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GeneE
26 sources retrieved Β· Most recent: April 2026 Β· Index updated 14 days ago
β“˜GeneE is for informational purposes only. It is not a substitute for professional medical advice, diagnosis, or treatment.
RBM10
RNA binding motif protein 10
Chromosome X Β· Xp11.3
NCBI Gene: 8241Ensembl: ENSG00000182872.17HGNC: HGNC:9896UniProt: A0A0S2Z4W4
235PubMed Papers
21Diseases
0Drugs
40Pathogenic Variants
FUNCTIONAL ROLE
Highly Constrained
RESEARCH IMPACT
Trending
CLINICAL
OMIM Disease Gene
DATA QUALITY
βœ“ Experimental GO Evidenceβœ“ Swiss-Prot Reviewed
nuclear speckRNA bindingprotein bindingmiRNA bindingTARP syndromelung adenocarcinomaneurodegenerative diseasepancreatic adenocarcinoma
✦AI Summary

RBM10 is a nuclear RNA-binding protein that primarily regulates alternative splicing of pre-mRNA transcripts 1. It binds to specific RNA sequences, including the consensus motif 5'-AGGUAA-3', with preference for poly(G) and poly(U) homopolymers, and may interact with miRNA hairpins 2. RBM10 functions as a splicing regulator that modulates exon inclusion/exclusion patterns; for example, it promotes exclusion of specific exons in hTERT transcripts to generate non-functional isoforms, thereby suppressing telomerase activity in pancreatic cancer 3. Clinically, RBM10 mutations occur frequently across multiple cancer types. In lung adenocarcinoma, RBM10 mutations are more common in males and represent recurrent somatic alterations 45. In colorectal cancer, RBM10 mutations associate with shorter progression-free survival in metastatic disease, and functional studies confirm RBM10 acts as a tumor suppressor 6. RBM10 loss enhances sensitivity to BCL2 inhibitor venetoclax in leukemia by causing mis-splicing of apoptotic regulators like XIAP and BCL2A1, while remaining dispensable for normal hematopoiesis 7. Additionally, mutations in RBM10 represent frequent alterations in poorly differentiated thyroid cancer, particularly in fatal cases 8. Germline RBM10 mutations cause TARP syndrome, an X-linked developmental disorder 1, establishing RBM10's critical role in both normal development and cancer pathogenesis.

Sources cited
1
RBM10 is a nuclear RNA-binding protein regulating alternative splicing; mutations cause TARP syndrome and various cancers
PMID: 33515724
2
RBM10 binds to ssRNA consensus sequence 5'-AGGUAA-3'
PMID: 21256132
3
RBM10 mutations are more common in males with lung adenocarcinoma
PMID: 25079552
4
RBM10 has recurrent truncating mutations in lung adenocarcinoma
PMID: 22980975
5
RBM10 mutations associate with shorter progression-free survival in metastatic colorectal cancer and function as tumor suppressor
PMID: 37146911
6
RBM10 regulates hTERT splicing to suppress telomerase activity and inhibits pancreatic cancer progression
PMID: 33520366
7
RBM10 loss enhances BCL2 inhibitor response in leukemia through mis-splicing of XIAP and BCL2A1
PMID: 36563682
8
RBM10 mutations occur at high rates (12%) in fatal poorly differentiated thyroid cancer
PMID: 30747050
9
RBM10 mutations are frequent in cancer and alter splice site recognition
PMID: 39146933
Disease Associationsβ“˜21
TARP syndromeOpen Targets
0.79Strong
lung adenocarcinomaOpen Targets
0.63Moderate
neurodegenerative diseaseOpen Targets
0.53Moderate
pancreatic adenocarcinomaOpen Targets
0.51Moderate
non-small cell lung carcinomaOpen Targets
0.51Moderate
colorectal adenocarcinomaOpen Targets
0.51Moderate
genetic disorderOpen Targets
0.47Moderate
urinary bladder cancerOpen Targets
0.40Weak
dengue diseaseOpen Targets
0.38Weak
cleft palateOpen Targets
0.37Weak
bladder transitional cell carcinomaOpen Targets
0.37Weak
Ampulla of Vater CarcinomaOpen Targets
0.37Weak
Endometrial Endometrioid AdenocarcinomaOpen Targets
0.37Weak
gastric carcinomaOpen Targets
0.37Weak
Ovarian Endometrioid Adenocarcinoma with Squamous DifferentiationOpen Targets
