POLL

gene
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Summary

POLL (DNA polymerase lambda, HGNC:9184) is a protein-coding gene on chromosome 10q24.32, encoding DNA polymerase lambda (Q9UGP5). DNA polymerase that functions in several pathways of DNA repair.

This gene encodes a DNA polymerase. DNA polymerases catalyze DNA-template-directed extension of the 3’-end of a DNA strand. This particular polymerase, which is a member of the X family of DNA polymerases, likely plays a role in non-homologous end joining and other DNA repair processes. Alternatively spliced transcript variants have been described.

Source: NCBI Gene 27343 — RefSeq curated summary.

At a glance

  • Clinical variants (ClinVar): 118 total — 1 pathogenic
  • Druggable target: yes
  • Dosage sensitivity (ClinGen): haploinsufficiency no evidence, triplosensitivity no evidence
  • MANE Select transcript: NM_001174084

Identifiers

Gene identifiers

FieldValue
HGNC IDHGNC:9184
Approved symbolPOLL
NameDNA polymerase lambda
Location10q24.32
Locus typegene with protein product
StatusApproved
Ensembl geneENSG00000166169
Ensembl biotypeprotein_coding
OMIM606343
Entrez27343

Gene structure

Transcript identifiers

Ensembl transcripts: 54 — 50 protein_coding, 4 protein_coding_CDS_not_defined

ENST00000299206, ENST00000339310, ENST00000370162, ENST00000370168, ENST00000370169, ENST00000370172, ENST00000413344, ENST00000415897, ENST00000426919, ENST00000429502, ENST00000430045, ENST00000454524, ENST00000461587, ENST00000463515, ENST00000470140, ENST00000485369, ENST00000628479, ENST00000882355, ENST00000882356, ENST00000882357, ENST00000882358, ENST00000882359, ENST00000882360, ENST00000882361, ENST00000882362, ENST00000882363, ENST00000882364, ENST00000882365, ENST00000882366, ENST00000882367, ENST00000937304, ENST00000937305, ENST00000937306, ENST00000937307, ENST00000937308, ENST00000937309, ENST00000937310, ENST00000937311, ENST00000937312, ENST00000937313, ENST00000937314, ENST00000937315, ENST00000937316, ENST00000937317, ENST00000937318, ENST00000937319, ENST00000937320, ENST00000937321, ENST00000937322, ENST00000942758, ENST00000942759, ENST00000942760, ENST00000942761, ENST00000942762

RefSeq mRNA: 4 — MANE Select: NM_001174084 NM_001174084, NM_001174085, NM_001308382, NM_013274

CCDS: CCDS7513, CCDS76332

Canonical transcript exons

ENST00000370162 — 9 exons

ExonStartEnd
ENSE00001424221101587822101588257
ENSE00003462420101582763101582891
ENSE00003475842101585316101585478
ENSE00003503918101578882101579817
ENSE00003508364101583508101583681
ENSE00003567328101585862101586156
ENSE00003626756101580248101580416
ENSE00003889827101584602101584919
ENSE00003891177101587246101587406

Expression profiles

Bgee: expression breadth ubiquitous, 240 present calls, max score 93.15.

FANTOM5 (CAGE): breadth ubiquitous, TPM avg 12.9084 / max 231.5970, expressed in 1791 samples.

FANTOM5 promoters (3 alternative TSS)

Promoter IDTPM avgSamples expressed
11109012.76831791
1110880.072713
1110890.067419

Top tissues by expression

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

TissueAnatomy IDExpression scoreQuality
right uterine tubeUBERON:000130293.15gold quality
body of pancreasUBERON:000115093.02gold quality
left testisUBERON:000453391.95gold quality
right testisUBERON:000453491.86gold quality
right lobe of thyroid glandUBERON:000111990.90gold quality
bloodUBERON:000017890.68gold quality
body of stomachUBERON:000116190.67gold quality
granulocyteCL:000009490.55gold quality
apex of heartUBERON:000209890.23gold quality
adenohypophysisUBERON:000219690.14gold quality
left lobe of thyroid glandUBERON:000112090.13gold quality
pituitary glandUBERON:000000790.02gold quality
hindlimb stylopod muscleUBERON:000425289.97gold quality
testisUBERON:000047389.89gold quality
tendon of biceps brachiiUBERON:000818889.72gold quality
thyroid glandUBERON:000204689.68gold quality
right adrenal glandUBERON:000123389.63gold quality
left ovaryUBERON:000211989.62gold quality
gastrocnemiusUBERON:000138889.42gold quality
right adrenal gland cortexUBERON:003582789.35gold quality
metanephros cortexUBERON:001053389.21gold quality
muscle of legUBERON:000138389.05gold quality
right ovaryUBERON:000211889.04gold quality
stomachUBERON:000094588.96gold quality
mucosa of stomachUBERON:000119988.82gold quality
pancreasUBERON:000126488.66gold quality
esophagogastric junction muscularis propriaUBERON:003584188.65gold quality
lower esophagusUBERON:001347388.59gold quality
lower esophagus muscularis layerUBERON:003583388.59gold quality
right lobe of liverUBERON:000111488.53gold quality

Single-cell (SCXA)

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

ExperimentMarker?Max mean expression
E-ANND-3yes4.97

Regulation

Is transcription factor: no

Upstream regulators (CollecTRI, top): CREB1, SP1, TP53, VSX2

miRNA regulators (miRDB)

22 targeting POLL, 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-450099.9972.722367
HSA-MIR-548AW99.9972.573559
HSA-LET-7A-5P99.9872.291790
HSA-LET-7B-5P99.9872.311790
HSA-LET-7C-5P99.9872.291790
HSA-LET-7E-5P99.9872.291790
HSA-LET-7F-5P99.9872.561784
HSA-LET-7G-5P99.9872.371784
HSA-LET-7I-5P99.9872.371788
HSA-MIR-98-5P99.9872.331787
HSA-LET-7D-5P99.9671.761632
HSA-MIR-445899.9671.641650
HSA-MIR-6892-3P99.6866.401178
HSA-MIR-486-3P99.5166.821901
HSA-MIR-149-5P99.2567.161315
HSA-MIR-6510-5P99.1466.591081
HSA-MIR-797798.6566.182590
HSA-MIR-471098.6165.961048
HSA-MIR-6873-5P98.4566.141417
HSA-MIR-445697.5064.881678
HSA-MIR-3192-5P96.9865.761926
HSA-MIR-18494.2464.40152

