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Q13952

- NFYC_HUMAN

UniProt

Q13952 - NFYC_HUMAN

Protein

Nuclear transcription factor Y subunit gamma

Gene

NFYC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 3 (23 Jan 2002)
      Previous versions | rss
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    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.

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. sequence-specific DNA binding Source: InterPro
    4. sequence-specific DNA binding transcription factor activity Source: ProtInc
    5. transcription coactivator activity Source: ProtInc

    GO - Biological processi

    1. cellular lipid metabolic process Source: Reactome
    2. positive regulation of transcription, DNA-templated Source: Ensembl
    3. protein folding Source: ProtInc
    4. regulation of transcription, DNA-templated Source: UniProtKB
    5. regulation of transcription from RNA polymerase II promoter Source: ProtInc
    6. small molecule metabolic process Source: Reactome
    7. 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_116145. PPARA activates gene expression.
    REACT_147904. Activation of gene expression by SREBF (SREBP).
    REACT_18355. ATF4 activates genes.
    REACT_18423. ATF6-alpha activates chaperone genes.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nuclear transcription factor Y subunit gamma
    Alternative name(s):
    CAAT box DNA-binding protein subunit C
    Nuclear transcription factor Y subunit C
    Short name:
    NF-YC
    Transactivator HSM-1/2
    Gene namesi
    Name:NFYC
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:7806. NFYC.

    Subcellular locationi

    GO - Cellular componenti

    1. CCAAT-binding factor complex Source: UniProtKB
    2. nucleoplasm Source: Reactome
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA31611.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 458458Nuclear transcription factor Y subunit gammaPRO_0000218246Add
    BLAST

    Proteomic databases

    MaxQBiQ13952.
    PaxDbiQ13952.
    PRIDEiQ13952.

    PTM databases

    PhosphoSiteiQ13952.

    Expressioni

    Gene expression databases

    ArrayExpressiQ13952.
    BgeeiQ13952.
    GenevestigatoriQ13952.

    Organism-specific databases

    HPAiHPA055011.

    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.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NFYAP235114EBI-389755,EBI-389739
    NFYBP252083EBI-389755,EBI-389728

    Protein-protein interaction databases

    BioGridi110868. 36 interactions.
    IntActiQ13952. 20 interactions.
    MINTiMINT-249381.

    Structurei

    Secondary structure

    1
    458
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi45 – 528
    Beta strandi55 – 573
    Helixi64 – 9027
    Beta strandi94 – 963
    Helixi98 – 1058
    Helixi109 – 1146
    Turni115 – 1173

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1N1JX-ray1.67B27-120[»]
    4AWLX-ray3.08C27-120[»]
    ProteinModelPortaliQ13952.
    SMRiQ13952. Positions 6-120.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13952.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the NFYC/HAP5 subunit family.Curated

    Phylogenomic databases

    eggNOGiCOG5208.
    HOGENOMiHOG000231074.
    HOVERGENiHBG002885.
    InParanoidiQ13952.
    KOiK08066.
    OMAiATNAQQI.
    OrthoDBiEOG7BGHNS.
    PhylomeDBiQ13952.
    TreeFamiTF354207.

    Family and domain databases

    Gene3Di1.10.20.10. 1 hit.
    InterProiIPR003958. CBFA_NFYB_domain.
    IPR009072. Histone-fold.
    IPR027170. NFYC/HAP5_su.
    [Graphical view]
    PANTHERiPTHR10252:SF8. PTHR10252:SF8. 1 hit.
    PfamiPF00808. CBFD_NFYB_HMF. 1 hit.
    [Graphical view]
    SUPFAMiSSF47113. SSF47113. 1 hit.

    Sequences (7)i

    Sequence statusi: Complete.

