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187","pred":"pobj","subj":"T3455","obj":"T3452"},{"id":"R2188","pred":"punct","subj":"T3456","obj":"T3434"}],"text":"Conclusions\nComparison of Mcoln1 isoform 1 to its human homologue shows striking similarity at both the amino acid and nucleotide level. All six of the transmembrane domains, as well as the putative cation channel are highly conserved. The putative di-leucine (L-L-X-X) motif at the C-terminus, which may act as a late endosomal/lysosomal targeting signal, is also conserved [9]. This speculation is supported by work with cup-5[13], the c. elegans homologue of MCOLN1, since cellular localization studies suggest that the protein is found in the late endosomes and/or lysosomes.\nThe mouse Mcoln1 gene has two alternatively spliced isoforms, with isoform 2 having a different c-terminal cytoplasmic tail. The unique 86 amino acid c-terminal tail lacks the lysosomal targeting signal and does not contain any conserved domains when compared against the current profile databases. We speculate that this protein may have similar channel function but an alternate subcellular localization, but this must be proven once isoform-specific antibodies are raised. However, our results suggest that phenotypic assessment of Mcoln1 knock-out mice may be complicated and that care must be taken when interpreting data on mouse gene expression and phenotype.\nInterestingly, the second Mcoln1 isoform is not seen in humans and the sequence of the alternatively spliced region is not conserved between man and mouse. To date, very few genes have been reported that show species specific alternative splice variants. MOG, myelin/oligodendrocyte glycoprotein, has many different splice variants in humans that are not found in mice [17]. ATP11B, a P-type ATPase, has a rabbit-specific splice variant that deletes a transmembrane domain and therefore likely alters the putative function of the protein [18]. Sequencing of the human genome has led to estimates of approximately 32,000 genes, a total surprise given the previous significantly higher estimates that were based on the number of expressed sequence tags (ESTs) in the public databases. This apparent disparity suggests a major role for alternative splicing in creating genetic complexity, and has brought the study of splicing regulation to the forefront of molecular genetics. It is likely that an abundance of species-specific splice variants will be identified as the characterization of alternatively spliced transcripts progresses."}

{"project":"craft-ca-core-dev","denotations":[{"id":"T2947","span":{"begin":26,"end":42},"obj":"PR:000043184"},{"id":"T2948","span":{"begin":33,"end":40},"obj":"SO:0001060"},{"id":"T2949","span":{"begin":50,"end":55},"obj":"NCBITaxon:9606"},{"id":"T2950","span":{"begin":56,"end":65},"obj":"SO:0000853"},{"id":"T2951","span":{"begin":157,"end":165},"obj":"GO:0016020"},{"id":"T2952","span":{"begin":166,"end":173},"obj":"SO:0000417"},{"id":"T2953","span":{"begin":199,"end":205},"obj":"CHEBI:36916"},{"id":"T2954","span":{"begin":314,"end":328},"obj":"GO:0005770"},{"id":"T2955","span":{"begin":319,"end":328},"obj":"_FRAGMENT"},{"id":"T2956","span":{"begin":339,"end":355},"obj":"SO:0001529"},{"id":"T2957","span":{"begin":329,"end":338},"obj":"GO:0005764"},{"id":"T2958","span":{"begin":329,"end":355},"obj":"SO:0001530"},{"id":"T2959","span":{"begin":423,"end":428},"obj":"PR:000010252"},{"id":"T2960","span":{"begin":438,"end":448},"obj":"NCBITaxon:6239"},{"id":"T2961","span":{"begin":449,"end":458},"obj":"SO:0000853"},{"id":"T2962","span":{"begin":462,"end":468},"obj":"PR:000010252"},{"id":"T2963","span":{"begin":547,"end":561},"obj":"GO:0005770"},{"id":"T2964","span":{"begin":569,"end":578},"obj":"GO:0005764"},{"id":"T2965","span":{"begin":