EXD2

gene
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Also known as FLJ10738

Summary

EXD2 (exonuclease 3’-5’ domain containing 2, HGNC:20217) is a protein-coding gene on chromosome 14q24.1, encoding Exonuclease 3’-5’ domain-containing protein 2 (Q9NVH0). Exonuclease that has both 3’-5’ exoribonuclease and exodeoxyribonuclease activities, depending on the divalent metal cation used as cofactor.

Enables 3’-5’ exonuclease activity; metal ion binding activity; and protein homodimerization activity. Involved in DNA double-strand break processing; double-strand break repair via homologous recombination; and replication fork processing. Located in intermediate filament cytoskeleton; mitochondrial outer membrane; and site of DNA damage.

Source: NCBI Gene 55218 — RefSeq curated summary.

At a glance

  • GWAS associations: 5
  • Clinical variants (ClinVar): 98 total
  • MANE Select transcript: NM_001193360

Identifiers

Gene identifiers

FieldValue
HGNC IDHGNC:20217
Approved symbolEXD2
Nameexonuclease 3’-5’ domain containing 2
Location14q24.1
Locus typegene with protein product
StatusApproved
AliasesFLJ10738
Ensembl geneENSG00000081177
Ensembl biotypeprotein_coding
OMIM616940
Entrez55218

Gene structure

Transcript identifiers

Ensembl transcripts: 31 — 25 protein_coding, 4 protein_coding_CDS_not_defined, 1 retained_intron, 1 nonsense_mediated_decay

ENST00000312994, ENST00000409014, ENST00000409018, ENST00000409242, ENST00000409675, ENST00000409949, ENST00000413191, ENST00000461908, ENST00000465286, ENST00000487724, ENST00000489133, ENST00000492815, ENST00000494629, ENST00000685843, ENST00000904158, ENST00000904159, ENST00000904160, ENST00000904161, ENST00000904162, ENST00000904163, ENST00000904164, ENST00000904165, ENST00000904166, ENST00000922337, ENST00000922338, ENST00000922339, ENST00000922340, ENST00000922341, ENST00000969916, ENST00000969917, ENST00000969918

RefSeq mRNA: 5 — MANE Select: NM_001193360 NM_001193360, NM_001193361, NM_001193362, NM_001193363, NM_018199

CCDS: CCDS53902, CCDS9793

Canonical transcript exons

ENST00000685843 — 10 exons

ExonStartEnd
ENSE000015353366920391769204000
ENSE000016423426923470069235031
ENSE000034892486923640769236542
ENSE000035325096923604669236152
ENSE000035414356920942469209803
ENSE000036288446922881669229072
ENSE000036314016923757569237931
ENSE000037847286923047269230598
ENSE000039229656919149869191591
ENSE000039293736924088469244018

Expression profiles

Bgee: expression breadth ubiquitous, 284 present calls, max score 91.77.

FANTOM5 (CAGE): breadth ubiquitous, TPM avg 10.1726 / max 162.8225, expressed in 1732 samples.

FANTOM5 promoters (2 alternative TSS)

Promoter IDTPM avgSamples expressed
1403248.20561719
1403251.9670830

Top tissues by expression

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

TissueAnatomy IDExpression scoreQuality
cortical plateUBERON:000534391.77gold quality
ventricular zoneUBERON:000305390.94gold quality
body of pancreasUBERON:000115090.55gold quality
ganglionic eminenceUBERON:000402389.37gold quality
C1 segment of cervical spinal cordUBERON:000646988.79gold quality
pancreasUBERON:000126488.34gold quality
spinal cordUBERON:000224088.03gold quality
islet of LangerhansUBERON:000000687.64gold quality
mucosa of paranasal sinusUBERON:000503087.46gold quality
adult organismUBERON:000702387.29gold quality
olfactory bulbUBERON:000226487.16gold quality
cerebellar hemisphereUBERON:000224587.03gold quality
prefrontal cortexUBERON:000045187.02gold quality
right uterine tubeUBERON:000130287.02gold quality
right hemisphere of cerebellumUBERON:001489087.00gold quality
caudate nucleusUBERON:000187386.91gold quality
cerebellar cortexUBERON:000212986.91gold quality
Brodmann (1909) area 9UBERON:001354086.57gold quality
right frontal lobeUBERON:000281086.40gold quality
putamenUBERON:000187486.27gold quality
smooth muscle tissueUBERON:000113586.19gold quality
cerebellumUBERON:000203786.08gold quality
primordial germ cell in gonadCL:0000670 ∩ UBERON:000099185.98gold quality
nucleus accumbensUBERON:000188285.98gold quality
diaphragmUBERON:000110385.96gold quality
epithelium of nasopharynxUBERON:000195185.90gold quality
nasopharynxUBERON:000172885.89gold quality
hair follicleUBERON:000207385.85silver quality
frontal cortexUBERON:000187085.75gold quality
tongue squamous epitheliumUBERON:000691985.75gold quality

