Details of the Target

General Information of Target

Target ID LDTP12285
Target Name Charged multivesicular body protein 1a (CHMP1A)
Gene Name CHMP1A
Gene ID 5119
Synonyms
CHMP1; KIAA0047; PCOLN3; PRSM1; Charged multivesicular body protein 1a; Chromatin-modifying protein 1a; CHMP1a; Vacuolar protein sorting-associated protein 46-1; Vps46-1; hVps46-1
3D Structure
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2D Sequence (FASTA)
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3D Structure (PDB)
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Sequence
MNRESFAAGERLVSPAYVRQGCEARRSHEHLIRLLLEKGKCPENGWDESTLELFLHELAI
MDSNNFLGNCGVGEREGRVASALVARRHYRFIHGIGRSGDISAVQPKAAGSSLLNKITNS
LVLDIIKLAGVHTVANCFVVPMATGMSLTLCFLTLRHKRPKAKYIIWPRIDQKSCFKSMI
TAGFEPVVIENVLEGDELRTDLKAVEAKVQELGPDCILCIHSTTSCFAPRVPDRLEELAV
ICANYDIPHIVNNAYGVQSSKCMHLIQQGARVGRIDAFVQSLDKNFMVPVGGAIIAGFND
SFIQEISKMYPGRASASPSLDVLITLLSLGSNGYKKLLKERKEMFSYLSNQIKKLSEAYN
ERLLHTPHNPISLAMTLKTLDEHRDKAVTQLGSMLFTRQVSGARVVPLGSMQTVSGYTFR
GFMSHTNNYPCAYLNAASAIGMKMQDVDLFIKRLDRCLKAVRKERSKESDDNYDKTEDVD
IEEMALKLDNVLLDTYQDASS
Target Bioclass
Other
Family
SNF7 family
Subcellular location
Cytoplasm
Function
Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Involved in cytokinesis. Involved in recruiting VPS4A and/or VPS4B to the midbody of dividing cells. May also be involved in chromosome condensation. Targets the Polycomb group (PcG) protein BMI1/PCGF4 to regions of condensed chromatin. May play a role in stable cell cycle progression and in PcG gene silencing.
Uniprot ID
Q9HD42
Ensemble ID
ENST00000397901.8
HGNC ID
HGNC:8740

Target Site Mutations in Different Cell Lines

Cell line Mutation details Probe for labeling this protein in this cell
KASUMI2 SNV: p.K24Q .
MOLT4 SNV: p.D25N IA-alkyne    Probe Info 

Probe(s) Labeling This Target

ABPP Probe
Click To Hide/Show 18 Probe Related to This Target
Probe name Structure Binding Site(Ratio) Interaction ID Ref
m-APA
 Probe Info  		14.93  LDD0402  [1]
STPyne
 Probe Info  		K107(3.27); K13(6.20); K17(5.88); K83(4.72)  LDD0277  [2]
BTD
 Probe Info  		C44(6.50)  LDD1699  [3]
Probe 1
 Probe Info  		Y48(57.70)  LDD3495  [4]
DBIA
 Probe Info  		C44(0.87)  LDD3316  [5]
HHS-475
 Probe Info  		Y48(0.87)  LDD0264  [6]
Acrolein
 Probe Info  		N.A.  LDD0222  [7]
ATP probe
 Probe Info  		K13(0.00); K40(0.00)  LDD0199  [8]
IA-alkyne
 Probe Info  		N.A.  LDD0162  [9]
ENE
 Probe Info  		N.A.  LDD0006  [10]
IPM
 Probe Info  		N.A.  LDD0005  [10]
SF
 Probe Info  		N.A.  LDD0028  [11]
TFBX
 Probe Info  		N.A.  LDD0148  [12]
Phosphinate-6
 Probe Info  		N.A.  LDD0018  [13]
1c-yne
 Probe Info  		N.A.  LDD0228  [14]
Methacrolein
 Probe Info  		N.A.  LDD0218  [7]
AOyne
 Probe Info  		15.00  LDD0443  [15]
HHS-465
 Probe Info  		N.A.  LDD2240  [16]
PAL-AfBPP Probe
Click To Hide/Show 1 Probe Related to This Target
Probe name Structure Binding Site(Ratio) Interaction ID Ref
C361
 Probe Info  		17.51  LDD2022  [17]

