PAN3

gene
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Summary

PAN3 (poly(A) specific ribonuclease subunit PAN3, HGNC:29991) is a protein-coding gene on chromosome 13q12.2, encoding PAN2-PAN3 deadenylation complex subunit PAN3 (Q58A45). Regulatory subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in general and miRNA-mediated mRNA turnover.

Contributes to poly(A)-specific ribonuclease activity. Predicted to be involved in nuclear-transcribed mRNA poly(A) tail shortening. Predicted to act upstream of or within deadenylation-dependent decapping of nuclear-transcribed mRNA; positive regulation of cytoplasmic mRNA processing body assembly; and protein targeting. Part of PAN complex.

Source: NCBI Gene 255967 — RefSeq curated summary.

At a glance

  • Clinical variants (ClinVar): 99 total — 1 likely-pathogenic
  • Druggable target: yes
  • MANE Select transcript: NM_175854

Identifiers

Gene identifiers

FieldValue
HGNC IDHGNC:29991
Approved symbolPAN3
Namepoly(A) specific ribonuclease subunit PAN3
Location13q12.2
Locus typegene with protein product
StatusApproved
Ensembl geneENSG00000152520
Ensembl biotypeprotein_coding
OMIM617448
Entrez255967

Gene structure

Transcript identifiers

Ensembl transcripts: 5 — 3 protein_coding, 1 protein_coding_CDS_not_defined, 1 retained_intron

ENST00000380958, ENST00000399613, ENST00000483842, ENST00000503791, ENST00000913194

RefSeq mRNA: 1 — MANE Select: NM_175854 NM_175854

CCDS: CCDS9329

Canonical transcript exons

ENST00000380958 — 19 exons

ExonStartEnd
ENSE000015968482828131528281379
ENSE000016346032828798428288122
ENSE000016453202828041228280541
ENSE000017654802827198128272071
ENSE000017670772829238228295335
ENSE000017857232827723728277376
ENSE000034647172826140128261458
ENSE000034700082826730028267401
ENSE000034862772817427228174393
ENSE000034919182822023128220378
ENSE000035433972826044728260551
ENSE000035468752817649328176559
ENSE000035558112819718528197346
ENSE000035728432813854528139087
ENSE000035872442827070128270866
ENSE000036022042817786528177935
ENSE000036483502826709528267211
ENSE000036552212825629228256539
ENSE000036732712826671528266876

Expression profiles

Bgee: expression breadth ubiquitous, 256 present calls, max score 99.65.

FANTOM5 (CAGE): breadth ubiquitous, TPM avg 22.3087 / max 375.8485, expressed in 1805 samples.

FANTOM5 promoters (11 alternative TSS)

Promoter IDTPM avgSamples expressed
13455212.38461750
1345585.74021639
1345591.7566765
1345601.3334895
1345570.2625117
1345560.2581116
1345530.199480
1345700.172263
1345550.115742
1345540.050814

Top tissues by expression

256 total, by Bgee expression score (0-100, higher = more expressed):

TissueAnatomy IDExpression scoreQuality
pancreatic ductal cellCL:000207999.65gold quality
oviduct epitheliumUBERON:000480499.17gold quality
secondary oocyteCL:000065599.05gold quality
epithelial cell of pancreasCL:000008398.58gold quality
thymusUBERON:000237098.33gold quality
oocyteCL:000002398.20gold quality
trabecular bone tissueUBERON:000248397.33gold quality
epithelium of nasopharynxUBERON:000195197.21gold quality
cerebellar vermisUBERON:000472097.16gold quality
upper arm skinUBERON:000426397.15gold quality
ileal mucosaUBERON:000033196.97gold quality
germinal epithelium of ovaryUBERON:000130496.97gold quality
corpus epididymisUBERON:000435996.76gold quality
parietal pleuraUBERON:000240096.73gold quality
upper leg skinUBERON:000426296.59gold quality
seminal vesicleUBERON:000099896.37gold quality
caput epididymisUBERON:000435896.33gold quality
nasal cavity epitheliumUBERON:000538496.24gold quality
spermCL:000001996.18gold quality
visceral pleuraUBERON:000240195.98gold quality
skin of hipUBERON:000155495.94gold quality
epithelium of mammary glandUBERON:000324495.94gold quality
mammary ductUBERON:000176595.93gold quality
endothelial cellCL:000011595.92gold quality
layer of synovial tissueUBERON:000761695.84gold quality
pylorusUBERON:000116695.55gold quality
esophagus squamous epitheliumUBERON:000692095.39gold quality
cauda epididymisUBERON:000436095.27gold quality
palpebral conjunctivaUBERON:000181295.21gold quality
amniotic fluidUBERON:000017395.13gold quality

