TRMT112

Summary

TRMT112 (tRNA methyltransferase activator subunit 11-2, HGNC:26940) is a protein-coding gene on chromosome 11q13.1, encoding Multifunctional methyltransferase subunit TRM112-like protein (Q9UI30). Acts as an activator of both rRNA/tRNA and protein methyltransferases. It is a common-essential gene (DepMap: required in 100.0% of cancer cell lines).

Enables protein heterodimerization activity; protein methyltransferase activity; and tRNA methyltransferase activator activity. Involved in macromolecule methylation and positive regulation of macromolecule metabolic process. Located in nucleoplasm and perinuclear region of cytoplasm. Part of protein-containing complex.

Source: NCBI Gene 51504 — RefSeq curated summary.

At a glance

• GWAS associations: 3
• Clinical variants (ClinVar): 21 total
• Druggable target: yes
• Cancer dependency (DepMap): dependent in 100.0% of screened cell lines (common-essential)
• MANE Select transcript: NM_016404

Identifiers

Gene identifiers

Field	Value
HGNC ID	HGNC:26940
Approved symbol	TRMT112
Name	tRNA methyltransferase activator subunit 11-2
Location	11q13.1
Locus type	gene with protein product
Status	Approved
Aliases	HSPC152, HSPC170, TRM112, TRMT11-2, hTrm112
Ensembl gene	ENSG00000173113
Ensembl biotype	protein_coding
OMIM	618630
Entrez	51504

Gene structure

Transcript identifiers

Ensembl transcripts: 14 — 10 protein_coding, 4 retained_intron

ENST00000308774, ENST00000535126, ENST00000535750, ENST00000537918, ENST00000539854, ENST00000544844, ENST00000715728, ENST00000905123, ENST00000927038, ENST00000927039, ENST00000927040, ENST00000927041, ENST00000965649, ENST00000965650

RefSeq mRNA: 5 — MANE Select: NM_016404 NM_001286082, NM_001286084, NM_001372071, NM_001372072, NM_016404

CCDS: CCDS66113, CCDS8068

Canonical transcript exons

ENST00000544844 — 4 exons

Exon	Start	End
ENSE00001195289	64317058	64317147
ENSE00001195296	64317264	64317365
ENSE00002259488	64317449	64317559
ENSE00003904140	64316460	64316968

Expression profiles

Bgee: expression breadth ubiquitous, 286 present calls, max score 99.84.

FANTOM5 (CAGE): breadth ubiquitous, TPM avg 169.4582 / max 1060.5571, expressed in 1827 samples.

FANTOM5 promoters (4 alternative TSS)

Promoter ID	TPM avg	Samples expressed
120385	162.2849	1827
120386	4.1413	1690
120384	1.7823	879
120387	1.2496	847

Top tissues by expression

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

Tissue	Anatomy ID	Expression score	Quality
oocyte	CL:0000023	99.84	gold quality
secondary oocyte	CL:0000655	99.66	gold quality
adult organism	UBERON:0007023	99.08	gold quality
right adrenal gland	UBERON:0001233	99.04	gold quality
left adrenal gland	UBERON:0001234	99.02	gold quality
left adrenal gland cortex	UBERON:0035825	99.01	gold quality
adenohypophysis	UBERON:0002196	98.95	gold quality
adrenal cortex	UBERON:0001235	98.94	gold quality
right adrenal gland cortex	UBERON:0035827	98.94	gold quality
pituitary gland	UBERON:0000007	98.92	gold quality
left ovary	UBERON:0002119	98.90	gold quality
tendon of biceps brachii	UBERON:0008188	98.88	gold quality
right ovary	UBERON:0002118	98.79	gold quality
ovary	UBERON:0000992	98.78	gold quality
adrenal gland	UBERON:0002369	98.78	gold quality
body of uterus	UBERON:0009853	98.64	gold quality
endocervix	UBERON:0000458	98.60	gold quality
ectocervix	UBERON:0012249	98.55	gold quality
lymph node	UBERON:0000029	98.53	gold quality
left uterine tube	UBERON:0001303	98.53	gold quality
pigmented layer of retina	UBERON:0001782	98.41	gold quality
stromal cell of endometrium	CL:0002255	98.40	gold quality
cartilage tissue	UBERON:0002418	98.35	gold quality
popliteal artery	UBERON:0002250	98.33	gold quality
tibial artery	UBERON:0007610	98.33	gold quality
right testis	UBERON:0004534	98.32	gold quality
esophagogastric junction muscularis propria	UBERON:0035841	98.31	gold quality
aorta	UBERON:0000947	98.30	gold quality
seminal vesicle	UBERON:0000998	98.29	gold quality
left coronary artery	UBERON:0001626	98.29	gold quality

Single-cell (SCXA)

Detected in 4 experiment(s), a significant marker in 4.

