TRIM11

Summary

TRIM11 (tripartite motif containing 11, HGNC:16281) is a protein-coding gene on chromosome 1q42.13, encoding E3 ubiquitin-protein ligase TRIM11 (Q96F44). E3 ubiquitin-protein ligase that promotes the degradation of insoluble ubiquitinated proteins, including insoluble PAX6, poly-Gln repeat expanded HTT and poly-Ala repeat expanded ARX.

The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. This protein localizes to the nucleus and the cytoplasm. Its function has not been identified.

Source: NCBI Gene 81559 — RefSeq curated summary.

At a glance

• GWAS associations: 2
• Clinical variants (ClinVar): 64 total
• MANE Select transcript: NM_145214

Identifiers

Gene identifiers

Field	Value
HGNC ID	HGNC:16281
Approved symbol	TRIM11
Name	tripartite motif containing 11
Location	1q42.13
Locus type	gene with protein product
Status	Approved
Aliases	RNF92, BIA1
Ensembl gene	ENSG00000154370
Ensembl biotype	protein_coding
OMIM	607868
Entrez	81559

Gene structure

Transcript identifiers

Ensembl transcripts: 9 — 8 protein_coding, 1 protein_coding_CDS_not_defined

ENST00000284551, ENST00000366699, ENST00000475775, ENST00000493030, ENST00000602308, ENST00000602582, ENST00000854560, ENST00000933006, ENST00000946665

RefSeq mRNA: 1 — MANE Select: NM_145214 NM_145214

CCDS: CCDS31048

Canonical transcript exons

ENST00000284551 — 6 exons

Exon	Start	End
ENSE00001227257	228397143	228397165
ENSE00001227277	228402066	228402161
ENSE00001227286	228393676	228395252
ENSE00001442349	228400964	228401194
ENSE00001920934	228406154	228406835
ENSE00003501320	228396947	228397047

Expression profiles

Bgee: expression breadth ubiquitous, 237 present calls, max score 93.75.

FANTOM5 (CAGE): breadth ubiquitous, TPM avg 27.5901 / max 237.8400, expressed in 1813 samples.

FANTOM5 promoters (4 alternative TSS)

Promoter ID	TPM avg	Samples expressed
17830	25.1567	1810
17829	2.2516	1195
17831	0.1579	77
17828	0.0239	8

Top tissues by expression

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

Tissue	Anatomy ID	Expression score	Quality
cerebellar hemisphere	UBERON:0002245	93.75	gold quality
cerebellar cortex	UBERON:0002129	93.68	gold quality
right hemisphere of cerebellum	UBERON:0014890	93.66	gold quality
cerebellum	UBERON:0002037	92.65	gold quality
granulocyte	CL:0000094	92.19	gold quality
oocyte	CL:0000023	89.16	gold quality
mucosa of transverse colon	UBERON:0004991	88.57	gold quality
lower esophagus mucosa	UBERON:0035834	87.27	gold quality
spleen	UBERON:0002106	86.39	gold quality
ileal mucosa	UBERON:0000331	86.36	gold quality
blood	UBERON:0000178	86.14	gold quality
cerebellar vermis	UBERON:0004720	86.09	gold quality
leukocyte	CL:0000738	85.50	gold quality
monocyte	CL:0000576	85.32	gold quality
putamen	UBERON:0001874	85.30	gold quality
nucleus accumbens	UBERON:0001882	85.07	gold quality
caudate nucleus	UBERON:0001873	84.97	gold quality
pancreatic ductal cell	CL:0002079	84.87	silver quality
esophagus mucosa	UBERON:0002469	84.87	gold quality
right frontal lobe	UBERON:0002810	84.58	gold quality
minor salivary gland	UBERON:0001830	84.10	gold quality
sperm	CL:0000019	84.02	gold quality
primordial germ cell in gonad	CL:0000670 ∩ UBERON:0000991	83.99	gold quality
secondary oocyte	CL:0000655	83.94	gold quality
transverse colon	UBERON:0001157	83.94	gold quality
apex of heart	UBERON:0002098	83.84	gold quality
skin of leg	UBERON:0001511	83.51	gold quality
small intestine Peyer’s patch	UBERON:0003454	83.43	gold quality
saliva-secreting gland	UBERON:0001044	83.30	gold quality
right testis	UBERON:0004534	83.30	gold quality

Single-cell (SCXA)

Detected in 1 experiment(s), a significant marker in 0.