Functional genomics

ClinGen dosage: haploinsufficiency 0 (no evidence), triplosensitivity 0 (no evidence). ClinGen Gene Dosage Map

Literature-anchored findings (GeneRIF, showing 40)

  • role in DNA repair (PMID:11821417)
  • role in dna replication and DNA repair (PMID:11974915)
  • complex between PCNA and pol lambda may play an important role in the bypass of abasic sites in human cells (PMID:12368291)
  • DNA polymerase lambda has an intrinsic terminal deoxyribonucleotidyl transferase activity that preferentially adds pyrimidines onto 3’OH ends of DNA oligonucleotides and elongates an RNA primer hybridized to a DNA template. (PMID:12683997)
  • mammalian Pol lambda has a role in non-homologous end-joining (PMID:12829698)
  • Polymerase lambda is the primary gap-filling polymerase for accurate nonhomologous end joining (PMID:14561766)
  • pol lambda Phe506Arg/Gly mutants possess very low polymerase and terminal transferase activities as well as greatly reduced abilities for processive DNA synthesis (PMID:14627824)
  • fills short-patched DNA gaps in base excision repair pathways and participates in mammalian nonhomologous end-joining pathways to repair double-stranded DNA breaks (PMID:15157109)
  • Results link p53 status with POLkappa expression and suggest that loss of p53 function may in part contribute to the observed POLkappa upregulation in human lung cancers. (PMID:15202001)
  • A molecular mechanism is suggested for the observed high in vivo rate of frameshift generation by pol lambda and the remarkable ability of pol lambda to promote microhomology pairing between two DNA strands. (PMID:15350147)
  • A helix-hairpin-helix domain of DNA polymerase lambda is important for primer binding and/or for proliferating cell nuclear antigen interaction. (PMID:15358682)
  • determined that Fyn phosphorylated MAP-2c on tyrosine 67 (PMID:15537631)
  • crystal structures of Pol lambda representing three steps in filling a single-nucleotide gap (PMID:15608652)
  • Human DNA polymerase kappa, an error-prone enzyme that is up-regulated in lung cancers, induces DNA breaks and stimulates DNA exchanges as well as aneuploidy. (PMID:15665310)
  • Results suggest that Pol lambda plays a role in the short-patch base excision repair rather than contributes to the long-patch base excision repair pathway. (PMID:15979954)
  • DNA polymerase lambda is phosphorylated in vitro by several cyclin-dependent kinase/cyclin complexes, including Cdk2/cyclin A, in its proline-serine-rich domain. (PMID:16174846)
  • DNA polymerase lambda has the ability to create base pair mismatches and human replication protein A can suppress this intrinsic in vitro mutator phenotype. (PMID:16522650)
  • DNA polymerase fidelity is controlled not by an accessory protein or a proofreading exonuclease domain but by an internal regulatory domain (PMID:16675458)
  • DNA polymerase lambda is unable to differentiate between matched and mismatched termini during the DNA binding step, thus accounting for the relatively high efficiency of mismatch extension. (PMID:16807316)
  • Kinetic studies on human DNA polymerase lambda reveal roles of a downstream strand and the 5’-terminal moieties (PMID:17005572)
  • The erroneous nucleotide incorporations catalyzed by DNA polymerases lambda and beta as well as the subsequent ligation catalyzed by a DNA ligase during base excision repair are a threat to genomic integrity. (PMID:17321545)
  • cloning, expression and tissue distribution in normal liver and hepatoma (PMID:17653665)
  • DNA pol lambda active site residue tyrosine 505 determined the nucleotide selectivity opposite 1,2-dihydro-2-oxoadenine during error-free bypass of the 1,2-dihydro-2-oxoadenine lesion. (PMID:17666409)
  • capacity of Pol lambda either to insert opposite 8oxoG or to extend correct base pairs containing such a damage could be beneficial for its role in NHEJ (PMID:17686665)
  • Pol lambda is stabilized during cell cycle progression in late S and G2 phases, most likely allowing Pol lambda to correctly conduct repair of damaged DNA during and after S phase. (PMID:18688254)
  • analysis of human DNA polymerase lambda with Mg2+ and Mn2+ from ab initio quantum mechanical/molecular mechanical studies (PMID:18692600)
  • RAGE is under genetic selection in the non-African populations. (PMID:19060005)
  • replication protein A and proliferating cell nuclear antigen act as molecular switches to activate the DNA pol lambda- dependent highly efficient and faithful repair of A:8-oxo-G mismatches in human cells and to repress DNA pol beta activity. (PMID:19104052)
  • dATP was a preferential substrate for DNA polymerase beta and dGMP was the only substrate for DNA polymerase lambda. (PMID:19120024)
  • These experiments suggest that polymerase lambda does not undergo major conformational changes during the catalysis in the solution phase. (PMID:19467241)
  • when bound to a 2-nucleotide gap, Pol lambda scrunches the template strand and binds the additional uncopied template base in an extrahelical position within a binding pocket that comprises three conserved amino acids. (PMID:19701199)
  • a natural mutator variant of human DNA polymerase lambda promotes chromosomal instability by compromising NHEJ (PMID:19806195)
  • observe specific recruitment of MUTYH, DNA pol lambda, proliferating cell nuclear antigen (PCNA), flap endonuclease 1 (FEN1) and DNA ligases I and III from human cell extracts to A:8-oxo-G DNA, but not to undamaged DNA. (PMID:19820168)
  • DNA polymerase lambda uses a novel sugar selection mechanism to discriminate against ribonucleotides, whereby the ribose 2’-hydroxyl group was excluded mostly by a backbone segment and slightly by the side chain of Y505. (PMID:19900463)
  • Both Pol lambda- and (Pol kappa)-positive staining were associated with shorter survival in glioma patients. (PMID:20164241)
  • analysis of the interaction between DNA Polymerase lambda and anticancer nucleoside analogs (PMID:20348107)
  • DNA polymerase lambda can bypass a thymine glycol lesion on the template strand of gapped DNA substrates. (PMID:20423048)
  • The results demonstrate that loop 1 is not essential for catalytic activity, but it is important for the fidelity of DNA synthesis and the accuracy of non-homologous end joining. (PMID:20435673)
  • study found expression of PollambdaR438W sensitizes cells to camptothecin by affecting the homologous recombination pathway, whereas overexpression of pollambdaWT did not impact cell survival; this effect depends entirely on its DNA polymerase activity (PMID:20693240)
  • both pol lambda and pol beta interact with the upstream DNA glycosylases for repair of alkylated and oxidized DNA bases (PMID:20805875)