Experiment	Marker?	Max mean expression
E-HCAD-5	yes	979.54
E-GEOD-93593	yes	652.34
E-CURD-114	yes	62.29
E-ANND-3	no	0.00

Regulation

Is transcription factor: no

miRNA regulators (miRDB)

15 targeting TRMT112, top 30 by miRDB confidence (max_score; target_count = how many genes the miRNA targets in total — lower means more specific):

miRNA	Max score	Avg score	miRNA target_count
HSA-MIR-6798-5P	100.00	65.77	699
HSA-MIR-1277-5P	100.00	73.95	5056
HSA-MIR-3065-5P	99.97	71.56	3281
HSA-MIR-141-3P	99.94	72.79	2421
HSA-MIR-200A-3P	99.94	72.68	2420
HSA-MIR-539-5P	99.93	70.30	2855
HSA-MIR-6857-5P	99.87	65.32	985
HSA-MIR-369-3P	99.85	70.52	2264
HSA-MIR-7159-5P	99.53	72.12	2472
HSA-MIR-4672	99.50	71.58	2893
HSA-MIR-3670	97.88	64.39	763
HSA-MIR-10397-3P	97.78	65.70	601
HSA-MIR-3173-5P	97.35	65.82	1282
HSA-MIR-6799-3P	97.35	65.60	1302
HSA-MIR-616-3P	96.82	66.99	784

Functional genomics

DepMap (CRISPR cell-line fitness): dependent in 100.0% of screened cell lines, common-essential.

Literature-anchored findings (GeneRIF, showing 8)

• DIMT1L and WBSCR22-TRMT112 are required for distinct pre-rRNA processing reactions leading to synthesis of 18S rRNA. Ribosome biogenesis requires the presence of the modification enzyme rather than its RNA-modifying catalytic activity. (PMID:25851604)
• The localization of the TRMT112 protein is determined by WBSCR22, and the WBSCR22-TRMT112 complex is localized in the cell nucleus. (PMID:26214185)
• METTL5-TRMT112 partners act by extruding the adenosine to be modified from a double-stranded nucleic acid. (PMID:31328227)
• The down-regulation of TRMT112 does not affect the N6AMT1 protein levels in cells, suggesting that the two proteins of TRMT112 network, WBSCR22 and N6AMT1, are differently regulated by their common cofactor. (PMID:31466382)
• Structural insight into HEMK2-TRMT112-mediated glutamine methylation. (PMID:32969463)
• THUMPD3-TRMT112 is a m2G methyltransferase working on a broad range of tRNA substrates. (PMID:34669960)
• Human TRMT112-Methyltransferase Network Consists of Seven Partners Interacting with a Common Co-Factor. (PMID:34948388)
• WBSCR22 and TRMT112 synergistically suppress cell proliferation, invasion and tumorigenesis in pancreatic cancer via transcriptional regulation of ISG15. (PMID:35088887)

Cross-species orthologs

5 orthologs

Organism	Symbol	Gene ID
danio_rerio	trmt112	ENSDARG00000071878
mus_musculus	Trmt112	ENSMUSG00000038812
rattus_norvegicus	Trmt112	ENSRNOG00000073020
drosophila_melanogaster	Trmt112	FBGN0037061
caenorhabditis_elegans		WBGENE00007312

Protein

Protein identifiers

Multifunctional methyltransferase subunit TRM112-like protein — Q9UI30 (reviewed: Q9UI30)