Experiment	Marker?	Max mean expression
E-ANND-3	no	3.11

Regulation

Is transcription factor: no

Upstream regulators (CollecTRI, top): PAX6

miRNA regulators (miRDB)

35 targeting TRIM11, 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-5193	100.00	67.26	1744
HSA-MIR-4283	100.00	66.42	2097
HSA-MIR-6721-5P	99.93	68.92	2981
HSA-MIR-95-5P	99.89	72.17	3973
HSA-MIR-124-3P	99.89	73.74	3043
HSA-MIR-506-3P	99.89	73.55	3057
HSA-MIR-6817-3P	99.79	68.35	2126
HSA-MIR-548AJ-5P	99.78	71.12	3085
HSA-MIR-548F-5P	99.78	71.02	3093
HSA-MIR-548G-5P	99.78	71.12	3085
HSA-MIR-548X-5P	99.78	71.12	3085
HSA-MIR-6764-5P	99.75	67.89	2304
HSA-MIR-2116-3P	99.74	64.32	889
HSA-MIR-5004-5P	99.68	66.63	1294
HSA-MIR-1224-5P	99.48	65.59	803
HSA-MIR-3182	99.40	68.15	2454
HSA-MIR-532-3P	99.34	65.76	1195
HSA-MIR-4311	99.31	70.47	3041
HSA-MIR-504-3P	99.30	67.18	1745
HSA-MIR-6749-3P	99.00	65.73	1443
HSA-MIR-4801	98.96	69.42	2096
HSA-MIR-760	98.81	66.65	1392
HSA-MIR-423-5P	98.69	67.48	1522
HSA-MIR-3944-5P	98.50	67.55	997
HSA-MIR-6792-3P	98.41	66.86	1359
HSA-MIR-4691-5P	98.41	66.77	1343
HSA-MIR-6784-3P	98.39	64.88	662
HSA-MIR-6881-5P	98.16	67.38	665
HSA-MIR-6862-3P	97.92	64.86	531
HSA-MIR-6791-3P	97.45	64.31	1123

Literature-anchored findings (GeneRIF, showing 38)