Single-cell (SCXA)

Detected in 2 experiment(s), a significant marker in 1.

ExperimentMarker?Max mean expression
E-ANND-3yes5.54
E-GEOD-99795no89.63

Regulation

Is transcription factor: no

miRNA regulators (miRDB)

144 targeting EXD2, 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-3163100.0077.238605
HSA-MIR-126-5P100.0072.713180
HSA-MIR-4776-3P100.0068.731340
HSA-MIR-4795-3P100.0074.624024
HSA-MIR-200B-3P100.0073.312693
HSA-MIR-200C-3P100.0073.352685
HSA-MIR-429100.0073.442698
HSA-MIR-4747-5P100.0067.902681
HSA-MIR-5196-5P100.0067.982761
HSA-MIR-4668-3P100.0068.742635
HSA-MIR-4510100.0066.602050
HSA-MIR-6127100.0066.762188
HSA-MIR-6129100.0066.462080
HSA-MIR-6130100.0066.692012
HSA-MIR-6133100.0066.482064
HSA-MIR-428299.9975.366408
HSA-MIR-453499.9966.581907
HSA-MIR-366299.9973.825684
HSA-MIR-548AW99.9972.573559
HSA-MIR-477599.9875.006394
HSA-MIR-3617-3P99.9867.86918
HSA-MIR-548N99.9871.944170
HSA-MIR-314899.9775.066478
HSA-MIR-60799.9773.625593
HSA-MIR-1468-3P99.9672.743797
HSA-MIR-808299.9567.271170
HSA-MIR-651-3P99.9473.485177
HSA-MIR-6845-3P99.9466.881439
HSA-MIR-218-5P99.9372.222103
HSA-MIR-539-5P99.9370.302855

Literature-anchored findings (GeneRIF, showing 4)

  • establish that EXD2 stimulates both short- and long-range DSB resection (PMID:26807646)
  • EXD2 re-locates to the nucleus following double-strand breaks and thus is unlikely to have a direct role in nuclear DNA repair. Knockdown or overexpression of EXD2 affects the cellular distribution of mitochondria. (PMID:29599527)
  • EXD2 is anchored to the mitochondrial outer membrane through a conserved N-terminal transmembrane domain, while the C-terminal region is cytosolic. Crystal structures of the exonuclease domain in complex with Mn2+/Mg2+ revealed a domain-swapped dimer in which the central alpha5-alpha7 helices are mutually crossed over, resulting in chimeric active sites. (PMID:31127291)
  • EXD2 deficiency leads to fork collapse, hypersensitivity to replication inhibitors, and genomic instability. Impeding fork regression by inactivation of SMARCAL1 or removal of RECQ1’s inhibition in EXD2(-/-) cells restores efficient fork restart and genome stability. Moreover, purified EXD2 efficiently processes substrates mimicking regressed forks. (PMID:31255466)

Cross-species orthologs

4 orthologs

OrganismSymbolGene ID
danio_rerioexd2ENSDARG00000016117
mus_musculusExd2ENSMUSG00000032705
rattus_norvegicusExd2ENSRNOG00000027707
drosophila_melanogasterExd2FBGN0037901

Paralogs (1): EXD3 (ENSG00000187609)

Protein

Protein identifiers

Exonuclease 3’-5’ domain-containing protein 2Q9NVH0 (reviewed: Q9NVH0)

Alternative names: 3’-5’ exoribonuclease EXD2, Exonuclease 3’-5’ domain-like-containing protein 2