Alternative names: tRNA methyltransferase 112 homolog

All UniProt accessions (1): Q9UI30

UniProt curated annotations — full annotation on UniProt →

Function. Acts as an activator of both rRNA/tRNA and protein methyltransferases. Together with methyltransferase BUD23, methylates the N(7) position of a guanine in 18S rRNA. The heterodimer with N6AMT1/HEMK2 catalyzes N5-methylation of ETF1 on ‘Gln-185’, using S-adenosyl L-methionine as methyl donor. The heterodimer with N6AMT1/HEMK2 also monomethylates ‘Lys-12’ of histone H4 (H4K12me1). The heterodimer with ALKBH8 catalyzes the methylation of 5-carboxymethyl uridine to 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in target tRNA species. Together with methyltransferase THUMPD3, catalyzes the formation of N(2)-methylguanosine at position 6 in a broad range of tRNA substrates and at position 7 of tRNA(Trp). Involved in the pre-rRNA processing steps leading to small-subunit rRNA production. Together with methyltransferase METTL5, specifically methylates the 6th position of adenine in position 1832 of 18S rRNA.

Subunit / interactions. Part of the heterodimeric BUD23-TRM112 methyltransferase complex; this heterodimerization is necessary for the metabolic stability and activity of the catalytic subunit BUD23. Part of the heterodimeric N6AMT1-TRM112 methyltransferase complex; this heterodimerization is necessary for S-adenosyl-L-methionine-binding to N6AMT1/HEMK2. Part of the heterodimeric ALKBH8-TRM112 methyltransferase complex. Part of the heterodimeric METTL5-TRM112 methyltransferase complex; this heterodimerization is necessary for the stability of the catalytic subunit METTL5. Part of the heterodimeric THUMPD3-TRM112 methyltransferase complex; this complex forms an active tRNA methyltransferase, where TRMT112 acts as an activator of the catalytic subunit THUMPD3. Part of the heterodimeric THUMPD2-TRM112 methyltransferase complex; this complex forms an active tRNA methyltransferase, where TRMT112 acts as an activator of the catalytic subunit THUMPD2. Part of the heterodimeric TRMT11-TRM112 methyltransferase complex; this complex forms an active tRNA methyltransferase, where TRMT112 acts as an activator of the catalytic subunit TRMT11.

Subcellular location. Nucleus. Nucleoplasm. Cytoplasm. Perinuclear region.

Similarity. Belongs to the TRM112 family.

Isoforms (2)

UniProt ID	Names	Canonical?
Q9UI30-1	1	yes
Q9UI30-2	2

RefSeq proteins (5): NP_001273011, NP_001273013, NP_001359000, NP_001359001, NP_057488* (*=MANE)

Domains & families (InterPro)

ID	Name	Type
IPR005651	Trm112-like	Family
IPR039127	Trm112	Family

Pfam: PF03966

UniProt features (33 total): mutagenesis site 13, helix 7, strand 4, turn 3, modified residue 2, chain 1, domain 1, sequence conflict 1, splice variant 1

Structure

Experimental structures (PDB)

27 structures.

PDB	Method	Resolution (Å)
9OHL	X-RAY DIFFRACTION	1.29
8QDG	X-RAY DIFFRACTION	1.39
9FKW	X-RAY DIFFRACTION	1.39
9FL5	X-RAY DIFFRACTION	1.39
8CNC	X-RAY DIFFRACTION	1.46
8QDI	X-RAY DIFFRACTION	1.47
9FKV	X-RAY DIFFRACTION	1.47
9FKM	X-RAY DIFFRACTION	1.5
9FKG	X-RAY DIFFRACTION	1.59
6H2U	X-RAY DIFFRACTION	1.6
9FIM	X-RAY DIFFRACTION	1.6
9FKE	X-RAY DIFFRACTION	1.6
9FL4	X-RAY DIFFRACTION	1.7
6KHS	X-RAY DIFFRACTION	1.9
6H1E	X-RAY DIFFRACTION	1.9
6H1D	X-RAY DIFFRACTION	1.94
6KMR	X-RAY DIFFRACTION	2
6K0X	X-RAY DIFFRACTION	2.2
6PED	X-RAY DIFFRACTION	2.3
6H2V	X-RAY DIFFRACTION	2.49
7WTU	ELECTRON MICROSCOPY	3
7WTT	ELECTRON MICROSCOPY	3.1
6KMS	X-RAY DIFFRACTION	3.2
7WTS	ELECTRON MICROSCOPY	3.2
7WTW	ELECTRON MICROSCOPY	3.2
7WTV	ELECTRON MICROSCOPY	3.5
6G4W	ELECTRON MICROSCOPY	4.5