Competitor(s) Related to This Target

Competitor ID Name Cell line Binding Site(Ratio) Interaction ID Ref
 LDCM0548  1-(4-(Benzo[d][1,3]dioxol-5-ylmethyl)piperazin-1-yl)-2-nitroethan-1-one MDA-MB-231 C44(1.07)  LDD2142  [3]
 LDCM0519  1-(6-methoxy-3,4-dihydroquinolin-1(2H)-yl)-2-nitroethan-1-one MDA-MB-231 C44(0.93)  LDD2112  [3]
 LDCM0524  2-Cyano-N-(2-morpholin-4-yl-ethyl)-acetamide MDA-MB-231 C44(1.00)  LDD2117  [3]
 LDCM0558  2-Cyano-N-phenylacetamide MDA-MB-231 C44(1.25)  LDD2152  [3]
 LDCM0510  3-(4-(Hydroxydiphenylmethyl)piperidin-1-yl)-3-oxopropanenitrile MDA-MB-231 C44(0.86)  LDD2103  [3]
 LDCM0545  Acetamide MDA-MB-231 C44(0.29)  LDD2138  [3]
 LDCM0520  AKOS000195272 MDA-MB-231 C44(0.63)  LDD2113  [3]
 LDCM0156  Aniline NCI-H1299 12.40  LDD0403  [1]
 LDCM0108  Chloroacetamide HeLa N.A.  LDD0222  [7]
 LDCM0198  Dimethyl Fumarate(DMF) T cell C44(11.88)  LDD0513  [18]
 LDCM0116  HHS-0101 DM93 Y48(0.87)  LDD0264  [6]
 LDCM0117  HHS-0201 DM93 Y48(0.83)  LDD0265  [6]
 LDCM0118  HHS-0301 DM93 Y48(0.91)  LDD0266  [6]
 LDCM0119  HHS-0401 DM93 Y48(0.86)  LDD0267  [6]
 LDCM0120  HHS-0701 DM93 Y48(0.81)  LDD0268  [6]
 LDCM0022  KB02 T cell C44(5.12)  LDD1703  [18]
 LDCM0023  KB03 MDA-MB-231 C44(1.71)  LDD1701  [3]
 LDCM0024  KB05 MEL167 C44(0.87)  LDD3316  [5]
 LDCM0509  N-(4-bromo-3,5-dimethylphenyl)-2-nitroacetamide MDA-MB-231 C44(0.99)  LDD2102  [3]
 LDCM0528  N-(4-bromophenyl)-2-cyano-N-phenylacetamide MDA-MB-231 C44(0.57)  LDD2121  [3]
 LDCM0496  Nucleophilic fragment 11a MDA-MB-231 C44(0.80)  LDD2089  [3]
 LDCM0499  Nucleophilic fragment 12b MDA-MB-231 C44(0.77)  LDD2092  [3]
 LDCM0500  Nucleophilic fragment 13a MDA-MB-231 C44(0.86)  LDD2093  [3]
 LDCM0504  Nucleophilic fragment 15a MDA-MB-231 C44(0.71)  LDD2097  [3]
 LDCM0506  Nucleophilic fragment 16a MDA-MB-231 C44(0.70)  LDD2099  [3]
 LDCM0507  Nucleophilic fragment 16b MDA-MB-231 C44(1.00)  LDD2100  [3]
 LDCM0508  Nucleophilic fragment 17a MDA-MB-231 C44(0.97)  LDD2101  [3]
 LDCM0511  Nucleophilic fragment 18b MDA-MB-231 C44(0.86)  LDD2104  [3]
 LDCM0512  Nucleophilic fragment 19a MDA-MB-231 C44(1.18)  LDD2105  [3]
 LDCM0513  Nucleophilic fragment 19b MDA-MB-231 C44(0.81)  LDD2106  [3]
 LDCM0514  Nucleophilic fragment 20a MDA-MB-231 C44(0.76)  LDD2107  [3]
 LDCM0515  Nucleophilic fragment 20b MDA-MB-231 C44(0.66)  LDD2108  [3]
 LDCM0516  Nucleophilic fragment 21a MDA-MB-231 C44(0.62)  LDD2109  [3]
 LDCM0518  Nucleophilic fragment 22a MDA-MB-231 C44(0.82)  LDD2111  [3]
 LDCM0521  Nucleophilic fragment 23b MDA-MB-231 C44(0.89)  LDD2114  [3]
 LDCM0522  Nucleophilic fragment 24a MDA-MB-231 C44(0.41)  LDD2115  [3]
 LDCM0527  Nucleophilic fragment 26b MDA-MB-231 C44(0.98)  LDD2120  [3]
 LDCM0530  Nucleophilic fragment 28a MDA-MB-231 C44(0.61)  LDD2123  [3]
 LDCM0532  Nucleophilic fragment 29a MDA-MB-231 C44(0.74)  LDD2125  [3]
 LDCM0533  Nucleophilic fragment 29b MDA-MB-231 C44(1.92)  LDD2126  [3]
 LDCM0534  Nucleophilic fragment 30a MDA-MB-231 C44(0.92)  LDD2127  [3]
 LDCM0536  Nucleophilic fragment 31 MDA-MB-231 C44(0.53)  LDD2129  [3]
 LDCM0540  Nucleophilic fragment 35 MDA-MB-231 C44(0.40)  LDD2133  [3]
 LDCM0541  Nucleophilic fragment 36 MDA-MB-231 C44(0.39)  LDD2134  [3]
 LDCM0543  Nucleophilic fragment 38 MDA-MB-231 C44(0.84)  LDD2136  [3]
 LDCM0544  Nucleophilic fragment 39 MDA-MB-231 C44(0.88)  LDD2137  [3]
 LDCM0211  Nucleophilic fragment 3b MDA-MB-231 C44(1.35)  LDD1700  [3]
 LDCM0547  Nucleophilic fragment 41 MDA-MB-231 C44(0.70)  LDD2141  [3]
 LDCM0549  Nucleophilic fragment 43 MDA-MB-231 C44(1.13)  LDD2143  [3]
 LDCM0550  Nucleophilic fragment 5a MDA-MB-231 C44(4.36)  LDD2144  [3]
 LDCM0552  Nucleophilic fragment 6a MDA-MB-231 C44(0.76)  LDD2146  [3]
 LDCM0554  Nucleophilic fragment 7a MDA-MB-231 C44(0.43)  LDD2148  [3]
 LDCM0559  Nucleophilic fragment 9b MDA-MB-231 C44(2.01)  LDD2153  [3]

