISPR screens.
DR ChiTaRS; NFYB; human.
DR EvolutionaryTrace; P25208; -.
DR GeneWiki; NFYB; -.
DR GenomeRNAi; 4801; -.
DR Pharos; P25208; Tbio.
DR PRO; PR:P25208; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P25208; protein.
DR Bgee; ENSG00000120837; Expressed in ganglionic eminence and 210 other tissues.
DR ExpressionAtlas; P25208; baseline and differential.
DR Genevisible; P25208; HS.
DR GO; GO:0016602; C:CCAAT-binding factor complex; IDA:UniProtKB.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032993; C:protein-DNA complex; IDA:ParkinsonsUK-UCL.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:NTNU_SB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IGI:ARUK-UCL.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
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; IDA:ARUK-UCL.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; IDA:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ARUK-UCL.
DR GO; GO:0035065; P:regulation of histone acetylation; IDA:ComplexPortal.
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; IDA:UniProtKB.
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 3D-structure; Activator; DNA-binding; Isopeptide bond; Nucleus;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..207
FT /note="Nuclear transcription factor Y subunit beta"
FT /id="PRO_0000204609"
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:0000269|PubMed:23332751"
FT CONFLICT 29
FT /note="I -> M (in Ref. 6; AAH07035)"
FT /evidence="ECO:0000305"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:4AWL"
FT HELIX 61..70
FT /evidence="ECO:0007829|PDB:4CSR"
FT HELIX 80..107
FT /evidence="ECO:0007829|PDB:4CSR"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:4CSR"
FT HELIX 115..124
FT /evidence="ECO:0007829|PDB:4CSR"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:4CSR"
FT HELIX 131..142
FT /evidence="ECO:0007829|PDB:4CSR"
SQ SEQUENCE 207 AA; 22831 MW; 1ADFA0E45F3CF972 CRC64;
MTMDGDSSTT DASQLGISAD YIGGSHYVIQ PHDDTEDSMN DHEDTNGSKE SFREQDIYLP
IANVARIMKN AIPQTGKIAK DAKECVQECV SEFISFITSE ASERCHQEKR KTINGEDILF
AMSTLGFDSY VEPLKLYLQK FREAMKGEKG IGGAVTATDG LSEELTEEAF TNQLPAGLIT
TDGQQQNVMV YTTSYQQISG VQQIQFS