Single-cell (SCXA)

Detected in 3 experiment(s), a significant marker in 2.

ExperimentMarker?Max mean expression
E-MTAB-6819yes9983.23
E-MTAB-9801no3.79
E-ANND-3no0.00

Regulation

Is transcription factor: no

miRNA regulators (miRDB)

321 targeting PAN3, top 30 by miRDB confidence (max_score; target_count = how many genes the miRNA targets in total — lower means more specific):

miRNAMax scoreAvg scoremiRNA target_count
HSA-MIR-3613-3P100.0076.367965
HSA-LET-7A-3P100.0074.033932
HSA-LET-7B-3P100.0074.083913
HSA-LET-7F-1-3P100.0074.023928
HSA-MIR-98-3P100.0074.083907
HSA-MIR-3646100.0073.565283
HSA-MIR-126-5P100.0072.713180
HSA-MIR-4668-3P100.0068.742635
HSA-MIR-1252-5P100.0069.802774
HSA-MIR-3925-3P100.0069.951237
HSA-MIR-4262100.0073.263931
HSA-MIR-3163100.0077.238605
HSA-MIR-340-5P100.0072.504437
HSA-MIR-4476100.0068.182030
HSA-MIR-6876-5P100.0067.682126
HSA-MIR-200B-3P100.0073.312693
HSA-MIR-200C-3P100.0073.352685
HSA-MIR-429100.0073.442698
HSA-MIR-4795-3P100.0074.624024
HSA-MIR-511-3P99.9968.851467
HSA-MIR-186-5P99.9970.833707
HSA-MIR-4789-3P99.9970.752484
HSA-MIR-428299.9975.366408
HSA-MIR-181A-5P99.9972.962995
HSA-MIR-181B-5P99.9972.972996
HSA-MIR-181C-5P99.9972.952996
HSA-MIR-181D-5P99.9973.042997
HSA-MIR-548C-3P99.9974.017587
HSA-MIR-1213699.9872.815713
HSA-MIR-4482-3P99.9872.503147

Literature-anchored findings (GeneRIF, showing 4)

  • hPan2 and hPan3 have roles in mRNA decay and exhibit cytoplasmic co-localization (PMID:14583602)
  • arsenite-induced oxidative stress inhibits deadenylation of mRNA primarily through downregulation of Tob and Pan3, both of which mediate the recruitment of deadenylases to mRNA (PMID:25446091)
  • These results reveal a new fundamental step governing mammalian mRNA metabolism. We propose that the first phase of deadenylation, coordinated through the interplay among the two Pan3 isoforms, Pan2, and PABP, represents a cytoplasmic mRNA maturation step important for proper mRNA turnover. (PMID:28559491)
  • the present study revealed that circPAN3 is most likely a key modulator for acquired drug resistance of AML, which may facilitate drug resistance in AML cells by regulating autophagy as an autophagy inducer via the AMPK/mTOR pathway. (PMID:31401408)

Cross-species orthologs

5 orthologs

OrganismSymbolGene ID
danio_reriopan3ENSDARG00000031637
mus_musculusPan3ENSMUSG00000029647
rattus_norvegicusPan3ENSRNOG00000000942
drosophila_melanogasterPAN3FBGN0035397
caenorhabditis_elegansWBGENE00014015

