General Information of Target

Target ID LDTP13305
Target Name SAP30-binding protein (SAP30BP)
Gene Name SAP30BP
Gene ID 29115
Synonyms
HCNGP; HTRG; HTRP; SAP30-binding protein; Transcriptional regulator protein HCNGP
3D Structure
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2D Sequence (FASTA)
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3D Structure (PDB)
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Sequence
MSRGPEEVNRLTESTYRNVMEQFNPGLRNLINLGKNYEKAVNAMILAGKAYYDGVAKIGE
IATGSPVSTELGHVLIEISSTHKKLNESLDENFKKFHKEIIHELEKKIELDVKYMNATLK
RYQTEHKNKLESLEKSQAELKKIRRKSQGSRNALKYEHKEIEYVETVTSRQSEIQKFIAD
GCKEALLEEKRRFCFLVDKHCGFANHIHYYHLQSAELLNSKLPRWQETCVDAIKVPEKIM
NMIEEIKTPASTPVSGTPQASPMIERSNVVRKDYDTLSKCSPKMPPAPSGRAYTSPLIDM
FNNPATAAPNSQRVNNSTGTSEDPSLQRSVSVATGLNMMKKQKVKTIFPHTAGSNKTLLS
FAQGDVITLLIPEEKDGWLYGEHDVSKARGWFPSSYTKLLEENETEAVTVPTPSPTPVRS
ISTVNLSENSSVVIPPPDYLECLSMGAAADRRADSARTTSTFKAPASKPETAAPNDANGT
AKPPFLSGENPFATVKLRPTVTNDRSAPIIR
Target Bioclass
Transcription factor
Family
HCNGP family
Subcellular location
Nucleus
Function
Plays a role in transcriptional repression by promoting histone deacetylase activity, leading to deacetylation of histone H3. May be involved in the regulation of beta-2-microglobulin genes.; (Microbial infection) Involved in transcriptional repression of HHV-1 genes TK and gC.
Uniprot ID
Q9UHR5
Ensemble ID
ENST00000355423.7
HGNC ID
HGNC:30785

Target Site Mutations in Different Cell Lines

Cell line Mutation details Probe for labeling this protein in this cell
HCT15 SNV: p.G3R .
JURKAT SNV: p.D89E Compound 10    Probe Info 
MCC13 SNV: p.S104F DBIA    Probe Info 

Probe(s) Labeling This Target

ABPP Probe
Click To Hide/Show 22 Probe Related to This Target
Probe name Structure Binding Site(Ratio) Interaction ID Ref
m-APA
 Probe Info 
12.55  LDD0402  [1]
STPyne
 Probe Info 
K228(5.88)  LDD0277  [2]
Probe 1
 Probe Info 
Y46(14.19); Y61(35.51); Y151(16.72)  LDD3495  [3]
DBIA
 Probe Info 
C127(2.26)  LDD3319  [4]
BTD
 Probe Info 
C127(0.59)  LDD2095  [5]
AHL-Pu-1
 Probe Info 
C172(6.92)  LDD0169  [6]
HHS-475
 Probe Info 
Y151(1.05)  LDD0264  [7]
HHS-465
 Probe Info 
Y151(10.00)  LDD2237  [8]
ATP probe
 Probe Info 
N.A.  LDD0199  [9]
IA-alkyne
 Probe Info 
N.A.  LDD0036  [10]
Lodoacetamide azide
 Probe Info 
N.A.  LDD0037  [10]
NAIA_4
 Probe Info 
C127(0.00); C172(0.00)  LDD2226  [11]
TFBX
 Probe Info 
N.A.  LDD0027  [12]
WYneN
 Probe Info 
N.A.  LDD0021  [13]
Compound 10
 Probe Info 
N.A.  LDD2216  [14]
Compound 11
 Probe Info 
N.A.  LDD2213  [14]
ENE
 Probe Info 
N.A.  LDD0006  [13]
IPM
 Probe Info 
N.A.  LDD0005  [13]
NPM
 Probe Info 
N.A.  LDD0016  [13]
Acrolein
 Probe Info 
N.A.  LDD0217  [15]
AOyne
 Probe Info 
15.00  LDD0443  [16]
NAIA_5
 Probe Info 
C127(0.00); C172(0.00)  LDD2223  [11]
PAL-AfBPP Probe
Click To Hide/Show 2 Probe Related to This Target
Probe name Structure Binding Site(Ratio) Interaction ID Ref
C040
 Probe Info 
6.87  LDD1740  [17]
C041
 Probe Info 
5.66  LDD1741  [17]