All UniProt accessions (3): Q9NVH0, A0A8I5KSH7, C9JLF4

UniProt curated annotations — full annotation on UniProt →

Function. Exonuclease that has both 3’-5’ exoribonuclease and exodeoxyribonuclease activities, depending on the divalent metal cation used as cofactor. In presence of Mg(2+), only shows 3’-5’ exoribonuclease activity, while it shows both exoribonuclease and exodeoxyribonuclease activities in presence of Mn(2+). Acts as an exoribonuclease in mitochondrion, possibly by regulating ATP production and mitochondrial translation. Also involved in the response to DNA damage. Acts as 3’-5’ exodeoxyribonuclease for double-strand breaks resection and efficient homologous recombination. Plays a key role in controlling the initial steps of chromosomal break repair, it is recruited to chromatin in a damage-dependent manner and functionally interacts with the MRN complex to accelerate resection through its 3’-5’ exonuclease activity, which efficiently processes double-stranded DNA substrates containing nicks. Also involved in response to replicative stress: recruited to stalled forks and is required to stabilize and restart stalled replication forks by restraining excessive fork regression, thereby suppressing their degradation.

Subunit / interactions. Homodimer. Interacts with RBBP8, MRE11 and BRCA1.

Subcellular location. Mitochondrion outer membrane. Mitochondrion matrix. Nucleus. Chromosome.

Cofactor. Divalent metal cations; Mg(2+) or Mn(2+). Acts as a 3’-5’ exoribonuclease in presence of Mg(2+), while it has no 3’-5’ exodeoxyribonuclease activity. Has both as a 3’-5’ exoribonuclease and exodeoxyribonuclease activities in presence of Mn(2+).

Similarity. Belongs to the EXD2 family.

Isoforms (2)

UniProt IDNamesCanonical?
Q9NVH0-11yes
Q9NVH0-22

RefSeq proteins (5): NP_001180289, NP_001180290, NP_001180291, NP_001180292, NP_060669 (=MANE)

Domains & families (InterPro)

IDNameType
IPR0025623’-5’_exonuclease_domDomain
IPR012337RNaseH-like_sfHomologous_superfamily
IPR036397RNaseH_sfHomologous_superfamily
IPR0511323-5_Exonuclease_domainFamily

Pfam: PF01612

UniProt features (41 total): helix 10, strand 8, mutagenesis site 6, binding site 4, topological domain 2, sequence variant 2, region of interest 2, chain 1, splice variant 1, transmembrane region 1, sequence conflict 1, turn 1, domain 1, compositionally biased region 1

Structure

Experimental structures (PDB)

8 structures.

PDBMethodResolution (Å)
6K17X-RAY DIFFRACTION1.6
6K19X-RAY DIFFRACTION2.2
6K18X-RAY DIFFRACTION2.3
6K1CX-RAY DIFFRACTION2.45
6K1AX-RAY DIFFRACTION2.6
6K1BX-RAY DIFFRACTION2.6
6K1EX-RAY DIFFRACTION2.9
6K1DX-RAY DIFFRACTION3

Predicted structure (AlphaFold)

ModelpLDDTFraction very-high
AF-Q9NVH0-F180.590.60

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 (4): 110; 246; 108; 108

Mutagenesis-validated functional residues (6):

PositionPhenotype
108–110loss of 3’-5’ exonuclease activity. impaired ability to stabilize and restart stalled replication forks in response to r
190abolished exodeoxyribonuclease activity.
195impaired exonuclease activity.
197impaired exonuclease activity.
221impaired exonuclease activity.
226abolished exonuclease activity.