    This entry describes 7 isoformsi produced by alternative splicing. Align

    Isoform 3 (identifier: Q13952-1) [UniParc]FASTAAdd to Basket

    Also known as: DS2.8

    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

    MSTEGGFGGT SSSDAQQSLQ SFWPRVMEEI RNLTVKDFRV QELPLARIKK    50
    IMKLDEDVKM ISAEAPVLFA KAAQIFITEL TLRAWIHTED NKRRTLQRND 100
    IAMAITKFDQ FDFLIDIVPR DELKPPKRQE EVRQSVTPAE PVQYYFTLAQ 150
    QPTAVQVQGQ QQGQQTTSST TTIQPGQIII AQPQQGQTTP VTMQVGEGQQ 200
    VQIVQAQPQG QAQQAQSGTG QTMQVMQQII TNTGEIQQIP VQLNAGQLQY 250
    IRLAQPVSGT QVVQGQIQTL ATNAQQGQRN ASQGKPRRCL KETLQITQTE 300
    VQQGQQQFSQ FTDGQRNSVQ QARVSELTGE AEPREVKATG NSTPCTSSLP 350
    TTHPPSHRAG ASCVCCSQPQ QSSTSPPPSD ALQWVVVEVS GTPNQLETHR 400
    ELHAPLPGMT SLSPLHPSQQ LYQIQQVTMP AGQDLAQPMF IQSANQPSDG 450
    QAPQVTGD 458
    Length:458
    Mass (Da):50,302
    Last modified:January 23, 2002 - v3
    Checksum:iB17B2C7F622653B9
    GO
    Isoform 1 (identifier: Q13952-2) [UniParc]FASTAAdd to Basket

    Also known as: Gamma

    The sequence of this isoform differs from the canonical sequence as follows:
         277-295: Missing.
         316-419: Missing.

    Show »
    Length:335
    Mass (Da):37,194
    Checksum:iD83635C1773C3895
    GO
    Isoform 2 (identifier: Q13952-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         277-295: Missing.

    Show »
    Length:439
    Mass (Da):48,150
    Checksum:iE3FED3512983A402
    GO
    Isoform 4 (identifier: Q13952-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         60-97: Missing.
         277-295: Missing.
         316-419: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:297
    Mass (Da):32,828
    Checksum:i6E5693FBF9D838ED
    GO
    Isoform 5 (identifier: Q13952-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         316-419: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:354
    Mass (Da):39,346
    Checksum:i80887376BB8125F3
    GO
    Isoform 6 (identifier: Q13952-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         186-219: Missing.
         277-295: Missing.
         316-419: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:301
    Mass (Da):33,702
    Checksum:i1BC4774E7E20894A
    GO
    Isoform 7 (identifier: Q13952-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         277-295: Missing.
         315-315: Missing.
         316-419: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:334
    Mass (Da):37,066
    Checksum:i685A01326BF0FFB1
    GO

    Sequence cautioni

    The sequence BAD92212.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti52 – 521M → I in CAA99055. (PubMed:9332362)Curated
    Sequence conflicti90 – 901D → N in BAA14051. (PubMed:10446203)Curated
    Sequence conflicti155 – 1551V → L in AAC50816. (PubMed:8910521)Curated
    Sequence conflicti158 – 1581Q → H in BAA14051. (PubMed:10446203)Curated
    Sequence conflicti171 – 1711T → N in BAA14051. (PubMed:10446203)Curated
    Sequence conflicti175 – 1751P → A in AAC50816. (PubMed:8910521)Curated
    Sequence conflicti179 – 1791I → F in BAA14051. (PubMed:10446203)Curated
    Sequence conflicti198 – 1981G → S in BAA12818. (PubMed:10446203)Curated
    Sequence conflicti198 – 1981G → S in BAA14051. (PubMed:10446203)Curated
    Sequence conflicti202 – 2021Q → K in BAA12818. (PubMed:10446203)Curated
    Sequence conflicti216 – 2172QS → HN in BAA14051. (PubMed:10446203)Curated
    Sequence conflicti248 – 2481L → V in AAC50816. (PubMed:8910521)Curated
    Sequence conflicti271 – 2711A → V in AAC50816. (PubMed:8910521)Curated
    Sequence conflicti451 – 4511Q → K in BAA14051. (PubMed:10446203)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti165 – 1651Q → H in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035702
    Natural varianti297 – 2971T → I.
    Corresponds to variant rs2230746 [ dbSNP | Ensembl ].
    VAR_059460