Competitor(s) Related to This Target

Competitor ID Name Cell line Binding Site(Ratio) Interaction ID Ref
 LDCM0502  1-(Cyanoacetyl)piperidine MDA-MB-231 C127(0.59)  LDD2095  [5]
 LDCM0524  2-Cyano-N-(2-morpholin-4-yl-ethyl)-acetamide MDA-MB-231 C127(1.27)  LDD2117  [5]
 LDCM0539  3-(4-Isopropylpiperazin-1-yl)-3-oxopropanenitrile MDA-MB-231 C127(0.47)  LDD2132  [5]
 LDCM0026  4SU-RNA+native RNA HEK-293T C172(6.92)  LDD0169  [6]
 LDCM0156  Aniline NCI-H1299 9.73  LDD0403  [1]
 LDCM0020  ARS-1620 HCC44 C172(1.07)  LDD2171  [18]
 LDCM0108  Chloroacetamide HeLa N.A.  LDD0222  [15]
 LDCM0632  CL-Sc Hep-G2 C127(1.34); C127(1.28); C172(0.98)  LDD2227  [11]
 LDCM0213  Electrophilic fragment 2 MDA-MB-231 C127(1.81)  LDD1702  [5]
 LDCM0625  F8 Ramos C127(1.18)  LDD2187  [19]
 LDCM0572  Fragment10 Ramos C127(1.78)  LDD2189  [19]
 LDCM0573  Fragment11 Ramos C127(20.00)  LDD2190  [19]
 LDCM0574  Fragment12 Ramos C127(1.52)  LDD2191  [19]
 LDCM0575  Fragment13 Ramos C127(2.07)  LDD2192  [19]
 LDCM0576  Fragment14 Ramos C127(1.04)  LDD2193  [19]
 LDCM0579  Fragment20 Ramos C127(1.85)  LDD2194  [19]
 LDCM0580  Fragment21 Ramos C127(1.89)  LDD2195  [19]
 LDCM0582  Fragment23 Ramos C127(0.90)  LDD2196  [19]
 LDCM0578  Fragment27 Ramos C127(5.39)  LDD2197  [19]
 LDCM0586  Fragment28 Ramos C127(1.06)  LDD2198  [19]
 LDCM0588  Fragment30 Ramos C127(1.32)  LDD2199  [19]
 LDCM0589  Fragment31 Ramos C127(1.50)  LDD2200  [19]
 LDCM0590  Fragment32 Ramos C127(2.13)  LDD2201  [19]
 LDCM0468  Fragment33 Ramos C127(1.41)  LDD2202  [19]
 LDCM0596  Fragment38 Ramos C127(1.79)  LDD2203  [19]
 LDCM0566  Fragment4 Ramos C127(0.86)  LDD2184  [19]
 LDCM0610  Fragment52 Ramos C127(2.03)  LDD2204  [19]
 LDCM0614  Fragment56 Ramos C127(1.40)  LDD2205  [19]
 LDCM0569  Fragment7 Ramos C127(0.89)  LDD2186  [19]
 LDCM0571  Fragment9 Ramos C127(1.53)  LDD2188  [19]
 LDCM0116  HHS-0101 DM93 Y151(1.05)  LDD0264  [7]
 LDCM0118  HHS-0301 DM93 Y151(0.90)  LDD0266  [7]
 LDCM0119  HHS-0401 DM93 Y151(1.67)  LDD0267  [7]
 LDCM0120  HHS-0701 DM93 Y151(2.11)  LDD0268  [7]
 LDCM0022  KB02 HEK-293T C127(0.98); C172(0.95)  LDD1492  [20]
 LDCM0023  KB03 HEK-293T C127(0.96); C172(1.07)  LDD1497  [20]
 LDCM0024  KB05 MEWO C127(2.26)  LDD3319  [4]
 LDCM0507  Nucleophilic fragment 16b MDA-MB-231 C127(0.45)  LDD2100  [5]
 LDCM0530  Nucleophilic fragment 28a MDA-MB-231 C127(1.20)  LDD2123  [5]
 LDCM0547  Nucleophilic fragment 41 MDA-MB-231 C127(0.71)  LDD2141  [5]
 LDCM0021  THZ1 HCT 116 C172(1.07)  LDD2173  [18]

The Interaction Atlas With This Target

The Protein(s) Related To This Target

Transcription factor
Click To Hide/Show 1 Protein(s) Interacting with This Target
Protein name Family Uniprot ID
THAP domain-containing protein 1 (THAP1) THAP1 family Q9NVV9
Other
Click To Hide/Show 6 Protein(s) Interacting with This Target
Protein name Family Uniprot ID
cAMP-dependent protein kinase type I-beta regulatory subunit (PRKAR1B) CAMP-dependent kinase regulatory chain family P31321
Cyclin-L1 (CCNL1) Cyclin family Q9UK58
Golgin subfamily A member 2 (GOLGA2) GOLGA2 family Q08379
Poly(U)-binding-splicing factor PUF60 (PUF60) RRM half pint family Q9UHX1
Tuftelin-interacting protein 11 (TFIP11) TFP11/STIP family Q9UBB9
Four and a half LIM domains protein 3 (FHL3) . Q13643