Cross-species orthologs

3 orthologs

OrganismSymbolGene ID
danio_reriopollENSDARG00000039613
mus_musculusPollENSMUSG00000025218
rattus_norvegicusPollENSRNOG00000016748

Paralogs (3): POLB (ENSG00000070501), DNTT (ENSG00000107447), POLM (ENSG00000122678)

Protein

Protein identifiers

DNA polymerase lambdaQ9UGP5 (reviewed: Q9UGP5)

Alternative names: DNA polymerase beta-2, DNA polymerase kappa

All UniProt accessions (11): A8K860, Q9UGP5, Q5JQN9, Q5JQP0, Q5JQP1, Q5JQP2, Q5JQP3, Q5JQP4, Q5JQP7, Q5JQP8, Q9HBN3

UniProt curated annotations — full annotation on UniProt →

Function. DNA polymerase that functions in several pathways of DNA repair. Involved in base excision repair (BER) responsible for repair of lesions that give rise to abasic (AP) sites in DNA. Also contributes to DNA double-strand break repair by non-homologous end joining and homologous recombination. Has both template-dependent and template-independent (terminal transferase) DNA polymerase activities. Also has a 5’-deoxyribose-5-phosphate lyase (dRP lyase) activity.

Subunit / interactions. Interacts with PCNA. Interacts with PAXX; promoting POLL recruitment to double-strand breaks (DSBs) and stimulation of the end-filling activity of POLL. Interacts with XRCC4; promoting POLL recruitment to double-strand breaks (DSBs) and stimulation of the end-filling activity of POLL. Interacts with NHEJ1/XLF; promoting POLL recruitment to double-strand breaks (DSBs) and stimulation of the end-filling activity of POLL.

Subcellular location. Nucleus. Chromosome.

Tissue specificity. Expressed in a number of tissues. Abundant in testis.

Similarity. Belongs to the DNA polymerase type-X family.

Isoforms (2)

UniProt IDNamesCanonical?
Q9UGP5-11yes
Q9UGP5-22

RefSeq proteins (4): NP_001167555, NP_001167556, NP_001295311, NP_037406 (=MANE)

Domains & families (InterPro)

IDNameType
IPR001357BRCT_domDomain
IPR002008DNA_pol_X_beta-likeFamily
IPR002054DNA-dir_DNA_pol_XDomain
IPR010996HHH_MUS81Domain
IPR018944DNA_pol_lambd_fingers_domainDomain
IPR019843DNA_pol-X_BSBinding_site
IPR022312DNA_pol_XFamily
IPR027421DNA_pol_lamdba_lyase_dom_sfHomologous_superfamily
IPR028207DNA_pol_B_palm_palmDomain
IPR029398PolB_thumbDomain
IPR036420BRCT_dom_sfHomologous_superfamily
IPR037160DNA_Pol_thumb_sfHomologous_superfamily
IPR043519NT_sfHomologous_superfamily

Pfam: PF10391, PF14716, PF14791, PF14792

Enzyme classification (BRENDA):

  • EC 4.2.99.B1 — (BRENDA: organisms, substrates, inhibitors, Km, kcat entries)

Catalyzed reactions (Rhea), 1 shown:

  • DNA(n) + a 2’-deoxyribonucleoside 5’-triphosphate = DNA(n+1) + diphosphate (RHEA:22508)

UniProt features (74 total): helix 26, strand 18, binding site 7, region of interest 5, mutagenesis site 5, splice variant 2, sequence variant 2, sequence conflict 2, turn 2, compositionally biased region 2, chain 1, domain 1, active site 1

Structure

Experimental structures (PDB)

96 structures, top 30 by resolution.

PDBMethodResolution (Å)
7M07X-RAY DIFFRACTION1.57
7M49X-RAY DIFFRACTION1.6
9NPUX-RAY DIFFRACTION1.63
7M47X-RAY DIFFRACTION1.65
2BCQX-RAY DIFFRACTION1.65
7M09X-RAY DIFFRACTION1.65
7M4BX-RAY DIFFRACTION1.66
7M08X-RAY DIFFRACTION1.7
7M4LX-RAY DIFFRACTION1.7
7M4KX-RAY DIFFRACTION1.72
5IIJX-RAY DIFFRACTION1.72
2BCRX-RAY DIFFRACTION1.75
5IIIX-RAY DIFFRACTION1.8
7M0DX-RAY DIFFRACTION1.8
7M4DX-RAY DIFFRACTION1.82
7M0AX-RAY DIFFRACTION1.83
7M4AX-RAY DIFFRACTION1.87
7M4GX-RAY DIFFRACTION1.88
7M45X-RAY DIFFRACTION1.89
2PFNX-RAY DIFFRACTION1.9
4XA5X-RAY DIFFRACTION1.9
8U0PX-RAY DIFFRACTION1.9
7M44X-RAY DIFFRACTION1.9
7M4EX-RAY DIFFRACTION1.9
7M46X-RAY DIFFRACTION1.92
7M4HX-RAY DIFFRACTION1.92
7M48X-RAY DIFFRACTION1.93
5IIMX-RAY DIFFRACTION1.94
7M4FX-RAY DIFFRACTION1.95
1XSNX-RAY DIFFRACTION1.95

Predicted structure (AlphaFold)

ModelpLDDTFraction very-high
AF-Q9UGP5-F180.900.59

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 (1): 312 (schiff-base intermediate with dna)

Ligand- & substrate-binding residues (7): 386; 417–420; 426–429; 427; 429; 490; 513

Mutagenesis-validated functional residues (5):

PositionPhenotype
312reduces drp lyase activity by over 90%.
427loss of polymerase activity; when associated with a-429.
429loss of polymerase activity; when associated with a-427.
505no effect on polymerase activity. reduces terminal transferase activities.
506strongly reduces polymerase and terminal transferase activities.