584,"end":589},"obj":"NCBITaxon:10088"},{"id":"T2966","span":{"begin":590,"end":596},"obj":"PR:000010252"},{"id":"T2967","span":{"begin":597,"end":601},"obj":"SO:0000704"},{"id":"T2968","span":{"begin":610,"end":631},"obj":"GO:0000380"},{"id":"T2969","span":{"begin":647,"end":654},"obj":"SO:0001060"},{"id":"T2970","span":{"begin":687,"end":698},"obj":"GO:0005737"},{"id":"T2971","span":{"begin":756,"end":765},"obj":"GO:0005764"},{"id":"T2972","span":{"begin":756,"end":782},"obj":"SO:0001530"},{"id":"T2973","span":{"begin":818,"end":825},"obj":"SO:0000417"},{"id":"T2974","span":{"begin":1016,"end":1023},"obj":"SO:0001060"},{"id":"T2975","span":{"begin":1033,"end":1043},"obj":"GO:0042571"},{"id":"T2976","span":{"begin":1115,"end":1121},"obj":"PR:000010252"},{"id":"T2977","span":{"begin":1132,"end":1136},"obj":"NCBITaxon:10088"},{"id":"T2978","span":{"begin":1210,"end":1215},"obj":"NCBITaxon:10088"},{"id":"T2979","span":{"begin":1216,"end":1220},"obj":"SO:0000704"},{"id":"T2980","span":{"begin":1216,"end":1231},"obj":"GO:0010467"},{"id":"T2981","span":{"begin":1273,"end":1279},"obj":"PR:000010252"},{"id":"T2982","span":{"begin":1280,"end":1287},"obj":"SO:0001060"},{"id":"T2983","span":{"begin":1303,"end":1309},"obj":"NCBITaxon:9606"},{"id":"T2984","span":{"begin":1334,"end":1355},"obj":"GO:0000380"},{"id":"T2985","span":{"begin":1388,"end":1391},"obj":"NCBITaxon:9606"},{"id":"T2986","span":{"begin":1396,"end":1401},"obj":"NCBITaxon:10088"},{"id":"T2987","span":{"begin":1421,"end":1426},"obj":"SO:0000704"},{"id":"T2988","span":{"begin":1456,"end":1463},"obj":"NCBITaxon:species"},{"id":"T2989","span":{"begin":1473,"end":1491},"obj":"GO:0000380"},{"id":"T2990","span":{"begin":1502,"end":1505},"obj":"PR:000010514"},{"id":"T2991","span":{"begin":1507,"end":1513},"obj":"UBERON:0000345"},{"id":"T2992","span":{"begin":1507,"end":1542},"obj":"PR:000010514"},{"id":"T2993","span":{"begin":1514,"end":1529},"obj":"CL:0000128"},{"id":"T2994","span":{"begin":1530,"end":1542},"obj":"CHEBI:17089"},{"id":"T2995","span":{"begin":1563,"end":1569},"obj":"GO:0008380"},{"id":"T2996","span":{"begin":1582,"end":1588},"obj":"NCBITaxon:9606"},{"id":"T2997","span":{"begin":1611,"end":1615},"obj":"NCBITaxon:10088"},{"id":"T2998","span":{"begin":1622,"end":1628},"obj":"PR:000031229"},{"id":"T2999","span":{"begin":1653,"end":1659},"obj":"NCBITaxon:9986"},{"id":"T3000","span":{"begin":1669,"end":1675},"obj":"GO:0008380"},{"id":"T3001","span":{"begin":1704,"end":1712},"obj":"GO:0016020"},{"id":"T3002","span":{"begin":1713,"end":1719},"obj":"SO:0000417"},{"id":"T3003","span":{"begin":1809,"end":1814},"obj":"NCBITaxon:9606"},{"id":"T3004","span":{"begin":1815,"end":1821},"obj":"SO:0001026"},{"id":"T3005","span":{"begin":1867,"end":1872},"obj":"SO:0000704"},{"id":"T3006","span":{"begin":1974,"end":1983},"obj":"GO:0010467"},{"id":"T3007","span":{"begin":1974,"end":1997},"obj":"SO:0000345"},{"id":"T3008","span":{"begin":1999,"end":2003},"obj":"SO:0000345"},{"id":"T3009","span":{"begin":2080,"end":2100},"obj":"GO:0000380"},{"id":"T3010","span":{"begin":2113,"end":2120},"obj":"SO:0000704"},{"id":"T3011","span":{"begin":2162,"end":2181},"obj":"GO:0043484"},{"id":"T3012","span":{"begin":2256,"end":2263},"obj":"NCBITaxon:species"},{"id":"T3013","span":{"begin":2273,"end":2279},"obj":"GO:0008380"},{"id":"T3014","span":{"begin":2335,"end":2356},"obj":"GO:0000380"},{"id":"T3015","span":{"begin":2335,"end":2368},"obj":"SO:1001187"}],"relations":[{"id":"R1776","pred":"_lexicallyChainedTo","subj":"T2956","obj":"T2955"}],"text":"Conclusions\nComparison of Mcoln1 isoform 1 to its human homologue shows striking similarity at both the amino acid and nucleotide level. All six of the transmembrane domains, as well as the putative cation channel are highly conserved. The putative di-leucine (L-L-X-X) motif at the C-terminus, which may act as a late endosomal/lysosomal targeting signal, is also conserved [9]. This speculation is supported by work with cup-5[13], the c. elegans homologue of MCOLN1, since cellular localization studies suggest that the protein is found in the late endosomes and/or lysosomes.