Full text data of NFYB
NFYB
(HAP3)
[Confidence: low (only semi-automatic identification from reviews)]
Nuclear transcription factor Y subunit beta (CAAT box DNA-binding protein subunit B; Nuclear transcription factor Y subunit B; NF-YB)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Nuclear transcription factor Y subunit beta (CAAT box DNA-binding protein subunit B; Nuclear transcription factor Y subunit B; NF-YB)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P25208
ID NFYB_HUMAN Reviewed; 207 AA.
AC P25208; A8K7B9; Q96IY8;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUL-1993, sequence version 2.
DT 22-JAN-2014, entry version 142.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1577736;
RA Li X.-Y., Hooft van Huijsduijnen R., Mantovani R., Benoist C.O.,
RA 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
RT class 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.,
RA Benoist C., Mathis D.;
RT "Evolutionary variation of the CCAAT-binding transcription factor NF-
RT 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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,
RT CBF/NF-Y, and inhibits CBF-mediated transcription activation in
RT 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.,
RA Buerckstuemmer T., 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
RT transcription 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;
RP NYFC 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: Stimulates the transcription of various genes by
CC recognizing and binding to a CCAAT motif in promoters, for example
CC in type 1 collagen, albumin and beta-actin genes.
CC -!- SUBUNIT: Heterotrimeric transcription factor composed of three
CC components, NF-YA, NF-YB and NF-YC. NF-YB and NF-YC must interact
CC and dimerize for NF-YA association and DNA binding. Interacts with
CC C1QBP.
CC -!- INTERACTION:
CC P23511:NFYA; NbExp=5; IntAct=EBI-389728, EBI-389739;
CC Q13952:NFYC; NbExp=3; IntAct=EBI-389728, EBI-389755;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DOMAIN: Can be divided into 3 domains: the weakly conserved A
CC domain, the highly conserved B domain thought to be involved in
CC subunit 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
CC H3 methylations as well as histone H2B monoubiquitination at 'Lys-
CC 121'.
CC -!- SIMILARITY: Belongs to the NFYB/HAP3 subunit family.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA42230.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 PIR; S22817; S22817.
DR RefSeq; NP_006157.1; NM_006166.3.
DR UniGene; Hs.84928; -.
DR PDB; 1N1J; X-ray; 1.67 A; A=51-143.
DR PDB; 4AWL; X-ray; 3.08 A; B=51-143.
DR PDBsum; 1N1J; -.
DR PDBsum; 4AWL; -.
DR ProteinModelPortal; P25208; -.
DR SMR; P25208; 57-143.
DR IntAct; P25208; 7.
DR MINT; MINT-146867; -.
DR STRING; 9606.ENSP00000240055; -.
DR PhosphoSite; P25208; -.
DR DMDM; 399193; -.
DR PaxDb; P25208; -.
DR PRIDE; P25208; -.
DR DNASU; 4801; -.
DR Ensembl; ENST00000240055; ENSP00000240055; ENSG00000120837.
DR Ensembl; ENST00000551727; ENSP00000447486; ENSG00000120837.
DR GeneID; 4801; -.
DR KEGG; hsa:4801; -.
DR UCSC; uc001tkl.1; human.
DR CTD; 4801; -.
DR GeneCards; GC12M104510; -.
DR HGNC; HGNC:7805; NFYB.
DR HPA; CAB004211; -.
DR MIM; 189904; gene.
DR neXtProt; NX_P25208; -.
DR PharmGKB; PA31610; -.
DR eggNOG; COG2036; -.
DR HOGENOM; HOG000211832; -.
DR HOVERGEN; HBG008864; -.
DR InParanoid; P25208; -.
DR KO; K08065; -.
DR OMA; TGEYMAS; -.
DR OrthoDB; EOG7RNK2W; -.
DR PhylomeDB; P25208; -.
DR Reactome; REACT_111217; Metabolism.
DR SignaLink; P25208; -.
DR ChiTaRS; NFYB; human.
DR EvolutionaryTrace; P25208; -.
DR GeneWiki; NFYB; -.
DR GenomeRNAi; 4801; -.
DR NextBio; 18506; -.
DR PRO; PR:P25208; -.
DR ArrayExpress; P25208; -.
DR Bgee; P25208; -.