Function

Pathways and Gene Ontology

Reactome pathways

1 pathways

IDPathway
R-HSA-5693571Nonhomologous End-Joining (NHEJ)

MSigDB gene sets: 123 (showing top): KAUFFMANN_DNA_REPAIR_GENES, CAGCTG_AP4_Q5, IRF7_01, GOBP_NUCLEOTIDE_EXCISION_REPAIR, GOMF_DNA_POLYMERASE_ACTIVITY, GOBP_IMMUNOGLOBULIN_PRODUCTION, GOBP_DNA_DAMAGE_RESPONSE, GOBP_SOMATIC_DIVERSIFICATION_OF_IMMUNE_RECEPTORS, GOBP_DNA_BIOSYNTHETIC_PROCESS, RFX1_02, GOBP_SOMATIC_DIVERSIFICATION_OF_IMMUNE_RECEPTORS_VIA_SOMATIC_MUTATION, REACTOME_DNA_REPAIR, GOBP_RECOMBINATIONAL_REPAIR, GOBP_DNA_REPLICATION, CETS1P54_01

GO Biological Process (10): double-strand break repair via homologous recombination (GO:0000724), DNA replication (GO:0006260), base-excision repair, gap-filling (GO:0006287), nucleotide-excision repair (GO:0006289), double-strand break repair via nonhomologous end joining (GO:0006303), somatic hypermutation of immunoglobulin genes (GO:0016446), DNA biosynthetic process (GO:0071897), DNA metabolic process (GO:0006259), DNA repair (GO:0006281), DNA damage response (GO:0006974)

GO Molecular Function (9): DNA binding (GO:0003677), DNA-directed DNA polymerase activity (GO:0003887), metal ion binding (GO:0046872), 5’-deoxyribose-5-phosphate lyase activity (GO:0051575), protein binding (GO:0005515), transferase activity (GO:0016740), nucleotidyltransferase activity (GO:0016779), lyase activity (GO:0016829), DNA polymerase activity (GO:0034061)

GO Cellular Component (4): nucleus (GO:0005634), nucleoplasm (GO:0005654), site of double-strand break (GO:0035861), chromosome (GO:0005694)

Reactome top-level categories

Rollup of top-1 pathways:

CategoryPathways
DNA Double-Strand Break Repair1

GO top-level categories

Rollup of top GO terms by namespace:

CategoryTerms
DNA metabolic process4
double-strand break repair2
DNA biosynthetic process2
catalytic activity, acting on DNA2
catalytic activity2
recombinational repair1
base-excision repair1
DNA repair1
somatic diversification of immune receptors via somatic mutation1
somatic diversification of immunoglobulins1
nucleic acid biosynthetic process1
nucleic acid metabolic process1
DNA damage response1
cellular response to stress1
nucleic acid binding1
DNA polymerase activity1
cation binding1
carbon-oxygen lyase activity1
binding1
transferase activity, transferring phosphorus-containing groups1
nucleotidyltransferase activity1
intracellular membrane-bounded organelle1
nuclear lumen1
cellular anatomical structure1
site of DNA damage1
intracellular membraneless organelle1

Protein interactions and networks

STRING

1174 interactions, top by confidence (×1000):

Protein AProtein BPartner UniProtScore
POLLREV1Q9UBZ9961
POLLTENT4AQ5XG87957
POLLRAD18Q9NS91916
POLLXRCC4Q13426899
POLLREV3LO60673879
POLLFBXW4P57775874
POLLLIG1P18858839
POLLLBX1P52954814
POLLXRCC6P12956805
POLLSMUG1Q53HV7792
POLLLIG4P49917791
POLLXRCC5P13010784
POLLPOLHQ9Y253772
POLLPOLIQ9UNA4769
POLLWRNQ14191764

IntAct

23 interactions, top by confidence:

ABTypeScore
POLLLDOC1psi-mi:“MI:0915”(physical association)0.550
LDOC1POLLpsi-mi:“MI:0915”(physical association)0.550
POLLBCKDHApsi-mi:“MI:0914”(association)0.510
MUTYHPOLLpsi-mi:“MI:0407”(direct interaction)0.440
POLLH2BC13psi-mi:“MI:0915”(physical association)0.400
POLLH2BC21psi-mi:“MI:0915”(physical association)0.400
POLLUBCpsi-mi:“MI:0915”(physical association)0.400
XRCC1POLLpsi-mi:“MI:0915”(physical association)0.400
POLLFAM9Bpsi-mi:“MI:0915”(physical association)0.370
POLLTFIP11psi-mi:“MI:0915”(physical association)0.370
DCUN1D1RGSL1psi-mi:“MI:0914”(association)0.350
POLLSULT1C2psi-mi:“MI:0914”(association)0.350
INKA2CDC42BPApsi-mi:“MI:0914”(association)0.350
POLLPGK2psi-mi:“MI:0914”(association)0.350
POLLRPA2psi-mi:“MI:0915”(physical association)0.000
POLLBCKDHBpsi-mi:“MI:0915”(physical association)0.000
POLLRPA1psi-mi:“MI:0915”(physical association)0.000
POLLRPA3psi-mi:“MI:0915”(physical association)0.000
POLLSSRP1psi-mi:“MI:0915”(physical association)0.000
POLLWRNpsi-mi:“MI:0915”(physical association)0.000
BCKDHAPOLLpsi-mi:“MI:0915”(physical association)0.000
POLLSUPT16Hpsi-mi:“MI:0915”(physical association)0.000

BioGRID (108): POLL (Two-hybrid), POLL (Two-hybrid), POLL (Two-hybrid), POLL (Two-hybrid), POLL (Two-hybrid), SSX2IP (Two-hybrid), FSD2 (Two-hybrid), KRT40 (Two-hybrid), FAM9B (Two-hybrid), KRTAP10-7 (Two-hybrid), KRTAP10-3 (Two-hybrid), C9orf64 (Affinity Capture-MS), SCGB1D1 (Affinity Capture-MS), SEMG2 (Affinity Capture-MS), SEMG1 (Affinity Capture-MS)

ESM2 similar proteins: A0A8C2MDK8, A7SLX5, A7YY46, D3ZEY4, D3ZX08, E9QAM5, O59713, O95822, P0C7A1, P48760, P52333, P52824, Q002B5, Q07071, Q14397, Q15477, Q2KI24, Q2M296, Q2NKY8, Q3SYT1, Q3T7C9, Q3U1Y4, Q3URQ7, Q4R380, Q52L34, Q567W6, Q568Y2, Q5I0I8, Q5NCQ5, Q5ZHX9, Q6GPQ5, Q6NZR5, Q6P5E8, Q8BUI3, Q8BX80, Q8C9A2, Q8NFF5, Q8NFI3, Q91X44, Q920F5

Diamond homologs: O57383, P06746, P06766, Q27958, Q4R380, Q5RKI3, Q67VC8, Q6DRD3, Q7T6Y4, Q8K409, Q9FNY4, Q9QXE2, Q9UGP5, P09838, Q9JIW4, Q9NP87, A4PCD4, O02789, O57486, P04053, P06526, P36195, P42118, Q92089, A8N936

SIGNOR signaling

9 interactions.