• PAX6 interacts with HOMER3, DNCL1, and TRIM11. Three C-terminal PAX6 mutations, previously identified in patients with eye malformations, all reduced or abolished the interactions. (PMID:16098226)
• These results suggest that TRIM11, with the ubiquitin-proteasome pathway, regulates ARC105 function in TGFbeta signaling. (PMID:16904669)
• Downregulation of TRIM11 and TRIM15 enhanced virus release suggesting that these proteins contribute to the endogenous restriction of retroviruses in cells. (PMID:18248090)
• This study suggests a potential role for Trim11 in the specification of NA phenotype by interaction with Phox2b. (PMID:18275850)
• Study shows that the E3 ubiquitin ligase TRIM11 plays a critical role in the clearance of mutant PHOX2B, which causes congenital central hypoventilation syndrome, through the proteasome. (PMID:22307522)
• TRIM11 is overexpressed in high-grade gliomas and promotes proliferation, invasion, migration and glial tumor growth. (PMID:23178488)
• TRIM11 negatively regulates IFN-beta production and antiviral activity by targeting TBK1. (PMID:23675467)
• TRIM11 is a host cellular factor that interferes with the early steps of HIV-1 replication and provides a connection between viral protein and host antiviral factors. (PMID:25105968)
• TRIM11 suppresses AIM2 inflammasome by degrading AIM2 via p62-dependent selective autophagy. (PMID:27498865)
• study identified TRIM11 as a new HIV-1 capsid binding protein; data also reveal that TRIM11 restricts HIV-1 reverse transcription by accelerating viral uncoating, and microtubule dynamics is implicated in TRIM11-imposed block to early events of HIV-1 replication (PMID:27737691)
• Data show that miR-24-3p downregulation contributes to tripartite motif-containing protein 11 (TRIM11) upregulation in cancer (CC). (PMID:27888625)
• data showed that tripartite motif-containing protein 11(TRIM11) expression was significantly elevated in hepatocellular carcinoma(HCC) tissues and overexpression of TRIM11 is closely associated with HCC progression and poor survival (PMID:28065743)
• TRIM11 to be overexpressed in HCC tissues and cell lines. Downregulation of TRIM11 inhibited HCC cell proliferation and invasion in vitro and in vivo as well as suppressed the epithelial-mesenchymal transition (EMT) process. (PMID:28244856)
• TRIM11 promotes the development and progression of HCC through regulating p53 and its downstream signals. (PMID:29190611)
• CRTC1-TRIM11 fusion appears to be specific of an unpigmented nodular tumor combining a melanocytic phenotype and low-grade tumor behavior. (PMID:29240581)
• findings identify TRIM11 as an important activator of the proteasome, define a pathway that adjusts proteasome activity, and reveal a mechanism by which tumor cells acquire higher degradative power to support oncogenic growth (PMID:29581427)
• TRIM11 locus is a genetic modifier of progressive supranuclear palsy phenotype. (PMID:30066433)
• During these processes, TRIM11 interacts with and stabilizes HSF1, increaseing HSF1 levels in the nucleus. These findings identify that TRIM11, through cooperation with HSF1, protects cells against the proteotoxic stress and promotes tumor cell survival. (PMID:30563406)
• TRIM11 was upregulated in prostate cancer tissue and was associated with reduced prognosis. TRIM11 expression increased cell proliferation in vitro and was downregulated by miR-5193. (PMID:30608062)
• Study detected high expression levels of TRIM11 in breast cancer tissues. Downregulation of TRIM11 in MCF7 and MDAMB231 cells inhibited cell proliferation and promoted cell apoptosis. (PMID:30816511)
• TRIM11 promotes lymphomas by activating the beta-catenin signaling and Axin1 ubiquitination degradation. (PMID:31786079)
• TRIM11 might suppress the translation of DUSP6 via improving its ubiquitination. Additionally, TRIM11 silencing in osteosarcoma (OS) cells significantly reduced its tumorigenicity in vivo. (PMID:31950060)
• Association of Tripartite Motif Containing 11 rs564309 With Tau Pathology in Progressive Supranuclear Palsy. (PMID:32142177)
• miR-5193, regulated by FUT1, suppresses proliferation and migration of ovarian cancer cells by targeting TRIM11. (PMID:32823233)
• TRIM11 stimulates the proliferation of gastric cancer through targeting CPEB3/EGFR axis. (PMID:33099959)
• TRIM11 Prevents and Reverses Protein Aggregation and Rescues a Mouse Model of Parkinson’s Disease. (PMID:33264628)
• Knockdown of TRIM5alpha or TRIM11 increases lentiviral vector transduction efficiency of human Muller cells. (PMID:33440192)
• Tripartite motif protein 11 (TRIM11), an oncogene for human lung cancer via the DUSP6-mediated ERK1/2 signaling pathway. (PMID:33970779)
• Downregulation of tripartite motif protein 11 attenuates cardiomyocyte apoptosis after ischemia/reperfusion injury via DUSP1-JNK1/2. (PMID:34694031)
• Tripartite motif-containing protein 11 promotes hepatocellular carcinogenesis through ubiquitin-proteasome-mediated degradation of pleckstrin homology domain leucine-rich repeats protein phosphatase 1. (PMID:34767673)
• Sex-determining Region Y-box transcription factor 13 promotes breast cancer cell proliferation and glycolysis by activating the tripartite motif containing 11-mediated Wnt/beta-catenin signaling pathway. (PMID:35611828)
• Cutaneous Melanocytic Tumor With CRTC1::TRIM11 Translocation : An Emerging Entity Analyzed in a Series of 41 Cases. (PMID:35993578)
• TRIM11, a new target of p53, facilitates the migration and invasion of nasopharyngeal carcinoma cells. (PMID:36376537)
• TRIM11 Posttranscriptionally Modulated by miR-5193 Facilitates Tumor Growth and Metastasis of Prostate Cancer. (PMID:37248611)
• TRIM11 protects against tauopathies and is down-regulated in Alzheimer’s disease. (PMID:37499037)
• TRIM11 promotes cell proliferation of non-small cell lung cancer through the inhibition of ferroptosis by AMPK. (PMID:37604203)
• TRIM11 attenuates Treg cell differentiation by p62-selective autophagic degradation of AIM2. (PMID:37804507)
• Tripartite Motif-containing Protein 11 Silencing Inhibits Proliferation and Glycolysis and Promotes Apoptosis of Esophageal Squamous Cell Carcinoma Cells by Inactivating Signal Transduction and Activation of Transcription Factor 3/c-Myc Signaling. (PMID:38780271)

Cross-species orthologs

2 orthologs

Organism	Symbol	Gene ID
mus_musculus	Trim11	ENSMUSG00000020455
rattus_norvegicus	Trim11	ENSRNOG00000002915