Predicted structure (AlphaFold)

Model	pLDDT	Fraction very-high
AF-Q9UI30-F1	92.39	0.80

Functional residue map

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

Post-translational modifications (2): 119, 125

Mutagenesis-validated functional residues (13):

Position	Phenotype
10	abolishes interaction with thumpd2. increases expression of exogenous trmt112. no effect on interaction with n6amt1, bud
45	abolishes interaction with mettl5 and thumpd3. reduces interaction with alkbh8 and thumpd2. no effect on interaction wit
48	abolishes interaction with thumpd2 and thumpd3. reduces interaction with trmt11, alkbh8 and n6amt1. no effect on interac
50	increases interaction with mettl5. no effect on interaction with trmt11, thumpd2, thumpd3, n6amt1, bud23 and alkbh8. no
92	reduces interaction with thumpd2, thumpd3, alkbh8, trmt11, n6amt1 and bud23. increases interaction with mettl5. reduces
107	abolishes interaction with bud23, thumpd2 and thumpd3. reduces interaction with trmt11, n6amt1, mettl5 and alkbh8. reduc
113	strongly reduced ability to promote n5-methylation of etf1 together with hemk2/n6amt1.
113	abolishes interaction with thumpd2 and thumpd3. reduces interaction with n6amt1, bud23, trmt11 and alkbh8. reduces expre
5	abolishes interaction with n6amt1, mettl5, trmt11, thumpd3 and thumpd2. reduces interaction with bud23 and alkbh8. reduc
5	loss of interaction with mettl5, thumpd3, thumpd2 and trmt11.
8	strongly reduced ability to promote n5-methylation of etf1 together with hemk2/n6amt1.
8	abolishes interaction with mettl5 and thumpd3. reduces interaction with alkbh8, thumpd2 and trmt11. no effect on interac
9	strongly reduced ability to promote n5-methylation of etf1 together with hemk2/n6amt1.

Function

Pathways and Gene Ontology

Reactome pathways

4 pathways

ID	Pathway
R-HSA-156581	Methylation
R-HSA-6782315	tRNA modification in the nucleus and cytosol
R-HSA-6790901	rRNA modification in the nucleus and cytosol
R-HSA-72764	Eukaryotic Translation Termination

MSigDB gene sets: 200 (showing top): GOBP_RIBOSOME_BIOGENESIS, REACTOME_BIOLOGICAL_OXIDATIONS, HNF3ALPHA_Q6, GGGNRMNNYCAT_UNKNOWN, GOBP_MATURATION_OF_SSU_RRNA, STARK_PREFRONTAL_CORTEX_22Q11_DELETION_DN, GOBP_TRNA_METABOLIC_PROCESS, GRAESSMANN_APOPTOSIS_BY_DOXORUBICIN_DN, GRAESSMANN_RESPONSE_TO_MC_AND_DOXORUBICIN_DN, GGGTGGRR_PAX4_03, chr11q13, GOBP_RNA_METHYLATION, NKX62_Q2, GOBP_RNA_MODIFICATION, GOBP_RIBOSOMAL_SMALL_SUBUNIT_BIOGENESIS

GO Biological Process (9): maturation of LSU-rRNA (GO:0000470), peptidyl-glutamine methylation (GO:0018364), tRNA methylation (GO:0030488), maturation of SSU-rRNA (GO:0030490), rRNA methylation (GO:0031167), transcription initiation-coupled chromatin remodeling (GO:0045815), rRNA (guanine-N7)-methylation (GO:0070476), positive regulation of rRNA processing (GO:2000234), rRNA processing (GO:0006364)

GO Molecular Function (4): protein methyltransferase activity (GO:0008276), protein heterodimerization activity (GO:0046982), tRNA methyltransferase activator activity (GO:0141106), protein binding (GO:0005515)

GO Cellular Component (7): nucleus (GO:0005634), nucleoplasm (GO:0005654), cytoplasm (GO:0005737), cytosol (GO:0005829), protein-containing complex (GO:0032991), tRNA (m2G10) methyltransferase complex (GO:0043528), perinuclear region of cytoplasm (GO:0048471)

