PIH1D1

gene
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Also known as FLJ20643Pih1MOT48DNAAF14

Summary

PIH1D1 (PIH1 domain containing 1, HGNC:26075) is a protein-coding gene on chromosome 19q13.33, encoding PIH1 domain-containing protein 1 (Q9NWS0). Involved in the assembly of C/D box small nucleolar ribonucleoprotein (snoRNP) particles.

Enables several functions, including enzyme binding activity; histone binding activity; and phosphoprotein binding activity. Involved in several processes, including positive regulation of macromolecule metabolic process; positive regulation of signal transduction; and protein-containing complex assembly. Located in cytoplasm and nucleolus. Part of R2TP complex; RPAP3/R2TP/prefoldin-like complex; and pre-snoRNP complex.

Source: NCBI Gene 55011 — RefSeq curated summary.

At a glance

  • Clinical variants (ClinVar): 54 total
  • MANE Select transcript: NM_017916

Identifiers

Gene identifiers

FieldValue
HGNC IDHGNC:26075
Approved symbolPIH1D1
NamePIH1 domain containing 1
Location19q13.33
Locus typegene with protein product
StatusApproved
AliasesFLJ20643, Pih1, MOT48, DNAAF14
Ensembl geneENSG00000104872
Ensembl biotypeprotein_coding
OMIM611480
Entrez55011

Gene structure

Transcript identifiers

Ensembl transcripts: 36 — 18 protein_coding, 9 nonsense_mediated_decay, 8 retained_intron, 1 protein_coding_CDS_not_defined

ENST00000262265, ENST00000593629, ENST00000593900, ENST00000594845, ENST00000595074, ENST00000595516, ENST00000595550, ENST00000595633, ENST00000596049, ENST00000596651, ENST00000596895, ENST00000596916, ENST00000597415, ENST00000597577, ENST00000598175, ENST00000598889, ENST00000599366, ENST00000599791, ENST00000600875, ENST00000601053, ENST00000601807, ENST00000601825, ENST00000602076, ENST00000602226, ENST00000715674, ENST00000715675, ENST00000911064, ENST00000911065, ENST00000911066, ENST00000911067, ENST00000911068, ENST00000911069, ENST00000911070, ENST00000911071, ENST00000919081, ENST00000943281

RefSeq mRNA: 1 — MANE Select: NM_017916 NM_017916

CCDS: CCDS12765

Canonical transcript exons

ENST00000262265 — 9 exons

ExonStartEnd
ENSE000029853134945148549451814
ENSE000034895214944947549449654
ENSE000035414744944782749447908
ENSE000035719644944800149448062
ENSE000036128834944733849447467
ENSE000036143724944702449447099
ENSE000036331244945078249450848
ENSE000036824274944655149446694
ENSE000038469624944629849446423

Expression profiles

Bgee: expression breadth ubiquitous, 287 present calls, max score 97.93.

FANTOM5 (CAGE): breadth ubiquitous, TPM avg 40.7470 / max 377.3761, expressed in 1820 samples.

FANTOM5 promoters (6 alternative TSS)

Promoter IDTPM avgSamples expressed
18204129.92961813
1820407.31931694
1820421.78781246
1820431.3904830
1820390.2893123
1820380.03078

Top tissues by expression

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

TissueAnatomy IDExpression scoreQuality
granulocyteCL:000009497.93gold quality
right hemisphere of cerebellumUBERON:001489097.46gold quality
cerebellar hemisphereUBERON:000224597.39gold quality
cerebellar cortexUBERON:000212997.27gold quality
right uterine tubeUBERON:000130297.08gold quality
mucosa of transverse colonUBERON:000499196.96gold quality
right lobe of thyroid glandUBERON:000111996.95gold quality
left lobe of thyroid glandUBERON:000112096.79gold quality
lower esophagus mucosaUBERON:003583496.72gold quality
small intestine Peyer’s patchUBERON:000345496.69gold quality
skin of legUBERON:000151196.64gold quality
skin of abdomenUBERON:000141696.58gold quality
metanephros cortexUBERON:001053396.49gold quality
right lobe of liverUBERON:000111496.47gold quality
spleenUBERON:000210696.47gold quality
endocervixUBERON:000045896.42gold quality
prefrontal cortexUBERON:000045196.39gold quality
cerebellumUBERON:000203796.37gold quality
minor salivary glandUBERON:000183096.34gold quality
body of stomachUBERON:000116196.29gold quality
adenohypophysisUBERON:000219696.21gold quality
ganglionic eminenceUBERON:000402396.21gold quality
body of uterusUBERON:000985396.15gold quality
pituitary glandUBERON:000000796.08gold quality
lower esophagusUBERON:001347396.08gold quality
lower esophagus muscularis layerUBERON:003583396.08gold quality
transverse colonUBERON:000115796.06gold quality
left ovaryUBERON:000211996.06gold quality
ventricular zoneUBERON:000305396.05gold quality
thyroid glandUBERON:000204696.02gold quality