DR CleanEx; HS_NFYB; -.
DR Genevestigator; P25208; -.
DR GO; GO:0016602; C:CCAAT-binding factor complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; TAS:ProtInc.
DR GO; GO:0044255; P:cellular lipid metabolic process; TAS:Reactome.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; IEA:Ensembl.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR003958; CBFA_NFYB_domain.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR003957; Transcrpt_fac_NFYB/HAP3.
DR InterPro; IPR003956; Transcrpt_fac_NFYB/HAP3_CS.
DR PANTHER; PTHR11064:SF9; PTHR11064:SF9; 1.
DR Pfam; PF00808; CBFD_NFYB_HMF; 1.
DR PRINTS; PR00615; CCAATSUBUNTA.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS00685; NFYB_HAP3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Complete proteome; DNA-binding;
KW Isopeptide bond; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1 207 Nuclear transcription factor Y subunit
FT beta.
FT /FTId=PRO_0000204609.
FT DNA_BIND 59 65 By similarity.
FT REGION 1 52 A domain.
FT REGION 53 142 B domain.
FT REGION 86 97 Subunit association domain (SAD) (By
FT similarity).
FT REGION 143 207 C domain.
FT CROSSLNK 140 140 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CONFLICT 29 29 I -> M (in Ref. 6; AAH07035).
FT HELIX 54 56
FT HELIX 61 70
FT HELIX 80 107
FT STRAND 111 113
FT HELIX 115 124
FT HELIX 128 130
FT HELIX 131 142
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
//
ID NFYB_HUMAN Reviewed; 207 AA.
AC P25208; A8K7B9; Q96IY8;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUL-1993, sequence version 2.
DT 22-JAN-2014, entry version 142.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1577736;
RA Li X.-Y., Hooft van Huijsduijnen R., Mantovani R., Benoist C.O.,
RA 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
RT class 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.,
RA Benoist C., Mathis D.;
RT "Evolutionary variation of the CCAAT-binding transcription factor NF-
RT 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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,
RT CBF/NF-Y, and inhibits CBF-mediated transcription activation in
RT 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.,
RA Buerckstuemmer T., 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
RT transcription 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;
RP NYFC 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: Stimulates the transcription of various genes by
CC recognizing and binding to a CCAAT motif in promoters, for example
CC in type 1 collagen, albumin and beta-actin genes.
CC -!- SUBUNIT: Heterotrimeric transcription factor composed of three
CC components, NF-YA, NF-YB and NF-YC. NF-YB and NF-YC must interact
CC and dimerize for NF-YA association and DNA binding. Interacts with
CC C1QBP.
CC -!- INTERACTION:
CC P23511:NFYA; NbExp=5; IntAct=EBI-389728, EBI-389739;
CC Q13952:NFYC; NbExp=3; IntAct=EBI-389728, EBI-389755;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DOMAIN: Can be divided into 3 domains: the weakly conserved A
CC domain, the highly conserved B domain thought to be involved in
CC subunit 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
CC H3 methylations as well as histone H2B monoubiquitination at 'Lys-
CC 121'.
CC -!- SIMILARITY: Belongs to the NFYB/HAP3 subunit family.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA42230.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 PIR; S22817; S22817.
DR RefSeq; NP_006157.1; NM_006166.3.
DR UniGene; Hs.84928; -.
DR PDB; 1N1J; X-ray; 1.67 A; A=51-143.
DR PDB; 4AWL; X-ray; 3.08 A; B=51-143.
DR PDBsum; 1N1J; -.
DR PDBsum; 4AWL; -.
DR ProteinModelPortal; P25208; -.
DR SMR; P25208; 57-143.
DR IntAct; P25208; 7.
DR MINT; MINT-146867; -.
DR STRING; 9606.ENSP00000240055; -.
DR PhosphoSite; P25208; -.
DR DMDM; 399193; -.
DR PaxDb; P25208; -.
DR PRIDE; P25208; -.
DR DNASU; 4801; -.
DR Ensembl; ENST00000240055; ENSP00000240055; ENSG00000120837.
DR Ensembl; ENST00000551727; ENSP00000447486; ENSG00000120837.
DR GeneID; 4801; -.
DR KEGG; hsa:4801; -.
DR UCSC; uc001tkl.1; human.
DR CTD; 4801; -.