AEffectBMechanism
HUWE1“down-regulates quantity by destabilization”POLLpolyubiquitination
ATM“up-regulates activity”POLLphosphorylation
CyclinA2/CDK2“up-regulates quantity by stabilization”POLLphosphorylation
PRKDC“up-regulates activity”POLLphosphorylation
CDK2“up-regulates quantity by stabilization”POLLphosphorylation
CDK2“up-regulates activity”POLLphosphorylation

Enriched among interaction partners

Reactome pathways and GO biological processes over-represented among this gene’s 22 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
Gap-filling DNA repair synthesis and ligation in GG-NER5115.6×5e-08
HDR through Homologous Recombination (HRR)550.1×1e-06
Gap-filling DNA repair synthesis and ligation in TC-NER547.0×2e-06
Regulation of TP53 Activity through Phosphorylation743.4×3e-08
Processing of DNA double-strand break ends742.1×3e-08
G2/M DNA damage checkpoint638.0×6e-07
Meiotic recombination534.1×6e-06

GO biological processes:

GO termPartnersFoldFDR
mismatch repair5162.0×5e-09
base-excision repair6140.4×2e-10
DNA replication649.6×5e-08
DNA repair516.0×1e-04

Disease & clinical

Clinical variants and AI predictions

ClinVar

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

ClassificationCount (floor)
Pathogenic1
Likely pathogenic0
Uncertain significance83
Likely benign11
Benign12

Top pathogenic / likely-pathogenic (1)

Variant IDHGVSClassification
815374GRCh37/hg19 10q24.31-24.32(chr10:102925257-103401586)x3Pathogenic

SpliceAI

1479 predictions. Top by Δscore:

VariantEffectΔscore
10:101582761:A:ACdonor_gain1.0000
10:101582762:C:CCdonor_gain1.0000
10:101582762:CTGT:Cdonor_gain1.0000
10:101582789:C:Adonor_gain1.0000
10:101582803:T:Adonor_gain1.0000
10:101582891:CCT:Cacceptor_loss1.0000
10:101582892:C:Gacceptor_loss1.0000
10:101582893:T:Gacceptor_loss1.0000
10:101583522:T:Cdonor_gain1.0000
10:101583546:C:Adonor_gain1.0000
10:101583586:A:ACdonor_gain1.0000
10:101583587:C:CCdonor_gain1.0000
10:101584920:C:CCacceptor_gain1.0000
10:101584921:T:Cacceptor_gain1.0000
10:101584921:T:TCacceptor_gain1.0000
10:101585864:A:ACdonor_gain1.0000
10:101585865:C:CCdonor_gain1.0000
10:101586153:CACT:Cacceptor_gain1.0000
10:101580250:T:TAdonor_gain0.9900
10:101580412:TGGAC:Tacceptor_gain0.9900
10:101580414:GAC:Gacceptor_gain0.9900
10:101580415:AC:Aacceptor_gain0.9900
10:101580416:CC:Cacceptor_gain0.9900
10:101580417:C:CCacceptor_gain0.9900
10:101582619:A:Cdonor_gain0.9900
10:101582740:A:ACdonor_gain0.9900
10:101582741:C:CCdonor_gain0.9900
10:101582741:CTG:Cdonor_gain0.9900
10:101582741:CTGCT:Cdonor_gain0.9900
10:101582761:ACTGT:Adonor_gain0.9900

AlphaMissense

3734 scored. Top likely-pathogenic:

VariantProtein changeam_pathogenicity
10:101584636:A:GL286P0.997
10:101583527:G:TA349D0.996
10:101579640:C:GR514P0.995
10:101583519:A:GW352R0.995
10:101583519:A:TW352R0.995
10:101579622:G:TA520D0.994
10:101579663:G:CF506L0.994
10:101579663:G:TF506L0.994
10:101579665:A:GF506L0.994
10:101584636:A:TL286H0.994
10:101584615:A:TV293D0.993
10:101584668:C:AR275S0.993
10:101584668:C:GR275S0.993
10:101580415:A:TV399D0.992
10:101584714:A:GL260P0.992
10:101579463:C:GR573P0.991
10:101579638:A:GS515P0.991
10:101579719:G:TR488S0.991
10:101579721:C:GR487P0.991
10:101580352:C:GR420P0.991
10:101584669:C:GR275T0.991
10:101585932:A:GW114R0.991
10:101585932:A:TW114R0.991
10:101580324:G:CD429E0.990
10:101580324:G:TD429E0.990
10:101579631:C:GR517P0.989
10:101583528:C:GA349P0.989
10:101580319:A:TL431H0.988
10:101584734:G:CN253K0.988
10:101584734:G:TN253K0.988

dbSNP variants (sampled 300 via entrez): RS1000354698 (10:101586782 A>C), RS1000400356 (10:101580204 T>C), RS1000599171 (10:101585794 A>C,T), RS1000630474 (10:101586108 C>T), RS1001012227 (10:101587069 T>C), RS1001187033 (10:101587593 G>T), RS1001607457 (10:101584208 G>A), RS1001638682 (10:101584540 C>T), RS1002722260 (10:101588830 T>C), RS1002752023 (10:101589083 G>A), RS1003005143 (10:101583826 G>A,T), RS1003020413 (10:101582337 C>T), RS1003343671 (10:101582108 C>T), RS1003617617 (10:101580709 G>A), RS1003627014 (10:101581818 T>C,G)

Disease associations

OMIM: gene MIM:606343 | 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): CHEMBL5367 (SINGLE PROTEIN)

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

Binding affinities (BindingDB)

2 measured of 29 human assays (29 total across all organisms); most potent 2 below. Values come from heterogeneous assays and are not directly comparable.