0.37Weak
cholangiocarcinomaOpen Targets
0.36Weak
Neurodevelopmental delayOpen Targets
0.34Weak
linear skin defects with multiple congenital anomalies 3Open Targets
0.31Weak
small cell lung carcinomaOpen Targets
0.29Weak
hepatocellular carcinomaOpen Targets
0.29Weak
TARP syndromeUniProt
Pathogenic Variants40
NM_005676.5(RBM10):c.2296C>T (p.Arg766Cys)Likely pathogenic
not provided|TARP syndrome
β˜…β˜…β˜†β˜†2026β†’ Residue 766
NM_005676.5(RBM10):c.292C>T (p.Arg98Ter)Pathogenic
Neurodevelopmental delay|TARP syndrome|not provided
β˜…β˜…β˜†β˜†2024β†’ Residue 98
NM_005676.5(RBM10):c.724+2T>CPathogenic
TARP syndrome|Nonpapillary renal cell carcinoma
β˜…β˜…β˜†β˜†2024
NM_005676.5(RBM10):c.331C>T (p.Gln111Ter)Likely pathogenic
TARP syndrome
β˜…β˜…β˜†β˜†2023β†’ Residue 111
NM_005676.5(RBM10):c.1352_1353del (p.Glu451fs)Pathogenic
Inborn genetic diseases|not provided
β˜…β˜…β˜†β˜†2022β†’ Residue 451
NM_005676.5(RBM10):c.94C>T (p.Arg32Ter)Likely pathogenic
TARP syndrome
β˜…β˜†β˜†β˜†2026β†’ Residue 32
NM_005676.5(RBM10):c.1861C>T (p.Gln621Ter)Likely pathogenic
TARP syndrome
β˜…β˜†β˜†β˜†2025β†’ Residue 621
NM_005676.5(RBM10):c.406_430del (p.Leu136fs)Pathogenic
not provided
β˜…β˜†β˜†β˜†2025β†’ Residue 136
NM_005676.5(RBM10):c.1064_1079del (p.Glu355fs)Likely pathogenic
TARP syndrome
β˜…β˜†β˜†β˜†2024β†’ Residue 355
NM_005676.5(RBM10):c.2214_2217del (p.Ser738fs)Pathogenic
not provided|Nephroblastoma
β˜…β˜†β˜†β˜†2023β†’ Residue 738
NM_005676.5(RBM10):c.2100+1G>ALikely pathogenic
TARP syndrome
β˜…β˜†β˜†β˜†2023
NM_005676.5(RBM10):c.579_586dup (p.Asn196fs)Pathogenic
TARP syndrome
β˜…β˜†β˜†β˜†2023β†’ Residue 196
NM_005676.5(RBM10):c.2038C>T (p.Arg680Ter)Pathogenic
not provided
β˜…β˜†β˜†β˜†2023β†’ Residue 680
NM_005676.5(RBM10):c.487C>T (p.Arg163Trp)Likely pathogenic
TARP syndrome
β˜…β˜†β˜†β˜†2023β†’ Residue 163
NM_005676.5(RBM10):c.901+2T>CLikely pathogenic
not provided
β˜…β˜†β˜†β˜†2022
NM_005676.5(RBM10):c.2537+1G>ALikely pathogenic
not provided
β˜…β˜†β˜†β˜†2022
NM_005676.5(RBM10):c.1993_1996del (p.Gln665fs)Pathogenic
TARP syndrome
β˜…β˜†β˜†β˜†2022β†’ Residue 665
NM_005676.5(RBM10):c.2537_2537+3delLikely pathogenic
not provided
β˜…β˜†β˜†β˜†2022
NM_005676.5(RBM10):c.1974G>C (p.Trp658Cys)Likely pathogenic
TARP syndrome
β˜…β˜†β˜†β˜†2022β†’ Residue 658
NM_005676.5(RBM10):c.2514C>G (p.Tyr838Ter)Likely pathogenic
TARP syndrome
β˜…β˜†β˜†β˜†2022β†’ Residue 838
View on ClinVar β†—
Related Genes
HNRNPA1L3Shared pathway100%RBMXL1Shared pathway100%RBMY1EShared pathway100%RBMY1DShared pathway100%RBM44Shared pathway100%HNRNPA3Shared pathway100%
Tissue Expression6 tissues
Ovary
100%
Bone Marrow
79%
Liver
75%
Lung
68%
Heart
53%
Brain
45%
Gene Interaction Network
Click a node to explore
RBM10HNRNPA1L3RBMXL1RBMY1ERBMY1DRBM44HNRNPA3
PROTEIN STRUCTURE
Preparing viewer…
PDB2LXI Β· NMR
View on RCSB β†—
Constraintβ“˜
LOEUFβ“˜
0.06Highly Constrained
pLIβ“˜
1.00Intolerant
Observed/Expected LoF0.01 [0.00–0.06]
RankingsWhere RBM10 stands among ~20K protein-coding genes
  • #1,692of 20,598
    Most Researched235 Β· top 10%
  • #1,535of 5,498
    Most Pathogenic Variants40
  • #8of 17,882
    Most Constrained (LOEUF)0.06 Β· top 1%
Genes detectedRBM10
Sources retrieved26 papers
Response timeβ€”
πŸ“„ Sources
26β–Ό
1
Comprehensive molecular profiling of lung adenocarcinoma.
PMID: 25079552
Nature Β· 2014
1.00
2
Molecular Profiling Provides Clinical Insights Into TargetedΒ andΒ Immunotherapies as Well as Colorectal CancerΒ Prognosis.
PMID: 37146911
Gastroenterology Β· 2023
0.90
3
Molecular impact of mutations in RNA splicing factors in cancer.
PMID: 39146933
Mol Cell Β· 2024
0.80
4
Modulation of RNA splicing enhances response to BCL2 inhibition in leukemia.
PMID: 36563682
Cancer Cell Β· 2023
0.70
5
RBM10 deficiency promotes brain metastasis by modulating sphingolipid metabolism in a BBB model of EGFR mutant lung adenocarcinoma.
PMID: 40069781
J Exp Clin Cancer Res Β· 2025
0.68