The Interaction Atlas With This Target

The Protein(s) Related To This Target

Enzyme
Click To Hide/Show 7 Protein(s) Interacting with This Target
Protein name Family Uniprot ID
Vacuolar protein sorting-associated protein 4A (VPS4A) AAA ATPase family Q9UN37
Vacuolar protein sorting-associated protein 4B (VPS4B) AAA ATPase family O75351
Ubiquitin carboxyl-terminal hydrolase 8 (USP8) Peptidase C19 family P40818
STAM-binding protein (STAMBP) Peptidase M67C family O95630
Proteasome subunit alpha type-1 (PSMA1) Peptidase T1A family P25786
Tyrosine-protein kinase Yes (YES1) Tyr protein kinase family P07947
Thioredoxin, mitochondrial (TXN2) Thioredoxin family Q99757
Transporter and channel
Click To Hide/Show 3 Protein(s) Interacting with This Target
Protein name Family Uniprot ID
Huntingtin (HTT) Huntingtin family P42858
Alpha-synuclein (SNCA) Synuclein family P37840
Syntenin-1 (SDCBP) . O00560
Other
Click To Hide/Show 6 Protein(s) Interacting with This Target
Protein name Family Uniprot ID
DNA damage-inducible transcript 4-like protein (DDIT4L) DDIT4 family Q96D03
Golgi reassembly-stacking protein 2 (GORASP2) GORASP family Q9H8Y8
Charged multivesicular body protein 1a (CHMP1A) SNF7 family Q9HD42
Vacuolar protein sorting-associated protein VTA1 homolog (VTA1) VTA1 family Q9NP79
MIT domain-containing protein 1 (MITD1) . Q8WV92
Uncharacterized protein C14orf119 (C14orf119) . Q9NWQ9

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 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
4 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.
5 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
6 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.
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 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.
9 SP3-FAIMS Chemoproteomics for High-Coverage Profiling of the Human Cysteinome*. Chembiochem. 2021 May 14;22(10):1841-1851. doi: 10.1002/cbic.202000870. Epub 2021 Feb 18.
Mass spectrometry data entry: PXD023056 , PXD023059 , PXD023058 , PXD023057 , PXD023060
10 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
11 Solid Phase Synthesis of Fluorosulfate Containing Macrocycles for Chemoproteomic Workflows. bioRxiv [Preprint]. 2023 Feb 18:2023.02.17.529022. doi: 10.1101/2023.02.17.529022.
Mass spectrometry data entry: PXD039931
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 DFT-Guided Discovery of Ethynyl-Triazolyl-Phosphinates as Modular Electrophiles for Chemoselective Cysteine Bioconjugation and Profiling. Angew Chem Int Ed Engl. 2022 Oct 10;61(41):e202205348. doi: 10.1002/anie.202205348. Epub 2022 Aug 22.
Mass spectrometry data entry: PXD033004
14 Tunable Amine-Reactive Electrophiles for Selective Profiling of Lysine. Angew Chem Int Ed Engl. 2022 Jan 26;61(5):e202112107. doi: 10.1002/anie.202112107. Epub 2021 Dec 16.
15 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.
16 Global profiling identifies a stress-responsive tyrosine site on EDC3 regulating biomolecular condensate formation. Cell Chem Biol. 2022 Dec 15;29(12):1709-1720.e7. doi: 10.1016/j.chembiol.2022.11.008. Epub 2022 Dec 6.
Mass spectrometry data entry: PXD038010
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 An Activity-Guided Map of Electrophile-Cysteine Interactions in Primary Human T Cells. Cell. 2020 Aug 20;182(4):1009-1026.e29. doi: 10.1016/j.cell.2020.07.001. Epub 2020 Jul 29.