\nThe mouse Mcoln1 gene has two alternatively spliced isoforms, with isoform 2 having a different c-terminal cytoplasmic tail. The unique 86 amino acid c-terminal tail lacks the lysosomal targeting signal and does not contain any conserved domains when compared against the current profile databases. We speculate that this protein may have similar channel function but an alternate subcellular localization, but this must be proven once isoform-specific antibodies are raised. However, our results suggest that phenotypic assessment of Mcoln1 knock-out mice may be complicated and that care must be taken when interpreting data on mouse gene expression and phenotype.\nInterestingly, the second Mcoln1 isoform is not seen in humans and the sequence of the alternatively spliced region is not conserved between man and mouse. To date, very few genes have been reported that show species specific alternative splice variants. MOG, myelin/oligodendrocyte glycoprotein, has many different splice variants in humans that are not found in mice [17]. ATP11B, a P-type ATPase, has a rabbit-specific splice variant that deletes a transmembrane domain and therefore likely alters the putative function of the protein [18]. Sequencing of the human genome has led to estimates of approximately 32,000 genes, a total surprise given the previous significantly higher estimates that were based on the number of expressed sequence tags (ESTs) in the public databases. This apparent disparity suggests a major role for alternative splicing in creating genetic complexity, and has brought the study of splicing regulation to the forefront of molecular genetics. It is likely that an abundance of species-specific splice variants will be identified as the characterization of alternatively spliced transcripts progresses."}

{"project":"2_test","denotations":[{"id":"11897010-11030752-10449851","span":{"begin":376,"end":377},"obj":"11030752"},{"id":"11897010-11326278-10449852","span":{"begin":429,"end":431},"obj":"11326278"},{"id":"11897010-8915905-10449853","span":{"begin":1617,"end":1619},"obj":"8915905"}],"text":"Conclusions\nComparison of Mcoln1 isoform 1 to its human homologue shows striking similarity at both the amino acid and nucleotide level. All six of the transmembrane domains, as well as the putative cation channel are highly conserved. The putative di-leucine (L-L-X-X) motif at the C-terminus, which may act as a late endosomal/lysosomal targeting signal, is also conserved [9]. This speculation is supported by work with cup-5[13], the c. elegans homologue of MCOLN1, since cellular localization studies suggest that the protein is found in the late endosomes and/or lysosomes.\nThe mouse Mcoln1 gene has two alternatively spliced isoforms, with isoform 2 having a different c-terminal cytoplasmic tail. The unique 86 amino acid c-terminal tail lacks the lysosomal targeting signal and does not contain any conserved domains when compared against the current profile databases. We speculate that this protein may have similar channel function but an alternate subcellular localization, but this must be proven once isoform-specific antibodies are raised. However, our results suggest that phenotypic assessment of Mcoln1 knock-out mice may be complicated and that care must be taken when interpreting data on mouse gene expression and phenotype.