| Note |
SMAP1 is a member in the ArfGAP protein family. |
| Description | There are two isoform proteins. One translated from an isoform A transcript is constituted by 467, and the other from an isoform B is by 440 aa residues. A protein diagram shown above represents an isoform B type. |
| Expression | Both isoform transcripts are detected in various human tissues. Expression appears to be almost ubiquitous. |
| Localisation | SMAP1 protein is detected in the cytoplasm of cells, and appears to be highly concentrated near the plasma membrane. |
| Function | SMAP1 functions as a GTPase-activating protein for an Arf6 GTPase. Arf6 is a Ras-related, small GTPase, and regulates clathrin-dependent and -independent endocytosis as well as actin dynamics. SMAP1 is specifically involved in the Arf6-regulated, clathrin-dependent endocytosis. This is achieved by direct interaction of SMAP1 with clathrin heavy chain. |
| Homology | As a highly homologous gene to SMAP1, SMAP2 is identified on 1p34.1-35.3. SMAP1 and SMAP2 constitute a small subfamily in the ArfGAP family. SMAP2 protein is specifically involved in the early endosomes to trans-Golgi network transport. |
| Entity | t(6;11)(q13;q23) in acute leukemia. |
| Note | Two cases have been reported so far.
|
| Disease | One case is from an M4 subtype of acute myeloid leukemia. A type of leukemia is not described for the other case. |
| Hybrid/Mutated Gene | One leukemia patient possessed the 46, XX, t(6;11)(q13;q23) karyotype. In this patient, reciprocal translocation occured between intron 11 of MLL gene and intron 6 of SMAP1 gene. The chimeric 5'-MLL-SMAP1-3' transcript encodes a chimeric MLL-SMAP1 protein. |
| Abnormal Protein | MLL-SMAP1 |
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| Schematic illustration of chimeric MLL-SMAP1 protein. The authentic MLL and SMAP1 proteins are also shown.
AT hook, an AT-hook domain; NLS, a nuclear localization signal; MT, a methyltransferase domain; PHD, a plant homeodomain zinc finger; BROMO, a bromo domain; SET, a su(var)3-9, enhancer-of-zeste, trithorax domain. GAP, an ArfGAP domain; K-rich, a lysine-rich region; CHC, a clathrin heavy chain-binding motif; CALM, a clathrin assembly protein (CALM)-binding domain. |
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