LigandMeasureValue
CHEMBL3898463IC506900 nM
CHEMBL3926514IC507400 nM

ChEMBL bioactivities

11 potent at pChembl≥5 of 15 total, top 11 by pChembl (potency: 10 = 0.1 nM, 6 = 1 µM).

pChemblTypeValueUnitMolecule
5.30IC505000nMCHEMBL3978947
5.28IC505200nMOBLONGIFOLIN C
5.27IC505400nMGUTTIFERONE K
5.25IC505600nMCHEMBL3889506
5.24IC505800nMCHEMBL3917534
5.24IC505700nMCHEMBL3976184
5.21IC506200nMCHEMBL3907489
5.16IC506900nMCHEMBL3898463
5.16IC507000nMCHEMBL1917196
5.13IC507400nMCHEMBL3926514
5.06IC508800nMCHEMBL3935433

PubChem BioAssay actives

35 with measured affinity, of 211 total; 35 most potent distinct compounds. Largely complementary to BindingDB; screening values are coarse (µM, 4 dp), so sub-nM hits tie at the floor.

CompoundAssayTypeValueUnit
(5Z)-5-[[4-(2-methylphenyl)sulfanyl-3-nitrophenyl]methylidene]-2-sulfanylidene-1,3-thiazolidin-4-one1800107: DNA Pol λ PEX Assay from Article 10.1021/cb4007562: “Expanding the Scope of Human DNA Polymerase ¿ and ß Inhibitors.”ic503.9000uM
(5Z)-5-[[3-bromo-4-(3-fluoro-4-methylphenyl)sulfanylphenyl]methylidene]-2-sulfanylidene-1,3-thiazolidin-4-one1800107: DNA Pol λ PEX Assay from Article 10.1021/cb4007562: “Expanding the Scope of Human DNA Polymerase ¿ and ß Inhibitors.”ic504.0000uM
(5Z)-5-[[2,4-bis[(4-methylphenyl)sulfanyl]phenyl]methylidene]-2-sulfanylidene-1,3-thiazolidin-4-one1800107: DNA Pol λ PEX Assay from Article 10.1021/cb4007562: “Expanding the Scope of Human DNA Polymerase ¿ and ß Inhibitors.”ic504.0000uM
(1R,3E,5S,6S,7R)-3-[(3,4-dihydroxyphenyl)-hydroxymethylidene]-7-[(2E,6R)-6-hydroxy-3,7-dimethylocta-2,7-dienyl]-6-methyl-1,5-bis(3-methylbut-2-enyl)-6-(4-methylpent-3-enyl)bicyclo[3.3.1]nonane-2,4,9-trione1323393: Inhibition of recombinant human His-tagged DNA polymerase lambda assessed as reduction in [3H]dTTP incorporation using poly(dA)/oligo(dT)18 as template/primer preincubated for 10 mins followed by template/primer addition measured after 60 minsic505.0000uM
(1R,3E,5S,6S,7R)-3-[(3,4-dihydroxyphenyl)-hydroxymethylidene]-7-[(2E)-3,7-dimethylocta-2,6-dienyl]-6-methyl-1,5-bis(3-methylbut-2-enyl)-6-(4-methylpent-3-enyl)bicyclo[3.3.1]nonane-2,4,9-trione1323393: Inhibition of recombinant human His-tagged DNA polymerase lambda assessed as reduction in [3H]dTTP incorporation using poly(dA)/oligo(dT)18 as template/primer preincubated for 10 mins followed by template/primer addition measured after 60 minsic505.2000uM
(1R,3E,5S,6S,7R)-3-[(3,4-dihydroxyphenyl)-hydroxymethylidene]-6-methyl-1,5,7-tris(3-methylbut-2-enyl)-6-(4-methylpent-3-enyl)bicyclo[3.3.1]nonane-2,4,9-trione1323393: Inhibition of recombinant human His-tagged DNA polymerase lambda assessed as reduction in [3H]dTTP incorporation using poly(dA)/oligo(dT)18 as template/primer preincubated for 10 mins followed by template/primer addition measured after 60 minsic505.4000uM
(1R,3E,5S,6S,7R)-3-[(3,4-dihydroxyphenyl)-hydroxymethylidene]-7-[(2E,5E)-7-hydroxy-3,7-dimethylocta-2,5-dienyl]-6-methyl-1,5-bis(3-methylbut-2-enyl)-6-(4-methylpent-3-enyl)bicyclo[3.3.1]nonane-2,4,9-trione1323393: Inhibition of recombinant human His-tagged DNA polymerase lambda assessed as reduction in [3H]dTTP incorporation using poly(dA)/oligo(dT)18 as template/primer preincubated for 10 mins followed by template/primer addition measured after 60 minsic505.6000uM
(1R,3E,5S,6S,7R)-3-[hydroxy-(3-hydroxyphenyl)methylidene]-6-methyl-1,5,7-tris(3-methylbut-2-enyl)-6-(4-methylpent-3-enyl)bicyclo[3.3.1]nonane-2,4,9-trione1323393: Inhibition of recombinant human His-tagged DNA polymerase lambda assessed as reduction in [3H]dTTP incorporation using poly(dA)/oligo(dT)18 as template/primer preincubated for 10 mins followed by template/primer addition measured after 60 minsic505.7000uM
(5Z)-5-[[3-chloro-4-(4-methylphenyl)sulfanylphenyl]methylidene]-2-sulfanylidene-1,3-thiazolidin-4-one1800107: DNA Pol λ PEX Assay from Article 10.1021/cb4007562: “Expanding the Scope of Human DNA Polymerase ¿ and ß Inhibitors.”ic505.7000uM
(1R,3E,5S,6S,7R)-3-[(3,4-dihydroxyphenyl)-hydroxymethylidene]-7-[(2E,6S)-6-hydroxy-3,7-dimethylocta-2,7-dienyl]-6-methyl-1,5-bis(3-methylbut-2-enyl)-6-(4-methylpent-3-enyl)bicyclo[3.3.1]nonane-2,4,9-trione1323393: Inhibition of recombinant human His-tagged DNA polymerase lambda assessed as reduction in [3H]dTTP incorporation using poly(dA)/oligo(dT)18 as template/primer preincubated for 10 mins followed by template/primer addition measured after 60 minsic505.8000uM
(5Z)-5-[[4-(4-methylphenyl)sulfanyl-3-nitrophenyl]methylidene]-2-sulfanylidene-1,3-thiazolidin-4-one1800107: DNA Pol λ PEX Assay from Article 10.1021/cb4007562: “Expanding the Scope of Human DNA Polymerase ¿ and ß Inhibitors.”ic505.9000uM
(5Z)-5-[[4-(3-methylphenyl)sulfanyl-3-nitrophenyl]methylidene]-2-sulfanylidene-1,3-thiazolidin-4-one1800107: DNA Pol λ PEX Assay from Article 10.1021/cb4007562: “Expanding the Scope of Human DNA Polymerase ¿ and ß Inhibitors.”ic506.0000uM
(6E)-6-[(3,4-dihydroxyphenyl)-hydroxymethylidene]-8-[(2E)-3,7-dimethylocta-2,6-dienyl]-2,2-dimethyl-8-(3-methylbut-2-enyl)chromene-5,7-dione1323393: Inhibition of recombinant human His-tagged DNA polymerase lambda assessed as reduction in [3H]dTTP incorporation using poly(dA)/oligo(dT)18 as template/primer preincubated for 10 mins followed by template/primer addition measured after 60 minsic506.2000uM
(1R,3Z,6R,9S,10R,13R)-3-[(3,4-dihydroxyphenyl)-hydroxymethylidene]-13-[(2E)-3,7-dimethylocta-2,6-dienyl]-6-(2-hydroxypropan-2-yl)-9-methyl-1,10-bis(3-methylbut-2-enyl)-5-oxatricyclo[7.2.2.04,10]tridecane-2,11-dione1323393: Inhibition of recombinant human His-tagged DNA polymerase lambda assessed as reduction in [3H]dTTP incorporation using poly(dA)/oligo(dT)18 as template/primer preincubated for 10 mins followed by template/primer addition measured after 60 minsic506.9000uM
