Alternative titles; symbols
HGNC Approved Gene Symbol: IGHMBP2
SNOMEDCT: 1187617004;
Cytogenetic location: 11q13.3 Genomic coordinates (GRCh38): 11:68,903,891-68,940,601 (from NCBI)
| Location | Phenotype |
Phenotype MIM number |
Inheritance |
Phenotype mapping key |
|---|---|---|---|---|
| 11q13.3 | Charcot-Marie-Tooth disease, axonal, type 2S | 616155 | Autosomal recessive | 3 |
| Neuronopathy, distal hereditary motor, autosomal recessive 1 | 604320 | Autosomal recessive | 3 |
Fukita et al. (1993) cloned the human homolog of the murine Smubp2 gene. The deduced 993-amino acid belongs to the putative helicase superfamily and shows 76.5% homology to the murine protein. A domain essential for DNA binding at residues 638 to 786 was identified. Expression of SMUBP2 mRNA was ubiquitous and augmented in spleen cells stimulated with lipopolysaccharide and interleukin-4 (IL4; 147780).
Sebastiani et al. (1995) noted that mouse Catf1 is a 989-amino acid protein that represents a novel type of mammalian transcription factor. Catf1 contains ATP-binding and helicase-like motifs and a DNA-binding domain with no homology to any known DNA-binding motif. Catf1 mRNA expression was highly controlled in a tissue-specific fashion in the newborn rat, with highest expression in heart. In adult mouse tissues, Sebastiani et al. (1995) detected the highest level of Catf1 mRNA in heart, with low levels in other tissues. Sebastiani et al. (1995) noted a high degree of amino acid sequence conservation between the rat Catf1 and the human and mouse SMUBP2 proteins and suggested that these are homologs.
Cottenie et al. (2014) found expression of the IGHMBP2 gene in the developing and adult human brain, with highest expression in the cerebellum. Expression in other body tissues was ubiquitous, with moderate expression in fibroblasts and lymphoblastic cell lines.
The IGHMBP2 gene contains 15 exons (Maystadt et al., 2004).
Fukita et al. (1993) used fluorescence in situ hybridization to map the human IGHMBP2 gene to chromosome 11q13.2-q13.4.
Using interspecific backcross analysis, Sebastiani et al. (1995) demonstrated that the mouse Ighmbp2 gene is on chromosome 19. This is a region of homology to the part of 11q where the human gene has been mapped.
Cardiac transcription factor-1 is a novel transcription factor that was first identified by McBride et al. (1993) through its interaction with a cis-acting myocyte-specific element located in the proximal enhancer of the atrial natriuretic factor (ANF; 108780).
Guenther et al. (2009) purified catalytically active recombinant IGHMBP2 and found that it functioned as an ATP-dependent 5-prime-to-3-prime helicase that unwound RNA and DNA duplexes in vitro. IGHMBP2 localized predominantly to the cytoplasm of neuronal and nonneuronal cells and associated with ribosomes. Distal spinal muscular atrophy type-1 (DSMA1; 604320)-causing amino acid substitutions in IGHMBP2 did not affect ribosome binding, but they severely impaired ATPase and helicase activity. The authors proposed that IGHMBP2 is functionally linked to translation and that mutations in its helicase domain interfere with this function in DSMA1 patients.
De Planell-Saguer et al. (2009) reported the biochemical characterization of IGHMBP2 and the isolation of a modifier locus that rescued the phenotype and motor neuron degeneration of nmd mice, the mouse model of SMARD1. The authors mapped and localized the modifier locus to mouse chromosome 13 and generated a 166-kb BAC transgene derived from CAST/EiJ mice and containing tRNA genes and activator of basal transcription-1 (Abt1), a protein-coding gene that is required for ribosome biogenesis. Ighmbp2 associated physically with tRNAs and in particular with tRNA-Tyr, which were present in the modifier, and Ighmbp2 associated with the Abt1 protein. Transcription factor IIIC-220 kD (GTF3C1; 603246), an essential factor required for tRNA transcription, and the helicases reptin (RUVBL2; 604788) and pontin (RUVBL1; 603449), which function in transcription and in ribosome biogenesis, were also part of Ighmbp2-containing complexes. De Planell-Saguer et al. (2009) suggested that IGHMBP2 may be a component of the translational machinery and that these components may be genetically manipulated to suppress motor neuron degeneration.