Protein

Protein identifiers

PAN2-PAN3 deadenylation complex subunit PAN3Q58A45 (reviewed: Q58A45)

Alternative names: PAB1P-dependent poly(A)-specific ribonuclease, Poly(A)-nuclease deadenylation complex subunit 3

All UniProt accessions (2): Q58A45, A0A0C4DFZ9

UniProt curated annotations — full annotation on UniProt →

Function. Regulatory subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in general and miRNA-mediated mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein (PABP). PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3’-5’ exonucleolytic degradation, or deadenylation-dependent mRNA decapping and subsequent 5’-3’ exonucleolytic degradation by XRN1. PAN3 acts as a regulator for PAN activity, recruiting the catalytic subunit PAN2 to mRNA via its interaction with RNA and PABP, and to miRNA targets via its interaction with GW182 family proteins. Decreases PAN2-mediated deadenylation, possibly by preventing progression into the second CCR4-NOT mediated stage of biphasic deadenylation. Has a significant effect on mRNA stability, generally stabilizing a subset of the transcriptome. Stabilizes mRNAs degraded by the AU-rich element (ARE)-mediated mRNA decay pathway but promotes degradation of mRNAs by the microRNA-mediated pathway. Its activity influences mRNP remodeling, specifically reducing formation of a subset of P-bodies containing GW220, an isoform of TNRC6A. Enhances PAN2 deadenylase activity and has an extensive effect on mRNA stability, generally enhancing mRNA decay across the transcriptome by multiple pathways, including the AU-rich element (ARE)-mediated pathway, microRNA-mediated pathway and the nonsense-mediated pathway (NMD). Its activity is required for efficient P-body formation. May be involved in regulating mRNAs of genes involved in cell cycle progression and cell proliferation.

Subunit / interactions. Homodimer. Forms a heterotrimer with a catalytic subunit PAN2 to form the poly(A)-nuclease (PAN) deadenylation complex. Interacts (via PAM-2 motif) with poly(A)-binding protein PABPC1 (via PABC domain), conferring substrate specificity of the enzyme complex. Interacts with the GW182 family proteins TNRC6A, TNRC6B and TNRC6. Interacts with YTHDF3. Interacts with HELZ. Interacts with PAN2. Interacts (via N-terminus) with PABPC1 at lower efficiency than isoform 3. Interacts with PAN2. Interacts (via N-terminus) with PABPC1 at higher efficiency than isoform 1.

Subcellular location. Cytoplasm. P-body Cytoplasm. Nucleus Cytoplasm.

Domain organisation. The N-terminal zinc finger binds to poly(A) RNA. Contains a pseudokinase domain. The protein kinase domain is predicted to be catalytically inactive because some of the residues important for catalytic activity are substituted and it lacks the equivalent of the binding site for a peptide substrate. However, it has retained an ATP-binding site and ATP-binding is required for mRNA degradation, stimulating the activity of the PAN2 nuclease in vitro. The nucleotide-binding site is juxtaposed to the RNase active site of PAN2 in the complex and may actually bind nucleosides of a poly(A) RNA rather than ATP, feeding the poly(A)-tail to the active site of the deadenylase and thus increasing the efficiency with which this distributive enzyme degrades oligo(A) RNAs. The pseudokinase domain, the coiled-coil (CC), and C-terminal knob domain (CK) form a structural unit (PKC) that forms an extensive high-affinity interaction surface for PAN2.

Similarity. Belongs to the protein kinase superfamily. PAN3 family.

