Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P63139

- NFYB_MOUSE

UniProt

P63139 - NFYB_MOUSE

Protein

Nuclear transcription factor Y subunit beta

Gene

Nfyb

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 1 (13 Sep 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Component of the sequence-specific heterotrimeric transcription factor (NF-Y) which specifically recognizes a 5'-CCAAT-3' box motif found in the promoters of its target genes. NF-Y can function as both an activator and a repressor, depending on its interacting cofactors.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi59 – 657By similarity

    GO - Molecular functioni

    1. DNA binding Source: MGI
    2. sequence-specific DNA binding Source: InterPro
    3. sequence-specific DNA binding transcription factor activity Source: MGI

    GO - Biological processi

    1. positive regulation of transcription, DNA-templated Source: MGI
    2. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_198602. PPARA activates gene expression.
    REACT_198969. Activation of gene expression by SREBF (SREBP).
    REACT_32838. ATF6-alpha activates chaperone genes.
    REACT_90370. ATF4 activates genes.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nuclear transcription factor Y subunit beta
    Alternative name(s):
    CAAT box DNA-binding protein subunit B
    Nuclear transcription factor Y subunit B
    Short name:
    NF-YB
    Gene namesi
    Name:Nfyb
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:97317. Nfyb.

    Subcellular locationi

    GO - Cellular componenti

    1. CCAAT-binding factor complex Source: Ensembl
    2. nucleoplasm Source: Reactome
    3. nucleus Source: MGI
    4. transcription factor complex Source: MGI

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 207207Nuclear transcription factor Y subunit betaPRO_0000204610Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki140 – 140Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

    Post-translational modificationi

    Monoubiquitination at Lys-140 plays an important role in transcriptional activation by allowing the deposition of histone H3 methylations as well as histone H2B monoubiquitination at 'Lys-121'.By similarity

    Keywords - PTMi

    Isopeptide bond, Ubl conjugation

    Proteomic databases

    MaxQBiP63139.
    PRIDEiP63139.

    PTM databases

    PhosphoSiteiP63139.

    Expressioni

    Gene expression databases

    ArrayExpressiP63139.
    BgeeiP63139.
    CleanExiMM_NFYB.
    GenevestigatoriP63139.

    Interactioni

    Subunit structurei

    Heterotrimeric transcription factor composed of three components, NF-YA, NF-YB and NF-YC. NF-YB and NF-YC must interact and dimerize for NF-YA association and DNA binding. Interacts with C1QBP By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP63139.
    SMRiP63139. Positions 57-143.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 5252A domainAdd
    BLAST
    Regioni53 – 14290B domainAdd
    BLAST
    Regioni86 – 9712Subunit association domain (SAD)By similarityAdd
    BLAST
    Regioni143 – 20765C domainAdd
    BLAST

    Domaini

    Can be divided into 3 domains: the weakly conserved A domain, the highly conserved B domain thought to be involved in subunit interaction and DNA binding, and the Glu-rich C domain.

    Sequence similaritiesi

    Belongs to the NFYB/HAP3 subunit family.Curated

    Phylogenomic databases

    eggNOGiCOG2036.
    GeneTreeiENSGT00550000074689.
    HOVERGENiHBG008864.
    InParanoidiP63139.
    KOiK08065.
    OMAiIAGDYIG.
    OrthoDBiEOG7RNK2W.
    TreeFamiTF314521.

    Family and domain databases

    Gene3Di1.10.20.10. 1 hit.
    InterProiIPR003958. CBFA_NFYB_domain.
    IPR009072. Histone-fold.
    IPR003956. Transcrpt_fac_NFYB/HAP3_CS.
    [Graphical view]
    PfamiPF00808. CBFD_NFYB_HMF. 1 hit.
    [Graphical view]
    SUPFAMiSSF47113. SSF47113. 1 hit.
    PROSITEiPS00685. NFYB_HAP3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    This entry describes 1 isoform i produced by alternative splicing. Align

    Note: 3 isoforms may be produced.