Autosomal Recessive Distal Hereditary Motor Neuronopathy 1
Grohmann et al. (2001) demonstrated that autosomal recessive distal hereditary motor neuronopathy-1 (HMNR1; 604320), also known as autosomal recessive distal spinal muscle atrophy type 1 (DSMA1) and spinal muscular atrophy with respiratory distress (SMARD1), results from mutations in the IGHMBP2 gene. In HMNR1 families, they detected 3 recessive missense mutations (exons 5, 11, and 12), 2 nonsense mutations (exons 2 and 5), 1 frameshift mutation (exon 5), and 1 splice donor site mutation (intron 13) (see, e.g., 600502.0001-600502.0007). The authors noted that mutations in mouse Ighmbp2 are responsible for spinal muscular atrophy in the nmd mouse, whose phenotype resembles the HMNR1 phenotype. Like the SMN1 gene (600354), which is mutated in spinal muscular atrophy (see 253300), IGHMBP2 colocalizes with the RNA processing machinery in both the cytoplasm and the nucleus. Grohmann et al. (2001) concluded that IGHMBP2 is the second gene found to be defective in spinal muscular atrophy and that IGHMBP2 and SMN share common functions important to motor neuron maintenance and integrity in mammals.
Among 29 infants with HMNR1, Grohmann et al. (2003) identified 26 novel mutations in the IGHMBP2 gene, including 14 missense, 6 nonsense, 4 frameshift, 1 in-frame deletion, and 1 frameshift insertion.
Pitt et al. (2003) identified mutations in the IGHMBP2 gene in 8 patients with severe infantile neuropathy with diaphragmatic weakness and progressive axonal neuropathy. The authors noted that the disorder in their patients was slightly different from that described in classic HMNR1 patients, most notably the absence of pathologic changes in the anterior horn in 1 patient examined.
In 5 of 28 (18%) infants whose clinical course was consistent with HMNR1, Maystadt et al. (2004) identified 9 novel mutations in the IGHMBP2 gene. Seven of the mutations occurred at highly conserved residues of the putative DNA helicase domain of the protein.
Guenther et al. (2007) identified 14 novel mutations in the IGHMBP2 gene in 10 patients with HMNR1. All missense mutations altered conserved residues within or adjacent to the putative DNA helicase domain.
Charcot-Marie-Tooth Disease, Axonal, Type 2S
In 15 patients from 11 families with childhood onset of autosomal recessive axonal Charcot-Marie-Tooth disease type 2S (CMT2S; 616155), Cottenie et al. (2014) identified biallelic mutations in the IGHMBP2 gene (see, e.g., 600502.0010-600502.0014). The mutations in the first family were found by whole-exome sequencing; mutations in the remaining 10 families were found by targeted sequencing of a cohort of 85 families with recessive CMT2. Most of the patients carried compound heterozygous mutations; many had a nonsense mutation in the 5-prime region and a mutation in the last exon. Patient fibroblasts and lymphoblastoid cells showed IGHMBP2 protein levels lower than controls, but higher than those observed in patients with DSMA1, suggesting that the milder phenotype in CMT2S may be related to residual protein levels. Functional studies of individual variants were not performed, but Cottenie et al. (2014) postulated a loss-of-function effect.
In 5 patients from 3 unrelated families with CMT2S, Schottmann et al. (2015) identified biallelic mutations in the IGHMBP2 gene (see, e.g., 600502.0010-600502.0011, 600502.0015).
The neuromuscular degeneration (nmd) mouse, a model of SMARD1, has progressive degeneration of spinal motor neurons and muscle atrophy. Cox et al. (1998) identified the mutated gene in the nmd mouse as the putative transcriptional activator and ATPase/DNA helicase previously described as Smbp2 or Catf1. Mutations were found in 2 alleles, a single amino acid deletion in nmd(J) and a splice donor mutation in nmd(2J). The selective vulnerability of motor neurons is striking in view of the widespread expression of this gene, although the pattern of degeneration may reflect a specific threshold since neither allele is null. In addition, Cox et al. (1998) found that the nmd phenotype is attenuated in a semidominant fashion by a major genetic locus on mouse chromosome 13. The identification of the nmd gene and the mapping of a major suppressor provided new opportunities for understanding mechanisms of motor neuron degeneration.