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei60 – 9738Missing in isoform 4. 1 PublicationVSP_043348Add
    BLAST
    Alternative sequencei186 – 21934Missing in isoform 6. 1 PublicationVSP_043349Add
    BLAST
    Alternative sequencei277 – 29519Missing in isoform 1, isoform 2, isoform 4, isoform 6 and isoform 7. 8 PublicationsVSP_000851Add
    BLAST
    Alternative sequencei315 – 3151Missing in isoform 7. 1 PublicationVSP_046350
    Alternative sequencei316 – 419104Missing in isoform 1, isoform 4, isoform 5, isoform 6 and isoform 7. 8 PublicationsVSP_000852Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U62296 mRNA. Translation: AAC50816.1.
    U78774 mRNA. Translation: AAC51669.1.
    Z74792 mRNA. Translation: CAA99055.1.
    D85425 mRNA. Translation: BAA12818.1.
    D89986 mRNA. Translation: BAA14051.1.
    AF191744 mRNA. Translation: AAG28389.1.
    AK000346 mRNA. Translation: BAA91100.1.
    AK127677 mRNA. Translation: BAG54549.1.
    AK300774 mRNA. Translation: BAG62438.1.
    AK301385 mRNA. Translation: BAG62925.1.
    BT020081 mRNA. Translation: AAV38884.1.
    AB208975 mRNA. Translation: BAD92212.1. Different initiation.
    AL031289 Genomic DNA. No translation available.
    AL354914, AC119677 Genomic DNA. Translation: CAI16530.1.
    AL354914, AC119677 Genomic DNA. Translation: CAI16531.1.
    AL354914, AC119677 Genomic DNA. Translation: CAI16532.1.
    AL354914, AC119677 Genomic DNA. Translation: CAI16533.1.
    CH471059 Genomic DNA. Translation: EAX07198.1.
    CH471059 Genomic DNA. Translation: EAX07201.1.
    CH471059 Genomic DNA. Translation: EAX07202.1.
    CH471059 Genomic DNA. Translation: EAX07203.1.
    BC005003 mRNA. Translation: AAH05003.1.
    CCDSiCCDS44120.1. [Q13952-5]
    CCDS44121.1. [Q13952-7]
    CCDS44122.1. [Q13952-6]
    CCDS44123.1. [Q13952-4]
    CCDS455.1. [Q13952-2]
    RefSeqiNP_001136059.1. NM_001142587.1. [Q13952-7]
    NP_001136060.1. NM_001142588.1. [Q13952-5]
    NP_001136061.1. NM_001142589.1. [Q13952-4]
    NP_001136062.1. NM_001142590.1. [Q13952-6]
    NP_055038.2. NM_014223.4. [Q13952-2]
    XP_005270950.1. XM_005270893.1. [Q13952-1]
    XP_005270951.1. XM_005270894.1. [Q13952-1]
    XP_005270953.1. XM_005270896.1. [Q13952-3]
    XP_006710724.1. XM_006710661.1. [Q13952-3]
    UniGeneiHs.713051.

    Genome annotation databases

    EnsembliENST00000308733; ENSP00000312617; ENSG00000066136. [Q13952-1]
    ENST00000372651; ENSP00000361734; ENSG00000066136. [Q13952-2]
    ENST00000372652; ENSP00000361736; ENSG00000066136. [Q13952-3]
    ENST00000372653; ENSP00000361737; ENSG00000066136. [Q13952-6]
    ENST00000372654; ENSP00000361738; ENSG00000066136. [Q13952-2]
    ENST00000425457; ENSP00000396620; ENSG00000066136. [Q13952-5]
    ENST00000427410; ENSP00000408315; ENSG00000066136. [Q13952-4]
    ENST00000440226; ENSP00000414299; ENSG00000066136. [Q13952-2]
    ENST00000447388; ENSP00000404427; ENSG00000066136. [Q13952-2]
    ENST00000456393; ENSP00000408867; ENSG00000066136. [Q13952-7]
    GeneIDi4802.
    KEGGihsa:4802.
    UCSCiuc001cfx.4. human. [Q13952-5]
    uc001cfy.4. human. [Q13952-2]
    uc001cgb.3. human. [Q13952-3]
    uc001cgc.3. human. [Q13952-6]
    uc001cge.3. human. [Q13952-1]
    uc010ojn.2. human. [Q13952-4]