DR GeneCards; GC12M104510; -.
DR HGNC; HGNC:7805; NFYB.
DR HPA; CAB004211; -.
DR MIM; 189904; gene.
DR neXtProt; NX_P25208; -.
DR PharmGKB; PA31610; -.
DR eggNOG; COG2036; -.
DR HOGENOM; HOG000211832; -.
DR HOVERGEN; HBG008864; -.
DR InParanoid; P25208; -.
DR KO; K08065; -.
DR OMA; TGEYMAS; -.
DR OrthoDB; EOG7RNK2W; -.
DR PhylomeDB; P25208; -.
DR Reactome; REACT_111217; Metabolism.
DR SignaLink; P25208; -.
DR ChiTaRS; NFYB; human.
DR EvolutionaryTrace; P25208; -.
DR GeneWiki; NFYB; -.
DR GenomeRNAi; 4801; -.
DR NextBio; 18506; -.
DR PRO; PR:P25208; -.
DR ArrayExpress; P25208; -.
DR Bgee; P25208; -.
DR CleanEx; HS_NFYB; -.
DR Genevestigator; P25208; -.
DR GO; GO:0016602; C:CCAAT-binding factor complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; TAS:ProtInc.
DR GO; GO:0044255; P:cellular lipid metabolic process; TAS:Reactome.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; IEA:Ensembl.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR003958; CBFA_NFYB_domain.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR003957; Transcrpt_fac_NFYB/HAP3.
DR InterPro; IPR003956; Transcrpt_fac_NFYB/HAP3_CS.
DR PANTHER; PTHR11064:SF9; PTHR11064:SF9; 1.
DR Pfam; PF00808; CBFD_NFYB_HMF; 1.
DR PRINTS; PR00615; CCAATSUBUNTA.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS00685; NFYB_HAP3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Complete proteome; DNA-binding;
KW Isopeptide bond; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1 207 Nuclear transcription factor Y subunit
FT beta.
FT /FTId=PRO_0000204609.
FT DNA_BIND 59 65 By similarity.
FT REGION 1 52 A domain.
FT REGION 53 142 B domain.
FT REGION 86 97 Subunit association domain (SAD) (By
FT similarity).
FT REGION 143 207 C domain.
FT CROSSLNK 140 140 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CONFLICT 29 29 I -> M (in Ref. 6; AAH07035).
FT HELIX 54 56
FT HELIX 61 70
FT HELIX 80 107
FT STRAND 111 113
FT HELIX 115 124
FT HELIX 128 130
FT HELIX 131 142
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
//
MIM
189904
*RECORD*
*FIELD* NO
189904
*FIELD* TI
*189904 NUCLEAR TRANSCRIPTION FACTOR Y, BETA; NFYB
;;TRANSCRIPTION FACTOR NF-Y, B SUBUNIT
read more*FIELD* TX
DESCRIPTION
NFYB is a subunit of a conserved transcription factor that binds
specifically to CCAAT elements in promoters (Chen et al., 2011).
GENE FUNCTION
Chen et al. (2011) had found that expression of DNA topoisomerase-2
(TOP2)-alpha (TOP2A; 126430) was inverse to expression of NFYB. They
found reduced TOP2-alpha and elevated NFYB expression in a CEM human
lymphoblastic leukemia subline that was resistant to teniposide, a
TOP2-alpha-targeting chemotherapeutic agent. MicroRNA profiling revealed
reduced expression of MIR485-3p (615385) in teniposide-resistant cells.
Overexpression of MIR485-3p downregulated NFYB via an MIR485-3p-binding
site in the 3-prime UTR of the NFYB transcript, resulting in upregulated
TOP2-alpha expression and restored sensitivity to teniposide.
Overexpression of MIR485-3p also enhanced etoposide sensitivity in
etoposide-resistant human rhabdomyosarcoma cells and in
teniposide-resistant CEM cells. Chen et al. (2011) concluded that
MIR485-3p-dependent downregulation of NFYB enhances cell sensitivity to
TOP2-alpha inhibitors.
MAPPING
Li et al. (1991) assigned the NFYB gene to human chromosome 12 by in
situ hybridization. They mapped the mouse gene to chromosome 10.