Maddatu et al. (2004) generated 2 independent lines of transgenic mice expressing the full-length Ighmbp2 cDNA specifically in neurons. Histopathologic evaluation of L4 ventral nerve roots revealed that transgenic expression of the Ighmbp2 cDNA prevented primary motor neuron degeneration, while restoring the normal axonal morphology and density in nmd mice. A similar neuronal improvement was found in mutant mice carrying the CAST/EiJ-derived modifier of nmd (MnmC). Both the transgenic and modified nmd mice went on to develop a previously unobserved cardiac and skeletal myopathy. Necropsy of nmd mice in end-stage heart failure revealed a primary dilated cardiomyopathy with secondary respiratory failure confirmed by ECG and echocardiographic measures. The authors suggested that reduced levels of IGHMBP2 in nmd mice may compromise the integrity and function not only of motor neurons but also of skeletal and cardiac myocytes.
Grohmann et al. (2004) showed that low levels of Ighmbp2 immunoreactivity were present in the nucleus of spinal motor neurons and high levels in cell bodies, axons and growth cones from wildtype mice. Ighmbp2 protein levels were greatly reduced in nmd mice, which showed severe motor neuron degeneration before first symptoms became apparent. Loss of motor neuron cell bodies in lumbar spinal cord was followed by axonal degeneration in corresponding nerves and loss of axon terminals at motor endplates. Myopathic changes contributed to muscle weakness and especially to respiratory failure. Cultured motor neurons from embryonic nmd mice did not show any abnormality with respect to survival, axonal growth, or growth cone size.
Maddatu et al. (2005) generated transgenic mice expressing the full-length Ighmbp2 cDNA specifically in myocytes under the control of the mouse titin promoter. This tissue-specific transgene increased the life span of nmd mice up to 8-fold by preventing primary dilated cardiomyopathy and showed complete functional correction as measured by ECG, echocardiography, and plasma creatine kinase-MB (see 123310). Double-transgenic nmd mice expressing Ighmbp2 both in myocytes and in neurons displayed correction of both dilated cardiomyopathy and motor neuron disease, resulting in an essentially wildtype appearance. Additionally, quantitative trait locus analysis in a CAST/EiJ backcross population identified 3 major CAST-derived cardiac modifiers of nmd on chromosomes 9, 10, and 16 that accounted for over 26% of the genetic variance.
From embryonic and adult mouse spinal cord, Corti et al. (2006) isolated neural stem cells characterized by increased ALDH (see, e.g., ALDH1A1, 100640) and low side scatter by FACS analysis. These cells were self-renewing, multipotent, and able to generate motor neurons in vitro and in vivo. Intrathecal treatment of neonatal nmd mice with these neural stem cells resulted in delayed disease progression, sparing of motor neurons and ventral root axons, and increased life span compared to untreated mice. Molecular studies showed that transplanted mice had a downregulation of genes involved in excitatory amino acid toxicity and oxidative stress, as well as an upregulation of genes involved in chromatin organization, cytoskeletal function, and neurogenesis compared to untreated mice.
In a southern Italian patient with autosomal recessive distal hereditary motor neuronopathy-1 (HMNR1; 604320) from a nonconsanguineous family, Grohmann et al. (2001) identified a homozygous G-to-A transition at nucleotide 1540 (c.1540G-A)in exon 11 resulting in a glutamic acid-to-lysine substitution at codon 514 (E514K). The patient presented with respiratory distress at 4 weeks of age. This mutation occurs in a highly conserved amino acid.
In 5 affected sibs in a consanguineous Lebanese family with autosomal recessive distal hereditary motor neuronopathy-1 (HMNR1; 604320), Grohmann et al. (2001) identified a homozygous A-to-G transition at nucleotide 638 (c.638A-G) of the IGHMBP2 gene, resulting in a histidine-to-arginine substitution at codon 213 (H213R) in exon 5. This mutation occurs in a highly conserved residue.
In a Turkish patient from a consanguineous family with autosomal recessive distal hereditary motor neuronopathy-1 (HMNR1; 604320), Grohmann et al. (2001) identified a homozygous G-to-A transition at nucleotide 1738 (c.1738G-A) in exon 12 of the IGHMBP2 gene, resulting in a valine-to-isoleucine substitution at codon 580 (V580I). This mutation occurs in a highly conserved amino acid.
In a nonconsanguineous family with 2 affected sibs with autosomal recessive distal hereditary motor neuronopathy-1 (HMNR1; 604320), Grohmann et al. (2001) identified a nonsense mutation, a C-to-T transition at nucleotide 121 (c.121C-T) of the IGHMBP2 gene resulting in a glutamine-to-termination substitution at codon 41 in exon 2. This mutation occurred in compound heterozygosity with a frameshift mutation (600502.0005).