Paralogs (80): MID2 (ENSG00000080561), TRIM9 (ENSG00000100505), MID1 (ENSG00000101871), MEFV (ENSG00000103313), TRIM35 (ENSG00000104228), TRIM14 (ENSG00000106785), TRIM37 (ENSG00000108395), TRIM2 (ENSG00000109654), TRIM3 (ENSG00000110171), TRIM38 (ENSG00000112343), TRIM62 (ENSG00000116525), TRIM67 (ENSG00000119283), TRIM32 (ENSG00000119401), BSPRY (ENSG00000119411), TRIM25 (ENSG00000121060), TRIM6 (ENSG00000121236), TRIM24 (ENSG00000122779), TRIM51 (ENSG00000124900), TRIM28 (ENSG00000130726), TRIM21 (ENSG00000132109), TRIM5 (ENSG00000132256), TRIM22 (ENSG00000132274), TRIM47 (ENSG00000132481), TRIM45 (ENSG00000134253), TRIM29 (ENSG00000137699), TRIM54 (ENSG00000138100), PML (ENSG00000140464), TRIM65 (ENSG00000141569), TRIM43B (ENSG00000144010), TRIM43 (ENSG00000144015), TRIM7 (ENSG00000146054), TRIM41 (ENSG00000146063), TRIM50 (ENSG00000146755), TRIM4 (ENSG00000146833), TRIM55 (ENSG00000147573), TRIM48 (ENSG00000150244), TRIM36 (ENSG00000152503), TRIM74 (ENSG00000155428), TRIM42 (ENSG00000155890), TRIM63 (ENSG00000158022)

Protein

Protein identifiers

E3 ubiquitin-protein ligase TRIM11 — Q96F44 (reviewed: Q96F44)

Alternative names: Protein BIA1, RING finger protein 92, Tripartite motif-containing protein 11

All UniProt accessions (4): Q96F44, R4GMV1, R4GNB9, R4GNC3

UniProt curated annotations — full annotation on UniProt →

Function. E3 ubiquitin-protein ligase that promotes the degradation of insoluble ubiquitinated proteins, including insoluble PAX6, poly-Gln repeat expanded HTT and poly-Ala repeat expanded ARX. Mediates PAX6 ubiquitination leading to proteasomal degradation, thereby modulating cortical neurogenesis. May also inhibit PAX6 transcriptional activity, possibly in part by preventing the binding of PAX6 to its consensus sequences. May contribute to the regulation of the intracellular level of HN (humanin) or HN-containing proteins through the proteasomal degradation pathway. Mediates MED15 ubiquitination leading to proteasomal degradation. May contribute to the innate restriction of retroviruses. Upon overexpression, reduces HIV-1 and murine leukemia virus infectivity, by suppressing viral gene expression. Antiviral activity depends on a functional E3 ubiquitin-protein ligase domain. May regulate TRIM5 turnover via the proteasome pathway, thus counteracting the TRIM5-mediated cross-species restriction of retroviral infection at early stages of the retroviral life cycle. Acts as an inhibitor of the AIM2 inflammasome by promoting autophagy-dependent degradation of AIM2. Mechanistically, undergoes autoubiquitination upon DNA stimulation, promoting interaction with AIM2 and SQSTM1/p62, leading to AIM2 recruitment to autophagosomes.

Subunit / interactions. Binds cytoplasmic tail of integrin alpha-1. Interacts with the HN peptide. Interacts with PHOX2B. Interacts (when autoubiquitinated) with SQSTM1/p62; promoting AIM2 recruitment to autophagosomes. Interacts with AIM2; promoting its autophagy-dependent degradation.

Subcellular location. Cytoplasm. Nucleus.

Tissue specificity. Ubiquitous.

Post-translational modifications. Autoubiquitinated upon DNA stimulation; autoubiquitination at Lys-458 promotes interaction with SQSTM1/p62 and recruitment of AIM2 to autophagosomes.

Domain organisation. The coiled-coil domain and the B30.2 domain are both necessary for interaction with HN and PAX6. They are also involved in MED15-binding. The B30.2 domain may be involved cellular protein quality control by promoting the degradation of insoluble ubiquitinated proteins.

Pathway. Protein modification; protein ubiquitination.

Miscellaneous. May be due to competing acceptor splice site.

Similarity. Belongs to the TRIM/RBCC family.

Isoforms (3)

UniProt ID	Names	Canonical?
Q96F44-1	1	yes
Q96F44-2	2
Q96F44-3	3

RefSeq proteins (1): NP_660215* (*=MANE)

Domains & families (InterPro)

ID	Name	Type
IPR000315	Znf_B-box	Domain
IPR001841	Znf_RING	Domain
IPR001870	B30.2/SPRY	Domain
IPR003877	SPRY_dom	Domain
IPR003879	Butyrophylin_SPRY	Domain
IPR006574	PRY	Domain
IPR013083	Znf_RING/FYVE/PHD	Homologous_superfamily
IPR013320	ConA-like_dom_sf	Homologous_superfamily
IPR017907	Znf_RING_CS	Conserved_site
IPR043136	B30.2/SPRY_sf	Homologous_superfamily
IPR050143	TRIM/RBCC	Family

Pfam: PF00622, PF00643, PF13765, PF15227

UniProt features (44 total): strand 13, sequence conflict 6, mutagenesis site 5, helix 4, binding site 4, splice variant 3, zinc finger region 2, turn 2, chain 1, domain 1, cross-link 1, coiled-coil region 1, modified residue 1

Structure

Experimental structures (PDB)

1 structures.