Function

Pathways and Gene Ontology

Reactome pathways

0 pathways

MSigDB gene sets: 173 (showing top): GOBP_DNA_TEMPLATED_DNA_REPLICATION_MAINTENANCE_OF_FIDELITY, GOMF_RNA_NUCLEASE_ACTIVITY, GOMF_NUCLEASE_ACTIVITY, MODULE_66, MODULE_118, chr14q24, MODULE_379, GOBP_DNA_DAMAGE_RESPONSE, GOCC_MITOCHONDRIAL_ENVELOPE, DOUGLAS_BMI1_TARGETS_DN, MODULE_88, MODULE_242, GOBP_RECOMBINATIONAL_REPAIR, GOMF_EXONUCLEASE_ACTIVITY, FREAC7_01

GO Biological Process (9): double-strand break repair via homologous recombination (GO:0000724), DNA double-strand break processing (GO:0000729), double-strand break repair (GO:0006302), replication fork processing (GO:0031297), nucleic acid metabolic process (GO:0090304), nucleobase-containing compound metabolic process (GO:0006139), DNA repair (GO:0006281), DNA recombination (GO:0006310), DNA damage response (GO:0006974)

GO Molecular Function (13): 3’-5’-RNA exonuclease activity (GO:0000175), magnesium ion binding (GO:0000287), nucleic acid binding (GO:0003676), 3’-5’-DNA exonuclease activity (GO:0008296), single-stranded DNA 3’-5’ DNA exonuclease activity (GO:0008310), 3’-5’ exonuclease activity (GO:0008408), manganese ion binding (GO:0030145), protein homodimerization activity (GO:0042803), nuclease activity (GO:0004518), exonuclease activity (GO:0004527), protein binding (GO:0005515), hydrolase activity (GO:0016787), metal ion binding (GO:0046872)

GO Cellular Component (10): nucleus (GO:0005634), cytoplasm (GO:0005737), mitochondrion (GO:0005739), mitochondrial outer membrane (GO:0005741), mitochondrial matrix (GO:0005759), intermediate filament cytoskeleton (GO:0045111), site of DNA damage (GO:0090734), chromosome (GO:0005694), membrane (GO:0016020), mitochondrial membrane (GO:0031966)

GO top-level categories

Rollup of top GO terms by namespace:

CategoryTerms
DNA metabolic process3
cellular anatomical structure3
double-strand break repair2
3’-5’ exonuclease activity2
binding2
intracellular membrane-bounded organelle2
mitochondrion2
recombinational repair1
5’-3’ DNA exonuclease activity1
DNA repair1
DNA-templated DNA replication maintenance of fidelity1
nucleobase-containing compound metabolic process1
macromolecule metabolic process1
primary metabolic process1
DNA damage response1
cellular response to stress1
RNA exonuclease activity, producing 5’-phosphomonoesters1
metal ion binding1
DNA exonuclease activity, producing 5’-phosphomonoesters1
3’-5’-DNA exonuclease activity1
single-stranded DNA exodeoxyribonuclease activity1
exonuclease activity1
transition metal ion binding1
identical protein binding1
protein dimerization activity1
catalytic activity, acting on a nucleic acid1
nuclease activity1
hydrolase activity, acting on ester bonds1
catalytic activity1
cation binding1
intracellular anatomical structure1
cytoplasm1
mitochondrial membrane1
organelle outer membrane1
intracellular organelle lumen1
cytoskeleton1
chromosome1
intracellular membraneless organelle1
mitochondrial envelope1
organelle membrane1

Protein interactions and networks

STRING

830 interactions, top by confidence (×1000):

Protein AProtein BPartner UniProtScore
EXD2TMEM214Q6NUQ4917
EXD2CNOT2Q9NZN8898
EXD2SEC61BP38390848
EXD2EXD1Q8NHP7685
EXD2SEC61GP38384684
EXD2NPR2P20594670
EXD2SEC62Q99442670
EXD2SEC63Q9UGP8650
EXD2TAFAZZINQ16635649
EXD2SEC61A1P38378571
EXD2EXO1Q9UQ84571
EXD2BRCA1P38398562
EXD2NPPCP23582548
EXD2DNA2P51530547
EXD2WRNIP1Q96S55523
EXD2RBBP8Q99708523

IntAct

65 interactions, top by confidence:

ABTypeScore
RBBP8MRE11psi-mi:“MI:0914”(association)0.670
ASPHSTXBP3psi-mi:“MI:0914”(association)0.640
NME3NME4psi-mi:“MI:0914”(association)0.640
NRASRGL2psi-mi:“MI:0914”(association)0.550
PEX19FAM20Bpsi-mi:“MI:0914”(association)0.530
GRAMD2BEFCAB14psi-mi:“MI:0914”(association)0.530
SLC31A1C2orf72psi-mi:“MI:0914”(association)0.530
PEX19MYO1Dpsi-mi:“MI:0914”(association)0.530
RBBP8EXD2psi-mi:“MI:0915”(physical association)0.500
HTRA2HAX1psi-mi:“MI:2364”(proximity)0.420
EXD2CLPXpsi-mi:“MI:0915”(physical association)0.400
JUNTPM3psi-mi:“MI:0914”(association)0.350
HIF1ANCNOT1psi-mi:“MI:0914”(association)0.350
EXD2BRCA1psi-mi:“MI:0914”(association)0.350
ESR1ESYT2psi-mi:“MI:0914”(association)0.350
DCTN2KLHL2psi-mi:“MI:0914”(association)0.350
NME3NME2psi-mi:“MI:0914”(association)0.350
EVLRPL23psi-mi:“MI:0914”(association)0.350
Mpsi-mi:“MI:0914”(association)0.350
MAGEA8METTL15psi-mi:“MI:0914”(association)0.350
EVLPFN2psi-mi:“MI:0914”(association)0.350
FAHD1VWA8psi-mi:“MI:0914”(association)0.350

BioGRID (436): EXD2 (Affinity Capture-MS), EXD2 (Affinity Capture-MS), EXD2 (Affinity Capture-MS), EXD2 (Affinity Capture-MS), EXD2 (Affinity Capture-MS), EXD2 (Affinity Capture-MS), EXD2 (Affinity Capture-MS), EXD2 (Affinity Capture-Western), RBBP8 (Affinity Capture-Western), BRCA1 (Affinity Capture-Western), MRE11A (Affinity Capture-Western), EXD2 (Affinity Capture-MS), EXD2 (Affinity Capture-MS), EXD2 (Affinity Capture-MS), EXD2 (Affinity Capture-MS)

ESM2 similar proteins: A1YIZ1, A2ARP1, A7Z050, B5DFG1, E1BPN0, E7FCP8, O14976, O18373, O35385, P0C644, P33402, P46489, P49903, P57075, P97364, P97874, Q05145, Q0VC82, Q38A34, Q3V3E1, Q42713, Q43307, Q4Q0M0, Q5R4H0, Q5RDF1, Q5RF87, Q66I14, Q6ESZ9, Q6GL12, Q6PF47, Q6PFW1, Q7Z3D6, Q7ZW38, Q80V31, Q84MA1, Q8BGG7, Q8BH69, Q8BH86, Q8C0D5, Q8H1E2

Diamond homologs: A1CJ18, A2QY39, A4R715, A6RY31, A8WK63, B3LWP6, B3NZ68, B4G5C9, B4I298, B4JF25, B4K934, B4M401, B4N9D3, B4PLB3, B4QUF6, D4ACP5, O09053, O18017, O34748, O88700, O93530, O94761, O94762, P0CQ96, P0CQ97, P15043, P35187, P40724, P46063, P50729, P54132, P71359, P73421, Q09181, Q09811, Q0U7S9, Q0WVW7, Q14191, Q19546, Q1E5R1

SIGNOR signaling

0 interactions.

Enriched among interaction partners

Reactome pathways and GO biological processes over-represented among this gene’s 82 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.

GO biological processes:

GO termPartnersFoldFDR
zinc ion transmembrane transport657.7×5e-07
intracellular zinc ion homeostasis639.6×3e-06

Disease & clinical

Clinical variants and AI predictions

ClinVar

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

ClassificationCount (floor)
Pathogenic0
Likely pathogenic0
Uncertain significance87
Likely benign2
Benign0

Top pathogenic / likely-pathogenic (0)

SpliceAI

2627 predictions. Top by Δscore:

VariantEffectΔscore
14:69229014:G:GTdonor_gain1.0000
14:69230470:A:AGacceptor_gain1.0000
14:69230471:G:GGacceptor_gain1.0000
14:69230594:ACCAG:Adonor_loss1.0000
14:69230597:AGG:Adonor_loss1.0000
14:69230598:GG:Gdonor_loss1.0000
14:69230599:G:GAdonor_loss1.0000
14:69234901:G:GTdonor_gain1.0000
14:69234977:G:GTdonor_gain1.0000
14:69234978:G:Tdonor_gain1.0000
14:69235002:A:Tdonor_gain1.0000
14:69236044:A:AGacceptor_gain1.0000
14:69236045:G:GGacceptor_gain1.0000
14:69236045:GAAA:Gacceptor_gain1.0000
14:69236404:A:AGacceptor_gain1.0000
14:69236405:A:Gacceptor_gain1.0000
14:69236406:G:GGacceptor_gain1.0000
14:69236406:GA:Gacceptor_gain1.0000
14:69236543:G:GGdonor_gain1.0000
14:69236543:GT:Gdonor_loss1.0000
14:69236544:T:Gdonor_loss1.0000
14:69237573:A:AGacceptor_gain1.0000
14:69237574:G:GGacceptor_gain1.0000
14:69237574:GGAA:Gacceptor_gain1.0000
14:69237945:G:GTdonor_gain1.0000
14:69191588:GCAG:Gdonor_gain0.9900
14:69191589:CAGG:Cdonor_loss0.9900
14:69191592:G:GGdonor_gain0.9900
14:69191592:GTAA:Gdonor_loss0.9900
14:69191593:T:Adonor_loss0.9900

AlphaMissense

0 scored. Top likely-pathogenic:

dbSNP variants (sampled 300 via entrez): RS1000018500 (14:69202876 A>G), RS1000063462 (14:69225168 G>T), RS1000090590 (14:69243294 A>G), RS1000102246 (14:69224426 A>G), RS1000130300 (14:69195947 G>A,T), RS1000180790 (14:69222444 C>T), RS1000182304 (14:69220260 T>A,C,G), RS1000193150 (14:69204344 A>G), RS1000277835 (14:69238202 A>C), RS1000387723 (14:69191411 C>A), RS1000405908 (14:69229265 T>C,G), RS1000536351 (14:69224151 C>T), RS1000671807 (14:69243611 A>G), RS1000724435 (14:69196174 C>A), RS1000790636 (14:69236722 AC>A)

Disease associations

OMIM: gene MIM:616940 | disease phenotypes:

GenCC curated gene-disease

Mondo (0):

Orphanet (0):

HPO phenotypes

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

GWAS associations

5 associations (top):

StudyTraitp-value
GCST005232_25Neuroticism4.000000e-08
GCST005316_534Intelligence (MTAG)5.000000e-09
GCST007709_126General factor of neuroticism1.000000e-08
GCST009391_1502Metabolite levels8.000000e-06
GCST010002_155Refractive error6.000000e-11

EFO canonical traits (3, from GWAS)

EFO IDTrait name
EFO:0007660neuroticism measurement
EFO:0004337intelligence
EFO:0010416triacylglycerol 52:4 measurement

Drugs & pharmacology

Drug and pharmacology data

Is drug target: no

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

CTD chemical–gene interactions

24 total (human), top 24 by PubMed support.

ChemicalActions (top 5)PubMed papers
Ozoneaffects cotreatment, increases oxidation, affects expression, increases abundance2
triphenyl phosphateaffects expression1
bisphenol Aaffects expression1
sodium arsenatedecreases expression1
beta-lapachoneincreases expression1
sodium arseniteincreases expression1
perfluorooctanoic acidincreases expression1
methacrylaldehydeaffects cotreatment, increases oxidation1
beta-methylcholineaffects expression1
torcetrapibincreases expression1
abrinedecreases expression1
Resveratrolaffects cotreatment, increases expression1
Temozolomideincreases expression1
Sunitinibincreases expression1
Acetaminophendecreases expression1
Acroleinaffects cotreatment, increases oxidation1
Air Pollutantsaffects expression, increases abundance1
Vehicle Emissionsincreases abundance, increases expression1
Doxorubicindecreases expression1
Leaddecreases expression1
Plant Extractsaffects cotreatment, increases expression1
Thiramdecreases expression1
Cadmium Chloridedecreases expression1
Particulate Matterincreases abundance, increases expression1

Cellosaurus cell lines

2 cell lines: 2 cancer cell line

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

CellosaurusNameCategorySex
CVCL_SM56HAP1 EXD2 (-) 1Cancer cell lineMale
CVCL_SM57HAP1 EXD2 (-) 2Cancer 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.