References

1 Quantitative and Site-Specific Chemoproteomic Profiling of Targets of Acrolein. Chem Res Toxicol. 2019 Mar 18;32(3):467-473. doi: 10.1021/acs.chemrestox.8b00343. Epub 2019 Jan 15.
2 A Paal-Knorr agent for chemoproteomic profiling of targets of isoketals in cells. Chem Sci. 2021 Oct 15;12(43):14557-14563. doi: 10.1039/d1sc02230j. eCollection 2021 Nov 10.
Mass spectrometry data entry: PXD028270
3 An Azo Coupling-Based Chemoproteomic Approach to Systematically Profile the Tyrosine Reactivity in the Human Proteome. Anal Chem. 2021 Jul 27;93(29):10334-10342. doi: 10.1021/acs.analchem.1c01935. Epub 2021 Jul 12.
4 DrugMap: A quantitative pan-cancer analysis of cysteine ligandability. Cell. 2024 May 9;187(10):2536-2556.e30. doi: 10.1016/j.cell.2024.03.027. Epub 2024 Apr 22.
Mass spectrometry data entry: PXD047840
5 Nucleophilic covalent ligand discovery for the cysteine redoxome. Nat Chem Biol. 2023 Nov;19(11):1309-1319. doi: 10.1038/s41589-023-01330-5. Epub 2023 May 29.
Mass spectrometry data entry: PXD039908 , PXD029761
6 Chemoproteomic capture of RNA binding activity in living cells. Nat Commun. 2023 Oct 7;14(1):6282. doi: 10.1038/s41467-023-41844-z.
Mass spectrometry data entry: PXD044625
7 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.
8 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.
9 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.
10 Enhancing Cysteine Chemoproteomic Coverage through Systematic Assessment of Click Chemistry Product Fragmentation. Anal Chem. 2022 Mar 8;94(9):3800-3810. doi: 10.1021/acs.analchem.1c04402. Epub 2022 Feb 23.
Mass spectrometry data entry: PXD028853
11 N-Acryloylindole-alkyne (NAIA) enables imaging and profiling new ligandable cysteines and oxidized thiols by chemoproteomics. Nat Commun. 2023 Jun 15;14(1):3564. doi: 10.1038/s41467-023-39268-w.
Mass spectrometry data entry: PXD041264
12 Chemoproteomic Profiling by Cysteine Fluoroalkylation Reveals Myrocin G as an Inhibitor of the Nonhomologous End Joining DNA Repair Pathway. J Am Chem Soc. 2021 Dec 8;143(48):20332-20342. doi: 10.1021/jacs.1c09724. Epub 2021 Nov 24.
Mass spectrometry data entry: PXD029255
13 A modification-centric assessment tool for the performance of chemoproteomic probes. Nat Chem Biol. 2022 Aug;18(8):904-912. doi: 10.1038/s41589-022-01074-8. Epub 2022 Jul 21.
Mass spectrometry data entry: PXD027758 , PXD027755 , PXD027760 , PXD027762 , PXD027756 , PXD027591 , PXD007149 , PXD030064 , PXD032392 , PXD027789 , PXD027767 , PXD027764
14 Multiplexed CuAAC Suzuki-Miyaura Labeling for Tandem Activity-Based Chemoproteomic Profiling. Anal Chem. 2021 Feb 2;93(4):2610-2618. doi: 10.1021/acs.analchem.0c04726. Epub 2021 Jan 20.
Mass spectrometry data entry: PXD022279
15 ACR-Based Probe for the Quantitative Profiling of Histidine Reactivity in the Human Proteome. J Am Chem Soc. 2023 Mar 8;145(9):5252-5260. doi: 10.1021/jacs.2c12653. Epub 2023 Feb 27.
16 Chemoproteomic profiling of targets of lipid-derived electrophiles by bioorthogonal aminooxy probe. Redox Biol. 2017 Aug;12:712-718. doi: 10.1016/j.redox.2017.04.001. Epub 2017 Apr 5.
17 Large-scale chemoproteomics expedites ligand discovery and predicts ligand behavior in cells. Science. 2024 Apr 26;384(6694):eadk5864. doi: 10.1126/science.adk5864. Epub 2024 Apr 26.
Mass spectrometry data entry: PXD041587
18 Reimagining high-throughput profiling of reactive cysteines for cell-based screening of large electrophile libraries. Nat Biotechnol. 2021 May;39(5):630-641. doi: 10.1038/s41587-020-00778-3. Epub 2021 Jan 4.
19 Site-specific quantitative cysteine profiling with data-independent acquisition-based mass spectrometry. Methods Enzymol. 2023;679:295-322. doi: 10.1016/bs.mie.2022.07.037. Epub 2022 Sep 7.
Mass spectrometry data entry: PXD027578
20 Accelerating multiplexed profiling of protein-ligand interactions: High-throughput plate-based reactive cysteine profiling with minimal input. Cell Chem Biol. 2024 Mar 21;31(3):565-576.e4. doi: 10.1016/j.chembiol.2023.11.015. Epub 2023 Dec 19.
Mass spectrometry data entry: PXD044402