    Isoform 1 (identifier: P63139-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MTMDGDSSTT DASQLGISAD YIGGSHYVIQ PHDDTEDSMN DHEDTNGSKE    50
    SFREQDIYLP IANVARIMKN AIPQTGKIAK DAKECVQECV SEFISFITSE 100
    ASERCHQEKR KTINGEDILF AMSTLGFDSY VEPLKLYLQK FREAMKGEKG 150
    IGGAVSATDG LSEELTEEAF TNQLPAGLIT ADGQQQNVMV YTTSYQQISG 200
    VQQIQFS 207
    Length:207
    Mass (Da):22,787
    Last modified:September 13, 2004 - v1
    Checksum:i1ADFB4B04A3CFC22
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X55316 mRNA. Translation: CAA39024.1.
    AK010762 mRNA. Translation: BAB27166.1.
    AK146168 mRNA. Translation: BAE26948.1.
    BC010719 mRNA. Translation: AAH10719.1.
    CCDSiCCDS48654.1.
    PIRiF38245.
    RefSeqiNP_035044.1. NM_010914.2. [P63139-1]
    UniGeneiMm.245998.

    Genome annotation databases

    EnsembliENSMUST00000130911; ENSMUSP00000122403; ENSMUSG00000020248. [P63139-1]
    GeneIDi18045.
    KEGGimmu:18045.
    UCSCiuc007gjv.1. mouse.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X55316 mRNA. Translation: CAA39024.1 .
    AK010762 mRNA. Translation: BAB27166.1 .
    AK146168 mRNA. Translation: BAE26948.1 .
    BC010719 mRNA. Translation: AAH10719.1 .
    CCDSi CCDS48654.1.
    PIRi F38245.
    RefSeqi NP_035044.1. NM_010914.2. [P63139-1 ]
    UniGenei Mm.245998.

    3D structure databases

    ProteinModelPortali P63139.
    SMRi P63139. Positions 57-143.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei P63139.

    Proteomic databases

    MaxQBi P63139.
    PRIDEi P63139.

    Protocols and materials databases

    DNASUi 18045.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000130911 ; ENSMUSP00000122403 ; ENSMUSG00000020248 . [P63139-1 ]
    GeneIDi 18045.
    KEGGi mmu:18045.
    UCSCi uc007gjv.1. mouse.

    Organism-specific databases

    CTDi 4801.
    MGIi MGI:97317. Nfyb.

    Phylogenomic databases

    eggNOGi COG2036.
    GeneTreei ENSGT00550000074689.
    HOVERGENi HBG008864.
    InParanoidi P63139.
    KOi K08065.
    OMAi IAGDYIG.
    OrthoDBi EOG7RNK2W.
    TreeFami TF314521.

    Enzyme and pathway databases

    Reactomei REACT_198602. PPARA activates gene expression.
    REACT_198969. Activation of gene expression by SREBF (SREBP).
    REACT_32838. ATF6-alpha activates chaperone genes.
    REACT_90370. ATF4 activates genes.

    Miscellaneous databases

    NextBioi 293161.
    PROi P63139.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P63139.
    Bgeei P63139.
    CleanExi MM_NFYB.
    Genevestigatori P63139.

    Family and domain databases

    Gene3Di 1.10.20.10. 1 hit.
    InterProi IPR003958. CBFA_NFYB_domain.
    IPR009072. Histone-fold.
    IPR003956. Transcrpt_fac_NFYB/HAP3_CS.
    [Graphical view ]
    Pfami PF00808. CBFD_NFYB_HMF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47113. SSF47113. 1 hit.
    PROSITEi PS00685. NFYB_HAP3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Co-evolution from yeast to mouse: cDNA cloning of the two NF-Y (CP-1/CBF) subunits."
      Hooft van Huijsduijnen R., Li X.-Y., Black D., Matthes H., Benoist C., Mathis D.
      EMBO J. 9:3119-3127(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 51-69; 137-140 AND 194-206.
    2. "Evolutionary variation of the CCAAT-binding transcription factor NF-Y."
      Li X.-Y., Mantovani R., Hooft van Huijsduijnen R., Andre I., Benoist C., Mathis D.
      Nucleic Acids Res. 20:1087-1091(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Intron-exon organization of the NF-Y genes. Tissue-specific splicing modifies an activation domain."
      Li X.-Y., Hooft van Huijsduijnen R., Mantovani R., Benoist C.O., Mathis D.
      J. Biol. Chem. 267:8984-8990(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
    4. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: BALB/c and C57BL/6J.
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.

    Entry informationi

    Entry nameiNFYB_MOUSE
    AccessioniPrimary (citable) accession number: P63139
    Secondary accession number(s): P22569, Q3UK54
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 13, 2004
    Last sequence update: September 13, 2004
    Last modified: October 1, 2014
    This is version 90 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3