In a nonconsanguineous German family with autosomal recessive distal hereditary motor neuronopathy-1 (HMNR1; 604320), Grohmann et al. (2001) identified a deletion of a single T at nucleotide 675 (c.675delT) of the IGHMBP2 gene, resulting in a frameshift. This mutation was found in compound heterozygosity with a nonsense mutation (604320.0004).
In a consanguineous Lebanese family with autosomal recessive distal hereditary motor neuronopathy-1 (HMNR1; 604320), Grohmann et al. (2001) identified a T-to-G transversion at nucleotide 707 (c.707T-G) of the IGHMBP2 gene, resulting in a leucine-to-termination substitution at codon 236 (L236X). The patient was homozygous for this mutation.
In a child with autosomal recessive distal hereditary motor neuronopathy-1 (HMNR1; 604320) from a consanguineous Sicilian family, Grohmann et al. (2001) identified a homozygous G-to-T transversion at the +1 position of intron 13 of the IGHMBP2 gene.
In a patient from a nonconsanguineous Italian family with autosomal recessive distal hereditary motor neuronopathy-1 (HMNR1; 604320), Guenther et al. (2004) identified compound heterozygosity for mutations in the IGHMBP2 gene: a c.1107C-G transversion in exon 8, resulting in a phe369-to-leu (F369L) substitution, and an 18.5-kb deletion encompassing exons 3-7 (600502.0009). The mutations were inherited from the mother and father, respectively. The authors noted that the 2 Alu repeats flanking the deletion were 81% identical, suggesting that Alu-mediated homologous recombination was the underlying genetic event.
For discussion of the 18.5-kb deletion in the IGHMBP2 gene that was found in compound heterozygous state in a patient with autosomal recessive distal hereditary motor neuronopathy-1 (HMNR1; 604320) by Guenther et al. (2004), see 600502.0008.
In 3 English patients, including 2 sisters, with childhood-onset Charcot-Marie-Tooth disease type 2S (CMT2S; 616155), Cottenie et al. (2014) identified compound heterozygous mutations in the IGHMBP2 gene: a c.138T-A transversion, resulting in a cys46-to-ter (C46X) substitution, and a 2-bp deletion (c.2911_2912delAG) in the last exon of the gene, resulting in a frameshift and premature termination (Arg971GlufsTer4; 600502.0011). The mutations in the sisters, which were found by whole-exome sequencing, segregated with the disorder in the family; they were not present in the 1000 Genomes Project database or in an in-house exome database of 480 control individuals. Patient cells did not show evidence of nonsense-mediated mRNA decay, and the truncated mutant proteins showed similar cellular localization as controls. Two Serbian sibs with the disorder were found to be compound heterozygous for C46X and a c.604T-G transversion, resulting in a phe202-to-val (F202V; 600502.0012) substitution at a conserved residue in part of an alpha-helix in domain 1A that is not central to the protein structure. Patient fibroblast and lymphoblastoid cells showed decreased protein levels compared to controls, but higher levels than those observed in patients with the more severe phenotype of distal spinal muscular atrophy-1 (DSMA1; 604320).
Schottmann et al. (2015) identified compound heterozygosity for the C46X and c.2911_2912delAG mutations in a woman with CMT2S from the United Kingdom. Her sister was reportedly similarly affected.
For discussion of the 2-bp deletion in the IGHMBP2 gene (c.2911_2912delAG) that was found in compound heterozygous state in patients with childhood-onset Charcot-Marie-Tooth disease type 2S (CMT2S; 616155) by Cottenie et al. (2014) and Schottmann et al. (2015), see 600502.0010.
For discussion of the phe202-to-val (F202V) mutation in the IGHMBP2 gene that was found in compound heterozygous state in patients with childhood-onset Charcot-Marie-Tooth disease type 2S (CMT2S; 616155) by Cottenie et al. (2014), see 600502.0010.
In 2 Italian sibs with Charcot-Marie-Tooth disease type 2S (CMT2S; 616155), Cottenie et al. (2014) identified compound heterozygous mutations in the IGHMBP2 gene: a c.1118T-G transversion, resulting in a val373-to-gly (V373G) substitution, and a c.1582G-A transition, resulting in an ala528-to-thr (A528T; 600502.0014) substitution. Both mutations occurred at conserved residues and were predicted to cause protein instability and a loss of function, but functional studies of the variants were not performed.