(5,8-dioxonaphthalen-1-yl) dodecanoate627886: Inhibition of His-tagged human DNA polymerase lambda using poly(dA)/oligo(dT)18 (A/T = 2/1) and dTTP as the DNA template-primer and nucleotide substrate after 60 minsic507.0000uM
(1R,3Z,6R,9S,10R,13R)-3-[(3,4-dihydroxyphenyl)-hydroxymethylidene]-6-(2-hydroxypropan-2-yl)-9-methyl-1,10,13-tris(3-methylbut-2-enyl)-5-oxatricyclo[7.2.2.04,10]tridecane-2,11-dione1323393: Inhibition of recombinant human His-tagged DNA polymerase lambda assessed as reduction in [3H]dTTP incorporation using poly(dA)/oligo(dT)18 as template/primer preincubated for 10 mins followed by template/primer addition measured after 60 minsic507.4000uM
(1R,3E,5S,6S,7S)-3-[(3,4-dihydroxyphenyl)-hydroxymethylidene]-7-(2-hydroxy-3-methylbut-3-enyl)-6-methyl-1,5-bis(3-methylbut-2-enyl)-6-(4-methylpent-3-enyl)bicyclo[3.3.1]nonane-2,4,9-trione1323393: Inhibition of recombinant human His-tagged DNA polymerase lambda assessed as reduction in [3H]dTTP incorporation using poly(dA)/oligo(dT)18 as template/primer preincubated for 10 mins followed by template/primer addition measured after 60 minsic508.8000uM
(5Z)-5-[[4-(4-methylphenyl)sulfanyl-3-nitrophenyl]methylidene]-1,3-thiazolidine-2,4-dione1800107: DNA Pol λ PEX Assay from Article 10.1021/cb4007562: “Expanding the Scope of Human DNA Polymerase ¿ and ß Inhibitors.”ic5010.0000uM
(5Z)-5-[(4-cyclohexylsulfanyl-3-nitrophenyl)methylidene]-2-sulfanylidene-1,3-thiazolidin-4-one1800107: DNA Pol λ PEX Assay from Article 10.1021/cb4007562: “Expanding the Scope of Human DNA Polymerase ¿ and ß Inhibitors.”ic5010.0000uM
(5Z)-5-[[4-(4-methylphenyl)sulfanylphenyl]methylidene]-2-sulfanylidene-1,3-thiazolidin-4-one1800107: DNA Pol λ PEX Assay from Article 10.1021/cb4007562: “Expanding the Scope of Human DNA Polymerase ¿ and ß Inhibitors.”ic5010.0000uM
(5Z)-5-[[3-fluoro-4-(4-methylphenyl)sulfanylphenyl]methylidene]-2-sulfanylidene-1,3-thiazolidin-4-one1800107: DNA Pol λ PEX Assay from Article 10.1021/cb4007562: “Expanding the Scope of Human DNA Polymerase ¿ and ß Inhibitors.”ic5010.0000uM
(5Z)-5-[[3-bromo-4-(4-methylphenyl)sulfanylphenyl]methylidene]-2-sulfanylidene-1,3-thiazolidin-4-one1800107: DNA Pol λ PEX Assay from Article 10.1021/cb4007562: “Expanding the Scope of Human DNA Polymerase ¿ and ß Inhibitors.”ic5010.0000uM
(5Z)-5-[[4-(4-methylphenyl)sulfanyl-3-(trifluoromethyl)phenyl]methylidene]-2-sulfanylidene-1,3-thiazolidin-4-one1800107: DNA Pol λ PEX Assay from Article 10.1021/cb4007562: “Expanding the Scope of Human DNA Polymerase ¿ and ß Inhibitors.”ic5010.0000uM
2-(4-methylphenyl)sulfanyl-5-[(Z)-(4-oxo-2-sulfanylidene-1,3-thiazolidin-5-ylidene)methyl]benzonitrile1800107: DNA Pol λ PEX Assay from Article 10.1021/cb4007562: “Expanding the Scope of Human DNA Polymerase ¿ and ß Inhibitors.”ic5010.0000uM
(5Z)-5-[[4-(4-ethylphenyl)sulfanyl-3-nitrophenyl]methylidene]-2-sulfanylidene-1,3-thiazolidin-4-one1800107: DNA Pol λ PEX Assay from Article 10.1021/cb4007562: “Expanding the Scope of Human DNA Polymerase ¿ and ß Inhibitors.”ic5010.0000uM
(5Z)-5-[[3-nitro-4-[4-(trifluoromethyl)phenyl]sulfanylphenyl]methylidene]-2-sulfanylidene-1,3-thiazolidin-4-one1800107: DNA Pol λ PEX Assay from Article 10.1021/cb4007562: “Expanding the Scope of Human DNA Polymerase ¿ and ß Inhibitors.”ic5010.0000uM
(5Z)-5-[[4-(3-fluoro-4-methylphenyl)sulfanyl-3-nitrophenyl]methylidene]-2-sulfanylidene-1,3-thiazolidin-4-one1800107: DNA Pol λ PEX Assay from Article 10.1021/cb4007562: “Expanding the Scope of Human DNA Polymerase ¿ and ß Inhibitors.”ic5010.0000uM
(5Z)-5-[[3-nitro-4-[2,3,5,6-tetrafluoro-4-(trifluoromethyl)phenyl]sulfanylphenyl]methylidene]-2-sulfanylidene-1,3-thiazolidin-4-one1800107: DNA Pol λ PEX Assay from Article 10.1021/cb4007562: “Expanding the Scope of Human DNA Polymerase ¿ and ß Inhibitors.”ic5010.0000uM
(5Z)-5-[[4-(3,5-dimethylphenyl)sulfanyl-3-nitrophenyl]methylidene]-2-sulfanylidene-1,3-thiazolidin-4-one1800107: DNA Pol λ PEX Assay from Article 10.1021/cb4007562: “Expanding the Scope of Human DNA Polymerase ¿ and ß Inhibitors.”ic5010.0000uM
(5Z)-5-[(4-naphthalen-2-ylsulfanyl-3-nitrophenyl)methylidene]-2-sulfanylidene-1,3-thiazolidin-4-one1800107: DNA Pol λ PEX Assay from Article 10.1021/cb4007562: “Expanding the Scope of Human DNA Polymerase ¿ and ß Inhibitors.”ic5010.0000uM
(5Z)-5-[[4-(2-methylphenyl)sulfanylphenyl]methylidene]-2-sulfanylidene-1,3-thiazolidin-4-one1800107: DNA Pol λ PEX Assay from Article 10.1021/cb4007562: “Expanding the Scope of Human DNA Polymerase ¿ and ß Inhibitors.”ic5010.0000uM
(5Z)-5-[[3-fluoro-4-(2-methylphenyl)sulfanylphenyl]methylidene]-2-sulfanylidene-1,3-thiazolidin-4-one1800107: DNA Pol λ PEX Assay from Article 10.1021/cb4007562: “Expanding the Scope of Human DNA Polymerase ¿ and ß Inhibitors.”ic5010.0000uM
(5Z)-5-[[4-(2-methylphenyl)sulfanyl-3-(trifluoromethyl)phenyl]methylidene]-2-sulfanylidene-1,3-thiazolidin-4-one1800107: DNA Pol λ PEX Assay from Article 10.1021/cb4007562: “Expanding the Scope of Human DNA Polymerase ¿ and ß Inhibitors.”ic5010.0000uM
(5Z)-5-[[4-bromo-5-(4-methylphenyl)sulfanylthiophen-2-yl]methylidene]-2-sulfanylidene-1,3-thiazolidin-4-one1800107: DNA Pol λ PEX Assay from Article 10.1021/cb4007562: “Expanding the Scope of Human DNA Polymerase ¿ and ß Inhibitors.”ic5010.0000uM
4-hydroxy-5-[1-[4-(4-methylphenyl)sulfanyl-3-nitrophenyl]ethenyl]-3H-1,3-thiazole-2-thione1800107: DNA Pol λ PEX Assay from Article 10.1021/cb4007562: “Expanding the Scope of Human DNA Polymerase ¿ and ß Inhibitors.”ic5010.0000uM