Isoforms (4)

UniProt IDNamesCanonical?
Q58A45-11, Pan3b, Pan3Lyes
Q58A45-22
Q58A45-33, Pan3S
Q58A45-44

RefSeq proteins (1): NP_787050* (*=MANE)

Domains & families (InterPro)

IDNameType
IPR000571Znf_CCCHDomain
IPR000719Prot_kinase_domDomain
IPR011009Kinase-like_dom_sfHomologous_superfamily
IPR030844PAN3Family
IPR036855Znf_CCCH_sfHomologous_superfamily
IPR041332Pan3_CKDomain

Pfam: PF18101

UniProt features (29 total): region of interest 6, splice variant 5, sequence conflict 4, compositionally biased region 3, binding site 3, modified residue 2, mutagenesis site 2, chain 1, zinc finger region 1, coiled-coil region 1, short sequence motif 1

Structure

Experimental structures (PDB)

1 structures.

PDBMethodResolution (Å)
9QTUELECTRON MICROSCOPY4.6

Predicted structure (AlphaFold)

ModelpLDDTFraction very-high
AF-Q58A45-F164.340.32

Functional residue map

Curated UniProt residues grouped by drug-discovery relevance — catalytic, ligand-binding, modification, and mutation-validated positions. Source: UniProtKB sequence features.

Ligand- & substrate-binding residues (3): 521; 570–577; 644–645

Post-translational modifications (2): 354, 361

Mutagenesis-validated functional residues (2):

PositionPhenotype
203reduces interaction with polyadenylate-binding protein.
293reduces interaction with polyadenylate-binding protein.

Function

Pathways and Gene Ontology

Reactome pathways

1 pathways

IDPathway
R-HSA-429947Deadenylation of mRNA

MSigDB gene sets: 269 (showing top): GOMF_RNA_NUCLEASE_ACTIVITY, GOBP_P_BODY_ASSEMBLY, GOBP_REGULATION_OF_MRNA_CATABOLIC_PROCESS, GOMF_NUCLEASE_ACTIVITY, GOBP_PROTEIN_TARGETING, GOBP_MACROMOLECULE_CATABOLIC_PROCESS, GCAAGGA_MIR502, GOBP_POSITIVE_REGULATION_OF_ORGANELLE_ORGANIZATION, GOBP_REGULATION_OF_CELLULAR_COMPONENT_BIOGENESIS, GTGCCTT_MIR506, GOBP_POST_TRANSCRIPTIONAL_REGULATION_OF_GENE_EXPRESSION, GOBP_POSITIVE_REGULATION_OF_CELLULAR_COMPONENT_BIOGENESIS, GOBP_REGULATION_OF_CATABOLIC_PROCESS, GOBP_POSITIVE_REGULATION_OF_CATABOLIC_PROCESS, REACTOME_DEADENYLATION_OF_MRNA

GO Biological Process (7): nuclear-transcribed mRNA poly(A) tail shortening (GO:0000289), deadenylation-dependent decapping of nuclear-transcribed mRNA (GO:0000290), mRNA processing (GO:0006397), protein targeting (GO:0006605), positive regulation of cytoplasmic mRNA processing body assembly (GO:0010606), nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay (GO:0000288), protein phosphorylation (GO:0006468)

GO Molecular Function (9): protein kinase activity (GO:0004672), ATP binding (GO:0005524), poly(A) binding (GO:0008143), zinc ion binding (GO:0008270), nucleotide binding (GO:0000166), RNA binding (GO:0003723), poly(A)-specific ribonuclease activity (GO:0004535), protein binding (GO:0005515), metal ion binding (GO:0046872)

GO Cellular Component (5): P-body (GO:0000932), nucleus (GO:0005634), cytosol (GO:0005829), PAN complex (GO:0031251), cytoplasm (GO:0005737)

Reactome top-level categories

Rollup of top-1 pathways:

CategoryPathways
Deadenylation-dependent mRNA decay1

GO top-level categories

Rollup of top GO terms by namespace:

CategoryTerms
nuclear-transcribed mRNA catabolic process3
nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay2
cytoplasm2
cellular anatomical structure2
mRNA methylguanosine-cap decapping1
RNA processing1
mRNA metabolic process1
establishment of protein localization1
regulation of cytoplasmic mRNA processing body assembly1
P-body assembly1
positive regulation of organelle assembly1
mRNA destabilization1
phosphorylation1
protein modification process1
kinase activity1
phosphotransferase activity, alcohol group as acceptor1
catalytic activity, acting on a protein1
adenyl ribonucleotide binding1
purine ribonucleoside triphosphate binding1
poly-purine tract binding1
transition metal ion binding1
nucleoside phosphate binding1
heterocyclic compound binding1
nucleic acid binding1
3’-5’-RNA exonuclease activity1
binding1
cation binding1
cytoplasmic ribonucleoprotein granule1
intracellular membrane-bounded organelle1
exoribonuclease complex1
intracellular anatomical structure1

Protein interactions and networks

STRING

671 interactions, top by confidence (×1000):

Protein AProtein BPartner UniProtScore
PAN3STKLD1Q8NE28517
PAN3PSKH2Q96QS6510
PAN3PEAK3Q6ZS72491
PAN3FAM20AQ96MK3488
PAN3PGGT1BP53609455
PAN3SELENOOQ9BVL4410
PAN3PEAK1Q9H792410
PAN3BTBD1Q9H0C5397
PAN3PABPC1P11940396
PAN3OTUD7AQ8TE49389
PAN3RIBC2Q9H4K1372
PAN3KSR1Q8IVT5371
PAN3NACC2Q96BF6359
PAN3PAN2Q504Q3353
PAN3XRN1Q8IZH2352

IntAct

50 interactions, top by confidence:

ABTypeScore
NHERF2PODXLpsi-mi:“MI:0914”(association)0.770
PAN3PAN2psi-mi:“MI:0915”(physical association)0.740
PAN2PAN3psi-mi:“MI:0915”(physical association)0.740
PAN3PAN2psi-mi:“MI:0403”(colocalization)0.740
PAN3PABPC1psi-mi:“MI:0914”(association)0.700
PABPC1PAN3psi-mi:“MI:0915”(physical association)0.700
PAN3PABPC1psi-mi:“MI:0407”(direct interaction)0.700
ASF1BHAT1psi-mi:“MI:0914”(association)0.640
ASF1AHAT1psi-mi:“MI:0914”(association)0.640
PAN3TNRC6Bpsi-mi:“MI:0915”(physical association)0.630
TNRC6BPAN3psi-mi:“MI:0407”(direct interaction)0.630
TNRC6BPAN3psi-mi:“MI:0915”(physical association)0.630
TNRC6CCNOT1psi-mi:“MI:0914”(association)0.620
TNRC6BCNOT1psi-mi:“MI:0914”(association)0.580
ASF1AMCM4psi-mi:“MI:0914”(association)0.530
CLEC11AVWA8psi-mi:“MI:0914”(association)0.530
TNRC6CPAN2psi-mi:“MI:0914”(association)0.530
TNRC6CPAN3psi-mi:“MI:0915”(physical association)0.500
PAN3TNRC6Apsi-mi:“MI:0915”(physical association)0.500
PAN3TNRC6Cpsi-mi:“MI:0915”(physical association)0.500
TNRC6ACNOT1psi-mi:“MI:0914”(association)0.500
PAN2PAN3psi-mi:“MI:0915”(physical association)0.400
PAN3SVILpsi-mi:“MI:0915”(physical association)0.370
Xpo1IFT56psi-mi:“MI:0914”(association)0.350
ASF1BHAT1psi-mi:“MI:0914”(association)0.350
PAN2ARCN1psi-mi:“MI:0914”(association)0.350