For discussion of the ala528-to-thr (A528T) mutation in the IGHMBP2 gene that was found in compound heterozygous state in patients with Charcot-Marie-Tooth disease type 2S (CMT2S; 616155) by Cottenie et al. (2014), see 600502.0013.
In 2 sibs, born of consanguineous Lebanese parents (family A), with Charcot-Marie-Tooth disease type 2S (CMT2S; 616155), Schottmann et al. (2015) identified a homozygous c.449+1G-T transversion in intron 3 of the IGHMPB2 gene, resulting in a splice site mutation and premature termination. The mutation, which was found by a combination of autozygosity mapping and whole-exome sequencing, segregated with the disorder in the family and was not found in the 1000 Genomes Project, Exome Variant Server, or dbSNP (build 138) databases, or in 130 in-house control exomes. Patient cells showed complete absence of the protein, consistent with a loss of function.
Corti, S., Locatelli, F., Papadimitriou, D., Donadoni, C., Del Bo, R., Crimi, M., Bordoni, A., Fortunato, F., Strazzer, S., Menozzi, G., Salani, S., Bresolin, N., Comi, G. P. Transplanted ALDH(hi)SSC(lo) neural stem cells generate motor neurons and delay disease progression of nmd mice, an animal model of SMARD1. Hum. Molec. Genet. 15: 167-187, 2006. [PubMed: 16339214] [Full Text: https://doi.org/10.1093/hmg/ddi446]
Cottenie, E., Kochanski, A., Jordanova, A., Bansagi, B., Zimon, M., Horga, A., Jaunmuktane, Z., Saveri, P., Rasic, V. M., Baets, J., Bartsakoulia, M., Ploski, R., and 28 others. Truncating and missense mutations in IGHMBP2 cause Charcot-Marie Tooth disease type 2. Am. J. Hum. Genet. 95: 590-601, 2014. [PubMed: 25439726] [Full Text: https://doi.org/10.1016/j.ajhg.2014.10.002]
Cox, G. A., Mahaffey, C. L., Frankel, W. N. Identification of mouse neuromuscular degeneration gene and mapping of a second site suppressor allele. Neuron 21: 1327-1337, 1998. [PubMed: 9883726] [Full Text: https://doi.org/10.1016/s0896-6273(00)80652-2]
de Planell-Saguer, M., Schroeder, D. G., Rodicio, M. C., Cox, G. A., Mourelatos, Z. Biochemical and genetic evidence for a role of IGHMBP2 in the translational machinery. Hum. Molec. Genet. 18: 2115-2126, 2009. [PubMed: 19299493] [Full Text: https://doi.org/10.1093/hmg/ddp134]
Fukita, Y., Mizuta, T., Shirozu, M., Ozawa, K., Shimuzu, A., Honjo, T. The human S-mu-bp2, a DNA-binding protein specific to the single-stranded guanine-rich sequence related to the immunoglobulin mu chain switch region. J. Biol. Chem. 268: 17463-17470, 1993. [PubMed: 8349627]
Grohmann, K., Rossoll, W., Kobsar, I., Holtmann, B., Jablonka, S., Wessig, C., Stoltenburg-Didinger, G., Fischer, U., Hubner, C., Martini, R., Sendtner, M. Characterization of Ighmbp2 in motor neurons and implications for the pathomechanism in a mouse model of human spinal muscular atrophy with respiratory distress type 1 (SMARD1). Hum. Molec. Genet. 13: 2031-2042, 2004. [PubMed: 15269181] [Full Text: https://doi.org/10.1093/hmg/ddh222]
Grohmann, K., Schuelke, M., Diers, A., Hoffmann, K., Lucke, B., Adams, C., Bertini, E., Leonhardt-Horti, H., Muntoni, F., Ouvrier, R., Pfeufer, A., Rossi, R., Van Maldergem, L., Wilmshurst, J. M., Wienker, T. F., Sendtner, M., Rudnik-Schoneborn, S., Zerres, K., Hubner, C. Mutations in the gene encoding immunoglobulin mu-binding protein 2 cause spinal muscular atrophy with respiratory distress type 1. Nature Genet. 29: 75-77, 2001. [PubMed: 11528396] [Full Text: https://doi.org/10.1038/ng703]