\nInterestingly, the second Mcoln1 isoform is not seen in humans and the sequence of the alternatively spliced region is not conserved between man and mouse. To date, very few genes have been reported that show species specific alternative splice variants. MOG, myelin/oligodendrocyte glycoprotein, has many different splice variants in humans that are not found in mice [17]. ATP11B, a P-type ATPase, has a rabbit-specific splice variant that deletes a transmembrane domain and therefore likely alters the putative function of the protein [18]. Sequencing of the human genome has led to estimates of approximately 32,000 genes, a total surprise given the previous significantly higher estimates that were based on the number of expressed sequence tags (ESTs) in the public databases. This apparent disparity suggests a major role for alternative splicing in creating genetic complexity, and has brought the study of splicing regulation to the forefront of molecular genetics. It is likely that an abundance of species-specific splice variants will be identified as the characterization of alternatively spliced transcripts progresses."}

{"project":"craft-ca-core-ex-dev","denotations":[{"id":"T3457","span":{"begin":26,"end":42},"obj":"PR_EXT:000043184"},{"id":"T3458","span":{"begin":33,"end":40},"obj":"SO_EXT:0001060"},{"id":"T3459","span":{"begin":50,"end":55},"obj":"NCBITaxon:9606"},{"id":"T3460","span":{"begin":56,"end":65},"obj":"SO_EXT:0000853"},{"id":"T3461","span":{"begin":104,"end":114},"obj":"CHEBI_SO_EXT:amino_acid"},{"id":"T3462","span":{"begin":119,"end":129},"obj":"CHEBI_SO_EXT:nucleotide"},{"id":"T3463","span":{"begin":157,"end":165},"obj":"GO:0016020"},{"id":"T3464","span":{"begin":166,"end":173},"obj":"SO_EXT:0000417"},{"id":"T3465","span":{"begin":199,"end":205},"obj":"CHEBI:36916"},{"id":"T3466","span":{"begin":199,"end":213},"obj":"GO_EXT:0005261"},{"id":"T3467","span":{"begin":225,"end":234},"obj":"SO_EXT:biological_conservation_process_or_quality"},{"id":"T3468","span":{"begin":252,"end":259},"obj":"CHEBI_SO_EXT:leucine"},{"id":"T3469","span":{"begin":270,"end":275},"obj":"SO_EXT:sequence_or_structure_motif"},{"id":"T3470","span":{"begin":283,"end":293},"obj":"CHEBI_SO_EXT:C_terminus_or_C_terminal_region"},{"id":"T3472","span":{"begin":319,"end":328},"obj":"_FRAGMENT"},{"id":"T3473","span":{"begin":339,"end":355},"obj":"SO_EXT:0001529"},{"id":"T3474","span":{"begin":329,"end":338},"obj":"GO:0005764"},{"id":"T3475","span":{"begin":329,"end":355},"obj":"SO_EXT:0001530"},{"id":"T3476","span":{"begin":339,"end":348},"obj":"GO_EXT:biological_routing_or_transport"},{"id":"T3477","span":{"begin":365,"end":374},"obj":"SO_EXT:biological_conservation_process_or_quality"},{"id":"T3478","span":{"begin":423,"end":428},"obj":"PR_EXT:000010252"},{"id":"T3479","span":{"begin":438,"end":448},"obj":"NCBITaxon:6239"},{"id":"T3480","span":{"begin":449,"end":458},"obj":"SO_EXT:0000853"},{"id":"T3481","span":{"begin":462,"end":468},"obj":"PR_EXT:000010252"},{"id":"T3482","span":{"begin":476,"end":484},"obj":"CL_GO_EXT:cell"},{"id":"T3483","span":{"begin":485,"end":497},"obj":"GO_PATO_EXT:biological_localization_process_or_quality"},{"id":"T3484","span":{"begin":523,"end":530},"obj":"CHEBI_PR_EXT:protein"},{"id":"T3485","span":{"begin":547,"end":561},"obj":"GO:0005770"},{"id":"T3486","span":{"begin":569,"end":578},"obj":"GO:0005764"},{"id":"T3487","span":{"begin":584,"end":589},"obj":"NCBITaxon:10088"},{"id":"T3488","span":{"begin":590,"end":596},"obj":"PR_EXT:000010252"},{"id":"T3489","span":{"begin":597,"end":601},"obj":"SO_EXT:0000704"},{"id":"T3490","span":{"begin":610,"end":631},"obj":"GO:0000380"},{"id":"T3491","span":{"begin":610,"end":640},"obj":"SO_EXT:alternative_splice_variant"},{"id":"T3492","span":{"begin":647,"end":654},"obj":"SO_EXT:0001060"},{"id":"T3493","span":{"begin":676,"end":686},"obj":"CHEBI_SO_EXT:C_terminus_or_C_terminal_region"},{"id":"T3494","span":{"begin":687,"end":698},"obj":"GO:0005737"},{"id":"T3495","span":{"begin":719,"end":729},"obj":"CHEBI_SO_EXT:amino_acid"},{"id":"T3496","span":{"begin":730,"end":740},"obj":"CHEBI_SO_EXT:C_terminus_or_C_terminal_region"},{"id":"T3497","span":{"begin":756,"end":765},"obj":"GO:0005764"},{"id":"T3498","span":{"begin":756,"end":782},"obj":"SO_EXT:0001530"},{"id":"T3499","span":{"begin":766,"end":775},"obj":"GO_EXT:biological_routing_or_transport"},{"id":"T3500","span":{"begin":808,"end":817},"obj":"SO_EXT:biological_conservation_process_or_quality"},{"id":"T3501","span":{"begin":818,"end":825},"obj":"SO_EXT:0000417"},{"id":"T3502","span":{"begin":902,"end":909},"obj":"CHEBI_PR_EXT:protein"},{"id":"T3503","span":{"begin":927,"end":934},"obj":"GO_EXT:0015267"},{"id":"T3504","span":{"begin":961,"end":972},"obj":"GO_UBERON_EXT:cellular_component_or_cell_part"},{"id":"T3505","span":{"begin":964,"end":972},"obj":"CL_GO_EXT:cell"},{"id":"T3506","span":{"begin":973,"end":985},"obj":"GO_PATO_EXT:biological_localization_process_or_quality"},{"id":"T3507","span":{"begin":1016,"end":1023},"obj":"SO_EXT:0001060"},{"id":"T3508","span":{"begin":1033,"end":1043},"obj":"GO:0042571"},{"id":"T3509","span":{"begin":1115,"end":1121},"obj":"PR_EXT:000010252"},{"id":"T3510","span":{"begin":1132,"end":1136},"obj":"NCBITaxon:10088"},{"id":"T3511","span":{"begin":1210,"end":1215},"obj":"NCBITaxon:10088"},{"id":"T3512","span":{"begin":1216,"end":1220},"obj":"SO_EXT:0000704"},{"id":"T3513","span":{"begin":1216,"end":1231},"obj":"GO:0010467"},{"id":"T3514","span":{"begin":1273,"end":1279},"obj":"PR_EXT:000010252"},{"id":"T3515","span":{"begin":1280,"end":1287},"obj":"SO_EXT:0001060"},{"id":"T3516","span":{"begin":1303,"end":1309},"obj":"NCBITaxon:9606"},{"id":"T3517","span":{"begin":1318,"end":1326},"obj":"SO_EXT:biological_sequence"},{"id":"T3518","span":{"begin":1334,"end":1355},"obj":"GO:0000380"},{"id":"T3519","span":{"begin":1370,"end":1379},"obj":"SO_EXT:biological_conservation_process_or_quality"},{"id":"T3520","span":{"begin":1388,"end":1391},"obj":"NCBITaxon:9606"},{"id":"T3521","span":{"begin":1396,"end":1401},"obj":"NCBITaxon:10088"},{"id":"T3522","span":{"begin":1421,"end":1426},"obj":"SO_EXT:0000704"},{"id":"T3523","span":{"begin":1456,"end":1463},"obj":"NCBITaxon:species"},{"id":"T3524","span":{"begin":1473,"end":1491},"obj":"GO:0000380"},{"id":"T3525","span":{"begin":1473,"end":1500},"obj":"SO_EXT:alternative_splice_variant"},{"id":"T3526","span":{"begin":1502,"end":1505},"obj":"PR_EXT:000010514"},{"id":"T3527","span":{"begin":1507,"end":1513},"obj":"UBERON:0000345"},{"id":"T3528","span":{"begin":1507,"end":1542},"obj":"PR_EXT:000010514"},{"id":"T3529","span":{"begin":1514,"end":1529},"obj":"CL:0000128"},{"id":"T3530","span":{"begin":1530,"end":1542},"obj":"CHEBI:17089"},{"id":"T3531","span":{"begin":1563,"end":1569},"obj":"GO:0008380"},{"id":"T3532","span":{"begin":1563,"end":1578},"obj":"SO_EXT:alternative_splice_variant"},{"id":"T3533","span":{"begin":1582,"end":1588},"obj":"NCBITaxon:9606"},{"id":"T3534","span":{"begin":1611,"end":1615},"obj":"NCBITaxon:10088"},{"id":"T3535","span":{"begin":1622,"end":1628},"obj":"PR_EXT:000031229"},{"id":"T3536","span":{"begin":1632,"end":1645},"obj":"GO_EXT:0015662"},{"id":"T3537","span":{"begin":1653,"end":1659},"obj":"NCBITaxon:9986"},{"id":"T3538","span":{"begin":1669,"end":1675},"obj":"GO:0008380"},{"id":"T3539","span":{"begin":1669,"end":1683},"obj":"SO_EXT:alternative_splice_variant"},{"id":"T3540","span":{"begin":1689,"end":1696},"obj":"SO_EXT:sequence_deletion_process"},{"id":"T3541","span":{"begin":1704,"end":1712},"obj":"GO:0016020"},{"id":"T3542","span":{"begin":1713,"end":1719},"obj":"SO_EXT:0000417"},{"id":"T3543","span":{"begin":1777,"end":1784},"obj":"CHEBI_PR_EXT:protein"},{"id":"T3544","span":{"begin":1809,"end":1814},"obj":"NCBITaxon:9606"},{"id":"T3545","span":{"begin":1815,"end":1821},"obj":"SO_EXT:0001026"},{"id":"T3546","span":{"begin":1867,"end":1872},"obj":"SO_EXT:0000704"},{"id":"T3547","span":{"begin":1974,"end":1983},"obj":"GO:0010467"},{"id":"T3548","span":{"begin":1974,"end":1997},"obj":"SO_EXT:0000345"},{"id":"T3549","span":{"begin":1993,"end":1997},"obj":"CHEBI_SO_EXT:molecular_indicator_or_label_or_marker_or_tag"},{"id":"T3550","span":{"begin":1999,"end":2003},"obj":"SO_EXT:0000345"},{"id":"T3551","span":{"begin":2080,"end":2100},"obj":"GO:0000380"},{"id":"T3552","span":{"begin":2113,"end":2120},"obj":"SO_EXT:0000704"},{"id":"T3553","span":{"begin":2162,"end":2181},"obj":"GO:0043484"},{"id":"T3554","span":{"begin":2202,"end":2211},"obj":"CHEBI_EXT:polyatomic_entity_or_group"},{"id":"T3555","span":{"begin":2212,"end":2220},"obj":"OBI_SO_EXT:gene_or_genetic_investigation_or_genetic_process"},{"id":"T3556","span":{"begin":2256,"end":2263},"obj":"NCBITaxon:species"},{"id":"T3557","span":{"begin":2273,"end":2279},"obj":"GO:0008380"},{"id":"T3558","span":{"begin":2273,"end":2288},"obj":"SO_EXT:alternative_splice_variant"},{"id":"T3559","span":{"begin":2335,"end":2356},"obj":"GO:0000380"},{"id":"T3560","span":{"begin":2335,"end":2368},"obj":"SO_EXT:1001187"},{"id":"T3471","span":{"begin":314,"end":328},"obj":"GO:0005770"}],"relations":[{"id":"R2189","pred":"_lexicallyChainedTo","subj":"T3473","obj":"T3472"}],"text":"Conclusions\nComparison of Mcoln1 isoform 1 to its human homologue shows striking similarity at both the amino acid and nucleotide level. All six of the transmembrane domains, as well as the putative cation channel are highly conserved. The putative di-leucine (L-L-X-X) motif at the C-terminus, which may act as a late endosomal/lysosomal targeting signal, is also conserved [9]. This speculation is supported by work with cup-5[13], the c. elegans homologue of MCOLN1, since cellular localization studies suggest that the protein is found in the late endosomes and/or lysosomes.\nThe mouse Mcoln1 gene has two alternatively spliced isoforms, with isoform 2 having a different c-terminal cytoplasmic tail. The unique 86 amino acid c-terminal tail lacks the lysosomal targeting signal and does not contain any conserved domains when compared against the current profile databases. We speculate that this protein may have similar channel function but an alternate subcellular localization, but this must be proven once isoform-specific antibodies are raised. However, our results suggest that phenotypic assessment of Mcoln1 knock-out mice may be complicated and that care must be taken when interpreting data on mouse gene expression and phenotype.\nInterestingly, the second Mcoln1 isoform is not seen in humans and the sequence of the alternatively spliced region is not conserved between man and mouse. To date, very few genes have been reported that show species specific alternative splice variants. MOG, myelin/oligodendrocyte glycoprotein, has many different splice variants in humans that are not found in mice [17]. ATP11B, a P-type ATPase, has a rabbit-specific splice variant that deletes a transmembrane domain and therefore likely alters the putative function of the protein [18]. Sequencing of the human genome has led to estimates of approximately 32,000 genes, a total surprise given the previous significantly higher estimates that were based on the number of expressed sequence tags (ESTs) in the public databases. This apparent disparity suggests a major role for alternative splicing in creating genetic complexity, and has brought the study of splicing regulation to the forefront of molecular genetics. It is likely that an abundance of species-specific splice variants will be identified as the characterization of alternatively spliced transcripts progresses."}