CTD chemical–gene interactions

27 total (human), top 27 by PubMed support.

ChemicalActions (top 5)PubMed papers
Benzo(a)pyreneincreases expression, increases methylation2
Estradioldecreases expression2
alpha-pineneaffects cotreatment, increases oxidation, increases abundance1
honokioldecreases activity1
methacrylaldehydeaffects cotreatment, increases oxidation, increases abundance1
benzo(a)pyrene diolepoxide Iincreases expression1
perfluorooctane sulfonic acidincreases expression1
abrineincreases expression1
Decitabinedecreases expression, decreases reaction1
Glyphosateincreases expression1
Acroleinincreases oxidation, increases abundance, affects cotreatment1
Air Pollutantsaffects cotreatment, increases abundance, increases oxidation1
Amiodaroneincreases expression1
Caffeineincreases phosphorylation1
Doxorubicindecreases expression1
Ozoneaffects cotreatment, increases oxidation, increases abundance1
Phthalic Acidsdecreases methylation1
Seleniumincreases expression, affects cotreatment1
Selenomethionineaffects expression1
Smokedecreases expression1
Thiramdecreases expression1
Tobacco Smoke Pollutiondecreases expression1
Vitamin Eincreases expression, affects cotreatment1
Aflatoxin B1decreases expression, increases methylation, decreases reaction1
Okadaic Aciddecreases expression1
Acrylamidedecreases expression1
Volatile Organic Compoundsaffects cotreatment, increases oxidation1

ChEMBL screening assays

21 unique, capped per target: 21 binding

Representative assays (with source publication via chembl_document):

Assay IDTypeDescriptionSource paper
CHEMBL1023129BindingInhibition of human DNA polymerase lambda at 100 uMPenicilliols A and B, novel inhibitors specific to mammalian Y-family DNA polymerases. — Bioorg Med Chem

Cellosaurus cell lines

4 cell lines: 4 cancer cell line

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

CellosaurusNameCategorySex
CVCL_B2BGAbcam HeLa POLL KOCancer cell lineFemale
CVCL_TF03HAP1 POLL (-) 1Cancer cell lineMale
CVCL_TF04HAP1 POLL (-) 2Cancer cell lineMale
CVCL_TF05HAP1 POLL (-) 3Cancer 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.