Details of the Target

General Information of Target

Target ID LDTP04981
Target Name Small nuclear ribonucleoprotein Sm D1 (SNRPD1)
Gene Name SNRPD1
Gene ID 6632
Synonyms
Small nuclear ribonucleoprotein Sm D1; Sm-D1; Sm-D autoantigen; snRNP core protein D1
3D Structure
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2D Sequence (FASTA)
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3D Structure (PDB)
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Sequence
MKLVRFLMKLSHETVTIELKNGTQVHGTITGVDVSMNTHLKAVKMTLKNREPVQLETLSI
RGNNIRYFILPDSLPLDTLLVDVEPKVKSKKREAVAGRGRGRGRGRGRGRGRGRGGPRR
Target Bioclass
Other
Family
SnRNP core protein family
Subcellular location
Cytoplasm, cytosol
Function
Plays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome . Component of both the pre-catalytic spliceosome B complex and activated spliceosome C complexes. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs. May act as a charged protein scaffold to promote snRNP assembly or strengthen snRNP-snRNP interactions through non-specific electrostatic contacts with RNA.
Uniprot ID
P62314
Ensemble ID
ENST00000300413.10
HGNC ID
HGNC:11158

Probe(s) Labeling This Target

ABPP Probe
Click To Hide/Show 8 Probe Related to This Target
Probe name Structure Binding Site(Ratio) Interaction ID Ref
P8
 Probe Info  		10.00  LDD0451  [1]
TH211
 Probe Info  		Y67(5.43)  LDD0260  [2]
STPyne
 Probe Info  		K44(10.00)  LDD0277  [3]
AZ-9
 Probe Info  		E51(1.07)  LDD2208  [4]
5E-2FA
 Probe Info  		H12(0.00); H26(0.00)  LDD2235  [5]
ATP probe
 Probe Info  		K41(0.00); K44(0.00)  LDD0199  [6]
m-APA
 Probe Info  		H12(0.00); H26(0.00)  LDD2231  [5]
Acrolein
 Probe Info  		N.A.  LDD0217  [7]
PAL-AfBPP Probe
Click To Hide/Show 1 Probe Related to This Target
Probe name Structure Binding Site(Ratio) Interaction ID Ref
FFF probe13
 Probe Info  		6.39  LDD0475  [8]

Competitor(s) Related to This Target

Competitor ID Name Cell line Binding Site(Ratio) Interaction ID Ref
 LDCM0108  Chloroacetamide HeLa N.A.  LDD0222  [7]
 LDCM0107  IAA HeLa N.A.  LDD0221  [7]
 LDCM0109  NEM HeLa N.A.  LDD0223  [7]

The Interaction Atlas With This Target

The Protein(s) Related To This Target

Transporter and channel
Click To Hide/Show 1 Protein(s) Interacting with This Target
Protein name Family Uniprot ID
Methylosome subunit pICln (CLNS1A) PICln (TC 1.A.47) family P54105
Other
Click To Hide/Show 3 Protein(s) Interacting with This Target
Protein name Family Uniprot ID
Survival motor neuron protein (SMN1; SMN2) SMN family Q16637
Small nuclear ribonucleoprotein Sm D2 (SNRPD2) SnRNP core protein family P62316
Gem-associated protein 6 (GEMIN6) . Q8WXD5

References

1 Comparison of Different Competitive Proteome Profiling Approaches in Target Identification of Covalent Inhibitors. Chembiochem. 2022 Dec 16;23(24):e202200389. doi: 10.1002/cbic.202200389. Epub 2022 Nov 22.
2 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.
3 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
4 2H-Azirine-Based Reagents for Chemoselective Bioconjugation at Carboxyl Residues Inside Live Cells. J Am Chem Soc. 2020 Apr 1;142(13):6051-6059. doi: 10.1021/jacs.9b12116. Epub 2020 Mar 23.
5 Global profiling of functional histidines in live cells using small-molecule photosensitizer and chemical probe relay labelling. Nat Chem. 2024 Jun 4. doi: 10.1038/s41557-024-01545-6. Online ahead of print.
Mass spectrometry data entry: PXD042377
6 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.
7 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.
8 Ligand and Target Discovery by Fragment-Based Screening in Human Cells. Cell. 2017 Jan 26;168(3):527-541.e29. doi: 10.1016/j.cell.2016.12.029. Epub 2017 Jan 19.