Single-cell (SCXA)

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

ExperimentMarker?Max mean expression
E-MTAB-6524no262.71
E-ANND-3no0.00

Regulation

Is transcription factor: no

Upstream regulators (CollecTRI, top): MTOR

Literature-anchored findings (GeneRIF, showing 8)

  • Is part of an RNA polymerase II-associated complex with possible chaperone activity. (PMID:19450687)
  • PIH1D1 may stabilize SNF5 by attenuating its proteasome degradation pathway. (PMID:20078948)
  • These results suggest that PIH1D1 may also function as a novel modulator of apoptosis pathway. (PMID:21078300)
  • Human PIH1 domain-containing protein 1 (PIH1) interacts directly with histone H4 and recruits the Brg1-SWI/SNF complex via SNF5 to human rRNA genes. (PMID:22368283)
  • this study investigated the interaction between RPAP3 and PIH1D1. (PMID:23159623)
  • PIH1D1 interacts with mTOR complex 1 and enhances ribosome RNA transcription. (PMID:24036451)
  • We propose that protein complexes assembled by the R2TP complex are defined by phosphorylation of a specific motif and recognition by the PIH1D1 subunit (PMID:24656813)
  • An RPAP3:PIH1D1 sub-complex is found demonstrating the need for a 34-residue insertion, specific of RPAP3 isoform 1, for the tight binding of PIH1D1. (PMID:30033218)

Cross-species orthologs

3 orthologs

OrganismSymbolGene ID
danio_reriopih1d1ENSDARG00000037955
mus_musculusPih1d1ENSMUSG00000003423
rattus_norvegicusPih1d1ENSRNOG00000020634

Paralogs (2): PIH1D2 (ENSG00000150773), DNAAF2 (ENSG00000165506)

Protein

Protein identifiers

PIH1 domain-containing protein 1Q9NWS0 (reviewed: Q9NWS0)

Alternative names: Nucleolar protein 17 homolog

All UniProt accessions (16): Q9NWS0, A0AAQ5BIG8, A0AAQ5BIK2, M0QXD5, M0QYA2, M0QYF4, M0QZ61, M0QZM3, M0QZZ1, M0R028, M0R0J2, M0R1R3, M0R2H3, M0R2P8, M0R3A4, M0R3A8

UniProt curated annotations — full annotation on UniProt →

Function. Involved in the assembly of C/D box small nucleolar ribonucleoprotein (snoRNP) particles. Recruits the SWI/SNF complex to the core promoter of rRNA genes and enhances pre-rRNA transcription. Mediates interaction of TELO2 with the R2TP complex which is necessary for the stability of MTOR and SMG1. Positively regulates the assembly and activity of the mTORC1 complex.

Subunit / interactions. Component of the R2TP complex composed at least of RUVBL1, RUVBL2, RPAP3 and PIHD1. Component of the PAQosome complex which is responsible for the biogenesis of several protein complexes and which consists of R2TP complex members RUVBL1, RUVBL2, RPAP3 and PIH1D1, URI complex members PFDN2, PFDN6, PDRG1, UXT and URI1 as well as ASDURF, POLR2E and DNAAF10/WDR92. Interacts with phosphorylated TELO2 and mediates interaction of TELO2 with the R2TP complex. Interacts with phosphorylated ECD, EFTUD2/SNRP116, RPB1 and UBR5 and with RPB1 in a phosphorylation-independent manner. Interacts with the core C/D box snoRNP particle components NOP58 and FBL and with RUVBL1/TIP49. Interacts with RPAP3 and DNAAF10. Interacts with histone H4 and with SWI/SNF complex member SMARCB1/SNF5. Interacts with the mTORC1 complex member RPTOR. Interacts with MSL1.