Gross (2013) mapped the NFYB gene to chromosome 12q23.3 based on an
alignment of the NFYB sequence (GenBank GENBANK BC005316) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Chen, C.-F.; He, X.; Arslan, A. D.; Mo, Y.-Y.; Reinhold, W. C.;
Pommier, Y.; Beck, W. T.: Novel regulation of nuclear factor-YB by
miR-485-3p affects the expression of DNA topoisomerase II-alpha and
drug responsiveness. Molec. Pharm. 79: 735-741, 2011.
2. Gross, M. B.: Personal Communication. Baltimore, Md. 8/28/2013.
3. Li, X.-Y.; Mattei, M. G.; Zaleska-Rutczynska, Z.; Hooft van Huijsduijnen,
R.; Figueroa, F.; Nadeau, J.; Benoist, C.; Mathis, D.: One subunit
of the transcription factor NF-Y maps close to the major histocompatibility
complex in murine and human chromosomes. Genomics 11: 630-634, 1991.
*FIELD* CN
Matthew B. Gross - updated: 08/28/2013
Patricia A. Hartz - updated: 8/28/2013
*FIELD* CD
Victor A. McKusick: 10/23/1991
*FIELD* ED
mgross: 08/28/2013
mgross: 8/28/2013
mark: 6/5/1997
supermim: 3/16/1992
carol: 10/23/1991
*RECORD*
*FIELD* NO
189904
*FIELD* TI
*189904 NUCLEAR TRANSCRIPTION FACTOR Y, BETA; NFYB
;;TRANSCRIPTION FACTOR NF-Y, B SUBUNIT
read more*FIELD* TX
DESCRIPTION
NFYB is a subunit of a conserved transcription factor that binds
specifically to CCAAT elements in promoters (Chen et al., 2011).
GENE FUNCTION
Chen et al. (2011) had found that expression of DNA topoisomerase-2
(TOP2)-alpha (TOP2A; 126430) was inverse to expression of NFYB. They
found reduced TOP2-alpha and elevated NFYB expression in a CEM human
lymphoblastic leukemia subline that was resistant to teniposide, a
TOP2-alpha-targeting chemotherapeutic agent. MicroRNA profiling revealed
reduced expression of MIR485-3p (615385) in teniposide-resistant cells.
Overexpression of MIR485-3p downregulated NFYB via an MIR485-3p-binding
site in the 3-prime UTR of the NFYB transcript, resulting in upregulated
TOP2-alpha expression and restored sensitivity to teniposide.
Overexpression of MIR485-3p also enhanced etoposide sensitivity in
etoposide-resistant human rhabdomyosarcoma cells and in
teniposide-resistant CEM cells. Chen et al. (2011) concluded that
MIR485-3p-dependent downregulation of NFYB enhances cell sensitivity to
TOP2-alpha inhibitors.
MAPPING
Li et al. (1991) assigned the NFYB gene to human chromosome 12 by in
situ hybridization. They mapped the mouse gene to chromosome 10.
Gross (2013) mapped the NFYB gene to chromosome 12q23.3 based on an
alignment of the NFYB sequence (GenBank GENBANK BC005316) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Chen, C.-F.; He, X.; Arslan, A. D.; Mo, Y.-Y.; Reinhold, W. C.;
Pommier, Y.; Beck, W. T.: Novel regulation of nuclear factor-YB by
miR-485-3p affects the expression of DNA topoisomerase II-alpha and
drug responsiveness. Molec. Pharm. 79: 735-741, 2011.
2. Gross, M. B.: Personal Communication. Baltimore, Md. 8/28/2013.
3. Li, X.-Y.; Mattei, M. G.; Zaleska-Rutczynska, Z.; Hooft van Huijsduijnen,
R.; Figueroa, F.; Nadeau, J.; Benoist, C.; Mathis, D.: One subunit
of the transcription factor NF-Y maps close to the major histocompatibility
complex in murine and human chromosomes. Genomics 11: 630-634, 1991.
*FIELD* CN
Matthew B. Gross - updated: 08/28/2013
Patricia A. Hartz - updated: 8/28/2013
*FIELD* CD
Victor A. McKusick: 10/23/1991
*FIELD* ED
mgross: 08/28/2013
mgross: 8/28/2013
mark: 6/5/1997
supermim: 3/16/1992
carol: 10/23/1991