Reactome top-level categories

Rollup of top-4 pathways:

Category	Pathways
Phase II - Conjugation of compounds	1
tRNA processing	1
rRNA processing in the nucleus and cytosol	1
Translation	1

GO top-level categories

Rollup of top GO terms by namespace:

Category	Terms
cellular anatomical structure	4
rRNA processing	3
RNA methylation	2
methyltransferase activity	2
cytoplasm	2
ribosomal large subunit biogenesis	1
protein methylation	1
tRNA modification	1
ribosomal small subunit biogenesis	1
rRNA modification	1
transcription initiation at RNA polymerase II promoter	1
positive regulation of gene expression, epigenetic	1
RNA (guanine-N7)-methylation	1
rRNA base methylation	1
positive regulation of RNA metabolic process	1
regulation of rRNA processing	1
RNA processing	1
rRNA metabolic process	1
ribosome biogenesis	1
catalytic activity, acting on a protein	1
protein dimerization activity	1
enzyme activator activity	1
methyltransferase regulator activity	1
binding	1
intracellular membrane-bounded organelle	1
nuclear lumen	1
intracellular anatomical structure	1
cellular_component	1
tRNA methyltransferase complex	1

Protein interactions and networks

STRING

2223 interactions, top by confidence (×1000):

Protein A	Protein B	Partner UniProt	Score
TRMT112	METTL5	Q9NRN9	996
TRMT112	ALKBH8	Q96BT7	988
TRMT112	TRMT11	Q7Z4G4	986
TRMT112	HEMK2	Q9Y5N5	980
TRMT112	BUD23	O43709	970
TRMT112	ZCCHC4	Q9H5U6	771
TRMT112	TRMT61A	Q96FX7	728
TRMT112	TRMT6	Q9UJA5	718
TRMT112	CTU1	Q7Z7A3	718
TRMT112	URM1	Q9BTM9	717
TRMT112	METTL1	Q9UBP6	710
TRMT112	WDR4	P57081	710
TRMT112	HEMK1	Q9Y5R4	696
TRMT112	TRMT9B	Q9P272	690
TRMT112	FTSJ1	Q9UET6	668

IntAct

117 interactions, top by confidence:

A	B	Type	Score
TRMT112	BUD23	psi-mi:“MI:0915”(physical association)	0.910
BUD23	TRMT112	psi-mi:“MI:0915”(physical association)	0.910
TRMT112	BUD23	psi-mi:“MI:0914”(association)	0.910
BUD23	TRMT112	psi-mi:“MI:0403”(colocalization)	0.910
MED29	MED19	psi-mi:“MI:0914”(association)	0.890
THUMPD3	TRMT112	psi-mi:“MI:0915”(physical association)	0.870
THUMPD3	TRMT112	psi-mi:“MI:0403”(colocalization)	0.870
TRMT112	ALKBH8	psi-mi:“MI:0915”(physical association)	0.790
ALKBH8	TRMT112	psi-mi:“MI:0915”(physical association)	0.790
ALKBH8	TRMT112	psi-mi:“MI:0403”(colocalization)	0.790
TRMT112	HEMK2	psi-mi:“MI:0915”(physical association)	0.750
HEMK2	TRMT112	psi-mi:“MI:0915”(physical association)	0.750
HEMK2	TRMT112	psi-mi:“MI:0403”(colocalization)	0.750
BUD23	UBE2O	psi-mi:“MI:0914”(association)	0.730

BioGRID (117): TRMT112 (Affinity Capture-MS), SCOC (Co-fractionation), TRMT112 (Co-fractionation), TRMT112 (Co-fractionation), TRMT112 (Affinity Capture-MS), TRMT112 (Affinity Capture-MS), TRMT112 (Affinity Capture-MS), TRMT112 (Affinity Capture-MS), TRMT112 (Affinity Capture-MS), TRMT112 (Affinity Capture-MS), TRMT112 (Affinity Capture-MS), TRMT112 (Affinity Capture-MS), TRMT112 (Affinity Capture-MS), TRMT112 (Affinity Capture-MS), TRMT112 (Affinity Capture-MS)