Subcellular location. Nucleus.

Tissue specificity. Expressed at low levels in normal mammary epithelial cells (at protein level). Highest expression in lung, leukocyte and placenta. Expressed at lower levels in brain, prostate, colon, heart, small intestine, liver, ovary, pancreas, skeletal muscle, spleen, testis and thymus.

Domain organisation. The N-terminal region is required for binding to phosphorylated substrates while the C-terminal region binds to the other R2TP complex components.

Similarity. Belongs to the PIH1 family.

Isoforms (3)

UniProt IDNamesCanonical?
Q9NWS0-11yes
Q9NWS0-22
Q9NWS0-33

RefSeq proteins (1): NP_060386* (*=MANE)

Domains & families (InterPro)

IDNameType
IPR012981PIH1_NDomain
IPR041442PIH1D1/2/3_CS-likeDomain
IPR050734PIH1/Kintoun_subfamilyFamily

Pfam: PF08190, PF18201

UniProt features (40 total): strand 13, mutagenesis site 8, sequence variant 5, site 3, helix 3, sequence conflict 2, modified residue 2, splice variant 2, chain 1, turn 1

Structure

Experimental structures (PDB)

8 structures.

PDBMethodResolution (Å)
7AVCX-RAY DIFFRACTION1.2
9THXX-RAY DIFFRACTION1.36
4PSFX-RAY DIFFRACTION1.58
9TIAX-RAY DIFFRACTION2.07
9TJQX-RAY DIFFRACTION2.19
4PSIX-RAY DIFFRACTION2.45
8BDUX-RAY DIFFRACTION2.47
6GXZX-RAY DIFFRACTION2.96

Predicted structure (AlphaFold)

ModelpLDDTFraction very-high
AF-Q9NWS0-F179.270.33

Functional residue map

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

Catalytic / active sites (3): 57 (interacts with telo2); 64 (interacts with telo2); 113 (interacts with telo2)

Post-translational modifications (2): 12, 173

Mutagenesis-validated functional residues (8):

PositionPhenotype
54abolishes binding to histone h4.
55no effect on binding to histone h4.
57abolishes binding to telo2.
64abolishes binding to ecd, eftud2, rpb1, telo2 and ubr5.
113reduces binding to telo2.
163reduces binding to telo2.
166reduces binding to telo2.
168abolishes binding to telo2.

Function

Pathways and Gene Ontology

Reactome pathways

0 pathways

MSigDB gene sets: 157 (showing top): GOBP_RIBOSOME_BIOGENESIS, GOBP_EPITHELIUM_DEVELOPMENT, MODULE_151, GOBP_CELLULAR_RESPONSE_TO_CARBOHYDRATE_STIMULUS, GOBP_POSITIVE_REGULATION_OF_TOR_SIGNALING, GOBP_CELLULAR_RESPONSE_TO_OXYGEN_CONTAINING_COMPOUND, GOBP_RRNA_TRANSCRIPTION, TERAMOTO_OPN_TARGETS_CLUSTER_6, GOBP_PROTEIN_STABILIZATION, GOBP_PROTEIN_RNA_COMPLEX_ORGANIZATION, GOBP_RESPONSE_TO_OXYGEN_CONTAINING_COMPOUND, GOBP_REGULATION_OF_PROTEIN_STABILITY, GOBP_POSITIVE_REGULATION_OF_INTRACELLULAR_SIGNAL_TRANSDUCTION, GOBP_INTRACELLULAR_GLUCOSE_HOMEOSTASIS, GOBP_CARBOHYDRATE_HOMEOSTASIS

GO Biological Process (10): box C/D snoRNP assembly (GO:0000492), chromatin remodeling (GO:0006338), rRNA processing (GO:0006364), epithelial cell differentiation (GO:0030855), snoRNA localization (GO:0048254), protein stabilization (GO:0050821), positive regulation of transcription of nucleolar large rRNA by RNA polymerase I (GO:1901838), positive regulation of glucose mediated signaling pathway (GO:1902661), positive regulation of TORC1 signaling (GO:1904263), TORC1 complex assembly (GO:1905669)

