General Information of Target

Target ID LDTP03240
Target Name Nuclear transcription factor Y subunit alpha (NFYA)
Gene Name NFYA
Gene ID 4800
Synonyms
Nuclear transcription factor Y subunit alpha; CAAT box DNA-binding protein subunit A; Nuclear transcription factor Y subunit A; NF-YA
3D Structure
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2D Sequence (FASTA)
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3D Structure (PDB)
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Sequence
MEQYTANSNSSTEQIVVQAGQIQQQQQGGVTAVQLQTEAQVASASGQQVQTLQVVQGQPL
MVQVSGGQLITSTGQPIMVQAVPGGQGQTIMQVPVSGTQGLQQIQLVPPGQIQIQGGQAV
QVQGQQGQTQQIIIQQPQTAVTAGQTQTQQQIAVQGQQVAQTAEGQTIVYQPVNADGTIL
QQVTVPVSGMITIPAASLAGAQIVQTGANTNTTSSGQGTVTVTLPVAGNVVNSGGMVMMV
PGAGSVPAIQRIPLPGAEMLEEEPLYVNAKQYHRILKRRQARAKLEAEGKIPKERRKYLH
ESRHRHAMARKRGEGGRFFSPKEKDSPHMQDPNQADEEAMTQIIRVS
Target Bioclass
Transcription factor
Family
NFYA/HAP2 subunit family
Subcellular location
Nucleus
Function
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. NF-YA positively regulates the transcription of the core clock component BMAL1.
Uniprot ID
P23511
Ensemble ID
ENST00000341376.11
HGNC ID
HGNC:7804

Target Site Mutations in Different Cell Lines

Cell line Mutation details Probe for labeling this protein in this cell
HCT15 SNV: p.Q34K .
HEC1 SNV: p.K322N .
HEC1B SNV: p.K322N .
NCIH446 SNV: p.R312P .

Probe(s) Labeling This Target

ABPP Probe
Click To Hide/Show 5 Probe Related to This Target
Probe name Structure Binding Site(Ratio) Interaction ID Ref
TH211
 Probe Info 
Y298(5.73)  LDD0257  [1]
HHS-475
 Probe Info 
Y298(0.05)  LDD0264  [2]
HHS-465
 Probe Info 
Y298(0.96)  LDD2237  [3]
ATP probe
 Probe Info 
N.A.  LDD0199  [4]
HHS-482
 Probe Info 
Y298(1.07)  LDD2239  [3]

Competitor(s) Related to This Target

Competitor ID Name Cell line Binding Site(Ratio) Interaction ID Ref
 LDCM0116  HHS-0101 DM93 Y298(0.05)  LDD0264  [2]
 LDCM0117  HHS-0201 DM93 Y298(0.11)  LDD0265  [2]
 LDCM0119  HHS-0401 DM93 Y298(0.22)  LDD0267  [2]

The Interaction Atlas With This Target

The Protein(s) Related To This Target

Enzyme
Click To Hide/Show 1 Protein(s) Interacting with This Target
Protein name Family Uniprot ID
Casein kinase II subunit alpha (CSNK2A1) Ser/Thr protein kinase family P68400
Transporter and channel
Click To Hide/Show 1 Protein(s) Interacting with This Target
Protein name Family Uniprot ID
Cellular tumor antigen p53 (TP53) P53 family P04637
Transcription factor
Click To Hide/Show 5 Protein(s) Interacting with This Target
Protein name Family Uniprot ID
Vascular endothelial zinc finger 1 (VEZF1) Krueppel C2H2-type zinc-finger protein family Q14119
Nuclear transcription factor Y subunit beta (NFYB) NFYB/HAP3 subunit family P25208
Nuclear transcription factor Y subunit gamma (NFYC) NFYC/HAP5 subunit family Q13952
Pogo transposable element with ZNF domain (POGZ) . Q7Z3K3
Transcriptional regulator QRICH1 (QRICH1) . Q2TAL8
Other
Click To Hide/Show 8 Protein(s) Interacting with This Target
Protein name Family Uniprot ID
Ataxin-1 (ATXN1) ATXN1 family P54253
Segment polarity protein dishevelled homolog DVL-3 (DVL3) DSH family Q92997
Putative RNA-binding protein Luc7-like 2 (LUC7L2) Luc7 family Q9Y383
Serine/arginine-rich splicing factor 1 (SRSF1) Splicing factor SR family Q07955
Transcription initiation factor IIA subunit 1 (GTF2A1) TFIIA subunit 1 family P52655
Amyloid protein-binding protein 2 (APPBP2) . Q92624
Ubiquitin-like protein 5 (UBL5) . Q9BZL1
Zinc finger CCCH domain-containing protein 10 (ZC3H10) . Q96K80

References

1 Chemoproteomic profiling of kinases in live cells using electrophilic sulfonyl triazole probes. Chem Sci. 2021 Jan 21;12(9):3295-3307. doi: 10.1039/d0sc06623k.
2 Discovery of a Cell-Active SuTEx Ligand of Prostaglandin Reductase 2. Chembiochem. 2021 Jun 15;22(12):2134-2139. doi: 10.1002/cbic.202000879. Epub 2021 Apr 29.
3 Global targeting of functional tyrosines using sulfur-triazole exchange chemistry. Nat Chem Biol. 2020 Feb;16(2):150-159. doi: 10.1038/s41589-019-0404-5. Epub 2019 Nov 25.
4 Targeted Proteomic Approaches for Proteome-Wide Characterizations of the AMP-Binding Capacities of Kinases. J Proteome Res. 2022 Aug 5;21(8):2063-2070. doi: 10.1021/acs.jproteome.2c00225. Epub 2022 Jul 12.