ESM2 similar proteins: A1Z9A2, A7SJ66, O13724, O14224, O16999, O45241, O61078, O74797, O82462, P12531, P13021, P20348, P25654, P27570, P30190, P34534, P34685, P40122, P53738, P54364, Q09541, Q09723, Q17693, Q196X4, Q20496, Q290L7, Q45EK7, Q55C72, Q5WNE3, Q615A2, Q61WR2, Q6CCK2, Q6CY34, Q8LFJ5, Q8X0S4, Q9BI88, Q9BM96, Q9BM98, Q9BM99, Q9C9R3

Diamond homologs: O45241, Q2KIA2, Q54N57, Q8LFJ5, Q9C9R3, Q9DCG9, Q9UI30, Q9VP65, P53738, Q09723, Q8X0S4

SIGNOR signaling

7 interactions.

A	Effect	B	Mechanism
TRMT112	“form complex”	“TRMT11-TRM112 methyltransferase complex”	binding
TRMT112	“form complex”	“METTL5-TRM112 methyltransferase complex”	binding
TRMT112	“form complex”	“THUMPD2-TRM112 methyltransferase complex”	binding
TRMT112	“form complex”	“ALKBH8-TRM112 methyltransferase complex”	binding
TRMT112	“form complex”	“N6AMT1-TRM112 methyltransferase complex”	binding
TRMT112	“form complex”	“BUD23-TRM112 methyltransferase complex”	binding
TRMT112	“form complex”	“THUMPD3-TRM112 methyltransferase complex”	binding

Disease & clinical

Clinical variants and AI predictions

ClinVar

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

Classification	Count (floor)
Pathogenic	0
Likely pathogenic	0
Uncertain significance	15
Likely benign	1
Benign	0

Top pathogenic / likely-pathogenic (0)

SpliceAI

342 predictions. Top by Δscore:

Variant	Effect	Δscore
11:64317052:TCTCA:T	donor_loss	1.0000
11:64317053:CTCAC:C	donor_loss	1.0000
11:64317054:TCA:T	donor_loss	1.0000
11:64317055:CA:C	donor_loss	1.0000
11:64317143:CGCAA:C	acceptor_gain	1.0000
11:64317145:CAA:C	acceptor_gain	1.0000
11:64317148:C:CC	acceptor_gain	1.0000
11:64317257:T:TA	donor_gain	1.0000
11:64317262:A:AC	donor_gain	1.0000
11:64317263:C:CT	donor_gain	1.0000
11:64317502:G:C	donor_gain	1.0000
11:64316967:ACCT:A	acceptor_loss	0.9900
11:64316968:CCT:C	acceptor_loss	0.9900
11:64316969:CTGC:C	acceptor_loss	0.9900
11:64316970:T:A	acceptor_loss	0.9900
11:64317059:T:TA	donor_gain	0.9900
11:64317144:GCAA:G	acceptor_gain	0.9900
11:64317145:CAAC:C	acceptor_gain	0.9900
11:64317146:AA:A	acceptor_gain	0.9900
11:64317147:AC:A	acceptor_loss	0.9900
11:64317149:T:G	acceptor_loss	0.9900
11:64317258:CCTCA:C	donor_loss	0.9900
11:64317259:CTCAC:C	donor_loss	0.9900
11:64317260:TCACG:T	donor_loss	0.9900
11:64317261:CACGT:C	donor_loss	0.9900
11:64317262:ACG:A	donor_loss	0.9900
11:64317263:C:G	donor_loss	0.9900
11:64317263:CG:C	donor_gain	0.9900
11:64317263:CGTT:C	donor_gain	0.9900
11:64317588:T:TA	donor_gain	0.9900

AlphaMissense

813 scored. Top likely-pathogenic:

Variant	Protein change	am_pathogenicity
11:64316918:G:C	F107L	0.999
11:64316918:G:T	F107L	0.999
11:64316920:A:G	F107L	0.999
11:64316898:G:T	P114H	0.998
11:64316913:A:T	I109N	0.998
11:64316953:C:G	G96R	0.998
11:64317293:A:G	W51R	0.998
11:64317293:A:T	W51R	0.998
11:64317464:G:C	F21L	0.998
11:64317464:G:T	F21L	0.998
11:64317466:A:G	F21L	0.998
11:64316919:A:C	F107C	0.997
11:64316919:A:G	F107S	0.997
11:64316892:A:G	M116T	0.996
11:64316941:A:G	C100R	0.996
11:64316946:A:G	L98P	0.996
11:64316952:C:A	G96V	0.996
11:64316953:C:A	G96C	0.996
11:64316913:A:C	I109S	0.995
11:64317291:C:A	W51C	0.995
11:64317291:C:G	W51C	0.995
11:64317506:A:C	N7K	0.995
11:64317506:A:T	N7K	0.995
11:64316904:C:A	G112V	0.994
11:64316904:C:T	G112E	0.994
11:64316913:A:G	I109T	0.994
11:64317075:G:C	H85D	0.994
11:64317504:A:G	L8P	0.994
11:64316901:A:G	I113T	0.993
11:64316920:A:C	F107V	0.992

dbSNP variants (sampled 300 via entrez): RS1000039151 (11:64317749 C>T), RS1000505630 (11:64320113 A>G), RS1002157591 (11:64318958 G>A,C,T), RS1002492776 (11:64318856 G>A,C,T), RS1002531308 (11:64319295 C>T), RS1003125682 (11:64320487 T>A), RS1003482317 (11:64318111 C>A,G,T), RS1003549748 (11:64317152 G>A,T), RS1003850845 (11:64317977 T>C), RS1004089110 (11:64319511 A>G), RS1004462251 (11:64316157 CGT>C), RS1005488491 (11:64317045 G>A,C), RS1007581684 (11:64317732 A>G), RS1007957209 (11:64318489 C>G,T), RS1007973441 (11:64318367 C>A)

Disease associations

OMIM: gene MIM:618630 | disease phenotypes:

GenCC curated gene-disease

Mondo (0):

Orphanet (0):

HPO phenotypes

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

GWAS associations

3 associations (top):

Study	Trait	p-value
GCST004132_98	Crohn’s disease	5.000000e-06
GCST004785_38	Vitiligo	5.000000e-08
GCST90002383_38	Hematocrit	1.000000e-10

EFO canonical traits (1, from GWAS)

EFO ID	Trait name
EFO:0004348	hematocrit

Drugs & pharmacology

Drug and pharmacology data

Is drug target: yes

ChEMBL targets (2): CHEMBL4295977 (SINGLE PROTEIN), CHEMBL5483089 (PROTEIN COMPLEX)

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

CTD chemical–gene interactions

29 total (human), top 29 by PubMed support.

Chemical	Actions (top 5)	PubMed papers
Cyclosporine	increases expression	3
sodium arsenite	affects expression, increases expression	2
chloropicrin	affects expression, decreases expression	2
Dronabinol	decreases expression, increases expression	2
triphenyl phosphate	affects expression	1
bisphenol A	affects expression	1
arsenite	affects binding, increases reaction	1
CGP 52608	affects binding, increases reaction	1
ICG 001	increases expression	1
abrine	decreases expression	1
quinocetone	decreases expression, increases expression	1
Sunitinib	increases expression	1
Acetaminophen	affects response to substance	1
Atrazine	decreases expression	1
Cadmium	increases abundance, increases expression	1
Caffeine	increases phosphorylation	1
Carbamazepine	affects expression	1
Diazinon	increases methylation	1
Doxorubicin	increases expression	1
Enzyme Inhibitors	increases O-linked glycosylation, decreases activity	1
Ivermectin	decreases expression	1
Smoke	decreases expression	1
Tunicamycin	decreases expression	1
Valproic Acid	increases expression	1
Vitamin E	increases expression	1
Sodium Selenite	increases expression	1
Cadmium Chloride	increases abundance, increases expression	1
Genistein	increases expression, increases reaction	1
Acrylamide	increases expression	1

ChEMBL screening assays

2 unique, capped per target: 2 binding

Representative assays (with source publication via chembl_document):

Assay ID	Type	Description	Source paper
CHEMBL4118607	Binding	Binding affinity to TRMT112 in human NCI-H23 cells at 1 uM by mass spectrometry based pull down assay	Studies of TAK1-centered polypharmacology with novel covalent TAK1 inhibitors. — Bioorg Med Chem

Clinical trials (associated diseases)

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