GO Molecular Function (6): protein kinase binding (GO:0019901), histone binding (GO:0042393), ATPase binding (GO:0051117), phosphoprotein binding (GO:0051219), histone reader activity (GO:0140566), protein binding (GO:0005515)

GO Cellular Component (7): nucleus (GO:0005634), nucleolus (GO:0005730), cytoplasm (GO:0005737), pre-snoRNP complex (GO:0070761), R2TP complex (GO:0097255), RPAP3/R2TP/prefoldin-like complex (GO:1990062), ribonucleoprotein complex (GO:1990904)

GO top-level categories

Rollup of top GO terms by namespace:

CategoryTerms
protein-containing complex3
protein binding2
small nucleolar ribonucleoprotein complex assembly1
chromatin organization1
RNA processing1
rRNA metabolic process1
ribosome biogenesis1
cell differentiation1
epithelium development1
RNA localization1
regulation of protein stability1
nucleolar large rRNA transcription by RNA polymerase I1
positive regulation of transcription by RNA polymerase I1
regulation of transcription of nucleolar large rRNA by RNA polymerase I1
positive regulation of signal transduction1
glucose mediated signaling pathway1
regulation of glucose mediated signaling pathway1
positive regulation of TOR signaling1
TORC1 signaling1
regulation of TORC1 signaling1
protein-containing complex assembly1
kinase binding1
enzyme binding1
nucleosome1
histone binding1
chromatin-protein adaptor activity1
binding1
intracellular membrane-bounded organelle1
nuclear lumen1
intracellular membraneless organelle1
intracellular anatomical structure1
cellular anatomical structure1
ribonucleoprotein complex1

Protein interactions and networks

STRING

2156 interactions, top by confidence (×1000):

Protein AProtein BPartner UniProtScore
PIH1D1RPAP3Q9H6T3998
PIH1D1RUVBL1P82276997
PIH1D1RUVBL2Q9Y230997
PIH1D1HSP90AA1P07900977
PIH1D1HSP90AB1P08238963
PIH1D1NOP58Q9Y2X3864
PIH1D1DNAAF10Q96MX6861
PIH1D1NOP56O00567835
PIH1D1ZNHIT3Q15649798
PIH1D1NUFIP1Q9UHK0790
PIH1D1SNU13P55769770
PIH1D1PFDN6O15212769
PIH1D1SPAG1Q07617754
PIH1D1PFDN2Q9UHV9750
PIH1D1RNF113AO15541739

IntAct

208 interactions, top by confidence:

ABTypeScore
RPTORMTORpsi-mi:“MI:0914”(association)0.980
PARD6APRKCIpsi-mi:“MI:0914”(association)0.950
NPHP1NPHP4psi-mi:“MI:2364”(proximity)0.930
POLR2EPOLR3Apsi-mi:“MI:0914”(association)0.870
PIH1D1RUVBL2psi-mi:“MI:0914”(association)0.860
POLR2JPOLR1Cpsi-mi:“MI:0914”(association)0.830
RPAP2PIH1D1psi-mi:“MI:0915”(physical association)0.800
ECDPIH1D1psi-mi:“MI:0915”(physical association)0.740
PIH1D1ECDpsi-mi:“MI:0914”(association)0.740
PIH1D1ECDpsi-mi:“MI:0915”(physical association)0.740
PPP1CCCCDC85Cpsi-mi:“MI:0914”(association)0.740
PIH1D1ECDpsi-mi:“MI:0407”(direct interaction)0.740
POLR2EMED19psi-mi:“MI:0914”(association)0.730
POLR2APOLR2Dpsi-mi:“MI:0914”(association)0.730
POLR3EPOLR3Apsi-mi:“MI:0914”(association)0.730
POLR2JPOLR2Dpsi-mi:“MI:0914”(association)0.730
RPRD1BPOLR2Dpsi-mi:“MI:0914”(association)0.730
PIH1D1RPAP3psi-mi:“MI:0914”(association)0.730
CFTRESYT2psi-mi:“MI:2364”(proximity)0.710