BioGRID (94): PAN3 (Affinity Capture-Western), PABPC1 (Affinity Capture-Western), PAN3 (Affinity Capture-Western), PAN3 (Affinity Capture-Western), PAN3 (Affinity Capture-Western), TNRC6C (Affinity Capture-Western), PAN3 (Reconstituted Complex), PAN3 (Co-fractionation), PAN3 (Affinity Capture-MS), PAN3 (Affinity Capture-MS), PAN3 (Affinity Capture-MS), KIAA0430 (Affinity Capture-MS), PAN3 (Affinity Capture-MS), PAN3 (Affinity Capture-RNA), PAN3 (Affinity Capture-Western)

ESM2 similar proteins: A0A1W2P872, A1L1C7, A4IIM2, B2RYD2, F1LQ48, O57406, O88532, O95319, P14866, P28659, P51513, P57723, P57724, Q28HE9, Q2PFW9, Q32PX7, Q3U0V1, Q3US41, Q4QQT3, Q4R535, Q58A45, Q5F3T7, Q5NVC8, Q5R8Y8, Q5R995, Q5U231, Q640Q5, Q6DGV1, Q6GPM1, Q6NXG1, Q6P0B1, Q6PF35, Q792H5, Q7T2T1, Q7TSY6, Q7ZXE2, Q80WA4, Q8R081, Q8UVD9, Q91WJ8

Diamond homologs: A1CP31, A1D1Y5, A1L1C7, A2QAQ3, A3LQL9, A5DCP8, A5E2Y4, G0S0Y3, P0CD65, P0CP50, P0CP51, P34653, P36102, Q0D0A1, Q0V0I4, Q1E2S2, Q2H401, Q2KFH6, Q2U0M4, Q58A45, Q5AK10, Q5BFB1, Q640Q5, Q6BRV5, Q6CBZ0, Q6CP23, Q6FKP2, Q6MY57, Q75BU9, Q7SDP4, Q95RR8, Q9UST1, O13865, P38070

SIGNOR signaling

1 interactions.

AEffectBMechanism
PAN3“form complex”“PAN2-PAN3 deadenylation complex”binding

Enriched among interaction partners

Reactome pathways and GO biological processes over-represented among this gene’s 43 IntAct physical interaction partners (hypergeometric vs the genome-wide background, BH-FDR, gene-set size 15–500, ranked by fold). A functional readout of the neighbourhood — distinct from this gene’s own memberships above, and biased toward well-studied / hub proteins, so read it as themes rather than proof.

Reactome pathways:

PathwayPartnersFoldFDR
TP53 Regulates Metabolic Genes737.9×5e-08
G2/M Checkpoints528.0×8e-06
Cell Cycle Checkpoints518.4×4e-05
Cell Cycle57.5×1e-03
Signaling by Rho GTPases57.1×2e-03
Signaling by Rho GTPases, Miro GTPases and RHOBTB357.0×2e-03

GO biological processes:

GO termPartnersFoldFDR
positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay5156.0×1e-08

Disease & clinical

Clinical variants and AI predictions

ClinVar

99 variants total. Per-class counts are floors (≥ shown; pagination cap):

ClassificationCount (floor)
Pathogenic0
Likely pathogenic1
Uncertain significance68
Likely benign2
Benign0

Top pathogenic / likely-pathogenic (1)

Variant IDHGVSClassification
1209857GRCh37/hg19 13q12.2-12.3(chr13:28669064-31367407)x1Likely pathogenic

SpliceAI

0 predictions. Top by Δscore:

AlphaMissense

5789 scored. Top likely-pathogenic:

VariantProtein changeam_pathogenicity
13:28138802:T:AC49S1.000
13:28138802:T:CC49R1.000
13:28138803:G:AC49Y1.000
13:28138803:G:CC49S1.000
13:28138804:C:GC49W1.000
13:28138829:T:AC58S1.000
13:28138829:T:CC58R1.000
13:28138830:G:AC58Y1.000
13:28138830:G:CC58S1.000
13:28138831:C:GC58W1.000
13:28138847:T:AC64S1.000
13:28138847:T:CC64R1.000
13:28138848:G:CC64S1.000
13:28138849:T:GC64W1.000
13:28138853:T:CF66L1.000
13:28138855:C:AF66L1.000
13:28138855:C:GF66L1.000
13:28256498:T:CY403H1.000
13:28256498:T:GY403D1.000
13:28256501:T:CF404L1.000
13:28256503:C:AF404L1.000
13:28256503:C:GF404L1.000
13:28260547:G:CR450P1.000
13:28261405:T:CL453P1.000
13:28266738:T:GY479D1.000
13:28266827:A:CK508N1.000
13:28266827:A:TK508N1.000
13:28266828:G:CA509P1.000
13:28266862:T:AL520H1.000
13:28266862:T:CL520P1.000

dbSNP variants (sampled 300 via entrez): RS1000002316 (13:28169209 T>A), RS1000016158 (13:28254074 C>T), RS1000022367 (13:28275295 A>T), RS1000023522 (13:28238085 G>A), RS1000030646 (13:28242045 C>T), RS1000077781 (13:28274763 T>C), RS1000082928 (13:28221686 C>T), RS1000095490 (13:28153725 C>T), RS1000120835 (13:28245538 C>T), RS1000131816 (13:28281908 C>G,T), RS1000139120 (13:28221136 G>A), RS1000159488 (13:28162956 T>G), RS1000171550 (13:28142794 T>A), RS1000179481 (13:28292158 C>T), RS1000182732 (13:28206510 T>C,G)

Disease associations

OMIM: gene MIM:617448 | disease phenotypes:

GenCC curated gene-disease

Mondo (0):

Orphanet (0):

HPO phenotypes

0 total (0 of 0 shown, HPO-id order):

GWAS associations

0 associations (top):

Drugs & pharmacology

Drug and pharmacology data

Is drug target: yes

ChEMBL targets (1): CHEMBL4105985 (SINGLE PROTEIN)

PharmGKB: 1 entry (VIP=true, CPIC=false)

CTD chemical–gene interactions

23 total (human), top 23 by PubMed support.

ChemicalActions (top 5)PubMed papers
Air Pollutantsaffects expression, increases abundance, decreases expression2
Valproic Aciddecreases expression, affects expression2
aristolochic acid Idecreases expression1
FR900359increases phosphorylation1
triphenyl phosphateaffects expression1
arseniteincreases degradation1
tris(1,3-dichloro-2-propyl)phosphateincreases expression1
butyraldehydedecreases expression1
benzo(e)pyreneincreases methylation1
pentanaldecreases expression1
di-n-butylphosphoric acidaffects expression1
jinfukangdecreases expression1
Irinotecandecreases expression1
Sunitinibincreases expression1
Caffeinedecreases phosphorylation1
Diazinonincreases methylation1
Hydrogen Peroxideaffects cotreatment, increases expression1
Methapyrileneincreases methylation1
Ozoneaffects expression, increases abundance1
Theophyllineaffects cotreatment, increases expression1
7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxidedecreases expression1
Particulate Matterdecreases expression, increases abundance1
Magnetite Nanoparticlesdecreases methylation1

ChEMBL screening assays

22 unique, capped per target: 22 binding

Representative assays (with source publication via chembl_document):

Assay IDTypeDescriptionSource paper
CHEMBL4034444BindingInhibition of PAN3 ATP binding site (unknown origin) at 10 uMDeveloping DYRK inhibitors derived from the meridianins as a means of increasing levels of NFAT in the nucleus. — Bioorg Med Chem Lett

Cellosaurus cell lines

2 cell lines: 2 cancer cell line

First 10 cell lines (id-ordered, not curated):

CellosaurusNameCategorySex
CVCL_B5KLHAP1 PAN3 (-) 2Cancer cell lineMale
CVCL_XR32HAP1 PAN3 (-) 1Cancer cell lineMale

Clinical trials (associated diseases)

0 trials via MONDO — disease-level, not drug-specific.

No linked Atlas pages yet — the cross-entity mesh grows as the corpus expands.