PDB	Method	Resolution (Å)
7QS1	X-RAY DIFFRACTION	1.93

Predicted structure (AlphaFold)

Model	pLDDT	Fraction very-high
AF-Q96F44-F1	89.08	0.65

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): 92; 95; 114; 120

Post-translational modifications (2): 458, 85

Mutagenesis-validated functional residues (5):

Position	Phenotype
53	abolished e3 ubiquitin-protein ligase activity.
56	abolished e3 ubiquitin-protein ligase activity.
169	does not affect autoubiquitination.
366	does not affect autoubiquitination.
458	reduced autoubiquitination, leading to abolish interaction with sqstm1/p62.

Function

Pathways and Gene Ontology

Reactome pathways

1 pathways

ID	Pathway
R-HSA-983168	Antigen processing: Ubiquitination & Proteasome degradation

MSigDB gene sets: 175 (showing top): GOBP_NEGATIVE_REGULATION_OF_PROTEIN_CONTAINING_COMPLEX_ASSEMBLY, GOBP_NEGATIVE_REGULATION_OF_CELL_DEVELOPMENT, REACTOME_ADAPTIVE_IMMUNE_SYSTEM, GOBP_INFLAMMATORY_RESPONSE, REACTOME_CLASS_I_MHC_MEDIATED_ANTIGEN_PROCESSING_PRESENTATION, REACTOME_ANTIGEN_PROCESSING_UBIQUITINATION_PROTEASOME_DEGRADATION, GOBP_NEGATIVE_REGULATION_OF_VIRAL_PROCESS, GRAESSMANN_APOPTOSIS_BY_DOXORUBICIN_UP, GRAESSMANN_RESPONSE_TO_MC_AND_DOXORUBICIN_UP, GOBP_MODULATION_OF_PROCESS_OF_ANOTHER_ORGANISM, GOBP_NEUROGENESIS, GOBP_REGULATION_OF_NERVOUS_SYSTEM_DEVELOPMENT, GOBP_REGULATION_OF_CELLULAR_COMPONENT_BIOGENESIS, GOBP_NEGATIVE_REGULATION_OF_NERVOUS_SYSTEM_DEVELOPMENT, GOBP_NEGATIVE_REGULATION_OF_INTRACELLULAR_SIGNAL_TRANSDUCTION

GO Biological Process (12): regulation of gene expression (GO:0010468), protein ubiquitination (GO:0016567), negative regulation of viral transcription (GO:0032897), suppression of viral release by host (GO:0044790), innate immune response (GO:0045087), negative regulation of DNA-templated transcription (GO:0045892), host-mediated suppression of symbiont invasion (GO:0046597), positive regulation of viral entry into host cell (GO:0046598), negative regulation of neurogenesis (GO:0050768), protein autoubiquitination (GO:0051865), negative regulation of AIM2 inflammasome complex assembly (GO:0140972), defense response to virus (GO:0051607)

GO Molecular Function (8): ubiquitin-protein transferase activity (GO:0004842), zinc ion binding (GO:0008270), protein domain specific binding (GO:0019904), protein-macromolecule adaptor activity (GO:0030674), ubiquitin protein ligase activity (GO:0061630), protein binding (GO:0005515), transferase activity (GO:0016740), metal ion binding (GO:0046872)

GO Cellular Component (4): nucleoplasm (GO:0005654), cytoplasm (GO:0005737), cytosol (GO:0005829), nucleus (GO:0005634)

Reactome top-level categories

Rollup of top-1 pathways:

Category	Pathways
Class I MHC mediated antigen processing & presentation	1

GO top-level categories

Rollup of top GO terms by namespace:

Category	Terms
cellular anatomical structure	3
protein binding	2
gene expression	1
regulation of macromolecule biosynthetic process	1
protein modification by small protein conjugation	1
viral transcription	1
regulation of viral transcription	1
negative regulation of viral process	1
defense response to virus	1
immune response	1
defense response to symbiont	1
DNA-templated transcription	1
regulation of DNA-templated transcription	1
negative regulation of RNA biosynthetic process	1
innate immune response	1
host-mediated perturbation of symbiont process	1
regulation of viral entry into host cell	1
symbiont entry into host cell	1
positive regulation by symbiont of entry into host	1
positive regulation of viral life cycle	1
negative regulation of cell development	1
neurogenesis	1
regulation of neurogenesis	1
negative regulation of nervous system development	1
protein ubiquitination	1
negative regulation of protein-containing complex assembly	1
AIM2 inflammasome complex assembly	1
regulation of AIM2 inflammasome complex assembly	1
negative regulation of inflammasome-mediated signaling pathway	1
defense response	1
response to virus	1
ubiquitin-like protein transferase activity	1
transition metal ion binding	1
molecular adaptor activity	1
ubiquitin-protein transferase activity	1
ubiquitin-like protein ligase activity	1
binding	1
catalytic activity	1
cation binding	1
nuclear lumen	1

Protein interactions and networks

STRING

1221 interactions, top by confidence (×1000):

Protein A	Protein B	Partner UniProt	Score
TRIM11	TRAT1	Q6PIZ9	845
TRIM11	AIM2	O14862	844
TRIM11	BBOX1	O75936	774
TRIM11	PLEKHF1	Q96S99	768
TRIM11	UBE2N	P61088	693
TRIM11	FPR2	P25090	683
TRIM11	PYCR1	P32322	667
TRIM11	TBK1	Q9UHD2	596
TRIM11	TRIM44	Q96DX7	588
TRIM11	TRIM66	O15016	587
TRIM11	TRIM37	O94972	536
TRIM11	TRIM33	Q9UPN9	533
TRIM11	TRIM28	Q13263	532
TRIM11	PRY	O14603	513
TRIM11	MT-ATP6	P00846	511

IntAct

84 interactions, top by confidence:

A	B	Type	Score
PSMD7	PSMD11	psi-mi:“MI:0914”(association)	0.730
PSMD12	PSMD11	psi-mi:“MI:0914”(association)	0.730
TEPSIN	AP4M1	psi-mi:“MI:0914”(association)	0.700
TANC2	TAX1BP3	psi-mi:“MI:0914”(association)	0.690
FAM9C	NDC80	psi-mi:“MI:0914”(association)	0.670
XAF1	AKT1	psi-mi:“MI:0914”(association)	0.670
UBE2N	UBA1	psi-mi:“MI:0914”(association)	0.640
NEUROG3	GXYLT2	psi-mi:“MI:0914”(association)	0.640
EFNB3	DENND11	psi-mi:“MI:0914”(association)	0.640
KANK4	TRAPPC3	psi-mi:“MI:0914”(association)	0.640
MCL1	PRKAB2	psi-mi:“MI:0914”(association)	0.640
TRIM44	CUL2	psi-mi:“MI:0914”(association)	0.640
HOXB5	VPS37C	psi-mi:“MI:0914”(association)	0.530
TRIM44	ODAD3	psi-mi:“MI:0914”(association)	0.530
LINGO2	GAPDHS	psi-mi:“MI:0914”(association)	0.530
ZSCAN26	LRP4	psi-mi:“MI:0914”(association)	0.530
NUFIP2	RELA	psi-mi:“MI:0914”(association)	0.530
ASB8	CUL5	psi-mi:“MI:0914”(association)	0.530
LINGO2	LGALS1	psi-mi:“MI:0914”(association)	0.530
CLPB	CLUH	psi-mi:“MI:0914”(association)	0.530
FAIM	WDR47	psi-mi:“MI:0914”(association)	0.500
MED15	TRIM11	psi-mi:“MI:0403”(colocalization)	0.460
MED15	TRIM11	psi-mi:“MI:0915”(physical association)	0.460
TRIM11	MED15	psi-mi:“MI:0915”(physical association)	0.460

BioGRID (282): TRIM11 (Affinity Capture-MS), TRIM11 (Affinity Capture-MS), TRIM11 (Affinity Capture-MS), TRIM11 (Affinity Capture-MS), TRIM11 (Affinity Capture-MS), TRIM11 (Affinity Capture-MS), TRIM11 (Affinity Capture-MS), TRIM11 (Affinity Capture-MS), TRIM11 (Affinity Capture-MS), TRIM11 (Affinity Capture-MS), TRIM11 (Affinity Capture-MS), TRIM11 (Affinity Capture-MS), CAMKK1 (Affinity Capture-MS), RLF (Affinity Capture-MS), USF1 (Affinity Capture-MS)

