RBM12

RBM12
Identifiers
Aliases	RBM12, HRIHFB2091, SWAN, RNA binding motif protein 12, SCZD19
External IDs	OMIM: 607179; MGI: 1922960; HomoloGene: 34993; GeneCards: RBM12; OMA:RBM12 - orthologs
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1WEL, 2CPY, 2DNN, 2EK1, 2EK6
Gene location (Human) Chr. Chromosome 20 (human) Band 20q11.22 Start 35,648,925 bp End 35,664,956 bp
Gene location (Mouse) Chr. Chromosome 2 (mouse) Band 2|2 H1 Start 155,933,878 bp End 155,953,898 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Achilles tendon epithelium of colon secondary oocyte bone marrow cell embryo ganglionic eminence islet of Langerhans amniotic fluid ventricular zone cartilage tissue Top expressed in primitive streak tail of embryo genital tubercle abdominal wall aortic valve mandibular prominence maxillary prominence ureter hair follicle somite More reference expression data BioGPS n/a
Orthologs Species Human Mouse Entrez 10137 75710 Ensembl ENSG00000244462 ENSMUSG00000089824 UniProt Q9NTZ6 Q8R4X3 RefSeq (mRNA) NM_152838 NM_001198838 NM_001198840 NM_006047 NM_029397 NM_170598 RefSeq (protein) NP_001185767 NP_001185769 NP_006038 NP_690051 NP_083673 NP_733486 Location (UCSC) Chr 20: 35.65 – 35.66 Mb Chr 2: 155.93 – 155.95 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

RNA-binding protein 12 is a protein that in humans is encoded by the RBM12 gene.

This gene encodes a protein that contains several RNA-binding motifs, potential transmembrane domains, and proline-rich regions. This gene and the gene for copine I overlap at map location 20q11.21. Alternative splicing in the 5' UTR results in two transcript variants. Both variants encode the same protein.

RMB12 is a protein encoded by the RBM12 gene and it still is not entirely known the full capacity, involvement, and function of the RBM12 protein, as of early 2026. There have been some studies that have linked the RMB12 protein in the suppression of fetal hemoglobin (HbF) production. In human fetuses, fetal hemoglobin is the primary oxygen-carrying protein in their red blood cells and facilitates the exchange of oxygen between the fetus and the mother. “RBM12 is a nuclear RBP with broad tissue expression that remains unchanged between fetal and erythroid stages (Wakabayashi, et al.).”^1 When primary erythroblasts and HeLa cells are stained with immunofluorescence, the staining showed RBM12 displaying nuclear localization suggesting it functions at pre-RNA level synthesis. It also showed to display expression across multiple different types of tissue and the expression does not seem to be developmentally selective. RBM12 has shown a preference in binding at the 5’UTR of its target mRNA’s.

Sickle cell anemia

Hemoglobin is made up of four different subunits. In adults, hemoglobin is made up of two alpha subunits and two beta subunits. In a fetus, hemoglobin is made up of two identical alpha subunits, but instead of the beta subunits it is made up of two gamma subunits. Sickle cell disease is caused by a mutation in the beta subunits of hemoglobin. Since fetal hemoglobin does not have the beta subunits and instead has the gamma subunits, they are not affected by sickle cell disease. HbF, fetal hemoglobin, has recently begun to be studied as a possible treatment for sickle cell disease. “Increased levels of HbF can diminish the propensity of sickle cell hemoglobin to polymerize under hypoxic conditions and thus inhibit the pathognomonic changes in cell shape (Wakabayashi, et al.).”

Mental health disorders

Studies have shown the RBM12 protein to have an influence on the development of different psychiatric disorders like schizophrenia and psychosis. “RBM12 is a high-penetrance risk factor for familial schizophrenia and psychosis… (Semesta, et al.).” The RBM12 protein can suppress the G protein-coupled receptor signaling axis. Loss of RMB12 can lead to a hyperactive cAMP production which then will increase PKA activity and can alter neuronal transcriptional responses.

Other disorders

RBM12 has been linked to certain cancers as well. An increase in RBM12 expression has been linked to a negative prognosis in different types of cancers. Some of those cancers include Meibomian, a rare and aggressive cancer of the oil glands in the eyelids, and hepatocellular cell carcinoma. Various mutations in RBM12 have also been linked to some endometrial, colorectal, and kidney cancer diagnoses.

References

Semesta K, Garces A, Tsvetanova N. The psychosis risk factor RBM12 encodes a novel repressor of GPCR/cAMP signal transduction. Journal of Biological Chemistry, 2023; 299

Aoi Wakabayashi, Maryanne Kihiu, Malini Sharma, A. Josephine Thrasher, Megan S. Saari, Mathieu Quesnel-Vallières, Osheiza Abdulmalik, Scott A. Peslak, Eugene Khandros, Cheryl A. Keller, Belinda M. Giardine, Yoseph Barash, Ross C. Hardison, Junwei Shi, Gerd A. Blobel; Identification and characterization of RBM12 as a novel regulator of fetal hemoglobin expression. Blood Adv2022; 6 (23): 5956–5968. doi: https://doi.org/10.1182/bloodadvances.2022007904

Craig, C., Eng, S., Manzo, J., & Tkacenko, A. (2021, January). PDB101: Molecule of the Month: Fetal Hemoglobin. RCSB: PDB-101. https://pdb101.rcsb.org/motm/257

RBM12. (n.d.). The Human Protein Atlas. Retrieved May 8, 2026, from https://www.proteinatlas.org/ENSG00000244462-RBM12

Further reading

• Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T (June 2002). "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones". DNA Research. 9 (3): 99–106. doi:10.1093/dnares/9.3.99. PMID 12168954.
• Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, et al. (November 2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–648. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.
• Kofler M, Motzny K, Freund C (November 2005). "GYF domain proteomics reveals interaction sites in known and novel target proteins". Molecular & Cellular Proteomics. 4 (11): 1797–1811. doi:10.1074/mcp.M500129-MCP200. PMID 16120600.
• Brill LM, Salomon AR, Ficarro SB, Mukherji M, Stettler-Gill M, Peters EC (May 2004). "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry". Analytical Chemistry. 76 (10): 2763–2772. doi:10.1021/ac035352d. PMID 15144186.
• Ueki N, Oda T, Kondo M, Yano K, Noguchi T, Muramatsu M (December 1998). "Selection system for genes encoding nuclear-targeted proteins". Nature Biotechnology. 16 (13): 1338–1342. doi:10.1038/4315. PMID 9853615. S2CID 20001769.

External links

• RBM12 human gene location in the UCSC Genome Browser.
• RBM12 human gene details in the UCSC Genome Browser.