    Polymorphism databases

    DMDMi20137773.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U62296 mRNA. Translation: AAC50816.1 .
    U78774 mRNA. Translation: AAC51669.1 .
    Z74792 mRNA. Translation: CAA99055.1 .
    D85425 mRNA. Translation: BAA12818.1 .
    D89986 mRNA. Translation: BAA14051.1 .
    AF191744 mRNA. Translation: AAG28389.1 .
    AK000346 mRNA. Translation: BAA91100.1 .
    AK127677 mRNA. Translation: BAG54549.1 .
    AK300774 mRNA. Translation: BAG62438.1 .
    AK301385 mRNA. Translation: BAG62925.1 .
    BT020081 mRNA. Translation: AAV38884.1 .
    AB208975 mRNA. Translation: BAD92212.1 . Different initiation.
    AL031289 Genomic DNA. No translation available.
    AL354914 , AC119677 Genomic DNA. Translation: CAI16530.1 .
    AL354914 , AC119677 Genomic DNA. Translation: CAI16531.1 .
    AL354914 , AC119677 Genomic DNA. Translation: CAI16532.1 .
    AL354914 , AC119677 Genomic DNA. Translation: CAI16533.1 .
    CH471059 Genomic DNA. Translation: EAX07198.1 .
    CH471059 Genomic DNA. Translation: EAX07201.1 .
    CH471059 Genomic DNA. Translation: EAX07202.1 .
    CH471059 Genomic DNA. Translation: EAX07203.1 .
    BC005003 mRNA. Translation: AAH05003.1 .
    CCDSi CCDS44120.1. [Q13952-5 ]
    CCDS44121.1. [Q13952-7 ]
    CCDS44122.1. [Q13952-6 ]
    CCDS44123.1. [Q13952-4 ]
    CCDS455.1. [Q13952-2 ]
    RefSeqi NP_001136059.1. NM_001142587.1. [Q13952-7 ]
    NP_001136060.1. NM_001142588.1. [Q13952-5 ]
    NP_001136061.1. NM_001142589.1. [Q13952-4 ]
    NP_001136062.1. NM_001142590.1. [Q13952-6 ]
    NP_055038.2. NM_014223.4. [Q13952-2 ]
    XP_005270950.1. XM_005270893.1. [Q13952-1 ]
    XP_005270951.1. XM_005270894.1. [Q13952-1 ]
    XP_005270953.1. XM_005270896.1. [Q13952-3 ]
    XP_006710724.1. XM_006710661.1. [Q13952-3 ]
    UniGenei Hs.713051.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1N1J X-ray 1.67 B 27-120 [» ]
    4AWL X-ray 3.08 C 27-120 [» ]
    ProteinModelPortali Q13952.
    SMRi Q13952. Positions 6-120.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110868. 36 interactions.
    IntActi Q13952. 20 interactions.
    MINTi MINT-249381.

    PTM databases

    PhosphoSitei Q13952.

    Polymorphism databases

    DMDMi 20137773.

    Proteomic databases

    MaxQBi Q13952.
    PaxDbi Q13952.
    PRIDEi Q13952.

    Protocols and materials databases

    DNASUi 4802.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000308733 ; ENSP00000312617 ; ENSG00000066136 . [Q13952-1 ]
    ENST00000372651 ; ENSP00000361734 ; ENSG00000066136 . [Q13952-2 ]
    ENST00000372652 ; ENSP00000361736 ; ENSG00000066136 . [Q13952-3 ]
    ENST00000372653 ; ENSP00000361737 ; ENSG00000066136 . [Q13952-6 ]
    ENST00000372654 ; ENSP00000361738 ; ENSG00000066136 . [Q13952-2 ]
    ENST00000425457 ; ENSP00000396620 ; ENSG00000066136 . [Q13952-5 ]
    ENST00000427410 ; ENSP00000408315 ; ENSG00000066136 . [Q13952-4 ]
    ENST00000440226 ; ENSP00000414299 ; ENSG00000066136 . [Q13952-2 ]
    ENST00000447388 ; ENSP00000404427 ; ENSG00000066136 . [Q13952-2 ]
    ENST00000456393 ; ENSP00000408867 ; ENSG00000066136 . [Q13952-7 ]
    GeneIDi 4802.
    KEGGi hsa:4802.
    UCSCi uc001cfx.4. human. [Q13952-5 ]
    uc001cfy.4. human. [Q13952-2 ]
    uc001cgb.3. human. [Q13952-3 ]
    uc001cgc.3. human. [Q13952-6 ]
    uc001cge.3. human. [Q13952-1 ]
    uc010ojn.2. human. [Q13952-4 ]