BioGRID (941): PIH1D1 (Two-hybrid), TSC22D4 (Two-hybrid), PIH1D1 (Affinity Capture-RNA), PIH1D1 (Affinity Capture-MS), PIH1D1 (Affinity Capture-MS), POLR2G (Affinity Capture-MS), PDRG1 (Affinity Capture-MS), RUVBL1 (Affinity Capture-MS), POLR1A (Affinity Capture-MS), POLR3A (Affinity Capture-MS), RPAP2 (Affinity Capture-MS), POLR3E (Affinity Capture-MS), UXT (Affinity Capture-MS), POLR2A (Affinity Capture-MS), POLR2M (Affinity Capture-MS)

ESM2 similar proteins: D3ZND0, F1MX48, O95382, P47823, Q0VCI6, Q1RM55, Q2KIJ6, Q2YD98, Q3SYU1, Q4V7F5, Q58CQ5, Q5PPF5, Q5PRB3, Q64350, Q66H85, Q6IUP3, Q6P5E6, Q6P6S4, Q6V7V2, Q7TMX5, Q80TT2, Q8BRN9, Q8C6B2, Q8CHW4, Q8N0W3, Q8VDM1, Q924T7, Q96EP0, Q96NY9, Q99L85, Q99PL6, Q9BST9, Q9BXL6, Q9BZV1, Q9CQJ2, Q9D479, Q9EPK6, Q9H173, Q9H8Y5, Q9NWS0

Diamond homologs: P38768, Q0VCI6, Q4V7F5, Q7Q9F6, Q9NWS0, P0CU29, Q1RM55, Q7ZWY2, Q9CQJ2, Q499A3, B5BUZ8, B4J4Y2

SIGNOR signaling

3 interactions.

AEffectBMechanism
PIH1D1“up-regulates quantity by stabilization”mTORC1binding
MRE11“up-regulates activity”PIH1D1binding
PIH1D1“form complex”“R2TP core co-chaperone”binding

Enriched among interaction partners

Reactome pathways and GO biological processes over-represented among this gene’s 128 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
RNA Polymerase III Chain Elongation860.4×4e-11
FGFR2 mutant receptor activation654.4×1e-08
Signaling by FGFR2 IIIa TM750.1×2e-09
Abortive elongation of HIV-1 transcript in the absence of Tat847.3×2e-10
RNA Polymerase III Transcription Termination847.3×2e-10
RNA Polymerase III Transcription Initiation From Type 2 Promoter945.3×4e-11
RNA Polymerase III Transcription Initiation From Type 1 Promoter943.7×4e-11
RNA Polymerase III Transcription Initiation From Type 3 Promoter943.7×4e-11

GO biological processes:

GO termPartnersFoldFDR
protein stabilization179.9×9e-10

Disease & clinical

Clinical variants and AI predictions

ClinVar

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

ClassificationCount (floor)
Pathogenic0
Likely pathogenic0
Uncertain significance41
Likely benign0
Benign0

Top pathogenic / likely-pathogenic (0)

SpliceAI

1665 predictions. Top by Δscore:

VariantEffectΔscore
19:49446548:CACCT:Cdonor_loss1.0000
19:49446559:T:TAdonor_gain1.0000
19:49446804:C:Tacceptor_gain1.0000
19:49446805:A:Tacceptor_gain1.0000
19:49447017:AACTC:Adonor_loss1.0000
19:49447018:ACTC:Adonor_loss1.0000
19:49447019:CTCA:Cdonor_loss1.0000
19:49447021:CA:Cdonor_loss1.0000
19:49447022:A:ACdonor_gain1.0000
19:49447022:ACCAG:Adonor_loss1.0000
19:49447023:C:CTdonor_gain1.0000
19:49447023:C:Tdonor_loss1.0000
19:49447023:CCAG:Cdonor_gain1.0000
19:49447095:CAGGC:Cacceptor_gain1.0000
19:49447097:GGC:Gacceptor_gain1.0000
19:49447099:CCTGA:Cacceptor_loss1.0000
19:49447100:C:CCacceptor_gain1.0000
19:49447100:CTGA:Cacceptor_loss1.0000
19:49447336:AC:Adonor_gain1.0000
19:49447337:CC:Cdonor_gain1.0000
19:49447347:G:Cdonor_gain1.0000
19:49447351:T:Adonor_gain1.0000
19:49447352:C:CAdonor_gain1.0000
19:49447821:CCTCA:Cdonor_loss1.0000
19:49447822:CTCAC:Cdonor_loss1.0000
19:49447823:TCA:Tdonor_loss1.0000
19:49447824:CA:Cdonor_loss1.0000
19:49447825:A:ACdonor_gain1.0000
19:49447825:A:ATdonor_loss1.0000
19:49447825:AC:Adonor_gain1.0000