Grohmann, K., Varon, R., Stolz, P., Schuelke, M., Janetzki, C., Bertini, E., Bushby, K., Muntoni, F., Ouvrier, R., Van Maldergem, L., Goemans, N. M. L. A., Lochmuller, H. {and 13 others}: Infantile spinal muscular atrophy with respiratory distress type 1 (SMARD1). Ann. Neurol. 54: 719-724, 2003. [PubMed: 14681881] [Full Text: https://doi.org/10.1002/ana.10755]
Guenther, U. P., Schuelke, M., Bertini, E., D'Amico, A., Goemans, N., Grohmann, K., Hubner, C., Varon, R. Genomic rearrangements at the IGHMBP2 gene locus in two patients with SMARD1. Hum. Genet. 115: 319-326, 2004. [PubMed: 15290238] [Full Text: https://doi.org/10.1007/s00439-004-1156-0]
Guenther, U.-P., Handoko, L., Laggerbauer, B., Jablonka, S., Chari, A., Alzheimer, M., Ohmer, J., Plottner, O., Gehring, N., Sickmann, A., von Au, K., Schuelke, M., Fischer, U. IGHMBP2 is a ribosome-associated helicase inactive in the neuromuscular disorder distal SMA type 1 (DSMA1). Hum. Molec. Genet. 18: 1288-1300, 2009. [PubMed: 19158098] [Full Text: https://doi.org/10.1093/hmg/ddp028]
Guenther, U.-P., Varon, R., Schlicke, M., Dutrannoy, V., Volk, A., Hubner, C., von Au, K., Schuelke, M. Clinical and mutational profile in spinal muscular atrophy with respiratory distress (SMARD): defining novel phenotypes through hierarchical cluster analysis. Hum. Mutat. 28: 808-815, 2007. [PubMed: 17431882] [Full Text: https://doi.org/10.1002/humu.20525]
Maddatu, T. P., Garvey, S. M., Schroeder, D. G., Hampton, T. G., Cox, G. A. Transgenic rescue of neurogenic atrophy in the nmd mouse reveals a role for Ighmbp2 in dilated cardiomyopathy. Hum. Molec. Genet. 13: 1105-1115, 2004. [PubMed: 15069027] [Full Text: https://doi.org/10.1093/hmg/ddh129]
Maddatu, T. P., Garvey, S. M., Schroeder, D. G., Zhang, W., Kim, S.-Y., Nicholson, A. I., Davis, C. J., Cox, G. A. Dilated cardiomyopathy in the nmd mouse: transgenic rescue and QTLs that improve cardiac function and survival. Hum. Molec. Genet. 14: 3179-3189, 2005. [PubMed: 16174646] [Full Text: https://doi.org/10.1093/hmg/ddi349]
Maystadt, I., Zarhrate, M., Landrieu, P., Boespflug-Tanguy, O., Sukno, S., Collignon, P., Melki, J., Verellen-Dumoulin, C., Munnich, A., Viollet, L. Allelic heterogeneity of SMARD1 at the IGHMBP2 locus. Hum. Mutat. 23: 525-526, 2004. [PubMed: 15108294] [Full Text: https://doi.org/10.1002/humu.9241]
McBride, K., Robitaille, L., Tremblay, S., Argentin, S., Nemer, M. Fos/jun repression of cardiac specific transcription is targeted at a tissue-specific cis element. Molec. Cell. Biol. 13: 600-612, 1993. [PubMed: 8417355] [Full Text: https://doi.org/10.1128/mcb.13.1.600-612.1993]
Pitt, M., Houlden, H., Jacobs, J., Mok, Q., Harding, B., Reilly, M., Surtees, R. Severe infantile neuropathy with diaphragmatic weakness and its relationship to SMARD1. Brain 126: 2682-2692, 2003. [PubMed: 14506069] [Full Text: https://doi.org/10.1093/brain/awg278]
Schottmann, G., Jungbluth, H., Schara, U., Knierim, E., Morales Gonzalez, S., Gill, E., Seifert, F., Norwood, F., Deshpande, C., von Au, K., Schuelke, M., Senderek, J. Recessive truncating IGHMBP2 mutations presenting as axonal sensorimotor neuropathy. Neurology 84: 523-531, 2015. [PubMed: 25568292] [Full Text: https://doi.org/10.1212/WNL.0000000000001220]
Sebastiani, G., Durocher, D., Gros, P., Nemer, M., Malo, D. Localization of the Catf1 transcription factor gene to mouse chromosome 19. Mammalian Genome 6: 147-148, 1995. [PubMed: 7767002] [Full Text: https://doi.org/10.1007/BF00303264]