    Organism-specific databases

    CTDi 4802.
    GeneCardsi GC01P041159.
    HGNCi HGNC:7806. NFYC.
    HPAi HPA055011.
    MIMi 605344. gene.
    neXtProti NX_Q13952.
    PharmGKBi PA31611.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5208.
    HOGENOMi HOG000231074.
    HOVERGENi HBG002885.
    InParanoidi Q13952.
    KOi K08066.
    OMAi ATNAQQI.
    OrthoDBi EOG7BGHNS.
    PhylomeDBi Q13952.
    TreeFami TF354207.

    Enzyme and pathway databases

    Reactomei REACT_116145. PPARA activates gene expression.
    REACT_147904. Activation of gene expression by SREBF (SREBP).
    REACT_18355. ATF4 activates genes.
    REACT_18423. ATF6-alpha activates chaperone genes.

    Miscellaneous databases

    ChiTaRSi NFYC. human.
    EvolutionaryTracei Q13952.
    GeneWikii NFYC.
    GenomeRNAii 4802.
    NextBioi 18510.
    PROi Q13952.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13952.
    Bgeei Q13952.
    Genevestigatori Q13952.

    Family and domain databases

    Gene3Di 1.10.20.10. 1 hit.
    InterProi IPR003958. CBFA_NFYB_domain.
    IPR009072. Histone-fold.
    IPR027170. NFYC/HAP5_su.
    [Graphical view ]
    PANTHERi PTHR10252:SF8. PTHR10252:SF8. 1 hit.
    Pfami PF00808. CBFD_NFYB_HMF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47113. SSF47113. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Subunit association and DNA binding activity of the heterotrimeric transcription factor NF-Y is regulated by cellular redox."
      Nakshatri H., Bhat-Nakshatri P., Currie R.A.
      J. Biol. Chem. 271:28784-28791(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Isolation and sequence analysis of the cDNA encoding subunit C of human CCAAT-binding transcription factor."
      Dmitrenko V.V., Garifulin O.M., Kavsan V.M.
      Gene 197:161-163(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    4. "Cell cycle-dependent switch of up- and down-regulation of human hsp70 gene expression by interaction between c-Myc and CBF/NF-Y."
      Taira T., Sawai M., Ikeda M., Tamai K., Iguchi-Ariga S.M.M., Ariga H.
      J. Biol. Chem. 274:24270-24279(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    5. "Cloning of a new variant of NFY-C."
      Bringuier P.P., Schalken J.A., Yamasaki H., Giroldi L.A.
      Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 4; 5 AND 6).
      Tissue: Synovium.
    7. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    8. "Homo sapiens protein coding cDNA."
      Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
      Tissue: Brain.
    9. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. "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] (ISOFORM 1).
      Tissue: Brain.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "The NF-YB/NF-YC structure gives insight into DNA binding and transcription regulation by CCAAT factor NF-Y."
      Romier C., Cocchiarella F., Mantovani R., Moras D.
      J. Biol. Chem. 278:1336-1345(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 27-120 IN COMPLEX WITH NF-YB.
    14. "Sequence-specific transcription factor NF-Y displays histone-like DNA binding and H2B-like ubiquitination."
      Nardini M., Gnesutta N., Donati G., Gatta R., Forni C., Fossati A., Vonrhein C., Moras D., Romier C., Bolognesi M., Mantovani R.
      Cell 152:132-143(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.08 ANGSTROMS) OF 27-120 IN COMPLEX WITH NYFA; NYFB AND PROMOTER DNA, SUBUNIT.
    15. Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-165.

    Entry informationi

    Entry nameiNFYC_HUMAN
    AccessioniPrimary (citable) accession number: Q13952
    Secondary accession number(s): B4DUS6
    , B4DW63, D3DPV9, F8VWM3, Q59GY4, Q5T6K8, Q5T6K9, Q5T6L1, Q5TZR6, Q92869, Q9HBX1, Q9NXB5, Q9UM67, Q9UML0, Q9UMT7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2002
    Last sequence update: January 23, 2002
    Last modified: October 1, 2014
    This is version 151 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3