ESM2 similar proteins: A0JN74, A6NCK2, A6NGJ6, A6NI03, B1H278, K7N6K2, O00478, O00481, P14373, P19474, Q13410, Q1ACD5, Q1ACD6, Q1ACD7, Q1ACD8, Q1XHU0, Q2YEM8, Q2YEM9, Q3ZEE5, Q587N6, Q5C8T6, Q5C8T8, Q5C8U1, Q5D7I9, Q5D7J0, Q5D7J1, Q5NCC9, Q5R996, Q62158, Q6MFZ5, Q7YR33, Q7YRV4, Q80V85, Q8BGE7, Q8NG06, Q923T7, Q96BQ3, Q96F44, Q99PP6, Q99PQ2

Diamond homologs: A0A2P1BRP3, A0A2P1BRQ0, A0ZSK3, A0ZSK4, B1H278, O95361, Q14142, Q1LY10, Q1XHU0, Q309B1, Q5BK82, Q5R760, Q6MFZ5, Q6P6S3, Q6UXG8, Q80X56, Q80YW5, Q8BVW3, Q8WV44, Q8WVV5, Q91453, Q96F44, Q98989, Q98993, Q99PP9, Q99PQ2, Q9ESN2, Q9HCM9, A0JN74, O19085, P14373, P19474, Q02084, Q5R7W8, Q62158, Q62556, Q7KYR7, Q86WT6, Q8N7C3, Q91431

SIGNOR signaling

2 interactions.

A	Effect	B	Mechanism
TRIM11	down-regulates	PHOX2B	ubiquitination
Ub:E2	“up-regulates activity”	TRIM11	ubiquitination

Enriched among interaction partners

Reactome pathways and GO biological processes over-represented among this gene’s 105 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:

Pathway	Partners	Fold	FDR
CLEC7A (Dectin-1) signaling	6	14.3×	1e-03
FCERI mediated NF-kB activation	5	13.0×	7e-03
Downstream TCR signaling	5	10.7×	8e-03
Interleukin-1 signaling	5	10.3×	8e-03
KEAP1-NFE2L2 pathway	5	10.0×	8e-03
Antigen processing: Ubiquitination & Proteasome degradation	10	6.2×	1e-03
Neddylation	7	5.5×	1e-02

Disease & clinical

Clinical variants and AI predictions

ClinVar

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

Classification	Count (floor)
Pathogenic	0
Likely pathogenic	0
Uncertain significance	53
Likely benign	0
Benign	2

Top pathogenic / likely-pathogenic (0)

SpliceAI

699 predictions. Top by Δscore:

Variant	Effect	Δscore
1:228395248:GTCCC:G	acceptor_gain	1.0000
1:228395249:TCCC:T	acceptor_gain	1.0000
1:228395249:TCCCC:T	acceptor_loss	1.0000
1:228395250:CCC:C	acceptor_gain	1.0000
1:228395250:CCCC:C	acceptor_gain	1.0000
1:228395250:CCCCT:C	acceptor_loss	1.0000
1:228395251:CC:C	acceptor_gain	1.0000
1:228395251:CCC:C	acceptor_gain	1.0000
1:228395252:CC:C	acceptor_gain	1.0000
1:228395253:C:CC	acceptor_gain	1.0000
1:228395254:T:G	acceptor_loss	1.0000
1:228396943:CTA:C	donor_loss	1.0000
1:228396944:TAC:T	donor_loss	1.0000
1:228396946:C:A	donor_loss	1.0000
1:228397045:ACC:A	acceptor_gain	1.0000
1:228397046:CC:C	acceptor_gain	1.0000
1:228397046:CCC:C	acceptor_gain	1.0000
1:228397047:CC:C	acceptor_gain	1.0000
1:228397048:C:CC	acceptor_gain	1.0000
1:228397048:CTAGA:C	acceptor_loss	1.0000
1:228397139:GTAC:G	donor_loss	1.0000
1:228400958:GCTCA:G	donor_loss	1.0000
1:228400959:CTCA:C	donor_loss	1.0000
1:228400960:TCA:T	donor_loss	1.0000
1:228400961:CA:C	donor_loss	1.0000
1:228401190:ATCTT:A	acceptor_gain	1.0000
1:228401191:TCTT:T	acceptor_loss	1.0000
1:228401192:CTT:C	acceptor_gain	1.0000
1:228401193:TT:T	acceptor_gain	1.0000
1:228401193:TTCT:T	acceptor_loss	1.0000

AlphaMissense

3010 scored. Top likely-pathogenic:

Variant	Protein change	am_pathogenicity
1:228406457:G:C	F35L	0.999
1:228406457:G:T	F35L	0.999
1:228406459:A:G	F35L	0.999
1:228406458:A:G	F35S	0.997
1:228406460:G:C	N34K	0.997
1:228406460:G:T	N34K	0.997
1:228406485:G:T	P26Q	0.997
1:228406507:A:G	C19R	0.997
1:228406516:A:G	C16R	0.997
1:228395137:A:C	F325L	0.996
1:228395137:A:T	F325L	0.996
1:228395139:A:G	F325L	0.996
1:228406350:A:T	L71H	0.995
1:228406456:A:G	C36R	0.995
1:228406458:A:C	F35C	0.995
1:228406463:G:C	H33Q	0.995
1:228406463:G:T	H33Q	0.995
1:228406494:A:G	F23S	0.995
1:228395213:A:G	L300P	0.994
1:228406358:G:C	N68K	0.994
1:228406358:G:T	N68K	0.994
1:228406506:C:G	C19S	0.994
1:228406507:A:T	C19S	0.994
1:228395042:C:T	G357E	0.993
1:228406405:A:G	C53R	0.993
1:228406447:A:G	C39R	0.993
1:228406455:C:T	C36Y	0.993
1:228406515:C:T	C16Y	0.993
1:228395082:A:G	W344R	0.992
1:228395082:A:T	W344R	0.992

dbSNP variants (sampled 300 via entrez): RS1000041747 (1:228399521 G>A), RS1000186223 (1:228401572 C>A,T), RS1000196921 (1:228406097 G>C,T), RS1000606044 (1:228395118 G>A), RS1000866911 (1:228405595 T>C), RS1001801488 (1:228394563 C>T), RS1002057632 (1:228399372 G>A), RS1002083648 (1:228405885 G>A,T), RS1002157271 (1:228405588 G>A), RS1002271260 (1:228404194 C>G), RS1002386027 (1:228399693 G>A), RS1002386326 (1:228398371 A>C), RS1002563309 (1:228401193 T>C), RS1002609501 (1:228407680 G>C), RS1002984349 (1:228398436 A>G)

Disease associations

OMIM: gene MIM:607868 | disease phenotypes:

GenCC curated gene-disease

Mondo (0):

Orphanet (0):

HPO phenotypes

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

GWAS associations

2 associations (top):

Study	Trait	p-value
GCST002641_2	Hip circumference (psychosocial stress interaction)	4.000000e-06
GCST006276_1	Non-Richardson’s syndrome vs Richardson’s syndrome in progressive supranuclear palsy	2.000000e-09

EFO canonical traits (1, from GWAS)

EFO ID	Trait name
EFO:0006783	psychosocial stress measurement

Drugs & pharmacology

Drug and pharmacology data

Is drug target: no

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

CTD chemical–gene interactions

31 total (human), top 30 by PubMed support.

Chemical	Actions (top 5)	PubMed papers
sodium arsenite	increases expression	2
Air Pollutants	decreases expression, increases abundance, increases expression, affects cotreatment	2
Benzo(a)pyrene	affects methylation, increases methylation	2
Smoke	decreases expression, increases abundance, increases expression	2
Tobacco Smoke Pollution	increases expression	2
aristolochic acid I	increases expression	1
3-((6-(2-methoxyphenyl)pyrimidin-4-yl)amino)phenyl)methane sulfonamide	decreases expression	1
methylmercuric chloride	increases expression	1
triphenyl phosphate	affects expression	1
alpha-pinene	decreases expression, increases abundance, affects cotreatment	1
methylparaben	increases expression	1
aflatoxin B2	decreases methylation	1
methacrylaldehyde	affects cotreatment, decreases expression, increases abundance	1
bisphenol S	decreases methylation	1
PCI 5002	affects cotreatment, increases expression	1
Sunitinib	increases expression	1
Acrolein	increases abundance, affects cotreatment, decreases expression	1
Benzene	increases expression	1
Lead	increases expression	1
Ozone	affects cotreatment, decreases expression, increases abundance	1
Quercetin	increases expression	1
Thiram	increases expression	1
Tunicamycin	increases expression	1
Urethane	increases expression	1
Valproic Acid	increases methylation	1
Zinc	affects cotreatment, increases expression	1
Cyclosporine	increases expression	1
Cadmium Chloride	decreases expression	1
Copper Sulfate	increases expression	1
Particulate Matter	decreases expression	1

Cellosaurus cell lines

1 cell lines: 1 cancer cell line

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

Cellosaurus	Name	Category	Sex
CVCL_TT81	HAP1 TRIM11 (-)	Cancer cell line	Male

Clinical trials (associated diseases)

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