AlphaMissense

1887 scored. Top likely-pathogenic:

VariantProtein changeam_pathogenicity
19:49449608:G:CN68K0.998
19:49449608:G:TN68K0.998
19:49449614:G:CF66L0.998
19:49449614:G:TF66L0.998
19:49449616:A:GF66L0.998
19:49447871:G:TA146D0.997
19:49448029:A:TV124D0.997
19:49448042:A:CY120D0.997
19:49449602:G:CC70W0.997
19:49449615:A:GF66S0.997
19:49449641:C:AK57N0.997
19:49449641:C:GK57N0.997
19:49447859:A:GL150P0.996
19:49447859:A:TL150H0.996
19:49448044:G:TA119D0.996
19:49449506:A:CS102R0.996
19:49449506:A:TS102R0.996
19:49449508:T:GS102R0.996
19:49449647:G:CC55W0.996
19:49449603:C:TC70Y0.995
19:49449604:A:GC70R0.995
19:49446419:A:GL279S0.994
19:49447435:C:GG172R0.994
19:49447849:T:AK153N0.994
19:49447849:T:GK153N0.994
19:49447850:T:AK153I0.994
19:49447872:C:GA146P0.994
19:49449516:A:GI99T0.994
19:49449610:T:CN68D0.994
19:49449612:A:TI67N0.994

dbSNP variants (sampled 300 via entrez): RS1000550973 (19:49451803 CG>C), RS1000594040 (19:49446686 G>A,T), RS1001046406 (19:49447006 C>G,T), RS1001156061 (19:49450356 G>A,T), RS1001831143 (19:49447613 C>A), RS1001981964 (19:49452895 T>C), RS1002988743 (19:49451676 G>C), RS1004063567 (19:49452067 T>G), RS1004332550 (19:49453508 G>A,C,T), RS1004622272 (19:49453658 A>C,G), RS1004664773 (19:49450774 T>C), RS1005222919 (19:49452595 A>G), RS1005531196 (19:49449325 G>A,C,T), RS1005749031 (19:49452345 G>A,C), RS1005783637 (19:49446035 C>A)

Disease associations

OMIM: gene MIM:611480 | 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: no

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

CTD chemical–gene interactions

26 total (human), top 26 by PubMed support.

ChemicalActions (top 5)PubMed papers
bisphenol Adecreases expression2
Valproic Acidincreases methylation, affects expression2
beta-lapachoneincreases expression1
arseniteaffects binding, increases reaction1
sodium arseniteaffects methylation1
cobaltous chloridedecreases expression1
di-n-butylphosphoric acidaffects expression1
CGP 52608affects binding, increases reaction1
ICG 001increases expression1
Grape Seed Proanthocyanidinsaffects cotreatment, decreases expression1
Temozolomideincreases expression1
Caffeinedecreases phosphorylation1
Carbamazepineaffects expression1
Carcinogensdecreases expression1
Catechinaffects cotreatment, decreases expression1
Coumestrolincreases expression1
Doxorubicindecreases expression1
Ivermectindecreases expression1
Seleniumincreases expression, affects cotreatment1
Smokedecreases expression1
Thiramdecreases expression1
Tobacco Smoke Pollutiondecreases expression1
Vitamin Eaffects cotreatment, increases expression1
Cyclosporinedecreases expression1
Copper Sulfatedecreases expression1
Lactic Aciddecreases expression1

Cellosaurus cell lines

1 cell lines: 1 cancer cell line

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

CellosaurusNameCategorySex
CVCL_XR60HAP1 PIH1D1 (-)Cancer 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.